|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
34-514 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 1006.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 34 NLKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLAD 113
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 114 LMERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLL 193
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 194 MFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLI 273
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 274 KEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGN 353
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 354 PLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSI 433
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 434 DDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 1958642200 514 K 514
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
38-511 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 900.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 38 QHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMER 117
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 118 DRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIW 197
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 198 KIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 277
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 278 GKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ 357
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 358 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVI 437
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642200 438 KRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
37-513 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 737.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 37 IQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLME 116
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 117 RDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFI 196
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 197 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 276
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 277 AGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLT 356
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 357 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 436
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642200 437 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
37-511 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 707.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 37 IQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPW-RTMDASERGRLLNKLADLM 115
Cdd:cd07143 4 EQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWgLKVSGSKRGRCLSKLADLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 116 ERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMF 195
Cdd:cd07143 82 ERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 196 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 275
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 276 AAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 355
Cdd:cd07143 242 AAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 356 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 435
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 436 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-511 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 705.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 19 AMSSPAQPAVpaplanlKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRT 98
Cdd:PLN02466 44 AVEEPITPPV-------QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 99 MDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREP 178
Cdd:PLN02466 116 MTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 179 IGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 258
Cdd:PLN02466 196 IGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 259 DKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEF 338
Cdd:PLN02466 276 DKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 339 VRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKE 418
Cdd:PLN02466 356 VEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 419 EIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELG 498
Cdd:PLN02466 436 EIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKG 515
|
490
....*....|...
gi 1958642200 499 EHGLYEYTELKTV 511
Cdd:PLN02466 516 IYSLNNYLQVKAV 528
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
38-514 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 686.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 38 QHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMER 117
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 118 DRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFI 196
Cdd:COG1012 81 RREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 197 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 276
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 277 AGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLT 356
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 357 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 435
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 436 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCY-MILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 514
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGtTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-511 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 678.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 38 QHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMER 117
Cdd:cd07144 6 QPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 118 DRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIW 197
Cdd:cd07144 84 NRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 198 KIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 277
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 278 GkSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKK-YVLGNPLT 356
Cdd:cd07144 244 A-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 357 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGG---GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSI 433
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 434 DDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-511 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 671.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 48 WHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEA 127
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 128 INGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGN 207
Cdd:pfam00171 77 LENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 208 TVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTL 287
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 288 ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDK 367
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 368 EQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL 447
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 448 AAGVFTKDLDRAITVSSALQAGVVWVNCYMILSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
36-515 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 667.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 36 KIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLM 115
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 116 ERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMF 195
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 196 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 275
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 276 AAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 355
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 356 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 435
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 436 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 515
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
43-511 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 622.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 202
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 203 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNL 282
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 283 KRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQG 362
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 363 PQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 438
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642200 439 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
80-513 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 619.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 80 DKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAnAYLSDLGGSIKALKYCAGWADKI 159
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 160 HGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVV 238
Cdd:cd07078 77 HGEVIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 239 NIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQ 318
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 319 GQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN-K 397
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 398 GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYM 477
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958642200 478 I-LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
54-511 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 613.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 54 GKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKV 133
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 134 FANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 213
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 214 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKS 293
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 294 PCIVFADA-DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDK 372
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 373 ILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAG 450
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642200 451 VFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
59-511 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 592.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVfanay 138
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKAL----KYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 213
Cdd:cd07114 75 IRETRAQVRYLaewyRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 214 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKS 293
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 294 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKI 373
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 374 LDLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAA 449
Cdd:cd07114 314 ERYVARAREEGARVLTGGERpsgaDLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642200 450 GVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
59-515 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 587.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 138
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGKSPCIVF 298
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 378
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDR 458
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642200 459 AITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 515
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
35-514 |
0e+00 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 579.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 35 LKIQHtKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADL 114
Cdd:cd07140 2 LKMPH-QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 115 MERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSD----GDIFTFTRREPIGVCGQIIPWNF 190
Cdd:cd07140 80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 191 PLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVG 270
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 271 KLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYV 350
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 351 LGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKF 430
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 431 KS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTEL 508
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*.
gi 1958642200 509 KTVAMK 514
Cdd:cd07140 480 KTVTIE 485
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
59-513 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 561.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 138
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 298
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 378
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTK 454
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 455 DLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
59-513 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 551.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 138
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQT 217
Cdd:cd07103 77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 218 PLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGK-LIKEAAgkSNLKRVTLELGGKSPCI 296
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 297 VFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDL 376
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 377 IESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDL 456
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642200 457 DRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
43-511 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 536.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLM-ERDRLL 121
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 122 lATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 201
Cdd:PRK13252 87 -AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 202 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSn 281
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 282 LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 361
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 362 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVI 437
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642200 438 KRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
42-512 |
0e+00 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 525.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 42 IFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMER--DR 119
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEAraDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 120 LLLATIEAINGGKVFANAY-----LSDLGGSIKALKYCAgWADKIHGQTIpsdgdiftftRREPIGVCGQIIPWNFPLLM 194
Cdd:cd07138 78 LAQAITLEMGAPITLARAAqvglgIGHLRAAADALKDFE-FEERRGNSLV----------VREPIGVCGLITPWNWPLNQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 195 FIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK 274
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 275 EAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP 354
Cdd:cd07138 227 EAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 355 LTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGG-GR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 431
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 432 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
.
gi 1958642200 512 A 512
Cdd:cd07138 465 Q 465
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
59-511 |
0e+00 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 523.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 138
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 298
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 378
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLECGGGRWGNK-----GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 453
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 454 KDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-513 |
0e+00 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 522.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 60 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAyL 139
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 140 SDLGGSIKALKYCAGWADKIHGQTIPSDG-DIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07118 80 GEIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 298
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 378
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLD 457
Cdd:cd07118 319 AGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 458 RAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
43-509 |
0e+00 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 521.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 202
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 203 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNL 282
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 283 KRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQG 362
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 363 PQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 438
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642200 439 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELK 509
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
41-509 |
0e+00 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 520.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 41 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 120
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 121 LLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 200
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 201 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKs 280
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 281 NLKRVTLELGGKSPCIVFADA-----DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 355
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 356 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 431
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 432 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELK 509
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
59-512 |
0e+00 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 519.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 138
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 lSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07109 79 -ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 298
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLtQGINQGPQIDKEQHDKILDLIE 378
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:cd07109 316 RARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 456 LDRAITVSSALQAGVVWVNCYMILSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 512
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
59-511 |
1.43e-174 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 499.57 E-value: 1.43e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 138
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LsDLGGSIKALKYCAGWADKIH---GQTIPSDGDIFT-FTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPA 214
Cdd:cd07110 78 W-DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 215 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 294
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 295 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 374
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 375 DLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 452
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 453 TKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
59-513 |
1.54e-172 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 494.45 E-value: 1.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRtMDASERGRLLNKLADLMERDR-LLLATIEAINGGKVfANA 137
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKeELRALLVAEVGAPV-MTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 138 YLSDLGGSIKALKYCAGWADKIHG-QTIPSDGDIFTFT----RREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVK 212
Cdd:cd07089 78 RAMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 213 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGK 292
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 293 SPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFvrksVERAKKYV----LGNPLTQGINQGPQIDKE 368
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEV----VEALAAAFealpVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 369 QHDKILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYG 446
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642200 447 LAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07089 393 LSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
84-513 |
2.53e-172 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 490.59 E-value: 2.53e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 84 KAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAnAYLSDLGGSIKALKYCAGWADKIHGQT 163
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 164 IPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVP 242
Cdd:cd06534 77 LPSpDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 243 GYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCC 322
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 323 VAASRIFVEESVYDEFVRKSVerakkyvlgnpltqginqgpqidkeqhdkildliesgkkegaklecgggrwgnkgffvq 402
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 403 pTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMIL-SA 481
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 1958642200 482 QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
41-511 |
7.83e-172 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 493.51 E-value: 7.83e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 41 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 120
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 121 LLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 200
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 201 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKs 280
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 281 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 360
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 361 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 436
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 437 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
59-511 |
5.43e-170 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 487.42 E-value: 5.43e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 138
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFP---GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LsDLGGSIKALKYCAGWADKIHgqTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07106 78 F-EVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAgFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 298
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 378
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDR 458
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958642200 459 AITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
43-513 |
8.49e-168 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 482.92 E-value: 8.49e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK---AWERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYLsDLGGSIKALKYCAGWADKIHGQTIPSDG---DIFTFtrREPIGVCGQIIPWNFPLLMFIWKI 199
Cdd:cd07088 78 AKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRpneNIFIF--KVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 200 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGK 279
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 280 sNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGI 359
Cdd:cd07088 235 -NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 360 NQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 438
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 439 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
27-518 |
2.37e-167 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 483.08 E-value: 2.37e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 27 AVPAPLANLkiqhtkiFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAF--QIGSPWRTMDASER 104
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 105 GRLLNKLADLMERDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHG-QTIPSDGDIFTF---TRREPIG 180
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAkQKAPVSLPMETFkgyVLKEPLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 181 VCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDK 260
Cdd:PLN02467 154 VVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 261 VAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVR 340
Cdd:PLN02467 234 IAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 341 KSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG--NKGFFVQPTVFSNVTDEMRIAKE 418
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 419 EIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELG 498
Cdd:PLN02467 393 EVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELG 472
|
490 500
....*....|....*....|
gi 1958642200 499 EHGLYEYTELKTVAMKISQK 518
Cdd:PLN02467 473 EWGLENYLSVKQVTKYISDE 492
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
59-511 |
7.28e-167 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 479.90 E-value: 7.28e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 138
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGqtiPSDGDIF----TFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPA 214
Cdd:cd07092 78 DDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 215 EQTPLTALHMASLIKEaGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 294
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 295 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 374
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 375 DLIEsGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTK 454
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642200 455 DLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
43-511 |
1.99e-166 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 479.44 E-value: 1.99e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKkfPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 121
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAF---PAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 122 LATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 200
Cdd:cd07097 79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPStRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 201 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkS 280
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 281 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 360
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 361 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 438
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 439 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI-LSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 511
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
42-513 |
7.48e-166 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 477.84 E-value: 7.48e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 42 IFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLL 121
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 122 LATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKI-HGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 200
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 201 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkS 280
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG-E 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 281 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 360
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 361 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 438
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 439 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMiLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
43-511 |
1.40e-165 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 477.61 E-value: 1.40e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 121
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 122 LATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 200
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 201 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKS 280
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 281 NlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 360
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 361 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 436
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642200 437 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI-LSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 511
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
39-516 |
9.33e-165 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 475.17 E-value: 9.33e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 39 HTKIFINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERD 118
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 119 RLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGqtiPSDG----DIFTFTRREPIGVCGQIIPWNFPLLM 194
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGeyleGHTSMIRRDPVGVVASIAPWNYPLMM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 195 FIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK 274
Cdd:PRK13473 155 AAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 275 EAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP 354
Cdd:PRK13473 234 SAAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 355 LTQGINQGPQIDKEQHDKILDLIESGKKEG-AKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSI 433
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 434 DDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
...
gi 1958642200 514 KIS 516
Cdd:PRK13473 473 KHT 475
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
59-511 |
1.99e-164 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 473.77 E-value: 1.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 138
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 298
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGV-FYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLI 377
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 378 ESGKKE-GAK-LECG---GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 452
Cdd:cd07108 316 DLGLSTsGATvLRGGplpGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642200 453 TKDLDRAITVSSALQAGVVWVN-CYMILSAQcPFGGFKMSGNGRELGEHGLYE-YTELKTV 511
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNqGGGQQPGQ-SYGGFKQSGLGREASLEGMLEhFTQKKTV 455
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
43-505 |
2.53e-163 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 471.88 E-value: 2.53e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKihgqtipSDGDiftFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 202
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTE---LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 203 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEA-AGKSn 281
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRAtAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 282 lKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 361
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 362 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRAN 441
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642200 442 NTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEY 505
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
57-513 |
1.98e-161 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 466.04 E-value: 1.98e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 57 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 136
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 137 AYLsDLGGSIKALKYCAGWADKIHGQTIPSDG-DIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 215
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 216 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPC 295
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 296 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 375
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 376 LIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 456 LDRAITVSSALQAGVVWVNCYMILS-AQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
16-513 |
2.09e-160 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 465.32 E-value: 2.09e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 16 AKPAMSSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsP 95
Cdd:PLN02278 1 PSTRASSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 96 WRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLSDLGGSiKALKYCAGWADKIHGQTIPS-DGDIFTFT 174
Cdd:PLN02278 78 WSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGA-SFLEYFAEEAKRVYGDIIPSpFPDRRLLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 175 RREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISS 254
Cdd:PLN02278 157 LKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 255 HMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESV 334
Cdd:PLN02278 237 SPKVRKITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 335 YDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMR 414
Cdd:PLN02278 316 YDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDML 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 415 IAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNG 494
Cdd:PLN02278 396 IFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLG 475
|
490
....*....|....*....
gi 1958642200 495 RELGEHGLYEYTELKTVAM 513
Cdd:PLN02278 476 REGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
78-513 |
1.12e-159 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 460.84 E-value: 1.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 78 DVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLsDLGGSIKALKYCAGWAD 157
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 158 KIHGQTIPSDGD-IFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLT-ALHMASLIKEAGFPP 235
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 236 GVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVF 315
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 316 YHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG 395
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 396 NkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNC 475
Cdd:cd07104 316 L---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958642200 476 YMIL-SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
43-514 |
6.96e-157 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 455.36 E-value: 6.96e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQT----IPS-DGDIFT-FTRREPIGVCGQIIPWNFPLLMFI 196
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSmQGERYTaFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 197 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEA 276
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 277 AgKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLT 356
Cdd:cd07113 240 A-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 357 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 436
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 437 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 514
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
33-515 |
1.27e-155 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 452.81 E-value: 1.27e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 33 ANLKIQhTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLA 112
Cdd:PRK09847 14 LSLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 113 DLMERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPL 192
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 193 LMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKL 272
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 273 IKEAAGKSNLKRVTLELGGKSPCIVFADA-DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVL 351
Cdd:PRK09847 252 LLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 352 GNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 431
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL--DGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 432 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
....
gi 1958642200 512 AMKI 515
Cdd:PRK09847 490 WISL 493
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
43-515 |
2.39e-155 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 451.95 E-value: 2.39e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYLSdlggSIKALKYCAGWADK----IHGQTIPSDgDIFTFTRREPIGVCGQIIPWNFPLLMFIWK 198
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQ----VIRAAENFRFFADKceeaMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 199 IGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKeAAG 278
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIM-RNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 279 KSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQG 358
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 359 INQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG-------NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 431
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 432 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
....
gi 1958642200 512 AMKI 515
Cdd:TIGR02299 475 ALAL 478
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
59-511 |
7.51e-154 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 446.82 E-value: 7.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAnAY 138
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 218
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 219 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPCIVF 298
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYH-QGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLI 377
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 378 ESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 453
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 454 KDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
57-513 |
2.10e-151 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 440.49 E-value: 2.10e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 57 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 136
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 137 AyLSDLGGSIKALKYCAGWADKIHGQTIPSDG-----DIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVV 211
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 212 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGksnLKRVTLELGG 291
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 292 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHD 371
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 372 KILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGV 451
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 452 FTKDLDRAITVSSALQAGVVWVNcyMILSAQC---PFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMIN--DSSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
37-515 |
2.54e-146 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 428.76 E-value: 2.54e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 37 IQHtkiFINNEWHDSvsGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLME 116
Cdd:TIGR03216 1 IRN---FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALK--GPWGKMTVAERADLLYAVADEIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 117 R--DRLLLAtiEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQ----TIPSDGDIFTFTRREPIGVCGQIIPWNF 190
Cdd:TIGR03216 74 RrfDDFLAA--EVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTEcfemATPDGKGALNYAVRKPLGVVGVISPWNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 191 PLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGP-TAGAAISSHMDVDKVAFTGSTQV 269
Cdd:TIGR03216 152 PLLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 270 GKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKY 349
Cdd:TIGR03216 232 GSAIMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 350 VLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGG--RWGNK---GFFVQPTVFSNVTDEMRIAKEEIFGPV 424
Cdd:TIGR03216 311 KIGVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGvpDFGDAlagGAWVQPTIWTGLPDSARVVTEEIFGPC 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 425 QQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYE 504
Cdd:TIGR03216 391 CHIAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEF 470
|
490
....*....|.
gi 1958642200 505 YTELKTVAMKI 515
Cdd:TIGR03216 471 YTELTNVCIKL 481
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-512 |
5.62e-145 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 424.07 E-value: 5.62e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 57 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 136
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 137 AYLsDLGGSIKALKYCAGWADKIHGQTIPSDGDIFT-----FTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVV 211
Cdd:cd07145 78 SRV-EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNerriaFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 212 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGG 291
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 292 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHD 371
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 372 KILDLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGV 451
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642200 452 FTKDLDRAITVSSALQAGVVWVNCYMILSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 512
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWdNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
38-515 |
1.18e-141 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 417.78 E-value: 1.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 38 QHTKIFINNEWHDSvsGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 116
Cdd:cd07124 31 REYPLVIGGKEVRT--EEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 117 RDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFI 196
Cdd:cd07124 106 RRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 197 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 276
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 277 AGK-----SNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVL 351
Cdd:cd07124 265 AAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 352 GNPLTQGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGN--KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMK 429
Cdd:cd07124 345 GDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 430 FKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN--CYMILSAQCPFGGFKMSG-NGRELGEHGLYEYT 506
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFM 503
|
....*....
gi 1958642200 507 ELKTVAMKI 515
Cdd:cd07124 504 QPKTVTENF 512
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
43-511 |
1.50e-140 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 413.88 E-value: 1.50e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 201
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 202 ALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGYGPtAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 277
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 278 GKSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ 357
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 358 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 435
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 436 VIKRANNTTYGLAAGVFTKDLDRAITVSSA--LQAGVVWVNCYMI-LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
60-513 |
8.58e-139 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 408.27 E-value: 8.58e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 60 LNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTmDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYL 139
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 140 sDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPL 219
Cdd:cd07120 80 -EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 220 TALHMASLIKEA-GFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 298
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP-TLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 378
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLECGGGRWG---NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTeglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 456 LDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
43-509 |
1.35e-138 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 408.76 E-value: 1.35e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 202
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 203 LSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNL 282
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 283 KRVTLELGGKSPCIVFA------DADLDIAVE----FAhhgvfYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLG 352
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEgfvmFA-----LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 353 NPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNvTDEMRIAKEEIFGPVQQIM 428
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelggLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 429 KFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTEL 508
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQT 472
|
.
gi 1958642200 509 K 509
Cdd:cd07116 473 K 473
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
46-514 |
7.49e-134 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 396.29 E-value: 7.49e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 46 NEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLME--RDRLLLA 123
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEerRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 124 TIEAINGGKVFANAylsDLGGSIKALKYCAGWADKIHGQTIPSDGD-----IFtftrREPIGVCGQIIPWNFPLLMFIWK 198
Cdd:cd07151 78 LIRESGSTRIKANI---EWGAAMAITREAATFPLRMEGRILPSDVPgkenrVY----REPLGVVGVISPWNFPLHLSMRS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 199 IGPALSCGNTVVVKPAEQTPLTA-LHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 277
Cdd:cd07151 151 VAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 278 GKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ 357
Cdd:cd07151 231 GR-HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 358 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVI 437
Cdd:cd07151 310 DTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 438 KRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMIL-SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 514
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
79-511 |
1.19e-128 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 381.42 E-value: 1.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 79 VDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYcagWADK 158
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRY---YAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 159 IHG----QTIPSDGDIfTFTRREPIGVCGQIIPWNFPLlmfiWKI----GPALSCGNTVVVKPAEQTPLTALHMASLIKE 230
Cdd:cd07100 74 AEAfladEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 231 AGFPPGVVNIVPGYGPTAGAAISSHMdVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFA 310
Cdd:cd07100 149 AGFPEGVFQNLLIDSDQVEAIIADPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 311 HHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECG 390
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 391 GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGV 470
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958642200 471 VWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
59-513 |
3.98e-127 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 378.70 E-value: 3.98e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 138
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPSD-----GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 213
Cdd:cd07094 79 RVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 214 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsnlKRVTLELGGKS 293
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG---KRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 294 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKI 373
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 374 LDLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 453
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642200 454 KDLDRAITVSSALQAGVVWVNCYMILSAQ-CPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
66-498 |
4.39e-127 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 378.17 E-value: 4.39e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 66 EVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAyLSDLGGS 145
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA-GFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 146 IKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTA-LHM 224
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 225 ASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLD 304
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 305 IAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEG 384
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 385 AKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSS 464
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1958642200 465 ALQAGVVWVNCYMIL-SAQCPFGGFKMSGNGRELG 498
Cdd:cd07152 393 RLRTGMLHINDQTVNdEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-512 |
3.18e-125 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 373.48 E-value: 3.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 60 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYL 139
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 140 sDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTR----REPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 215
Cdd:cd07099 78 -EVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKatveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 216 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISShmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPC 295
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 296 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 375
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 376 LIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 456 LDRAITVSSALQAGVVWVNCYMILSAQC--PFGGFKMSGNGRELGEHGLYEYTELKTVA 512
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPalPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
40-514 |
5.04e-123 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 368.77 E-value: 5.04e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 40 TKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDR 119
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP---AWSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 120 LLLATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTIP-SDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWK 198
Cdd:cd07085 78 DELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 199 IGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAG 278
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 279 KSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQG 358
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 359 INQGPQIDKEQHDKILDLIESGKKEGAKLECgGGRwGNK------GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKS 432
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVL-DGR-GVKvpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 433 IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYM-ILSAQCPFGGFKMS--GNGRELGEHGLYEYTELK 509
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSffGDLHFYGKDGVRFYTQTK 472
|
....*
gi 1958642200 510 TVAMK 514
Cdd:cd07085 473 TVTSR 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
41-496 |
1.47e-122 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 367.67 E-value: 1.47e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 41 KIFINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRL 120
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 121 LLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFT-----FTRREPIGVCGQIIPWNFPLLMF 195
Cdd:cd07082 80 EVANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 196 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 275
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 276 AAGKsnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 355
Cdd:cd07082 239 QHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 356 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 435
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 436 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCymilsaQC-------PFGGFKMSGNGRE 496
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS------KCqrgpdhfPFLGRKDSGIGTQ 455
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
38-515 |
1.65e-122 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 368.88 E-value: 1.65e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 38 QHTKIFINNEWHDSvsGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 116
Cdd:PRK03137 35 QDYPLIIGGERITT--EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 117 RDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKI-HGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMF 195
Cdd:PRK03137 110 RRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 196 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 275
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 276 AAGKSN-----LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYV 350
Cdd:PRK03137 269 RAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 351 LGNPlTQGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKF 430
Cdd:PRK03137 349 VGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 431 KSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN--CYMILSAQCPFGGFKMSG-NGRELGEHGLYEYTE 507
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGtDSKAGGPDYLLLFLQ 506
|
....*...
gi 1958642200 508 LKTVAMKI 515
Cdd:PRK03137 507 AKTVSEMF 514
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
78-511 |
2.10e-121 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 363.05 E-value: 2.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 78 DVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLLLATIEAINGGKVFANaylSDLGGSIKALKYCAGW 155
Cdd:cd07105 1 DADQAVEAAAAAFPA---WSKTPPSERRDILLKAADLLEsrRDEFIEAMMEETGATAAWAG---FNVDLAAGMLREAASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 156 ADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFP 234
Cdd:cd07105 75 ITQIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 235 PGVVNIV---PGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAH 311
Cdd:cd07105 155 KGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 312 HGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTqginqGPQIDKEQHDKILDLIESGKKEGAKLECGG 391
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 392 -GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGV 470
Cdd:cd07105 309 lADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958642200 471 VWVN-CYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07105 389 VHINgMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
50-512 |
4.77e-118 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 357.65 E-value: 4.77e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 50 DSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLM-ERDRLLLATIEAI 128
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVlENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 129 NGgKVFANAYLSDLGGSIKALKYcAGWADKI-----HGQTIPsdgdIFTFTR--REPIGVCGQIIPWNFPLLMFIWKIGP 201
Cdd:PRK09407 104 TG-KARRHAFEEVLDVALTARYY-ARRAPKLlaprrRAGALP----VLTKTTelRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 202 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdVDKVAFTGSTQVGKLIKEAAGkSN 281
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG-RR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 282 LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 361
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 362 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRA 440
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 441 NNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN-CYMIL--SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 512
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAwgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
43-515 |
3.14e-117 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 354.21 E-value: 3.14e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 201
Cdd:PRK11241 91 ARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPGhQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 202 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsN 281
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-D 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 282 LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 361
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 362 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRAN 441
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642200 442 NTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 515
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-513 |
9.86e-117 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 351.93 E-value: 9.86e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 57 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 136
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 137 AYlSDLGGSIKALKYCAGWADKIHGQTIPSDGD-----IFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVV 211
Cdd:cd07147 78 AR-GEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 212 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGygPTAGAAI-SSHMDVDKVAFTGSTQVGKLIKEAAGKsnlKRVTLELG 290
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 291 GKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQH 370
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 371 DKILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAG 450
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 451 VFTKDLDRAITVSSALQAGVVWVN---CYMILSAqcPFGGFKMSGNGRELGEHGLYEYTELKTVAM 513
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdvpTFRVDHM--PYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
59-511 |
4.13e-114 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 345.11 E-value: 4.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAArqafqiGSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 138
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIPSD-----GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 213
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 214 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGksnLKRVTLELGGKS 293
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 294 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKI 373
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 374 LDLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 453
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642200 454 KDLDRAITVSSALQAGVVWVN---CYMilSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 511
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNevpGFR--SELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
62-512 |
4.50e-114 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 345.06 E-value: 4.50e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 62 PATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLSD 141
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 142 LGGSIKALKYC----AGWADKIHGQTIPsdgdIFTFTR--REPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 215
Cdd:cd07101 80 LDVAIVARYYArraeRLLKPRRRRGAIP----VLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 216 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGKSPC 295
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 296 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 375
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 376 LIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTK 454
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642200 455 DLDRAITVSSALQAGVVWVN-CYMIL--SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 512
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
60-511 |
2.13e-112 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 340.76 E-value: 2.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 60 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAyl 139
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 140 sdlGGSIKALKYCAGW----ADKIHGQTIPSDGDIFT-FTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPA 214
Cdd:cd07102 76 ---GGEIRGMLERARYmisiAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 215 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 294
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 295 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 374
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 375 DLIESGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGV 451
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 452 FTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
108-511 |
1.64e-107 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 326.69 E-value: 1.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 108 LNKLADLM-ERDRLLLATIEAiNGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD---GDIFTFTRrePIGVCG 183
Cdd:PRK10090 1 LRKIAAGIrERASEISALIVE-EGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 184 QIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAF 263
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 264 TGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSV 343
Cdd:PRK10090 157 TGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 344 ERAKKYVLGNPLTQG-INQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFG 422
Cdd:PRK10090 236 EAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 423 PVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGL 502
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGL 395
|
....*....
gi 1958642200 503 YEYTELKTV 511
Cdd:PRK10090 396 HEYLQTQVV 404
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
61-512 |
4.04e-104 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 320.02 E-value: 4.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 61 NPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLS 140
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQ---REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 141 DLGGSIKALKYCAGWADKiHGQTIPSDGDIFTFTRR-----EPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 215
Cdd:cd07098 79 EILVTCEKIRWTLKHGEK-ALRPESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 216 QTPLTALHMASLIKEA----GFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGG 291
Cdd:cd07098 158 QVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 292 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHD 371
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 372 KILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL 447
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 448 AAGVFTKDLDRAITVSSALQAGVVWVN----CYMILsaQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 512
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQ--QLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
60-511 |
6.10e-92 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 288.17 E-value: 6.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 60 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYl 139
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 140 SDLGGSIKALKYCAGWADKIHGQTiPSD----GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 215
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADE-PADaaavGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 216 QTPLTALHMASLIKEAGFPPGVVNIVPgYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPC 295
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 296 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 375
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 376 LIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 456 LDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:PRK09406 399 EAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
38-515 |
1.41e-89 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 283.32 E-value: 1.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 38 QHTKIFINNEWHDSvsGKKFPVLNP-ATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 116
Cdd:cd07083 17 RAYPLVIGGEWVDT--KERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 117 RDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTI------PSDGDIFTftrrEPIGVCGQIIPWNF 190
Cdd:cd07083 92 RRRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESFY----VGLGAGVVISPWNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 191 PLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVG 270
Cdd:cd07083 167 PVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 271 KLIKEAAGK-----SNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVER 345
Cdd:cd07083 247 KKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 346 AKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQ 425
Cdd:cd07083 327 AERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 426 QIMKFKSID--DVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI--LSAQCPFGGFKMSG-NGRELGEH 500
Cdd:cd07083 406 SVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGtNAKTGGPH 485
|
490
....*....|....*
gi 1958642200 501 GLYEYTELKTVAMKI 515
Cdd:cd07083 486 YLRRFLEMKAVAERF 500
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
45-498 |
9.77e-87 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 275.24 E-value: 9.77e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 45 NNEWhdSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLAT 124
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 125 IEAINGGKVFANAYlsdlgGSIKAL----KYCAGWADKIHGQTIPSDgdiftftrR---------EPIGVCGQIIPWNFP 191
Cdd:cd07130 79 LVSLEMGKILPEGL-----GEVQEMidicDFAVGLSRQLYGLTIPSE--------RpghrmmeqwNPLGVVGVITAFNFP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 192 LLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGST 267
Cdd:cd07130 146 VAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 268 QVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVE---FAHHGVfyhQGQCCVAASRIFVEESVYDEFVRKSVE 344
Cdd:cd07130 225 AVGRQVGQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAVRavlFAAVGT---AGQRCTTTRRLIVHESIYDEVLERLKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 345 RAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDeMRIAKEEIFGPV 424
Cdd:cd07130 301 AYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 425 QQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQA--GVVWVNCYM----ILSAqcpFGGFKMSGNGRELG 498
Cdd:cd07130 380 LYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIGTsgaeIGGA---FGGEKETGGGRESG 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
31-498 |
3.46e-85 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 272.53 E-value: 3.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 31 PLANLKIQHTKiFINNEWHDS--VSGKKF------PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDA 101
Cdd:cd07125 15 PLEALADALKA-FDEKEWEAIpiINGEETetgegaPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 102 SERGRLLNKLADLMERDR---LLLATIEAingGKVFANAyLSDLGGSIKALKYCAGWADKI--HGQTIPSDG--DIFTFT 174
Cdd:cd07125 91 EERAEILEKAADLLEANRgelIALAAAEA---GKTLADA-DAEVREAIDFCRYYAAQARELfsDPELPGPTGelNGLELH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 175 RREpIGVCgqIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISS 254
Cdd:cd07125 167 GRG-VFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 255 HMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEE 332
Cdd:cd07125 244 HPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 333 SVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEgAKLECGGGRWGNKGFFVQPTVFSNVTDE 412
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 413 MRiaKEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYM---ILSAQcPFGG 487
Cdd:cd07125 403 DL--TTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNItgaIVGRQ-PFGG 479
|
490
....*....|.
gi 1958642200 488 FKMSGNGRELG 498
Cdd:cd07125 480 WGLSGTGPKAG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
59-494 |
1.84e-82 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 263.51 E-value: 1.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 59 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWrtMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 138
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIKALKYCAGWADKIHGQTIP------SDGDIfTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVK 212
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPmgltpaSAGRI-AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 213 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdvdKVA---FTGSTQVGKLI--KEAAGKsnlkRVTL 287
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDP----RVAffsFIGSARVGWMLrsKLAPGT----RCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 288 ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDK 367
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 368 EQHDKILDLIESGKKEGAKLECGGGRWGNKGFfvQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL 447
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958642200 448 AAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQ-CPFGGFKMSGNG 494
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
41-511 |
6.91e-80 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 257.50 E-value: 6.91e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 41 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRL 120
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 121 LLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKI 199
Cdd:TIGR01722 79 EIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 200 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGK 279
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 280 SNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVyDEFVRKSVERAKKYVLGNPLTQGI 359
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 360 NQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGF----FVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 435
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 436 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcyMILSAQCP---FGGFKMS--GNGRELGEHGLYEYTELKT 510
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN--VPIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYTRGKT 472
|
.
gi 1958642200 511 V 511
Cdd:TIGR01722 473 V 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-495 |
1.65e-74 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 242.18 E-value: 1.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 78 DVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVF------ANAYLSDLGGSIKALKY 151
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 152 CAGWADKihgqtipSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA 231
Cdd:cd07095 78 RTGERAT-------PMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 232 GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAH 311
Cdd:cd07095 151 GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 312 HGVFYHQGQCCVAASRIFVEES-VYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL----DLIESGKK---E 383
Cdd:cd07095 230 QSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLlaqqDLLALGGEpllA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 384 GAKLECGGGrwgnkgfFVQPTVFsNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD---LDRAI 460
Cdd:cd07095 310 MERLVAGTA-------FLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDealFERFL 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958642200 461 TvssALQAGVV-WVNCYMILSAQCPFGGFKMSGNGR 495
Cdd:cd07095 382 A---RIRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
41-494 |
1.38e-73 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 241.58 E-value: 1.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 41 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRL 120
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 121 LLATIEAINGGKVFANAyLSDLGGSIKALKYCA-------GWADKIHGQTIPSDG-DIFTFTRREPIGVCGQIIPWNFPL 192
Cdd:PLN00412 94 PIAECLVKEIAKPAKDA-VTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNErNKYCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 193 LMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGStQVGKL 272
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 273 IKEAAGKSNLKrvtLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLG 352
Cdd:PLN00412 252 ISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 353 NPlTQGINQGPQIDKEQHDKILDLIESGKKEGAKLEcggGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKS 432
Cdd:PLN00412 329 PP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 433 IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcymilSAQC------PFGGFKMSGNG 494
Cdd:PLN00412 405 VEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN-----SAPArgpdhfPFQGLKDSGIG 467
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
29-494 |
3.86e-73 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 252.09 E-value: 3.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 29 PAPLANLKIQHTKiFINNEWH-------DSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMD 100
Cdd:PRK11905 535 EATLAALDEALNA-FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 101 ASERGRLLNKLADLMERDR---LLLATIEAingGKVFANAyLSDLGGSIKALKYCAGWADkihgqtipsdgDIFTFTRRE 177
Cdd:PRK11905 611 AAERAAILERAADLMEAHMpelFALAVREA---GKTLANA-IAEVREAVDFLRYYAAQAR-----------RLLNGPGHK 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 178 PIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 257
Cdd:PRK11905 676 PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPR 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 258 VDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCvAASRI-FVEESV 334
Cdd:PRK11905 756 IAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRC-SALRVlCLQEDV 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 335 YDEFVRKSVERAKKYVLGNP--LTQGInqGPQIDKEQHDKILDLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFSnvTD 411
Cdd:PRK11905 835 ADRVLTMLKGAMDELRIGDPwrLSTDV--GPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--ID 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 412 EMRIAKEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI---LSAQcPFG 486
Cdd:PRK11905 911 SISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIgavVGVQ-PFG 989
|
....*...
gi 1958642200 487 GFKMSGNG 494
Cdd:PRK11905 990 GEGLSGTG 997
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
175-511 |
8.42e-72 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 235.20 E-value: 8.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 175 RREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGygptaGAAISS 254
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DAEVAQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 255 H---MDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVE 331
Cdd:cd07134 171 AlleLPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 332 ESVYDEFV---RKSVER---AKKYVLGNP-LTQGINQGpqidkeQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVqPT 404
Cdd:cd07134 250 ESVKDAFVehlKAEIEKfygKDAARKASPdLARIVNDR------HFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIA-PT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 405 VFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDlDRAI-TVSSALQAGVVWVNCYMI--LSA 481
Cdd:cd07134 323 VLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD-KANVnKVLARTSSGGVVVNDVVLhfLNP 401
|
330 340 350
....*....|....*....|....*....|
gi 1958642200 482 QCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-494 |
1.79e-71 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 247.16 E-value: 1.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 50 DSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLL-LATI 125
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEahRAELMaLLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 126 EAingGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTipsdgdiftfTRREPIGVCGQIIPWNFPLLMFIWKIGPALSC 205
Cdd:COG4230 642 EA---GKTLPDA-IAEVREAVDFCRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 206 GNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA-AGKSNlKR 284
Cdd:COG4230 708 GNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTlAARDG-PI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 285 VTL--ELGGKSPCIVfaD---------ADldiAVEFAhhgvFYHQGQCCVAAsRI-FVEESVYDEFvrksVER----AKK 348
Cdd:COG4230 787 VPLiaETGGQNAMIV--DssalpeqvvDD---VLASA----FDSAGQRCSAL-RVlCVQEDIADRV----LEMlkgaMAE 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 349 YVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFsnvtdEM-RIA--KEEIFGPV 424
Cdd:COG4230 853 LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-----EIdSISdlEREVFGPV 927
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 425 QQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMIlSA----QcPFGGFKMSGNG 494
Cdd:COG4230 928 LHVVRYKAdeLDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNII-GAvvgvQ-PFGGEGLSGTG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
58-509 |
1.06e-70 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 234.03 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 58 PVLNPAT-EEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 136
Cdd:TIGR01238 54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPT---WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 137 AyLSDLGGSIKALKYCAGWADkihgqtipsdgDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQ 216
Cdd:TIGR01238 131 A-IAEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 217 TPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSP 294
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 295 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 374
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 375 DLIESGKKEG---AKLECGGGRWGNKGFFVQPTVFSnvTDEMRIAKEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAA 449
Cdd:TIGR01238 359 AHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTM 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642200 450 GVFTKDLDRAITVSSALQAGVVWVNCYM---ILSAQcPFGGFKMSGNG-RELGEHGLYEYTELK 509
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQvgaVVGVQ-PFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
43-511 |
1.21e-70 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 243.95 E-value: 1.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWH----DSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMER 117
Cdd:PRK11904 546 FLEKQWQagpiINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 118 DR---LLLATIEAingGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGdiftFT------RREPIGV--CgqII 186
Cdd:PRK11904 623 NRaelIALCVREA---GKTLQDA-IAEVREAVDFCRYYAAQARRLFGAPEKLPG----PTgesnelRLHGRGVfvC--IS 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 187 PWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS 266
Cdd:PRK11904 693 PWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGS 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 267 TQVGKLIKEA-AGKSNlKRVTL--ELGGKSPCIVFADADL----DIAVEFAhhgvFYHQGQCCVAASRIFVEESVYDEFV 339
Cdd:PRK11904 773 TETARIINRTlAARDG-PIVPLiaETGGQNAMIVDSTALPeqvvDDVVTSA----FRSAGQRCSALRVLFVQEDIADRVI 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 340 RKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEG---AKLECGGGrwGNKGFFVQPTVFSnvTDEMRIA 416
Cdd:PRK11904 848 EMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPAG--TENGHFVAPTAFE--IDSISQL 923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 417 KEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI---LSAQcPFGGFKMS 491
Cdd:PRK11904 924 EREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIgavVGVQ-PFGGQGLS 1002
|
490 500
....*....|....*....|.
gi 1958642200 492 GNG-RELGEHGLYEYTELKTV 511
Cdd:PRK11904 1003 GTGpKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
87-511 |
2.06e-70 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 231.61 E-value: 2.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 87 RQAFQI-GSPwrtmDASERGRLLNKLADLM--ERDRLllatIEAIN---GGKVFANAYLSDLGGSIKALKYC----AGW- 155
Cdd:cd07133 8 KAAFLAnPPP----SLEERRDRLDRLKALLldNQDAL----AEAISadfGHRSRHETLLAEILPSIAGIKHArkhlKKWm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 156 -ADKIHG--QTIPSDGDIftftRREPIGVCGQIIPWNFPLLMfiwKIGP---ALSCGNTVVVKPAEQTPLTALHMASLIK 229
Cdd:cd07133 80 kPSRRHVglLFLPAKAEV----EYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 230 EAgFPPGVVNIVPGyGPTAGAAISShMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEF 309
Cdd:cd07133 153 EY-FDEDEVAVVTG-GADVAAAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 310 AHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKY---VLGNP-LTQGINQGpqidkeQHDKILDLIESGKKEGA 385
Cdd:cd07133 229 IAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPdYTSIINER------HYARLQGLLEDARAKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 386 KL-ECG-GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVS 463
Cdd:cd07133 303 RViELNpAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958642200 464 SALQAGVVWVNCYMILSAQ--CPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07133 383 RRTHSGGVTINDTLLHVAQddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
43-495 |
3.62e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 229.84 E-value: 3.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVF------ANAYLSDLGGSIKALKycagwadKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFI 196
Cdd:PRK09457 80 AEVIARETGKPLweaateVTAMINKIAISIQAYH-------ERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 197 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLI-KE 275
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 276 AAGKSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVY-DEFVRKSVERAKKYVLGNP 354
Cdd:PRK09457 232 FAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 355 LTQgiNQ---GPQIDKEQHDKILD----LIESGKK---EGAKLECGGGrwgnkgfFVQPTVFsNVTDEMRIAKEEIFGPV 424
Cdd:PRK09457 311 DAE--PQpfmGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEEYFGPL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642200 425 QQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVV-WVNCYMILSAQCPFGGFKMSGNGR 495
Cdd:PRK09457 381 LQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
8-514 |
6.94e-69 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 231.94 E-value: 6.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 8 RPNRTDTRAKPAMSSP---AQPAVPAPLANLkiqhtkifINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVK 84
Cdd:PLN02419 87 RPQFLALRSSWLSTSPeqsTQPQMPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 85 AARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTI 164
Cdd:PLN02419 159 AAKQAFPL---WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEYL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 165 P--SDGdIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVP 242
Cdd:PLN02419 235 PnvSNG-VDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVH 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 243 GYGPTAGaAISSHMDVDKVAFTGSTQVGKLI-KEAAGKSnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQC 321
Cdd:PLN02419 314 GTNDTVN-AICDDEDIRAVSFVGSNTAGMHIyARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 322 CVAASR-IFVEESvyDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGR----WGN 396
Cdd:PLN02419 391 CMALSTvVFVGDA--KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpGYE 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 397 KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcy 476
Cdd:PLN02419 469 KGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN-- 546
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958642200 477 MILSAQCPFggFKMSGNGREL-------GEHGLYEYTELKTVAMK 514
Cdd:PLN02419 547 VPIPVPLPF--FSFTGNKASFagdlnfyGKAGVDFFTQIKLVTQK 589
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
60-511 |
7.34e-69 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 228.21 E-value: 7.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 60 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYl 139
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 140 sdlGGSIKALKYCAGWADkiHG-------QTIPSDGDIFTFTRrePIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVK 212
Cdd:PRK13968 88 ---AEVAKSANLCDWYAE--HGpamlkaePTLVENQQAVIEYR--PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 213 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMdVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGK 292
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 293 SPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDK 372
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 373 ILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 452
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 453 TKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
82-511 |
1.36e-68 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 226.25 E-value: 1.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 82 AVKAARQAFQIGspwRTMDASERGRLLNKLadlmerDRLLLATIEAING------GKVFANAYLSDLG---GSIK-ALKY 151
Cdd:cd07087 3 LVARLRETFLTG---KTRSLEWRKAQLKAL------KRMLTENEEEIAAalyadlGKPPAEAYLTEIAvvlGEIDhALKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 152 CAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA 231
Cdd:cd07087 74 LKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 232 gFPPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAH 311
Cdd:cd07087 154 -FDPEAVAVVEG-GVEVATALLAE-PFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 312 HGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGiNQGPQIDKEQHDKILDLIESGKKEGaklecgG 391
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDGKVVI------G 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 392 GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVV 471
Cdd:cd07087 303 GQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958642200 472 WVNCYMI--LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07087 383 CVNDVLLhaAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
81-511 |
3.96e-67 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 223.15 E-value: 3.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 81 KAVKAARQAFQIGspwRTMDASERGRLLNKLADLMER--DRLLlatiEAING--GKVFANAYLSDLG---GSIK-ALKYC 152
Cdd:cd07136 2 SLVEKQRAFFKTG---ATKDVEFRIEQLKKLKQAIKKyeNEIL----EALKKdlGKSEFEAYMTEIGfvlSEINyAIKHL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 153 AGWADKIHGQT----IPSDGdiftFTRREPIGVCGQIIPWNFPLLMfiwKIGP---ALSCGNTVVVKPAEQTPLTALHMA 225
Cdd:cd07136 75 KKWMKPKRVKTpllnFPSKS----YIYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 226 SLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDvdKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDI 305
Cdd:cd07136 148 KIIEET-FDEEYVAVVEGGVEENQELLDQKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 306 AVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGinQGPQIDKEQH-DKILDLIESGKkeg 384
Cdd:cd07136 224 AAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP--DYGRIINEKHfDRLAGLLDNGK--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 385 akLECGGGrwGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVS 463
Cdd:cd07136 299 --IVFGGN--TDREtLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958642200 464 SALQAGVVWVN-CYM-ILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:cd07136 375 ENLSFGGGCINdTIMhLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
77-512 |
1.50e-65 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 218.63 E-value: 1.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 77 ADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLM-ERDRLLLATIEAINGGKVFaNAYLSDLGGS----IKALKY 151
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVkDNEEAIVEALKKDLGRPPF-ETLLTEVSGVkndiLHMLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 152 CAGWA-DKIhgqtiPSDGDIF-----TFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMA 225
Cdd:cd07135 81 LKKWAkDEK-----VKDGPLAfmfgkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 226 SLIKEAgFPPGVVNIVPGYGPTAGAAISSHMdvDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDI 305
Cdd:cd07135 156 ELVPKY-LDPDAFQVVQGGVPETTALLEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 306 AvefAHH---GVFYHQGQCCVAASRIFVEESVYDEFvrksVERAKKyVLGNPLTQGINQGPQ----IDKEQHDKILDLIE 378
Cdd:cd07135 232 A---AKRilwGKFGNAGQICVAPDYVLVDPSVYDEF----VEELKK-VLDEFYPGGANASPDytriVNPRHFNRLKSLLD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKkegAKLECGGGRwGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD--- 455
Cdd:cd07135 304 TTK---GKVVIGGEM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDkse 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 456 LDRAITvsSALQAGVVWVNCYM-ILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 512
Cdd:cd07135 380 IDHILT--RTRSGGVVINDTLIhVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
58-505 |
1.39e-59 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 213.30 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 58 PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERD-RLLLATI--EAingGKV 133
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPI---WFATPPAERAAILERAADLMEAQmQTLMGLLvrEA---GKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 134 FANAyLSDLGGSIKALKYCAGWADkihgqtipsdgDIFTFTRREPIG--VCgqIIPWNFPLLMFIWKIGPALSCGNTVVV 211
Cdd:PRK11809 736 FSNA-IAEVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 212 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK-------EAAGKSnlkr 284
Cdd:PRK11809 802 KPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQrnlagrlDPQGRP---- 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 285 VTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP--LTQGIn 360
Cdd:PRK11809 878 IPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPdrLSTDI- 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 361 qGPQIDKEQHDKILDLIESGKKEGAK---LECGGGRWGNKGFFVQPTVFS-NVTDEMriaKEEIFGPVQQIMKFKS--ID 434
Cdd:PRK11809 957 -GPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNRnqLD 1032
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 435 DVIKRANNTTYGLAAGVFTKdLDRAIT-VSSALQAGVVWVNCYMI---LSAQcPFGGFKMSGNGRELGehG-LYEY 505
Cdd:PRK11809 1033 ELIEQINASGYGLTLGVHTR-IDETIAqVTGSAHVGNLYVNRNMVgavVGVQ-PFGGEGLSGTGPKAG--GpLYLY 1104
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
43-510 |
8.30e-56 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 194.67 E-value: 8.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWhdSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 201
Cdd:PLN02315 99 GRLVSLEMGKILAEG-IGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 202 ALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 277
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 278 gKSNLKRVTLELGGKSPCIVFADADLDIAVE---FAHHGVfyhQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP 354
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRsvlFAAVGT---AGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 355 LTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSnVTDEMRIAKEEIFGPVQQIMKFKSID 434
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 435 DVIKRANNTTYGLAAGVFTKDLDRAITVSSALQA--GVVWVNCYM----ILSAqcpFGGFKMSGNGRELGEHGLYEYTEL 508
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIPTngaeIGGA---FGGEKATGGGREAGSDSWKQYMRR 488
|
..
gi 1958642200 509 KT 510
Cdd:PLN02315 489 ST 490
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
172-514 |
8.99e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.48 E-value: 8.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 172 TFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAA 251
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 252 ISSHMDVdkVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVE 331
Cdd:PTZ00381 182 LKEPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 332 ESVYDEFVRKSVERAKKYVLGNPLTQgiNQGPQIDKEQH-DKILDLIESGKKEGAKlecgGGRWGNKGFFVQPTVFSNVT 410
Cdd:PTZ00381 259 RSIKDKFIEALKEAIKEFFGEDPKKS--EDYSRIVNEFHtKRLAELIKDHGGKVVY----GGEVDIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 411 DEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN-CYMILSAQ-CPFGGF 488
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLLNPnLPFGGV 412
|
330 340
....*....|....*....|....*.
gi 1958642200 489 KMSGNGRELGEHGLYEYTELKTVAMK 514
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
67-492 |
4.45e-54 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 190.49 E-value: 4.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 67 VICHVEEGDKADVDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLME---RDRLLLATieAINGGKvfaNAYLSDLG 143
Cdd:cd07123 59 VLATYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAAT--MLGQGK---NVWQAEID 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 144 GS---IKALKYCAGWADKI-HGQTIPSDGDIFTFTRREPI-GVCGQIIPWNF----------PLLMfiwkigpalscGNT 208
Cdd:cd07123 131 AAcelIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFtaiggnlagaPALM-----------GNV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 209 VVVKPAEqtplTALHMASLI----KEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKS---- 280
Cdd:cd07123 200 VLWKPSD----TAVLSNYLVykilEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldry 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 281 -NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGI 359
Cdd:cd07123 276 rTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 360 NQGPQIDKEQHDKILDLIESGKKE-GAKLECGGGRWGNKGFFVQPTVFSnVTDEM-RIAKEEIFGPVQQIM-----KFKS 432
Cdd:cd07123 356 FMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIE-TTDPKhKLMTEEIFGPVLTVYvypdsDFEE 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642200 433 IDDVIkraNNTT-YGLAAGVFTKDLDRAITVSSALQ--AGVVWVN--CYMILSAQCPFGGFKMSG 492
Cdd:cd07123 435 TLELV---DTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
81-514 |
1.90e-48 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 173.18 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 81 KAVKAARQAFQIGspwRTMDASERGRLLNKLADLME--RDRLLLATIEAINggKVFANAYLSDLGGSIK----ALKYCAG 154
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEenEDEIVEALAKDLR--KPKFEAVLSEILLVKNeikyAISNLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 155 WAdkihgQTIPSDGDIFT-----FTRREPIGVCGQIIPWNFPL-LMFIWKIGpALSCGNTVVVKPAEQTPLTALHMASLI 228
Cdd:cd07132 77 WM-----KPEPVKKNLATllddvYIYKEPLGVVLIIGAWNYPLqLTLVPLVG-AIAAGNCVVIKPSEVSPATAKLLAELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 229 -----KEAgFPpgVVnivpgygpTAGAAISSHM---DVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFAD 300
Cdd:cd07132 151 pkyldKEC-YP--VV--------LGGVEETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 301 ADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYvLGNPLTQGINQGPQIDKEQHDKILDLIESG 380
Cdd:cd07132 219 CDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 381 KKegakleCGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT---KDLD 457
Cdd:cd07132 298 KV------AIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSnnkKVIN 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642200 458 RAITVSSalqAGVVWVNCYMILSA--QCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 514
Cdd:cd07132 372 KILSNTS---SGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
83-505 |
1.96e-45 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 164.89 E-value: 1.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 83 VKAARQAFQIGspwRTMDASERGRLLNKLADLM-ERDRLLLATIEAiNGGKVFANAYLSDLG---GSIK-ALKYCAGWAD 157
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSvlvSSCKlAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 158 ----KIHGQTIPSDGDIFTftrrEPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgF 233
Cdd:cd07137 81 pekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 234 PPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHG 313
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 314 VF-YHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGinQGPQIDKEQHDKILDLIESGKKEGAKLECGGG 392
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK--DLSRIVNSHHFQRLSRLLDDPSVADKIVHGGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 393 RwGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVW 472
Cdd:cd07137 311 R-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVT 389
|
410 420 430
....*....|....*....|....*....|....*
gi 1958642200 473 VNCYMI--LSAQCPFGGFKMSGNGRelgEHGLYEY 505
Cdd:cd07137 390 FNDTVVqyAIDTLPFGGVGESGFGA---YHGKFSF 421
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
43-498 |
1.12e-38 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 147.93 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSvSGKKFPVLNPATEEVICHVEeGDKADVDKAVKAARQafQIGSPWRTMDASERGRLLNKLADLMERDRLLL 122
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 123 ATIEAINGGKVFANAYLsDLGGSIKALKYCAGWADKIHGQTIPSDGD--------------IFTFTRrepiGVCGQIIPW 188
Cdd:PRK11903 84 YDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpafqgqhVLVPTR----GVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 189 NFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG-FPPGVVNIVPGygptAGAAISSH---MDVdkVAFT 264
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHlqpFDV--VSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 265 GSTQVGKLIK-EAAGKSNLKRVTLELGGKSPCIVFADADLDIAvEFAhhgVFYHQ---------GQCCVAASRIFVEESV 334
Cdd:PRK11903 233 GSAETAAVLRsHPAVVQRSVRVNVEADSLNSALLGPDAAPGSE-AFD---LFVKEvvremtvksGQKCTAIRRIFVPEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 335 YDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIEsGKKEGAKLECGGGRWG------NKGFFVQPTVF-- 406
Cdd:PRK11903 309 YDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLga 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 407 SNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLD--------------RAITVSSALQA---- 468
Cdd:PRK11903 388 SDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAflaaaaleladshgRVHVISPDVAAlhtg 467
|
490 500 510
....*....|....*....|....*....|.
gi 1958642200 469 -GVVwvncyMilsAQCPFGGFKMSGNGRELG 498
Cdd:PRK11903 468 hGNV-----M---PQSLHGGPGRAGGGEELG 490
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
72-505 |
7.60e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 136.78 E-value: 7.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 72 EEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLM--ERDRLLLATIEAIngGKVFANAYLSDLGGSIKAL 149
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESG---RTRSLEWRKSQLKGLLRLLkdNEEAIFKALHQDL--GKHRVEAYRDEVGVLTKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 150 KY---CAG-WADKIHGQ----TIPSDGDIFTftrrEPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTA 221
Cdd:PLN02203 76 NLalsNLKkWMAPKKAKlplvAFPATAEVVP----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 222 LHMASLIKeAGFPPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIV---F 298
Cdd:PLN02203 152 AFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdslS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 299 ADADLDIAVEFAHHGVFYH-QGQCCVAASRIFVEE---SVYDEFVRKSVeraKKYVLGNPLTQGinQGPQIDKEQH-DKI 373
Cdd:PLN02203 228 SSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEErfaPILIELLKSTI---KKFFGENPRESK--SMARILNKKHfQRL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 374 LDLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 453
Cdd:PLN02203 303 SNLLKDPRVAASIVH--GGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFT 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 454 KD--LDRAITvsSALQAGVVWVNCYMILSA--QCPFGGFKMSGNGRelgEHGLYEY 505
Cdd:PLN02203 381 NNekLKRRIL--SETSSGSVTFNDAIIQYAcdSLPFGGVGESGFGR---YHGKYSF 431
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
43-455 |
2.48e-33 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 132.78 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 43 FINNEWHDSvSGKKFPVLNPATEEVICHVEeGDKADVDKAVKAARQafqIGSP-WRTMDASERGRLLNKLAD-LMERDRL 120
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYARE---KGGPaLRALTFHERAAMLKALAKyLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 121 LLAtIEAINGGKVFANAYlsDLGGSIKALKYCAGWADK-IHGQTIPSDGDIFTFTRREPI----------GVCGQIIPWN 189
Cdd:cd07128 79 LYA-LSAATGATRRDSWI--DIDGGIGTLFAYASLGRReLPNAHFLVEGDVEPLSKDGTFvgqhiltprrGVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 190 FPllmfIW----KIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG-FPPGVVNIVPGygptAGAAISSHMDV-DKVAF 263
Cdd:cd07128 156 FP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGDLLDHLGEqDVVAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 264 TGSTQVGKLIKEAAG-KSNLKRVTLELGGKSPCIVFADADLDIAvEFAhhgVFYHQ---------GQCCVAASRIFVEES 333
Cdd:cd07128 228 TGSAATAAKLRAHPNiVARSIRFNAEADSLNAAILGPDATPGTP-EFD---LFVKEvaremtvkaGQKCTAIRRAFVPEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 334 VYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEgAKLECGG-------GRWGNKGFFVQPTVF 406
Cdd:cd07128 304 RVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfevvGADAEKGAFFPPTLL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958642200 407 -SNVTDEMRIAKE-EIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:cd07128 383 lCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
139-511 |
9.28e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 124.77 E-value: 9.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 139 LSDLGGSIK-ALKYCAGW----ADKIHGQTIPSDGDIFTftrrEPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 213
Cdd:PLN02174 72 VSLLRNSIKlALKQLKNWmapeKAKTSLTTFPASAEIVS----EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 214 AEQTPLTALHMASLIkEAGFPPGVVNIVPGYGPTAGAAISSHMdvDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKS 293
Cdd:PLN02174 148 SELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW--DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 294 PCIVFADADLDIAVEFAHHGVF-YHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLtQGINQGPQIDKEQHDK 372
Cdd:PLN02174 224 PVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 373 ILDLIEsgKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 452
Cdd:PLN02174 303 LSKLLD--EKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLF 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642200 453 TKDLDRAITVSSALQAGVVWVNCYMILSA--QCPFGGFKMSGNGRELGEHGLYEYTELKTV 511
Cdd:PLN02174 381 THNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
79-455 |
2.18e-29 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 120.42 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 79 VDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKvfANAYLSDLGGSIKALKYCA--GWA 156
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGK--GWMFAENICGDQVQLRARAfvIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 157 DKIHGQTIPSDGDIFTFTRRE---PIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG- 232
Cdd:cd07084 76 YRIPHEPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 233 FPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVG-KLIKEAAgksnLKRVTLELGGKSPCIVFADADL--DIAVEF 309
Cdd:cd07084 156 LPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAeKLALDAK----QARIYLELAGFNWKVLGPDAQAvdYVAWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 310 AHHGVFYhQGQCCVAASRIFVEEsvyDEFVRKSVERAKKYvlgnpLTQGINQGPQIDKEQHDKILDLIES-GKKEGAKLE 388
Cdd:cd07084 231 VQDMTAC-SGQKCTAQSMLFVPE---NWSKTPLVEKLKAL-----LARRKLEDLLLGPVQTFTTLAMIAHmENLLGSVLL 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 389 CGG------GRWGNKGFFVQPTVFSNVTDEMRIAK---EEIFGPVQQIMKFK--SIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:cd07084 302 FSGkelknhSIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdQLALVLELLERMHGSLTAAIYSND 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
79-376 |
5.52e-16 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 79.96 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 79 VDKAVKAARQA-FQIGSPWRTMDASERGRLLNKLADLMERdRLLLATieainggkvfanaylSDLGGSIKALKYCAGWAD 157
Cdd:cd07077 18 RDLIINAIANAlYDTRQRLASEAVSERGAYIRSLIANWIA-MMGCSE---------------SKLYKNIDTERGITASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 158 KIHGQTIPSDGDifTFTRREPIGVCGQIIPWNFPLLMfIWKIGPALSCGNTVVVKPAEQTPLTAlHMASLIKEAGFPPGV 237
Cdd:cd07077 82 HIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 238 VNIVPGYGPTAGAAIS----SHMDVDKVAFTGSTQVgklIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHG 313
Cdd:cd07077 158 PKILVLYVPHPSDELAeellSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642200 314 VFYHQGQCCVAASRIFVE---ESVYDEFVRKSVErAKKYVLGNPLTQGINQGPQIDKEQHDKILDL 376
Cdd:cd07077 235 KFFDQNACASEQNLYVVDdvlDPLYEEFKLKLVV-EGLKVPQETKPLSKETTPSFDDEALESMTPL 299
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
79-441 |
9.27e-15 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 76.43 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 79 VDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME--RDRLL-LATIEA------INGG--------KVFANAYLSd 141
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEalGDELVaRAHAETglpearLQGElgrttgqlRLFADLVRE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 142 lgGSikalkycagWADKI------HGQTIPSdGDIftftRRE-----PIGVCGqiiPWNFPLLMFIwkIG----PALSCG 206
Cdd:cd07129 77 --GS---------WLDARidpadpDRQPLPR-PDL----RRMlvplgPVAVFG---ASNFPLAFSV--AGgdtaSALAAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 207 NTVVVKPAEQTPLTALHMASLI----KEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAgksnL 282
Cdd:cd07129 136 CPVVVKAHPAHPGTSELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA----A 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 283 KR-----VTLELGGKSPCIVFADAdL-----DIAVEFAHH---GVfyhqGQCCVAASRIFVEESV-YDEFVRKSVERAKK 348
Cdd:cd07129 212 ARpepipFYAELGSVNPVFILPGA-LaergeAIAQGFVGSltlGA----GQFCTNPGLVLVPAGPaGDAFIAALAEALAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 349 YVLGNPLTQGINQGPQIDKEQ---HDKILDLIESGKKEGaklecgggrwgnkGFFVQPTVFsnVTDEMRIAK-----EEI 420
Cdd:cd07129 287 APAQTMLTPGIAEAYRQGVEAlaaAPGVRVLAGGAAAEG-------------GNQAAPTLF--KVDAAAFLAdpalqEEV 351
|
410 420
....*....|....*....|.
gi 1958642200 421 FGPVQQIMKFKSIDDVIKRAN 441
Cdd:cd07129 352 FGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
176-455 |
1.49e-09 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 60.20 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 176 REPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSh 255
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 256 MDVDKVAFTGSTQVG-KLIKEAAGKsnlkrVTLELGGKSPCIVFAD-ADLDIAVEFAHHGVFYHQGQCCVAASRIFVEES 333
Cdd:cd07126 219 ANPRMTLFTGSSKVAeRLALELHGK-----VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 334 -VYDEFVRKSVERAKKYVLGNpLTQG--INQGPQIDKEQHDKILDLiesgkkEGAKLECGGGRWGNKGF-----FVQPT- 404
Cdd:cd07126 294 wVQAGILDKLKALAEQRKLED-LTIGpvLTWTTERILDHVDKLLAI------PGAKVLFGGKPLTNHSIpsiygAYEPTa 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 405 VF-----SNVTDEMRIAKEEIFGPVQQIMKFK--SIDDVIKRANNTTYGLAAGVFTKD 455
Cdd:cd07126 367 VFvpleeIAIEENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
77-458 |
4.45e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 55.32 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 77 ADVDKAVKAARQAFQIgspWRTMDASERGRLLN--KLADLMERDRLLLATIEAINGG----KVFANAYLSDLGGSIKALK 150
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ---YRKCTLADREKIIEaiREALLSNAEELAEMAVEETGMGrvedKIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 151 YCAGWADkiHGqtipsdgdiFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP---AEQTPLTALHMAS- 226
Cdd:cd07121 81 TTAWSGD--NG---------LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELINk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 227 LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKlikeAAGKSNlKRVTLELGGKSPCIVFADADLDIA 306
Cdd:cd07121 150 AIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVK----AALSSG-KKAIGAGAGNPPVVVDETADIEKA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 307 VEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKsVERAKKYVLGNPLTQGI-------NQGPQIDKE----QHDKILD 375
Cdd:cd07121 225 ARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAA-MQRNGAYVLNDEQAEQLlevvlltNKGATPNKKwvgkDASKILK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 376 LIesGKKEGAKLECgggrwgnkgffvqptVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL--AAGVFT 453
Cdd:cd07121 304 AA--GIEVPADIRL---------------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHS 366
|
....*
gi 1958642200 454 KDLDR 458
Cdd:cd07121 367 KNVEN 371
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
75-474 |
1.46e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 54.02 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 75 DKADVDKAVKAARQAFQigsPWRtmDASERGRL---LNKLADLMERDrLLLATIEAINGGKVFANAYLSdlGGS------ 145
Cdd:cd07127 82 PQCDPDALLAAARAAMP---GWR--DAGARARAgvcLEILQRLNARS-FEMAHAVMHTTGQAFMMAFQA--GGPhaqdrg 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 146 IKALKYCAGWADKIHGQTIPsdgdIFTFTRREPI-----------GV-----CGQIIPWN-FPLLMfiwkigPALSCGNT 208
Cdd:cd07127 154 LEAVAYAWREMSRIPPTAEW----EKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 209 VVVKPAeqtPLTALHMASLIK-------EAGFPPGVVNIV--PGYGPTAGaAISSHMDVDKVAFTGSTQVGKLIKEAAGK 279
Cdd:cd07127 224 VIVKPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadTPEEPIAQ-TLATRPEVRIIDFTGSNAFGDWLEANARQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 280 snlKRVTLELGGKSPCIVFADADL-----DIAVEFAhhgvfYHQGQCCVAASRIFV---------EESVYDEfVRKSVER 345
Cdd:cd07127 300 ---AQVYTEKAGVNTVVVDSTDDLkamlrNLAFSLS-----LYSGQMCTTPQNIYVprdgiqtddGRKSFDE-VAADLAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 346 AKKYVLGNP-----LTQGInqgpqidkeQHDKILDLIESGKKEGAKLECGGGRwGNKGF---FVQPTVFSNVTDEMRIA- 416
Cdd:cd07127 371 AIDGLLADParaaaLLGAI---------QSPDTLARIAEARQLGEVLLASEAV-AHPEFpdaRVRTPLLLKLDASDEAAy 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642200 417 KEEIFGPVQQIMKFKSIDDVIKRANNT--TYG-LAAGVFTKD---LDRaiTVSSALQAGV---------VWVN 474
Cdd:cd07127 441 AEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDpevVER--VQEAALDAGValsinltggVFVN 511
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
77-376 |
5.48e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 52.21 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 77 ADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGG------KVFANAYLSDLGGSIKALK 150
Cdd:PRK15398 36 ASVDDAVAAAKVAQQR---YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNVAAAEKTPGVEDLT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 151 YCAGWADkiHGqtipsdgdiFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP---AEQTPLTALHMAS- 226
Cdd:PRK15398 113 TEALTGD--NG---------LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgAKKVSLRAIELLNe 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 227 LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGstqvGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLDIA 306
Cdd:PRK15398 182 AIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVVVDETADIEKA 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 307 VEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRkSVERAKKYvlgnpltqginqgpQIDKEQHDKILDL 376
Cdd:PRK15398 257 ARDIVKGASFDNNLPCIAEKEVIVVDSVADELMR-LMEKNGAV--------------LLTAEQAEKLQKV 311
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
150-495 |
1.05e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 51.11 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 150 KYCagwaDKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIK 229
Cdd:cd07081 71 VYK----DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 230 EA----GFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGstqvGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLDI 305
Cdd:cd07081 147 QAavaaGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 306 AVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ-------GINQGPQIDKEQHDKILDLIE 378
Cdd:cd07081 222 AVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQvqpvilkNGDVNRDIVGQDAYKIAAAAG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 379 SGKKEGAKLecgggrwgnkgFFVQPTVFsnvtDEMRIAKEEIFGPVQQIMKFKSIDDVIKRA----NNTTYGLAAGVFT- 453
Cdd:cd07081 302 LKVPQETRI-----------LIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSd 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958642200 454 --KDLDRAITVSSALQAGVVWVNcymilsAQCPFGGFKMSGNGR 495
Cdd:cd07081 367 niKAIENMNQFANAMKTSRFVKN------GPCSQGGLGDLYNFR 404
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
173-349 |
1.20e-05 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 47.82 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 173 FTRREPIGVCGQIIPWNFPLLMFiWKIGPALSCGNTVVVKPAEQTP-LTALHMASLIK--EAGFPPGVVNIVPGYGPTAG 249
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVPLLPV-MSILMGLLVKNVNLLKVSSSDPfTAAALLASFADldPTHPLADSLSVVYWDGGSTQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 250 AAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGV-FYHQgQCCVAASRI 328
Cdd:pfam05893 162 LEDLIVANADVVIAWGGEDAINAIRECLKPG--KQWIDFGAKISFAVVDREAALDKAAERAADDIcVFDQ-QACLSPQTV 238
|
170 180
....*....|....*....|....
gi 1958642200 329 FVE---ESVYDEFVRKSVERAKKY 349
Cdd:pfam05893 239 FVEsddKITPDEFAERLAAALAKR 262
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
177-475 |
2.18e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 46.72 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 177 EPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPgyGPT--AGA 250
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIE--EPSieLTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 251 AISSHMDVDKVAFTGStqvGKLIKEA--AGKSNlkrvtleLG---GKSPCIVFADADLDIAVE-------FAHhgvfyhq 318
Cdd:cd07122 172 ELMKHPDVDLILATGG---PGMVKAAysSGKPA-------IGvgpGNVPAYIDETADIKRAVKdiilsktFDN------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 319 GQCCVAASRIFVEESVYDEFVRKsVERAKKYVLgnpltqginqgpqiDKEQHDKILDLIesgkkegakLECGGGRwgNK- 397
Cdd:cd07122 235 GTICASEQSVIVDDEIYDEVRAE-LKRRGAYFL--------------NEEEKEKLEKAL---------FDDGGTL--NPd 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 398 -------------GFFVQPTV------FSNVTDEMRIAKEEIFgPVQQIMKFKSIDDVIKRAN-NTTYGLA---AGVFTK 454
Cdd:cd07122 289 ivgksaqkiaelaGIEVPEDTkvlvaeETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKAReLLEYGGAghtAVIHSN 367
|
330 340
....*....|....*....|.
gi 1958642200 455 DLDRAITVSSALQAGVVWVNC 475
Cdd:cd07122 368 DEEVIEEFALRMPVSRILVNT 388
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
173-333 |
3.22e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 39.95 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 173 FTRREPIGVCGQIIPWNFPLLMFiWKIGPALSCGNTVVVKPAEQTPLTALHMA-SLIKEAGFPPGVVNI----VPGYGPT 247
Cdd:cd07080 107 YIRAQPRGLVVHIIAGNVPLLPV-WSIVRGLLVKNVNLLKMSSSDPLTATALLrSLADVDPNHPLTDSIsvvyWPGGDAE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642200 248 AGAAISSHMDVdKVAFTGSTQVgKLIKEAAGKSnlKRvTLELGGK-SPCIV----FADADL-DIAVEFAHHGVFYHQgQC 321
Cdd:cd07080 186 LEERILASADA-VVAWGGEEAV-KAIRSLLPPG--CR-LIDFGPKySFAVIdreaLESEKLaEVADALAEDICRYDQ-QA 259
|
170
....*....|..
gi 1958642200 322 CVAASRIFVEES 333
Cdd:cd07080 260 CSSPQVVFVEKD 271
|
|
| DUF1487 |
pfam07368 |
Protein of unknown function (DUF1487); This family consists of several uncharacterized ... |
292-354 |
5.81e-03 |
|
Protein of unknown function (DUF1487); This family consists of several uncharacterized proteins from Drosophila melanogaster. The function of this family is unknown.
Pssm-ID: 254173 Cd Length: 215 Bit Score: 38.50 E-value: 5.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642200 292 KSPC--IVFADADLDIAVEFAHHGVfyHQGQCCVAASRIFVEESVYDEF---VRKSVERAKKYVLGNP 354
Cdd:pfam07368 3 NSPRlmVIFEDGDVNSALHALVESL--HNPFAPGAVATVLVQESIRDEFverVRSRLKPLSERVANHP 68
|
|
| |
