|
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 ... |
15-494 |
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: 992.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 15 NLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLAD 94
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 95 LMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLI 174
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 175 IFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLI 254
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 255 KEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGN 334
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 335 PLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
19-492 |
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: 883.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 19 QHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMER 98
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 99 DRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTW 178
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 179 KLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAA 258
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 259 GKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNS 338
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 339 GINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVI 418
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 419 KRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
18-494 |
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: 730.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 18 IQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 98 RDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFT 177
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 178 WKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEA 257
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 258 AGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLN 337
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 338 SGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
4-492 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 690.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 4 PAQPAVpaplanlKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDAS 83
Cdd:PLN02466 48 PITPPV-------QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 84 ERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVC 163
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 164 GQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVS 243
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 244 FTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRS 323
Cdd:PLN02466 280 FTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 324 VERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFG 403
Cdd:PLN02466 360 KARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 404 PVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGL 483
Cdd:PLN02466 440 PVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSL 519
|
....*....
gi 7106242 484 YEYTELKTV 492
Cdd:PLN02466 520 NNYLQVKAV 528
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-495 |
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: 689.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 19 QHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMER 98
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 99 DRLLLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFT 177
Cdd:COG1012 81 RREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 178 WKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEA 257
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 258 AGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLN 337
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 338 SGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPV-QCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQ 495
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVpQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
18-492 |
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: 684.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 18 IQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPW-RTMDASERGRLLNKLADLM 96
Cdd:cd07143 4 EQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWgLKVSGSKRGRCLSKLADLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 97 ERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIF 176
Cdd:cd07143 82 ERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 177 TWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKE 256
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 257 AAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:cd07143 242 AAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242 417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
29-492 |
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: 672.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 29 WHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMES 108
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 109 MNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGN 188
Cdd:pfam00171 77 LENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 189 TVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTL 268
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 269 ELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDK 348
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 349 EQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGL 428
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242 429 AAGVFTKDLDKAITVSSALQAGMVWVNCYLAV-PVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
19-492 |
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: 666.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 19 QHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMER 98
Cdd:cd07144 6 QPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 99 DRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTW 178
Cdd:cd07144 84 NRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 179 KLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAA 258
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 259 GkSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKK-YILGNPLN 337
Cdd:cd07144 244 A-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 338 SGINQGPQIDKEQHNKILGLIESGKKEGAKLECGG---GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
17-496 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 658.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 17 KIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLM 96
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 97 ERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIF 176
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 177 TWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKE 256
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 257 AAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQI 496
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-492 |
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: 620.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:cd07119 80 ARLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNL 263
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 264 KRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQG 343
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 344 PQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7106242 420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
36-492 |
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: 616.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 36 KKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVF 115
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 116 AHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPA 195
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 196 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSP 275
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 276 CIVFADA-DLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKI 354
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 355 LGLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 433 FTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-494 |
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: 612.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 61 DKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAhAYLLDVEISIKALQYFAGWADKI 140
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 141 HGQTIPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVV 219
Cdd:cd07078 77 HGEVIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 220 NIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQ 299
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 300 GQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN-K 378
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 379 GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYL 458
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 7106242 459 AVPV-QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07078 396 VGAEpSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
40-496 |
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: 598.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNLKRVTLELGGKSPCIVF 279
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDK 439
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 440 AITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQI 496
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
40-492 |
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: 598.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH-- 117
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIREtr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 118 ---AYLldveisIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVK 193
Cdd:cd07114 80 aqvRYL------AEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 194 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGK 273
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 274 SPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNK 353
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 354 ILGLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLA 429
Cdd:cd07114 313 VERYVARAREEGARVLTGGERpsgaDLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7106242 430 AGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
40-494 |
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: 586.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 360 SGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242 436 DLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
16-495 |
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: 583.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 16 LKIQHtKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADL 95
Cdd:cd07140 2 LKMPH-QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 96 MERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSD----GNIFTYTRREPIGVCGQIIPWNG 171
Cdd:cd07140 80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 172 PLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVG 251
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 252 KLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYI 331
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 332 LGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKF 411
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 412 KS--MDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*.
gi 7106242 490 KTVAMQ 495
Cdd:cd07140 480 KTVTIE 485
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
24-492 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 553.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLM-ERDRLL 102
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 103 lATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGP 182
Cdd:PRK13252 87 -AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 183 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSn 262
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 263 LKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQ 342
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 343 GPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVI 418
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 419 KRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-494 |
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: 549.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQT 198
Cdd:cd07103 77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 199 PLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGK-LIKEAAgkSNLKRVTLELGGKSPCI 277
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 278 VFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGL 357
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 358 IESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDL 437
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 438 DKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
40-492 |
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: 539.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 360 SGKKEGAKLECGGGRWGNK-----GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 435 KDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
23-493 |
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: 533.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 23 IFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMER--DR 100
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEAraDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 101 LLLATMESMNAGKVFAHAY-----LLDVEISIKALQYFAgWADKIHGQTIpsdgniftytRREPIGVCGQIIPWNGPLII 175
Cdd:cd07138 78 LAQAITLEMGAPITLARAAqvglgIGHLRAAADALKDFE-FEERRGNSLV----------VREPIGVCGLITPWNWPLNQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 176 FTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIK 255
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 256 EAAGKSnLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNP 335
Cdd:cd07138 227 EAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 336 LNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGG-GR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNcYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
.
gi 7106242 493 A 493
Cdd:cd07138 465 Q 465
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-493 |
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: 531.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LlDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07109 79 A-DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLnSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 360 SGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07109 316 RARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 437 LDKAITVSSALQAGMVWVNCYLAVP-VQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
24-490 |
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: 529.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNL 263
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 264 KRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQG 343
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 344 PQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7106242 420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-490 |
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: 527.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 22 KIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 102 LLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKs 261
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 262 NLKRVTLELGGKSPCIVFADA-----DLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
41-494 |
1.09e-180 |
|
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: 514.19 E-value: 1.09e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAyL 120
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 121 LDVEISIKALQYFAGWADKIHGQTIPSDG-NIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07118 80 GEIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 360 SGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLD 438
Cdd:cd07118 319 AGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242 439 KAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-494 |
3.94e-174 |
|
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: 497.92 E-value: 3.94e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRtMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHG-QTIPSDGNIFTYT----RREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKP 194
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNLKRVTLELGGKS 274
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 275 PCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKI 354
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 355 LGLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242 433 FTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
40-492 |
3.04e-173 |
|
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: 495.33 E-value: 3.04e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIH---GQTIPSDGNIFT-YTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPA 195
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 196 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 276 CIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKIL 355
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 356 GLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVF 433
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242 434 TKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-492 |
1.00e-171 |
|
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: 491.27 E-value: 1.00e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFP---GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LlDVEISIKALQYFAGWADKIHgqTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07106 78 F-EVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAgFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDK 439
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 7106242 440 AITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-492 |
2.79e-171 |
|
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: 491.20 E-value: 2.79e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 22 KIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 102 LLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKs 261
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 262 NLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGIN 341
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 342 QGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242 418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-492 |
2.49e-170 |
|
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: 488.68 E-value: 2.49e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKkfPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAF---PAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 103 LATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07097 79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPStRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkS 261
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 262 NLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGIN 341
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 342 QGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242 420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLA-VPVQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
65-494 |
2.61e-170 |
|
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: 484.43 E-value: 2.61e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 65 KAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAhAYLLDVEISIKALQYFAGWADKIHGQT 144
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 145 IPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVP 223
Cdd:cd06534 77 LPSpDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 224 GYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQIC 303
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 304 VAASRLFVEESIYDEFVRRSVerakkyilgnplnsginqgpqidkeqhnkilgliesgkkegaklecgggrwgnkgffvq 383
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 384 pTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLA-VPV 462
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 7106242 463 QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-492 |
5.34e-169 |
|
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: 485.70 E-value: 5.34e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 103 LATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKS 261
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 262 NlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGIN 341
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 342 QGPQIDKEQHNKILGLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNC-YLAVPVQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNApTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-494 |
6.08e-169 |
|
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: 484.85 E-value: 6.08e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK---AWERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIPSDG---NIFTYtrREPIGVCGQIIPWNGPLIIFTWKL 180
Cdd:cd07088 78 AKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRpneNIFIF--KVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGK 260
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 261 sNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGI 340
Cdd:cd07088 235 -NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 341 NQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242 420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-492 |
2.59e-168 |
|
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: 483.02 E-value: 2.59e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFH-QGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLI 358
Cdd:cd07108 236 PDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 359 ESGKKE-GAK-LECG---GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVF 433
Cdd:cd07108 316 DLGLSTsGATvLRGGplpGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 434 TKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYE-YTELKTV 492
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQKKTV 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-494 |
7.85e-167 |
|
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: 479.76 E-value: 7.85e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 23 IFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 103 LATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADK---IHGQTIPSDGNifTYTRREPIGVCGQIIPWNGPLIIFTWK 179
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 180 LGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAG 259
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 260 kSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSG 339
Cdd:cd07139 237 -ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 340 INQGPQIDKEQHNKILGLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNcYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-499 |
2.43e-164 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 474.61 E-value: 2.43e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 8 AVPAPLANLkiqhtkiFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAF--QIGSPWRTMDASER 85
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 86 GRLLNKLADLMERDRLLLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQ-----TIPSDgNIFTYTRREPI 160
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 161 GVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDID 240
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 241 KVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFV 320
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 321 RRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWG--NKGFFVQPTVFSNVTDEMRIAK 398
Cdd:PLN02467 312 EKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 399 EEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGREL 478
Cdd:PLN02467 392 EEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGREL 471
|
490 500
....*....|....*....|.
gi 7106242 479 GEHGLYEYTELKTVAMQISQK 499
Cdd:PLN02467 472 GEWGLENYLSVKQVTKYISDE 492
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
24-486 |
8.36e-164 |
|
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: 472.27 E-value: 8.36e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWAdkihgQTIPSDGNiftytRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWA-----QLLDTELA-----GWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEA-AGKSn 262
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRAtAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 263 lKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQ 342
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 343 GPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRAN 422
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 423 NTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEY 486
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-492 |
1.04e-162 |
|
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: 468.34 E-value: 1.04e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGqtiPSDG----NIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPA 195
Cdd:cd07092 78 DDELPGAVDNFRFFAGAARTLEG---PAAGeylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 196 EQTPLTALHMASLIKEaGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 276 CIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKIL 355
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 356 GLIEsGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 436 DLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
24-496 |
1.12e-162 |
|
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: 469.67 E-value: 1.12e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAYlldvEISIKALQYFAGWADK----IHGQTIPSDGNIfTYTRREPIGVCGQIIPWNGPLIIFTWK 179
Cdd:TIGR02299 81 AVLECLDCGQPLRQTR----QQVIRAAENFRFFADKceeaMDGRTYPVDTHL-NYTVRVPVGPVGLITPWNAPFMLSTWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 180 LGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKeAAG 259
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIM-RNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 260 KSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSG 339
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 340 INQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWG-------NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
....
gi 7106242 493 AMQI 496
Cdd:TIGR02299 475 ALAL 478
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
38-494 |
3.34e-160 |
|
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: 462.18 E-value: 3.34e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH 117
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 118 AYLlDVEISIKALQYFAGWADKIHGQTIPSDGN-IFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAE 196
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 197 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPC 276
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 277 IVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILG 356
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 357 LIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242 437 LDKAITVSSALQAGMVWVNCylaVPV----QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07150 393 LQRAFKLAERLESGMVHIND---PTIldeaHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
20-492 |
6.18e-159 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 459.76 E-value: 6.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 20 HTKIFINNEWHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERD 99
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 100 RLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGqtiPSDGNI---FT-YTRREPIGVCGQIIPWNGPLII 175
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGEYlegHTsMIRRDPVGVVASIAPWNYPLMM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 176 FTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIK 255
Cdd:PRK13473 155 AAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 256 EAAGKSnLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNP 335
Cdd:PRK13473 234 SAAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 336 LNSGINQGPQIDKEQHNKILGLIESGKKEG-AKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
24-494 |
3.05e-156 |
|
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: 453.05 E-value: 3.05e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQT----IPS-DGNIFT-YTRREPIGVCGQIIPWNGPLIIFT 177
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSmQGERYTaFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 178 WKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEA 257
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 258 AgKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLN 337
Cdd:cd07113 240 A-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 338 SGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
59-494 |
3.81e-156 |
|
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: 450.83 E-value: 3.81e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 59 DVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDR----LLLATmESmnaGKVFAHAYLlDVEISIKALQYFA 134
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRdeiaDWLIR-ES---GSTRPKAAF-EVGAAIAILREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 135 GWADKIHGQTIPSDGN-IFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLT-ALHMASLIKEA 212
Cdd:cd07104 73 GLPRRPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 213 GFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAH 292
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 293 QGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGG 372
Cdd:cd07104 232 FGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 373 GRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMV 452
Cdd:cd07104 312 TYEGL---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 7106242 453 WVNCylaVPVQC----PFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07104 389 HIND---QTVNDephvPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
2-494 |
3.53e-155 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 451.07 E-value: 3.53e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 2 SSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMD 81
Cdd:PLN02278 6 SSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 82 ASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYlldVEISIKA--LQYFAGWADKIHGQTIPS---DGNIFTYtr 156
Cdd:PLN02278 83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAI---GEVAYGAsfLEYFAEEAKRVYGDIIPSpfpDRRLLVL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 157 REPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSH 236
Cdd:PLN02278 158 KQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 237 MDIDKVSFTGSTEVGKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIY 316
Cdd:PLN02278 238 PKVRKITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 317 DEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRI 396
Cdd:PLN02278 317 DKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 397 AKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGR 476
Cdd:PLN02278 397 FREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGR 476
|
490
....*....|....*...
gi 7106242 477 ELGEHGLYEYTELKTVAM 494
Cdd:PLN02278 477 EGSKYGIDEYLEIKYVCL 494
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
14-496 |
2.44e-154 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 448.96 E-value: 2.44e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 14 ANLKIQhTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLA 93
Cdd:PRK09847 14 LSLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 94 DLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPL 173
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 174 IIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKL 253
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 254 IKEAAGKSNLKRVTLELGGKSPCIVFADA-DLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYIL 332
Cdd:PRK09847 252 LLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 333 GNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL--DGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
....
gi 7106242 493 AMQI 496
Cdd:PRK09847 490 WISL 493
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-496 |
2.67e-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: 447.21 E-value: 2.67e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAhAY 119
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSnLKRVTLELGGKSPCIVF 279
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFH-QGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLI 358
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 359 ESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242 435 KDLDKAITVSSALQAGMVWVNC----YLAVpvqcPFGGFKMSGNGRELGEHGLYEYTELKTVAMQI 496
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGssrhFLGA----PFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-494 |
3.42e-150 |
|
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: 436.64 E-value: 3.42e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH 117
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 118 AyLLDVEISIKALQYFAGWADKIHGQTIPSDG-----NIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVV 192
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGksnLKRVTLELGG 272
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 273 KSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHN 352
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 353 KILGLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242 433 FTKDLDKAITVSSALQAGMVWVNcylAVPV----QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMIN---DSSTfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
18-492 |
2.32e-148 |
|
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: 432.99 E-value: 2.32e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 18 IQHtkiFINNEWhdsVSSKK-FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLM 96
Cdd:TIGR03216 1 IRN---FINGAF---VESGKtFANINPVDGRVIARVHEAGAAEVDAAVAAARAALK--GPWGKMTVAERADLLYAVADEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 97 ER--DRLLLAtmESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQ----TIPSDGNIFTYTRREPIGVCGQIIPWN 170
Cdd:TIGR03216 73 ERrfDDFLAA--EVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTEcfemATPDGKGALNYAVRKPLGVVGVISPWN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 171 GPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGP-TAGGAISSHMDIDKVSFTGSTE 249
Cdd:TIGR03216 151 LPLLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 250 VGKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKK 329
Cdd:TIGR03216 231 TGSAIMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 330 YILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGG--RWGNK---GFFVQPTVFSNVTDEMRIAKEEIFGP 404
Cdd:TIGR03216 310 LKIGVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGvpDFGDAlagGAWVQPTIWTGLPDSARVVTEEIFGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 405 VQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLY 484
Cdd:TIGR03216 390 CCHIAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLE 469
|
....*...
gi 7106242 485 EYTELKTV 492
Cdd:TIGR03216 470 FYTELTNV 477
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-492 |
3.48e-145 |
|
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: 424.67 E-value: 3.48e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGP 182
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 183 ALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGYGPtAGGAISSHMDIDKVSFTGSTEVGKLIKEAA 258
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 259 GKSNlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNS 338
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 339 GINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 417 VIKRANNTTYGLAAGVFTKDLDKAITVSSA--LQAGMVWVNcylaVP-----VQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVN----IPtsgaeIGGAFGGEKETGGGRESGSDAWKQYMRR 470
|
...
gi 7106242 490 KTV 492
Cdd:cd07086 471 STC 473
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
38-493 |
3.53e-144 |
|
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: 421.37 E-value: 3.53e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH 117
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 118 AyLLDVEISIKALQYFAGWADKIHGQTIPSDG-----NIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVV 192
Cdd:cd07145 78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNLKRVTLELGG 272
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 273 KSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHN 352
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 353 KILGLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242 433 FTKDLDKAITVSSALQAGMVWVNCYLAV-PVQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-494 |
1.04e-142 |
|
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: 419.71 E-value: 1.04e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 19 QHTKIFINNEWHDSvsSKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07124 31 REYPLVIGGKEVRT--EEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 98 RDRLLLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFT 177
Cdd:cd07124 106 RRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 178 WKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEA 257
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 258 AGK-----SNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYIL 332
Cdd:cd07124 265 AAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 333 GNPLNSGINQGPQIDKEQHNKILGLIESGKKEGaKLECGGGRWGN--KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMK 410
Cdd:cd07124 345 GDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 411 FKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVN--CYLAVPVQCPFGGFKMSG-NGRELGEHGLYEYT 487
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFM 503
|
....*..
gi 7106242 488 ELKTVAM 494
Cdd:cd07124 504 QPKTVTE 510
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
24-490 |
1.75e-142 |
|
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: 418.01 E-value: 1.75e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNL 263
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 264 KRVTLELGGKSPCIVFA------DADLDSAVE----FAhqgvfFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILG 333
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEgfvmFA-----LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 334 NPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNvTDEMRIAKEEIFGPVQQIM 409
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelggLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 410 KFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQT 472
|
.
gi 7106242 490 K 490
Cdd:cd07116 473 K 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
41-494 |
1.95e-137 |
|
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: 404.42 E-value: 1.95e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTmDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYL 120
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 121 lDVEISIKALQYFAGWADKIHGQTI-PSDGNiFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07120 80 -EISGAISELRYYAGLARTEAGRMIePEPGS-FSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEA-GFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIV 278
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP-TLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 279 FADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLI 358
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 359 ESGKKEGAKLECGGGRWG---NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTeglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242 436 DLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-495 |
1.08e-132 |
|
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: 392.44 E-value: 1.08e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 27 NEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLMERDRLLLATM 106
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 107 ESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSD-----GNIFtytrREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07151 78 LIRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvpgkeNRVY----REPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 182 PALSCGNTVVVKPAEQTPLTA-LHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGK 260
Cdd:cd07151 153 PALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 261 sNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGI 340
Cdd:cd07151 233 -HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 341 NQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKR 420
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALEL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242 421 ANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNcylAVPVQ----CPFGGFKMSGNGRELGEHGLYEYTELKTVAMQ 495
Cdd:cd07151 389 ANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN---DQPVNdephVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
19-493 |
9.69e-129 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 384.29 E-value: 9.69e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 19 QHTKIFINNEWHDSvsSKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:PRK03137 35 QDYPLIIGGERITT--EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 98 RDRLLLATMESMNAGKVFAHAyllDVEIS--IKALQYFA----GWADKIHGQTIPSDGNIFTYtrrEPIGVCGQIIPWNG 171
Cdd:PRK03137 110 RRKHEFSAWLVKEAGKPWAEA---DADTAeaIDFLEYYArqmlKLADGKPVESRPGEHNRYFY---IPLGVGVVISPWNF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 172 PLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVG 251
Cdd:PRK03137 184 PFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 252 KLIKEAAGKSN-----LKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVER 326
Cdd:PRK03137 264 LRIYERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 327 AKKYILGNPLNSGiNQGPQIDKEQHNKILGLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQ 406
Cdd:PRK03137 344 TKELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 407 QIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVN--CYLA-VPVQcPFGGFKMSG-NGRELGEHG 482
Cdd:PRK03137 422 AFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAiVGYH-PFGGFNMSGtDSKAGGPDY 500
|
490
....*....|.
gi 7106242 483 LYEYTELKTVA 493
Cdd:PRK03137 501 LLLFLQAKTVS 511
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
60-492 |
5.07e-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: 379.11 E-value: 5.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 60 VDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAyLLDVEISIKALQYFAGwadk 139
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 140 iHG------QTIPSDGNIfTYTRREPIGVCGQIIPWNGPLiiftWK----LGPALSCGNTVVVKPAEQTPLTALHMASLI 209
Cdd:cd07100 73 -NAeafladEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 210 KEAGFPPGVVNIVPGYGPTAGGAISSHMdIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVE 289
Cdd:cd07100 147 REAGFPEGVFQNLLIDSDQVEAIIADPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 290 FAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLE 369
Cdd:cd07100 225 TAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 370 CGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQA 449
Cdd:cd07100 305 LGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEA 384
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 7106242 450 GMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07100 385 GMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-492 |
2.74e-126 |
|
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: 376.47 E-value: 2.74e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 21 TKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDR 100
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP---AWSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 101 LLLATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIP-SDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWK 179
Cdd:cd07085 78 DELARLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 180 LGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAG 259
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 260 KSNlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSG 339
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 340 INQGPQIDKEQHNKILGLIESGKKEGAKLECgGGRwGNK------GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKS 413
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVL-DGR-GVKvpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 414 MDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQC-PFGGFKMS--GNGRELGEHGLYEYTELK 490
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFfSFGGWKGSffGDLHFYGKDGVRFYTQTK 472
|
..
gi 7106242 491 TV 492
Cdd:cd07085 473 TV 474
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-494 |
1.35e-125 |
|
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: 374.08 E-value: 1.35e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPSD-----GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKP 194
Cdd:cd07094 79 RVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsnlKRVTLELGGKS 274
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG---KRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 275 PCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKI 354
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 355 LGLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242 435 KDLDKAITVSSALQAGMVWVN--CYLAVPVQcPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNdsSAFRTDWM-PFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
59-492 |
1.25e-124 |
|
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: 370.75 E-value: 1.25e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 59 DVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLLLATMESMNAGKVFAHaylLDVEISIKALQYFAGW 136
Cdd:cd07105 1 DADQAVEAAAAAFPA---WSKTPPSERRDILLKAADLLEsrRDEFIEAMMEETGATAAWAG---FNVDLAAGMLREAASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 137 ADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFP 215
Cdd:cd07105 75 ITQIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 216 PGVVNIV---PGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAH 292
Cdd:cd07105 155 KGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 293 QGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLnsginQGPQIDKEQHNKILGLIESGKKEGAKLECGG 372
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 373 -GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGM 451
Cdd:cd07105 309 lADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 7106242 452 VWVN-CYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07105 389 VHINgMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
22-477 |
1.49e-123 |
|
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: 369.21 E-value: 1.49e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 22 KIFINNEWHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 102 LLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFT-----YTRREPIGVCGQIIPWNGPLIIF 176
Cdd:cd07082 80 EVANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 177 TWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKE 256
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 257 AAGKsnlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:cd07082 239 QHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242 417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAV-PVQCPFGGFKMSGNGRE 477
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgPDHFPFLGRKDSGIGTQ 455
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
47-479 |
9.90e-123 |
|
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: 366.23 E-value: 9.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 47 EVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAyLLDVEIS 126
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA-GFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 127 IKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTA-LHM 205
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 206 ASLIKEAGFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLD 285
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 286 SAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEG 365
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 366 AKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSS 445
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|....*
gi 7106242 446 ALQAGMVWVN-CYLAVPVQCPFGGFKMSGNGRELG 479
Cdd:cd07152 393 RLRTGMLHINdQTVNDEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
41-493 |
5.27e-121 |
|
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: 362.31 E-value: 5.27e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVfAHAYL 120
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 121 LDVEISIKALQYFAGWADKIHGQTIPSDGNIF----TYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAE 196
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVLAPRKVPTGLLMpnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 197 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISShmDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPC 276
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 277 IVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILG 356
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 357 LIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242 437 LDKAITVSSALQAGMVWVNCYLAVPVQC--PFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPalPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-495 |
5.72e-121 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 364.58 E-value: 5.72e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 31 DSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLMERDRLLLATMESMN 110
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 111 AGKVFAHAY--LLDVEISIKalqYFAGWADKI-----HGQTIPsdgnIFTYTR--REPIGVCGQIIPWNGPLiiftwKLG 181
Cdd:PRK09407 104 TGKARRHAFeeVLDVALTAR---YYARRAPKLlaprrRAGALP----VLTKTTelRQPKGVVGVISPWNYPL-----TLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 182 -----PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHmdIDKVSFTGSTEVGKLIKE 256
Cdd:PRK09407 172 vsdaiPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 257 AAGkSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:PRK09407 250 QAG-RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMD 415
Cdd:PRK09407 329 DYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 416 DVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVN-CYLAV--PVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09407 409 EAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAwgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
...
gi 7106242 493 AMQ 495
Cdd:PRK09407 489 ATQ 491
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
43-493 |
4.24e-118 |
|
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: 354.69 E-value: 4.24e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 43 PATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY--L 120
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFeeV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 121 LDVEISIKalqYFAGWADKI-----HGQTIPsdgnIFTYTR--REPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVK 193
Cdd:cd07101 80 LDVAIVAR---YYARRAERLlkprrRRGAIP----VLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 194 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIdkVSFTGSTEVGKLIKEAAGkSNLKRVTLELGGK 273
Cdd:cd07101 153 PDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 274 SPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNK 353
Cdd:cd07101 230 NPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 354 ILGLIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:cd07101 310 VTAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 433 FTKDLDKAITVSSALQAGMVWVN-CYLAV--PVQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
24-496 |
2.13e-117 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 353.83 E-value: 2.13e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVFAHAyllDVEISIKA--LQYFAGWADKIHGQTIP---SDGNIFTYtrREPIGVCGQIIPWNGPLIIFTW 178
Cdd:PRK11241 91 ARLMTLEQGKPLAEA---KGEISYAAsfIEWFAEEGKRIYGDTIPghqADKRLIVI--KQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 179 KLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAA 258
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 259 GKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNS 338
Cdd:PRK11241 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 339 GINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVI 418
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 419 KRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQI 496
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
38-494 |
5.58e-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: 5.58e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH 117
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 118 AYLlDVEISIKALQYFAGWADKIHGQTIPSDGN-----IFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVV 192
Cdd:cd07147 78 ARG-EVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGygPTAGGAI-SSHMDIDKVSFTGSTEVGKLIKEAAGKsnlKRVTLELG 271
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 272 GKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQH 351
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 352 NKILGLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAG 431
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 432 VFTKDLDKAITVSSALQAGMVWVNcylAVPV----QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVIN---DVPTfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
40-492 |
1.13e-111 |
|
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: 338.18 E-value: 1.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAArqafqiGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 LLDVEISIKALQYFAGWADKIHGQTIPSD-----GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKP 194
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGksnLKRVTLELGGKS 274
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 275 PCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKI 354
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 355 LGLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7106242 435 KDLDKAITVSSALQAGMVWVNcylAVP----VQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVN---EVPgfrsELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
89-495 |
1.38e-109 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 331.32 E-value: 1.38e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 89 LNKLADLMERDRLLLATMESMNAGKVFAhayLLDVEISIKA--LQYFAGWADKIHGQTIPSD---GNIFTYTRrePIGVC 163
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQ---LAEVEVAFTAdyIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 164 GQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVS 243
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 244 FTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRS 323
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 324 VERAKKYILGNPL-NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIF 402
Cdd:PRK10090 235 GEAMQAVQFGNPAeRNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 403 GPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHG 482
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHG 394
|
410
....*....|...
gi 7106242 483 LYEYTELKTVAMQ 495
Cdd:PRK10090 395 LHEYLQTQVVYLQ 407
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
41-492 |
8.78e-105 |
|
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: 320.35 E-value: 8.78e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAyl 120
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 121 lDVEIS--IKALQYFAGWADK-IHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQ 197
Cdd:cd07102 76 -GGEIRgmLERARYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 198 TPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHmDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCI 277
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 278 VFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGL 357
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 358 IESGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07102 313 IADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 435 KDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
42-493 |
6.74e-103 |
|
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: 316.16 E-value: 6.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 42 NPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLL 121
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQ---REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 122 DVEISIKALQYFAGWADKiHGQTIPSDGNIFTYTRR-----EPIGVCGQIIPWNGPliiFTWKLGPALSC---GNTVVVK 193
Cdd:cd07098 79 EILVTCEKIRWTLKHGEK-ALRPESRPGGLLMFYKRarveyEPLGVVGAIVSWNYP---FHNLLGPIIAAlfaGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 194 PAEQTPLTALHMASLIKEA----GFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSnLKRVTLE 269
Cdd:cd07098 155 VSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 270 LGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKE 349
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 350 QHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTT 425
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242 426 YGLAAGVFTKDLDKAITVSSALQAGMVWVN----CYLAvpVQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07098 393 YGLGASVFGKDIKRARRIASQLETGMVAINdfgvNYYV--QQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-493 |
7.91e-93 |
|
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: 291.40 E-value: 7.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 19 QHTKIFINNEWHDSvsSKKFPVLNP-ATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07083 17 RAYPLVIGGEWVDT--KERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 98 RDRLLLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTI------PSDGNIFTytrrEPIGVCGQIIPWNG 171
Cdd:cd07083 92 RRRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESFY----VGLGAGVVISPWNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 172 PLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVG 251
Cdd:cd07083 167 PVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 252 KLIKEAAGK-----SNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVER 326
Cdd:cd07083 247 KKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 327 AKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQ 406
Cdd:cd07083 327 AERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 407 QIMKFKSMD--DVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYL--AVPVQCPFGGFKMSG-NGRELGEH 481
Cdd:cd07083 406 SVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKItgALVGVQPFGGFKLSGtNAKTGGPH 485
|
490
....*....|..
gi 7106242 482 GLYEYTELKTVA 493
Cdd:cd07083 486 YLRRFLEMKAVA 497
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
41-492 |
2.59e-90 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 283.55 E-value: 2.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYL 120
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 121 lDVEISIKALQYFAGWADKIHGQTiPSD----GNIFTYTRREPIGVCGQIIPWNGPLiiftWKL----GPALSCGNTVVV 192
Cdd:PRK09406 83 -EALKCAKGFRYYAEHAEALLADE-PADaaavGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPgYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSnLKRVTLELGG 272
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 273 KSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHN 352
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 353 KILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:PRK09406 315 EVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 433 FTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
26-479 |
3.60e-89 |
|
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: 281.02 E-value: 3.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 26 NNEWhdSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLAT 105
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 106 MESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPAL 184
Cdd:cd07130 79 LVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 185 SCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGK 260
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 261 sNLKRVTLELGGKSPCIVFADADLDSAVefahQGVFFH----QGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:cd07130 237 -RFGRSLLELGGNNAIIVMEDADLDLAV----RAVLFAavgtAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDeMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLEE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQA--GMVWVNcylaVP-----VQCPFGGFKMSGNGRELG 479
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVN----IGtsgaeIGGAFGGEKETGGGRESG 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
12-479 |
2.10e-86 |
|
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: 275.23 E-value: 2.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 12 PLANLKIQHTKiFINNEWHDS--VSSKKF------PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDA 82
Cdd:cd07125 15 PLEALADALKA-FDEKEWEAIpiINGEETetgegaPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 83 SERGRLLNKLADLMERDR---LLLATMEsmnAGKVFAHAyllDVEIS--IKALQYFAGWADKI--HGQTIPSDG--NIFT 153
Cdd:cd07125 91 EERAEILEKAADLLEANRgelIALAAAE---AGKTLADA---DAEVReaIDFCRYYAAQARELfsDPELPGPTGelNGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 154 YTRREpIGVCgqIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAI 233
Cdd:cd07125 165 LHGRG-VFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 234 SSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFV 311
Cdd:cd07125 242 VAHPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 312 EESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEgAKLECGGGRWGNKGFFVQPTVFSNVT 391
Cdd:cd07125 322 QEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 392 DEMRiaKEEIFGPVQQIMKFKS--MDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGmvwvNCYL-------AVPV 462
Cdd:cd07125 401 IFDL--TTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYInrnitgaIVGR 474
|
490
....*....|....*..
gi 7106242 463 QcPFGGFKMSGNGRELG 479
Cdd:cd07125 475 Q-PFGGWGLSGTGPKAG 490
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-495 |
8.31e-83 |
|
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: 264.44 E-value: 8.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 22 KIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 102 LLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKL 180
Cdd:TIGR01722 79 EIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGK 260
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 261 SNlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIyDEFVRRSVERAKKYILGNPLNSGI 340
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 341 NQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGF----FVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQC-PFGGFKMS--GNGRELGEHGLYEYTELKTVA 493
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYfSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
..
gi 7106242 494 MQ 495
Cdd:TIGR01722 475 TR 476
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
40-475 |
5.35e-80 |
|
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: 256.58 E-value: 5.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWrtMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 120 L-----LD-VEISIKALQYFAGwaDKI-HGQTIPSDGNIfTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVV 192
Cdd:cd07148 81 VevtraIDgVELAADELGQLGG--REIpMGLTPASAGRI-AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPgygptAGGAISSHMDIDK----VSFTGSTEVGKLI--KEAAGKsnlkRV 266
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVP-----CENAVAEKLVTDPrvafFSFIGSARVGWMLrsKLAPGT----RC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 267 TLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQI 346
Cdd:cd07148 229 ALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 347 DKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFfvQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTY 426
Cdd:cd07148 309 RPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 7106242 427 GLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQ-CPFGGFKMSGNG 475
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
59-476 |
8.13e-77 |
|
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: 247.57 E-value: 8.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 59 DVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVF------AHAYLLDVEISIKALQY 132
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 133 FAGWADKihgqtipSDGNIFTYTRREPIGVCGQIIPWNGPL------IIftwklgPALSCGNTVVVKPAEQTPLTALHMA 206
Cdd:cd07095 78 RTGERAT-------PMAQGRAVLRHRPHGVMAVFGPFNFPGhlpnghIV------PALLAGNTVVFKPSELTPAVAELMV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 207 SLIKEAGFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDS 286
Cdd:cd07095 145 ELWEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 287 AVEFAHQGVFFHQGQICVAASRLFVEESIY-DEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEG 365
Cdd:cd07095 224 AAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 366 AKLECGGGRWGNKGFFVQPTVFsNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSS 445
Cdd:cd07095 304 GEPLLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430
....*....|....*....|....*....|..
gi 7106242 446 ALQAGMVWVNCYLA-VPVQCPFGGFKMSGNGR 476
Cdd:cd07095 383 RIRAGIVNWNRPTTgASSTAPFGGVGLSGNHR 414
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
22-475 |
9.20e-74 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 241.58 E-value: 9.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 22 KIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRL 101
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 102 LLATMESMNAGKVFAHAyLLDVEISIKALQYFA-------GWADKIHGQTIPSDG-NIFTYTRREPIGVCGQIIPWNGPL 173
Cdd:PLN00412 94 PIAECLVKEIAKPAKDA-VTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNErNKYCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 174 IIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGStEVGKL 253
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 254 IKEAAGKSNLKrvtLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILG 333
Cdd:PLN00412 252 ISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 334 NPL-NSGINqgPQIDKEQHNKILGLIESGKKEGAKLEcggGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:PLN00412 329 PPEdDCDIT--PVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAV-PVQCPFGGFKMSGNG 475
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARgPDHFPFQGLKDSGIG 467
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-495 |
3.88e-72 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 240.03 E-value: 3.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 6 QPAVPAPLANLkiqhtkifINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASER 85
Cdd:PLN02419 107 QPQMPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 86 GRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIPSDGN-IFTYTRREPIGVCG 164
Cdd:PLN02419 176 QRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNgVDTYSIREPLGVCA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 165 QIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAgGAISSHMDIDKVSF 244
Cdd:PLN02419 255 GICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 245 TGSTEVGKLI-KEAAGKSnlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASR-LFV--EESIYDEFV 320
Cdd:PLN02419 334 VGSNTAGMHIyARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVgdAKSWEDKLV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 321 RRSveRAKKYILGNPLNSGInqGPQIDKEQHNKILGLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRI 396
Cdd:PLN02419 412 ERA--KALKVTCGSEPDADL--GPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpGYEKGNFIGPTILSGVTPDMEC 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 397 AKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNcyLAVPVQCPFggFKMSGNGR 476
Cdd:PLN02419 488 YKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--VPIPVPLPF--FSFTGNKA 563
|
490 500
....*....|....*....|....*.
gi 7106242 477 EL-------GEHGLYEYTELKTVAMQ 495
Cdd:PLN02419 564 SFagdlnfyGKAGVDFFTQIKLVTQK 589
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
39-490 |
1.63e-71 |
|
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: 235.57 E-value: 1.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 39 PVLNPAT-EEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH 117
Cdd:TIGR01238 54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPT---WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 118 AyLLDVEISIKALQYFAGWADKIHGQtipsdgniFTYtrrEPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQ 197
Cdd:TIGR01238 131 A-IAEVREAVDFCRYYAKQVRDVLGE--------FSV---ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 198 TPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTL--ELGGKSP 275
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 276 CIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKIL 355
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 356 GLIESGKKEG---AKLECGGGRWGNKGFFVQPTVFSnvTDEMRIAKEEIFGPVQQIMKFKS--MDDVIKRANNTTYGLAA 430
Cdd:TIGR01238 359 AHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTM 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 431 GVFTKDLDKAITVSSALQAGMVWVNCYL---AVPVQcPFGGFKMSGNG-RELGEHGLYEYTELK 490
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQvgaVVGVQ-PFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
156-492 |
1.28e-70 |
|
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: 231.35 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 156 RREPIGVCGQIIPWNGPliiFTWKLGP---ALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGA 232
Cdd:cd07134 97 RYEPKGVCLIISPWNYP---FNLAFGPlvsAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 233 ISshMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVE 312
Cdd:cd07134 173 LE--LPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 313 ESIYDEFvrrsVERAKKYILGNPLNSGINQGPQ-----IDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVqPTVF 387
Cdd:cd07134 250 ESVKDAF----VEHLKAEIEKFYGKDAARKASPdlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIA-PTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 388 SNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDlDKAI-TVSSALQAGMVWVNCYLA--VPVQC 464
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD-KANVnKVLARTSSGGVVVNDVVLhfLNPNL 403
|
330 340
....*....|....*....|....*...
gi 7106242 465 PFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07134 404 PFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
10-475 |
8.84e-70 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 242.08 E-value: 8.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 10 PAPLANLKIQHTKiFINNEWH-------DSVSSKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMD 81
Cdd:PRK11905 535 EATLAALDEALNA-FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 82 ASERGRLLNKLADLMERDR---LLLATMEsmnAGKVFAHAyLLDVEISIKALQYFAgwadkihgQTIPSDgniFTYTRRE 158
Cdd:PRK11905 611 AAERAAILERAADLMEAHMpelFALAVRE---AGKTLANA-IAEVREAVDFLRYYA--------AQARRL---LNGPGHK 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 159 PIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMD 238
Cdd:PRK11905 676 PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPR 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 239 IDKVSFTGSTEVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVfadadlDSAVeFAHQGV-------FFHQGQICVAASRL 309
Cdd:PRK11905 756 IAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIV------DSSA-LPEQVVadviasaFDSAGQRCSALRVL 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 310 FVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFS 388
Cdd:PRK11905 829 CLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 389 nvTDEMRIAKEEIFGPVQQIMKFKS--MDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYL---AVPVQ 463
Cdd:PRK11905 909 --IDSISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIigaVVGVQ 986
|
490
....*....|..
gi 7106242 464 cPFGGFKMSGNG 475
Cdd:PRK11905 987 -PFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
39-475 |
2.83e-69 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 240.22 E-value: 2.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 39 PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLL-LATMEsmnAGKV 114
Cdd:COG4230 573 PVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEahRAELMaLLVRE---AGKT 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 115 FAHAyLLDVEISIKALQYFAGWADKIHGQTipsdgniftyTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKP 194
Cdd:COG4230 647 LPDA-IAEVREAVDFCRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEA-AGKSNlKRVTL--ELG 271
Cdd:COG4230 716 AEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTlAARDG-PIVPLiaETG 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 272 GKSPCIVfaD---------AD-LDSAvefahqgvFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGIN 341
Cdd:COG4230 795 GQNAMIV--DssalpeqvvDDvLASA--------FDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTD 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 342 QGPQIDKEQHNKILGLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFsnvtdEM-RIA--KEEIFGPVQQIMKFKS--MD 415
Cdd:COG4230 865 VGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-----EIdSISdlEREVFGPVLHVVRYKAdeLD 939
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 416 DVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGmvwvNCYL-------AVPVQcPFGGFKMSGNG 475
Cdd:COG4230 940 KVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYVnrniigaVVGVQ-PFGGEGLSGTG 1001
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
153-492 |
2.88e-69 |
|
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: 227.79 E-value: 2.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 153 TYTRREPIGVCGQIIPWN-------GPLIiftwklgPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGy 225
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNyplqlalAPLI-------GAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 226 gptaGGAISSHM---DIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQI 302
Cdd:cd07087 165 ----GVEVATALlaePFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 303 CVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGiNQGPQIDKEQHNKILGLIESGKKEGaklecgGGRWGNKGFFV 382
Cdd:cd07087 240 CIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDGKVVI------GGQVDKEERYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 383 QPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNcylAVPV 462
Cdd:cd07087 313 APTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN---DVLL 389
|
330 340 350
....*....|....*....|....*....|....*
gi 7106242 463 QC-----PFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07087 390 HAaipnlPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
24-492 |
5.90e-68 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 235.86 E-value: 5.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWH----DSVSSKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMER 98
Cdd:PRK11904 546 FLEKQWQagpiINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 99 DR---LLLATMEsmnAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSDGniFT----YTRREPIGV--CgqIIPW 169
Cdd:PRK11904 623 NRaelIALCVRE---AGKTLQDA-IAEVREAVDFCRYYAAQARRLFGAPEKLPG--PTgesnELRLHGRGVfvC--ISPW 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 170 NGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTE 249
Cdd:PRK11904 695 NFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTE 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 250 VGKLIKEA-AGKSNlKRVTL--ELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVER 326
Cdd:PRK11904 775 TARIINRTlAARDG-PIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGA 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 327 AKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEG---AKLECGGGrwGNKGFFVQPTVFSnvTDEMRIAKEEIFG 403
Cdd:PRK11904 854 MAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPAG--TENGHFVAPTAFE--IDSISQLEREVFG 929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 404 PVQQIMKFKS--MDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGmvwvNCYL-------AVPVQcPFGGFKMSGN 474
Cdd:PRK11904 930 PILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVG----NVYVnrnqigaVVGVQ-PFGGQGLSGT 1004
|
490
....*....|....*....
gi 7106242 475 G-RELGEHGLYEYTELKTV 492
Cdd:PRK11904 1005 GpKAGGPHYLLRFATEKTV 1023
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
24-476 |
8.18e-68 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 225.61 E-value: 8.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 104 ATMESMNAGKVF------AHAYLLDVEISIKALQYFAGwadkiHGQTIPSDGNIFTytRREPIGVCGQIIPWNGPLIIFT 177
Cdd:PRK09457 80 AEVIARETGKPLweaateVTAMINKIAISIQAYHERTG-----EKRSEMADGAAVL--RHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 178 WKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLI-KE 256
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 257 AAGKSNlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIY-DEFVRRSVERAKKYILGNP 335
Cdd:PRK09457 232 FAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 336 lnsgiNQ------GPQIDKEQHNKILG----LIESGKK---EGAKLECGGGrwgnkgfFVQPTVFsNVTDEMRIAKEEIF 402
Cdd:PRK09457 311 -----DAepqpfmGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEEYF 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242 403 GPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMV-WVNCYLAVPVQCPFGGFKMSGNGR 476
Cdd:PRK09457 378 GPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
41-492 |
2.00e-67 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 223.97 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYL 120
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 121 lDVEISIKALQYFAGwadkiHGQT--------IPSDGNIFTYtrrEPIGVCGQIIPWNGPLiiftWKL----GPALSCGN 188
Cdd:PRK13968 89 -EVAKSANLCDWYAE-----HGPAmlkaeptlVENQQAVIEY---RPLGTILAIMPWNFPL----WQVmrgaVPILLAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 189 TVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMdIDKVSFTGSTEVGKLIKEAAGKSnLKRVTL 268
Cdd:PRK13968 156 GYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAA-LKKCVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 269 ELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDK 348
Cdd:PRK13968 234 ELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 349 EQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGL 428
Cdd:PRK13968 314 DLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 429 AAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13968 394 SATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
154-492 |
2.78e-66 |
|
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: 220.45 E-value: 2.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 154 YTRREPIGVCGQIIPWNGPliiFTWKLGP---ALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAG 230
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYP---FQLALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 231 GAISSHMDidKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLF 310
Cdd:cd07136 171 ELLDQKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 311 VEESIYDEFVRRSVERAKKYILGNPLNSGinQGPQIDKEQH-NKILGLIESGKkegakLECGGGrwGNKG-FFVQPTVFS 388
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGEDPLESP--DYGRIINEKHfDRLAGLLDNGK-----IVFGGN--TDREtLYIEPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 389 NVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVN---CYLAVPvQCP 465
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtiMHLANP-YLP 397
|
330 340
....*....|....*....|....*..
gi 7106242 466 FGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07136 398 FGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
58-493 |
2.18e-63 |
|
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: 212.46 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 58 ADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLME--RDRLLLA--------TMESMNAGKVFAHAYLLDVeisI 127
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKdnEEAIVEAlkkdlgrpPFETLLTEVSGVKNDILHM---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 128 KALQYFAgwADKIhgqtiPSDGNIF-----TYTRREPIGVCGQIIPWNGPLIIftwKLGP---ALSCGNTVVVKPAEQTP 199
Cdd:cd07135 79 KNLKKWA--KDEK-----VKDGPLAfmfgkPRIRKEPLGVVLIIGPWNYPVLL---ALSPlvgAIAAGCTVVLKPSELTP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 200 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDidKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07135 149 HTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVrrsvERAKKYilgnpLN----SGINQGPQ----IDKEQH 351
Cdd:cd07135 225 KNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFV----EELKKV-----LDefypGGANASPDytriVNPRHF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 352 NKILGLIESGKkegAKLECGGGRwGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAG 431
Cdd:cd07135 296 NRLKSLLDTTK---GKVVIGGEM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALY 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242 432 VFTKDLDKAITVSSALQAGMVWVN-CYLAVPV-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07135 372 IFTDDKSEIDHILTRTRSGGVVINdTLIHVGVdNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
68-492 |
5.11e-63 |
|
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: 211.57 E-value: 5.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 68 RQAFQI-GSPwrtmDASERGRLLNKLADLM--ERDRLLLA---------TMESMnagkvfahayLLDVEISIKALQY--- 132
Cdd:cd07133 8 KAAFLAnPPP----SLEERRDRLDRLKALLldNQDALAEAisadfghrsRHETL----------LAEILPSIAGIKHark 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 133 -FAGW--ADKIHG--QTIPSDGNIftytRREPIGVCGQIIPWNGPLIIftwKLGP---ALSCGNTVVVKPAEQTPLTALH 204
Cdd:cd07133 74 hLKKWmkPSRRHVglLFLPAKAEV----EYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 205 MASLIKEAgFPPGVVNIVPGyGPTAGGAISShMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADL 284
Cdd:cd07133 147 LAELLAEY-FDEDEVAVVTG-GADVAAAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 285 DSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKY---ILGNPLNSGInqgpqIDKEQHNKILGLIESG 361
Cdd:cd07133 223 AKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPDYTSI-----INERHYARLQGLLEDA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 362 KKEGAKL-ECG-GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDK 439
Cdd:cd07133 298 RAKGARViELNpAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAE 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242 440 AITVSSALQAGMVWVN-CYLAVpVQ--CPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07133 378 QDRVLRRTHSGGVTINdTLLHV-AQddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-486 |
9.76e-61 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 215.99 E-value: 9.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 39 PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMErdrlllATMESM------NA 111
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPI---WFATPPAERAAILERAADLME------AQMQTLmgllvrEA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 112 GKVFAHAyLLDVEISIKALQYFAGwadkihgQTIPSDGNiftYTRRePIG--VCgqIIPWNGPLIIFTWKLGPALSCGNT 189
Cdd:PRK11809 733 GKTFSNA-IAEVREAVDFLRYYAG-------QVRDDFDN---DTHR-PLGpvVC--ISPWNFPLAIFTGQVAAALAAGNS 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 190 VVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIK-------EAAGKSn 262
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQrnlagrlDPQGRP- 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 263 lkrVTL--ELGGKSPCIVfadadlDSAVeFAHQGV-------FFHQGQICVAASRLFVEESIYDefvrRSVERAK----K 329
Cdd:PRK11809 878 ---IPLiaETGGQNAMIV------DSSA-LTEQVVadvlasaFDSAGQRCSALRVLCLQDDVAD----RTLKMLRgamaE 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 330 YILGNP--LNSGInqGPQIDKEQHNKILGLIESGKKEGAK---LECGGGRWGNKGFFVQPTVFS-NVTDEMriaKEEIFG 403
Cdd:PRK11809 944 CRMGNPdrLSTDI--GPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLIElDSFDEL---KREVFG 1018
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 404 PVQQIMKFKS--MDDVIKRANNTTYGLAAGVFTKdLDKAIT-VSSALQAGMVWVNCYL---AVPVQcPFGGFKMSGNGRE 477
Cdd:PRK11809 1019 PVLHVVRYNRnqLDELIEQINASGYGLTLGVHTR-IDETIAqVTGSAHVGNLYVNRNMvgaVVGVQ-PFGGEGLSGTGPK 1096
|
490
....*....|
gi 7106242 478 LGehG-LYEY 486
Cdd:PRK11809 1097 AG--GpLYLY 1104
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
3-473 |
8.79e-60 |
|
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: 205.13 E-value: 8.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 3 SPAQPAVPAPLANLKIQHTKI--FINNEWHDSVSSKKfpVLNPAT-EEVICHVEEGDKADVDKAVKAARQAfqiGSPWRT 79
Cdd:cd07123 13 SPERAKLQEALAELKSLTVEIplVIGGKEVRTGNTGK--QVMPHDhAHVLATYHYADAALVEKAIEAALEA---RKEWAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 80 MDASERGRLLNKLADLME---RDRLLLATMesMNAGKVFAHAylldvEI-----SIKALQYFAGWADKI-HGQTIPSDGN 150
Cdd:cd07123 88 MPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQA-----EIdaaceLIDFLRFNVKYAEELyAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 151 IFTYTRREPI-GVCGQIIPWNGPLIIFTWKLGPALsCGNTVVVKPAEqtplTALHMASLI----KEAGFPPGVVNIVPGY 225
Cdd:cd07123 161 VWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSD----TAVLSNYLVykilEEAGLPPGVINFVPGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 226 GPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKS-----NLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQG 300
Cdd:cd07123 236 GPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 301 QICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKE-GAKLECGGGRWGNKG 379
Cdd:cd07123 316 QKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 380 FFVQPTVFSnVTDEM-RIAKEEIFGPVQQIM-----KFKSMDDVIkraNNTT-YGLAAGVFTKDlDKAI-TVSSALQ--A 449
Cdd:cd07123 396 YFVEPTVIE-TTDPKhKLMTEEIFGPVLTVYvypdsDFEETLELV---DTTSpYALTGAIFAQD-RKAIrEATDALRnaA 470
|
490 500
....*....|....*....|....*.
gi 7106242 450 GMVWVN--CYLAVPVQCPFGGFKMSG 473
Cdd:cd07123 471 GNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
24-491 |
1.43e-56 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 196.21 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDS---VSSkkfpvLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDR 100
Cdd:PLN02315 24 YVGGEWRANgplVSS-----VNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 101 LLLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWK 179
Cdd:PLN02315 96 DYLGRLVSLEMGKILAEG-IGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 180 LGPALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIK 255
Cdd:PLN02315 175 ACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 256 EAAgKSNLKRVTLELGGKSPCIVFADADLDSAVE---FAHQGVffhQGQICVAASRLFVEESIYDEFVRRSVERAKKYIL 332
Cdd:PLN02315 254 QTV-NARFGKCLLELSGNNAIIVMDDADIQLAVRsvlFAAVGT---AGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 333 GNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSnVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:PLN02315 330 GDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQA--GMVWVNcylaVP-----VQCPFGGFKMSGNGRELGEHGLYE 485
Cdd:PLN02315 409 TLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVN----IPtngaeIGGAFGGEKATGGGREAGSDSWKQ 484
|
....*.
gi 7106242 486 YTELKT 491
Cdd:PLN02315 485 YMRRST 490
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
153-501 |
1.60e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 196.02 E-value: 1.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 153 TYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGyGPTAGGA 232
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 233 ISSHmDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVE 312
Cdd:PTZ00381 181 LLKE-PFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 313 ESIYDEFVRRSVERAKKYILGNPLNSgiNQGPQIDKEQH-NKILGLIESGKKEGAKlecgGGRWGNKGFFVQPTVFSNVT 391
Cdd:PTZ00381 259 RSIKDKFIEALKEAIKEFFGEDPKKS--EDYSRIVNEFHtKRLAELIKDHGGKVVY----GGEVDIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 392 DEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVN-CYLAV-PVQCPFGGF 469
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLlNPNLPFGGV 412
|
330 340 350
....*....|....*....|....*....|..
gi 7106242 470 KMSGNGRELGEHGLYEYTELKTVaMQISQKNS 501
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPV-LNKSTGNS 443
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
62-482 |
7.98e-49 |
|
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: 173.95 E-value: 7.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 62 KAVKAARQAFQIGspwRTMDASERGRLLNKLADLME--RDRLLLATMESMNAGKVfaHAYLLDVEISIK----ALQYFAG 135
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEenEDEIVEALAKDLRKPKF--EAVLSEILLVKNeikyAISNLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 136 WAdkihgQTIPSDGNIFT-----YTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLI- 209
Cdd:cd07132 77 WM-----KPEPVKKNLATllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 210 ----KEAgFPpgVVNivpgygptagGAISSHMDI-----DKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFA 280
Cdd:cd07132 152 kyldKEC-YP--VVL----------GGVEETTELlkqrfDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 281 DADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGiNQGPQIDKEQHNKILGLIES 360
Cdd:cd07132 218 SCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLLSG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 361 GKKegakleCGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT---KDL 437
Cdd:cd07132 297 GKV------AIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSnnkKVI 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 7106242 438 DKAITVSSalqAGMVWVNCYL--AVPVQCPFGGFKMSGNGRELGEHG 482
Cdd:cd07132 371 NKILSNTS---SGGVCVNDTImhYTLDSLPFGGVGNSGMGAYHGKYS 414
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
64-486 |
6.44e-43 |
|
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: 157.57 E-value: 6.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 64 VKAARQAFQIGspwRTMDASERGRLLNKLADLM-ERDRLLLATMESmNAGKVFAHAYLLDVEISIK----ALQYFAGWAD 138
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSscklAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 139 ----KIHGQTIPSDGNIFTytrrEPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgF 214
Cdd:cd07137 81 pekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 215 PPGVVNIVPGyGPTAGGAISSHmDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQG 294
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 295 VF-FHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGinQGPQIDKEQHNKILGLIESGKKEGAKLECGGG 373
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK--DLSRIVNSHHFQRLSRLLDDPSVADKIVHGGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 374 RWGNKgFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT--KDLDKAItVSSALQAGM 451
Cdd:cd07137 311 RDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRI-VAETSSGGV 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 7106242 452 VWVNCYLAVPV-QCPFGGFKMSGNGRelgEHGLYEY 486
Cdd:cd07137 389 TFNDTVVQYAIdTLPFGGVGESGFGA---YHGKFSF 421
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
39-436 |
2.93e-35 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 137.91 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 39 PVLNPATEEVICHVEeGDKADVDKAVKAARQafQIGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHA 118
Cdd:PRK11903 22 PLFDPVTGEELVRVS-ATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 119 yLLDVEISIKALQYFAGWADKIHGQTIPSDG--------------NIFTYTRrepiGVCGQIIPWNGPliifTW----KL 180
Cdd:PRK11903 99 -AVDIDGGIFTLGYYAKLGAALGDARLLRDGeavqlgkdpafqgqHVLVPTR----GVALFINAFNFP----AWglweKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAG-FPPGVVNIVPGygpTAGGAISSHMDIDKVSFTGSTEVGKLIK-EAA 258
Cdd:PRK11903 170 APALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---SSAGLLDHLQPFDVVSFTGSAETAAVLRsHPA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 259 GKSNLKRVTLELGGKSPCIVFADADLDSAvEFAhqgVFFHQ---------GQICVAASRLFVEESIYDEFVRRSVERAKK 329
Cdd:PRK11903 247 VVQRSVRVNVEADSLNSALLGPDAAPGSE-AFD---LFVKEvvremtvksGQKCTAIRRIFVPEALYDAVAEALAARLAK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 330 YILGNPLNSGINQGPQIDKEQHNKILGLIEsGKKEGAKLECGGGRWG------NKGFFVQPTVF--SNVTDEMRIAKEEI 401
Cdd:PRK11903 323 TTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDPDAATAVHDVEV 401
|
410 420 430
....*....|....*....|....*....|....*
gi 7106242 402 FGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:PRK11903 402 FGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
53-486 |
2.65e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 126.38 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 53 EEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLM--ERDRLLLATMESMnaGKVFAHAYLLDVEISIK-- 128
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESG---RTRSLEWRKSQLKGLLRLLkdNEEAIFKALHQDL--GKHRVEAYRDEVGVLTKsa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 129 --ALQYFAGWADKIHGQ----TIPSDGNIFTytrrEPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTA 202
Cdd:PLN02203 76 nlALSNLKKWMAPKKAKlplvAFPATAEVVP----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 203 LHMASLIKeAGFPPGVVNIVPGyGPTAGGAISSHmDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIV---F 279
Cdd:PLN02203 152 AFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdslS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 280 ADADLDSAVEFAHQGVFFH-QGQICVAASRLFVEE---SIYDEFVRRSVeraKKYILGNPLNSGinQGPQIDKEQH-NKI 354
Cdd:PLN02203 228 SSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEErfaPILIELLKSTI---KKFFGENPRESK--SMARILNKKHfQRL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 355 LGLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:PLN02203 303 SNLLKDPRVAASIVH--GGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFT 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 435 KDLDKAITVSSALQAGMVWVNcylAVPVQ-----CPFGGFKMSGNGRelgEHGLYEY 486
Cdd:PLN02203 381 NNEKLKRRILSETSSGSVTFN---DAIIQyacdsLPFGGVGESGFGR---YHGKYSF 431
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
24-440 |
9.30e-30 |
|
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: 121.99 E-value: 9.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSvSSKKFPVLNPATEEVICHVEeGDKADVDKAVKAARQafqIGSP-WRTMDASERGRLLNKLAD-LMERDRL 101
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYARE---KGGPaLRALTFHERAAMLKALAKyLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 102 L--LATMESMNAGKVFahaylLDVEISIKALQYFAGWADK--------IHGQTIP-SDGNIFT----YTRREpiGVCGQI 166
Cdd:cd07128 79 LyaLSAATGATRRDSW-----IDIDGGIGTLFAYASLGRRelpnahflVEGDVEPlSKDGTFVgqhiLTPRR--GVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 167 IPWNGPLiiftW----KLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG-FPPGVVNIVPGygptAGGAISSHMDI-D 240
Cdd:cd07128 152 NAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGDLLDHLGEqD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 241 KVSFTGSTEVGKLIK-EAAGKSNLKRVTLELGGKSPCIVFADADLDSAvEFAhqgVFFHQ---------GQICVAASRLF 310
Cdd:cd07128 224 VVAFTGSAATAAKLRaHPNIVARSIRFNAEADSLNAAILGPDATPGTP-EFD---LFVKEvaremtvkaGQKCTAIRRAF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 311 VEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEgAKLECGG-------GRWGNKGFFVQ 383
Cdd:cd07128 300 VPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfevvGADAEKGAFFP 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242 384 PTVF-SNVTDEMRIAKE-EIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKA 440
Cdd:cd07128 379 PTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFA 437
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
60-436 |
1.61e-26 |
|
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: 111.95 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 60 VDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADK 139
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 140 IH---GQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG-FP 215
Cdd:cd07084 78 IPhepGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 216 PGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVG-KLIKEAAgksnLKRVTLELGGKSPCIVFADADLDSAveFAHQG 294
Cdd:cd07084 158 PEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAeKLALDAK----QARIYLELAGFNWKVLGPDAQAVDY--VAWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 295 VF---FHQGQICVAASRLFVEEsiyDEFVRRSVERAKKYilgnpLNSGINQGPQIDKEQHNKILGLIES-GKKEGAKLEC 370
Cdd:cd07084 231 VQdmtACSGQKCTAQSMLFVPE---NWSKTPLVEKLKAL-----LARRKLEDLLLGPVQTFTTLAMIAHmENLLGSVLLF 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242 371 GG------GRWGNKGFFVQPTVFSNVTDEMRIAK---EEIFGPVQQIMKFK--SMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07084 303 SGkelknhSIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdQLALVLELLERMHGSLTAAIYSND 379
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
123-492 |
4.62e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.91 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 123 VEISIKALQ-YFAGWADKIHGQTIPSDGNIFTytrrEPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLT 201
Cdd:PLN02174 79 IKLALKQLKnWMAPEKAKTSLTTFPASAEIVS----EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPAS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 202 ALHMASLIkEAGFPPGVVNIVPGYGPTAGGAISSHMdiDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFAD 281
Cdd:PLN02174 155 SALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW--DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 282 ADLDSAVEFAHQGVF-FHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGiNQGPQIDKEQHNKILGLIEs 360
Cdd:PLN02174 231 TDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLD- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 361 gKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKA 440
Cdd:PLN02174 309 -EKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLK 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 7106242 441 ITVSSALQAGMVWVN---CYLAVPVqCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PLN02174 388 ERFAATVSAGGIVVNdiaVHLALHT-LPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
60-322 |
2.40e-15 |
|
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: 77.65 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 60 VDKAVKAARQA-FQIGSPWRTMDASERGRLLNKLAdlmerdRLLLATMeSMNAGKVFAHAYlldveisikALQYFAGWAD 138
Cdd:cd07077 18 RDLIINAIANAlYDTRQRLASEAVSERGAYIRSLI------ANWIAMM-GCSESKLYKNID---------TERGITASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 139 KIHGQTIPSDGNifTYTRREPIGVCGQIIPWNGPLIIFTwKLGPALSCGNTVVVKPAEQTPLTAlHMASLIKEAGFPPGV 218
Cdd:cd07077 82 HIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 219 VNIVPGYGPTAGGAIS----SHMDIDKVSFTGSTEVgklIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQG 294
Cdd:cd07077 158 PKILVLYVPHPSDELAeellSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260
....*....|....*....|....*...
gi 7106242 295 VFFHQgQICVAASRLFVEESIYDEFVRR 322
Cdd:cd07077 235 KFFDQ-NACASEQNLYVVDDVLDPLYEE 261
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
60-405 |
3.04e-13 |
|
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: 71.42 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 60 VDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME--RDRLLLATMESMNAGKVfahayLLDVEIS--IKALQYFA- 134
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEalGDELVARAHAETGLPEA-----RLQGELGrtTGQLRLFAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 135 -----GWADKI------HGQTIP-SDgniftyTRREPIGVcgqiipwnGPLIIFtwklGP----------------ALSC 186
Cdd:cd07129 73 lvregSWLDARidpadpDRQPLPrPD------LRRMLVPL--------GPVAVF----GAsnfplafsvaggdtasALAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 187 GNTVVVKPAEQTPLTALHMASLI----KEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAgksn 262
Cdd:cd07129 135 GCPVVVKAHPAHPGTSELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 263 LKR-----VTLELGGKSPCIVFADADLDSAVEFAH-------QGVffhqGQICVAASRLFVEESI-YDEFVRRSVERAKK 329
Cdd:cd07129 211 AARpepipFYAELGSVNPVFILPGALAERGEAIAQgfvgsltLGA----GQFCTNPGLVLVPAGPaGDAFIAALAEALAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 330 YILGNPLNSGINQGPQIDKEQ---HNKILGLIESGKKEGaklecgggrwgnkGFFVQPTVFsnVTDEMRIAK-----EEI 401
Cdd:cd07129 287 APAQTMLTPGIAEAYRQGVEAlaaAPGVRVLAGGAAAEG-------------GNQAAPTLF--KVDAAAFLAdpalqEEV 351
|
....
gi 7106242 402 FGPV 405
Cdd:cd07129 352 FGPA 355
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
24-436 |
3.63e-11 |
|
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: 65.21 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 24 FINNEWHDSVSSKKfpVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIG--SPWRtmdASER----GRLLNKLADLME 97
Cdd:cd07126 2 LVAGKWKGASNYTT--LLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhNPLK---NPERyllyGDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 98 RDRL--LLATMESMNAGKVFAHAyLLDVEISIKALQYFAGwaDKIH----GQTIPSD--GNIfTYTRREPIGVCGQIIPW 169
Cdd:cd07126 77 KPEVedFFARLIQRVAPKSDAQA-LGEVVVTRKFLENFAG--DQVRflarSFNVPGDhqGQQ-SSGYRWPYGPVAIITPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 170 NGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAgGAISSHMDIDKVSFTGSTE 249
Cdd:cd07126 153 NFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTM-NKILLEANPRMTLFTGSSK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 250 VG-KLIKEAAGKsnlkrVTLELGGKSPCIVFAD-ADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDE-FVRRSVER 326
Cdd:cd07126 232 VAeRLALELHGK-----VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 327 AKKYILGNplnsgINQGP------QIDKEQHNKILGLiesgkkEGAKLECGGGRWGNKGF-----FVQPT-VF-----SN 389
Cdd:cd07126 307 AEQRKLED-----LTIGPvltwttERILDHVDKLLAI------PGAKVLFGGKPLTNHSIpsiygAYEPTaVFvpleeIA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 7106242 390 VTDEMRIAKEEIFGPVQQIMKFK--SMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07126 376 IEENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSND 424
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
58-332 |
6.59e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.99 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 58 ADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAG------KVFAHAYLLDVEISIKALQ 131
Cdd:PRK15398 36 ASVDDAVAAAKVAQQR---YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNVAAAEKTPGVEDLT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 132 YFAGWADkiHGQTIpsdgniFTYTrrePIGVCGQIIPWNGPL--IIftwklGPA---LSCGNTVVVKP---AEQTPLTAL 203
Cdd:PRK15398 113 TEALTGD--NGLTL------IEYA---PFGVIGAVTPSTNPTetII-----NNAismLAAGNSVVFSPhpgAKKVSLRAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 204 HMAS-LIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGstevGKLIKEAAGKSNlKRVTLELGGKSPCIVFADA 282
Cdd:PRK15398 177 ELLNeAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVVVDETA 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 7106242 283 DLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRsVERAKKYIL 332
Cdd:PRK15398 252 DIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRL-MEKNGAVLL 300
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
58-335 |
7.99e-09 |
|
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: 57.63 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 58 ADVDKAVKAARQAFQIgspWRTMDASERGRLLN--KLADLMERDRLLLATMESMNAG----KVFAHAYLLDVEISIKALQ 131
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ---YRKCTLADREKIIEaiREALLSNAEELAEMAVEETGMGrvedKIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 132 YFAGWADkiHGQTIpsdgniftyTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKP---AEQTPLTALHMAS- 207
Cdd:cd07121 81 TTAWSGD--NGLTL---------VEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELINk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 208 LIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGstevGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLDSA 287
Cdd:cd07121 150 AIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSSG-KKAIGAGAGNPPVVVDETADIEKA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 7106242 288 VEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRsVERAKKYILGNP 335
Cdd:cd07121 225 ARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAA-MQRNGAYVLNDE 271
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
138-476 |
2.84e-08 |
|
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: 56.12 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 138 DKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEA----G 213
Cdd:cd07081 74 DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 214 FPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGstevGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLDSAVEFAHQ 293
Cdd:cd07081 154 APENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKRAVQSIVK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 294 GVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNS-------GINQGPQIDKEQHNKILGLIESGKKEGA 366
Cdd:cd07081 229 SKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQvqpvilkNGDVNRDIVGQDAYKIAAAAGLKVPQET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 367 KLecgggrwgnkgFFVQPTVFsnvtDEMRIAKEEIFGPVQQIMKFKSMDDVIKRA----NNTTYGLAAGVFT---KDLDK 439
Cdd:cd07081 309 RI-----------LIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSdniKAIEN 373
|
330 340 350
....*....|....*....|....*....|....*..
gi 7106242 440 AITVSSALQAGMVWVNcylavpVQCPFGGFKMSGNGR 476
Cdd:cd07081 374 MNQFANAMKTSRFVKN------GPCSQGGLGDLYNFR 404
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
56-455 |
4.64e-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: 52.48 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 56 DKADVDKAVKAARQAFQigsPWRtmDASERGRL---LNKLADLMERD-RLLLATMESmnAGKVF--------AHAylLDV 123
Cdd:cd07127 82 PQCDPDALLAAARAAMP---GWR--DAGARARAgvcLEILQRLNARSfEMAHAVMHT--TGQAFmmafqaggPHA--QDR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 124 eiSIKALQYFAGWADKIHGQTI---PSDGN-------IFTYTRRepiGV-----CGQIIPWNGPLIIFTwklgpALSCGN 188
Cdd:cd07127 153 --GLEAVAYAWREMSRIPPTAEwekPQGKHdplamekTFTVVPR---GValvigCSTFPTWNGYPGLFA-----SLATGN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 189 TVVVKPAeqtPLTALHMASLIK-------EAGFPPGVVNIV--PGYGPTAgGAISSHMDIDKVSFTGSTEVGKLIKEAAG 259
Cdd:cd07127 223 PVIVKPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadTPEEPIA-QTLATRPEVRIIDFTGSNAFGDWLEANAR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 260 KsnlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFV---------EESIYDEfVRRSVERAKKY 330
Cdd:cd07127 299 Q---AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDE-VAADLAAAIDG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 331 ILGNP-----LNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRwgnkgffVQPTVFSNVTDEMRIA-KEEIFGP 404
Cdd:cd07127 375 LLADParaaaLLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDAR-------VRTPLLLKLDASDEAAyAEERFGP 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242 405 VQQIMKFKSMDDVIKRANNT--TYG-LAAGVFTKD-----------LDKAITVSSALQAGmVWVN 455
Cdd:cd07127 448 IAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDpevvervqeaaLDAGVALSINLTGG-VFVN 511
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
154-330 |
3.18e-06 |
|
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: 49.36 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 154 YTRREPIGVCGQIIPWNGPLIIFtWKLGPALSCGNTVVVKPAEQTP-LTALHMASLIK--EAGFPPGVVNIVPGYGPTAG 230
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVPLLPV-MSILMGLLVKNVNLLKVSSSDPfTAAALLASFADldPTHPLADSLSVVYWDGGSTQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 231 GAISSHMDIDKVSFTGSTEVGKLIKEAAGKSnlKRVTLELGGKSPCIVFADADLDSAVE-FAHQGVFFHQgQICVAASRL 309
Cdd:pfam05893 162 LEDLIVANADVVIAWGGEDAINAIRECLKPG--KQWIDFGAKISFAVVDREAALDKAAErAADDICVFDQ-QACLSPQTV 238
|
170 180
....*....|....*....|....
gi 7106242 310 FVE---ESIYDEFVRRSVERAKKY 330
Cdd:pfam05893 239 FVEsddKITPDEFAERLAAALAKR 262
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
158-332 |
6.12e-06 |
|
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: 48.64 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 158 EPIGVCGQIIPWNGP--------LIiftwklgpALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGy 225
Cdd:cd07122 94 EPVGVIAALIPSTNPtstaifkaLI--------ALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEE- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 226 gPT--AGGAISSHMDIDKVSFTGSTevgKLIKEA--AGKSNLkrvtlelG---GKSPCIVFADADLDSAVEfahQGVF-- 296
Cdd:cd07122 165 -PSieLTQELMKHPDVDLILATGGP---GMVKAAysSGKPAI-------GvgpGNVPAYIDETADIKRAVK---DIILsk 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 7106242 297 -FHQGQICVAASRLFVEESIYDEFVRRsVERAKKYIL 332
Cdd:cd07122 231 tFDNGTICASEQSVIVDDEIYDEVRAE-LKRRGAYFL 266
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
154-330 |
2.20e-04 |
|
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: 43.42 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 154 YTRREPIGVCGQIIPWNGPLIIFtWKLGPALSCGNTVVVKPAEQTPLTALHMA-SLIKEAGFPPGVVNI----VPGYGPT 228
Cdd:cd07080 107 YIRAQPRGLVVHIIAGNVPLLPV-WSIVRGLLVKNVNLLKMSSSDPLTATALLrSLADVDPNHPLTDSIsvvyWPGGDAE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242 229 AGGAISSHMdiDKVSFTGSTEVGKLIKEAAGKSnlKRvTLELGGK-SPCIV----FADADLDSAVE-FAHQGVFFHQgQI 302
Cdd:cd07080 186 LEERILASA--DAVVAWGGEEAVKAIRSLLPPG--CR-LIDFGPKySFAVIdreaLESEKLAEVADaLAEDICRYDQ-QA 259
|
170 180
....*....|....*....|....*...
gi 7106242 303 CVAASRLFVEESIyDEFVRRSVERAKKY 330
Cdd:cd07080 260 CSSPQVVFVEKDD-DEELREFAEALAAA 286
|
|
| DUF1487 |
pfam07368 |
Protein of unknown function (DUF1487); This family consists of several uncharacterized ... |
273-335 |
8.76e-04 |
|
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: 40.82 E-value: 8.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242 273 KSPC--IVFADADLDSAVEFAHQGVffHQGQICVAASRLFVEESIYDEF---VRRSVERAKKYILGNP 335
Cdd:pfam07368 3 NSPRlmVIFEDGDVNSALHALVESL--HNPFAPGAVATVLVQESIRDEFverVRSRLKPLSERVANHP 68
|
|
| |
