|
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 ... |
14-491 |
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: 997.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 14 IKLKLIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVE 93
Cdd:cd07141 4 IKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 94 RDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 173
Cdd:cd07141 84 RDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 174 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 253
Cdd:cd07141 164 WKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 254 AGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 333
Cdd:cd07141 244 AGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 334 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 491
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
19-490 |
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: 869.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07091 6 LFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSN 258
Cdd:cd07091 165 ALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:cd07091 245 LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERAN 418
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332634711 419 NSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07091 405 DTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
14-488 |
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: 731.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 14 IKLKLIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVE 93
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGP-WPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 94 RDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 173
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 174 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 253
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 254 AGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 333
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 334 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
14-496 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 710.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 14 IKLKLIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVE 93
Cdd:PLN02466 55 VSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGP-WPKMTAYERSRILLRFADLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 94 RDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 173
Cdd:PLN02466 134 KHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 174 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 253
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 254 AGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 333
Cdd:PLN02466 294 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 334 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVkiP 493
Cdd:PLN02466 454 IRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT--P 531
|
...
gi 332634711 494 QKN 496
Cdd:PLN02466 532 LKN 534
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
19-492 |
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: 709.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE-TDWGLKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSN 258
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERAN 418
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAN 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332634711 419 NSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 492
Cdd:cd07143 408 DSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
20-491 |
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: 694.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:COG1012 9 FIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:COG1012 86 AALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsN 258
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE-N 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERA 417
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 418 NNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 491
Cdd:COG1012 404 NDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
25-488 |
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: 688.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 25 WQNSESGRvFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMES 104
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 105 LNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGN 184
Cdd:pfam00171 77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 185 TVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTL 264
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 265 ELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDK 344
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 345 KQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGL 424
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 425 VAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
10-490 |
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: 675.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 10 LKSPIKLkliFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLA 89
Cdd:cd07144 4 YDQPTGL---FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 90 DLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPL 169
Cdd:cd07144 79 DLVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 170 LMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKL 249
Cdd:cd07144 159 AMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 250 IQEAAGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRR-VV 328
Cdd:cd07144 239 VMKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 329 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEIL 405
Cdd:cd07144 318 GSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 406 RFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEV 485
Cdd:cd07144 398 KFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQT 477
|
....*
gi 332634711 486 KTVTV 490
Cdd:cd07144 478 KAVHI 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
14-493 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 644.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 14 IKLKLIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVE 93
Cdd:PLN02766 18 IKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGP-WPRMSGFERGRIMMKFADLIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 94 RDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 173
Cdd:PLN02766 97 EHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 174 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 253
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 254 AGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 333
Cdd:PLN02766 257 AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 334 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIP 493
Cdd:PLN02766 417 IKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPLY 496
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
20-488 |
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: 640.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 179
Cdd:cd07119 80 ARLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 180 LCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNL 259
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 260 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 339
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 340 PQIDKKQYNKILELIQSGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 415
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332634711 416 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-490 |
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: 630.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 57 DKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKI 136
Cdd:cd07078 1 DAAVAAARAAFK---AWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 137 HGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVI 215
Cdd:cd07078 77 HGEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 216 NILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQ 295
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 296 GQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR-K 374
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 375 GFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYN 454
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 332634711 455 A-LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
31-488 |
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: 629.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 31 GRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKP 110
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESG-VWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 111 FLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKS 270
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 271 PNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNK 349
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 350 ILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 427
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332634711 428 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
36-490 |
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: 619.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPF---- 111
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIretr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 112 LQAFYVdlqgvIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:cd07114 80 AQVRYL-----AEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKS 270
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 271 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 350
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 351 LELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVA 426
Cdd:cd07114 314 ERYVARAREEGARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332634711 427 AVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-492 |
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: 610.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 38 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYV 117
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 118 DLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLS 197
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 198 ALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVG-KLIQEAAGrsNLKRVTLELGGKSPNIIFA 276
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGrKIMQGAAG--NLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 277 DADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQS 356
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 357 GVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKA 436
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 332634711 437 LTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 492
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
36-490 |
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: 589.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 115
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 195
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 196 LSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIF 275
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 276 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 355
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 356 SGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 431
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 332634711 432 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
19-491 |
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: 583.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07140 8 LFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAW 174
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 175 KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 254
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 255 GRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 334
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 335 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT--MDE 412
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332634711 413 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 491
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
20-490 |
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: 563.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 179
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 180 LCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNL 259
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 260 KRVTLELGGKSPNIIFADA-----DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 334
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 335 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 410
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 411 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
19-489 |
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: 545.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP---AWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LA---TMESlngGKPFLQAFYVDLQGVIKTFRYYAGWADKIHgMTIPVDGdyfTFTRHEPIGVCGQIIPWNFPLLMFAWK 175
Cdd:cd07138 78 LAqaiTLEM---GAPITLARAAQVGLGIGHLRAAADALKDFE-FEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 176 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAG 255
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 256 RSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 335
Cdd:cd07138 231 DT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 336 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 412
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332634711 413 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 489
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
36-490 |
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: 543.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 115
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 195
Cdd:cd07109 78 RADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 196 LSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIF 275
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 276 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG-SPFDPttEQGPQIDKKQYNKILELI 354
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpGLEDP--DLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 355 QSGVAEGAKLECGG---KGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 431
Cdd:cd07109 315 ARARARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 432 DINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
20-490 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 541.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLV-ERDRAv 98
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK---IWAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSn 258
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 414
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332634711 415 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
36-490 |
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: 541.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 115
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK---EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 195
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 196 LSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIF 275
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 276 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 355
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 356 SGVAEGAKLECGGKGLG-----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 430
Cdd:cd07090 315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 431 NDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
36-490 |
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: 537.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 115
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFK---TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQT 194
Cdd:cd07103 77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 195 PLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGK-LIQEAAgrSNLKRVTLELGGKSPNI 273
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 274 IFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILEL 353
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 354 IQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI 433
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 332634711 434 NKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
20-486 |
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: 531.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 179
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 180 LCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNL 259
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 260 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 339
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 340 PQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 415
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332634711 416 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVK 486
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-490 |
0e+00 |
|
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: 526.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:cd07117 80 LAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsN 258
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 414
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332634711 415 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
39-490 |
0e+00 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 524.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 39 PATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVD 118
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 119 LQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLS 197
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 198 ALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFAD 277
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 278 ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSG 357
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 358 VAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKA 436
Cdd:cd07118 321 RAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 332634711 437 LTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
36-489 |
0e+00 |
|
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: 521.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 115
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP---RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YvDLQGVIKTFRYYAGWADKIH---GMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 191
Cdd:cd07110 78 W-DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 192 EQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 271
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 272 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 351
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 352 ELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 429
Cdd:cd07110 316 SFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 430 TNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 489
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
20-492 |
2.05e-180 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 514.07 E-value: 2.05e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSEsGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PRK13473 6 LINGELVAGE-GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP---EWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGmtiPVDGDY---FT-FTRHEPIGVCGQIIPWNFPLLMFAWK 175
Cdd:PRK13473 82 ARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGEYlegHTsMIRRDPVGVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 176 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAG 255
Cdd:PRK13473 159 LAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 256 RSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 335
Cdd:PRK13473 238 DS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 336 TEQGPQIDKKQYNKILELIQSGVAEG-AKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 414
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 415 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 492
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKH 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
36-490 |
1.18e-178 |
|
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: 508.79 E-value: 1.18e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 115
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGmtiPVDGDYF----TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 191
Cdd:cd07092 78 DDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 192 EQTPLSALYMGALIKEaGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 271
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 272 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 351
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 352 ELIqSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 431
Cdd:cd07092 313 GFV-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 332634711 432 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-484 |
1.57e-174 |
|
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: 499.61 E-value: 1.57e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 5 CETVWLKSPIKLKLIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRL 84
Cdd:cd07111 10 CALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 85 LDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIhgmtipvdgDYfTFTRHEPIGVCGQIIP 164
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLL---------DT-ELAGWKPVGVVGQIVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 165 WNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGST 244
Cdd:cd07111 157 WNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 245 EVGKLIQEA-AGRSnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERA 323
Cdd:cd07111 236 EVGRALRRAtAGTG--KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 324 KRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQE 403
Cdd:cd07111 314 SHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 404 ILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYS 483
Cdd:cd07111 394 VLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
.
gi 332634711 484 E 484
Cdd:cd07111 474 R 474
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
61-490 |
2.71e-174 |
|
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: 494.44 E-value: 2.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 61 QAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMT 140
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 141 IP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILP 219
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 220 GYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 299
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 300 TAGSRIFVEESIYEEFVRRSVerakrrvvgspfdptteqgpqidkkqynkileliqsgvaegaklecggkglgrkgffie 379
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 380 pTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-A 458
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgP 335
|
410 420 430
....*....|....*....|....*....|..
gi 332634711 459 QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
36-488 |
9.20e-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: 496.77 E-value: 9.20e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRrMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 115
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHG-MTIPVDGDYFTFT----RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKS 270
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 271 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 350
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 351 LELIQSGVAEGAKLECGGK---GLGrKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 427
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGrpaGLD-KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332634711 428 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
36-490 |
2.75e-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: 490.12 E-value: 2.75e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 115
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGwadkihgMTIPV-----DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:cd07106 77 QFEVGGAVAWLRYTAS-------LDLPDeviedDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAgFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKS 270
Cdd:cd07106 150 SPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGND 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 271 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 350
Cdd:cd07106 227 AAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 351 LELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 430
Cdd:cd07106 307 KELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 431 NDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
20-488 |
4.84e-171 |
|
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: 490.22 E-value: 4.84e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRvfPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 177
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 178 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrS 257
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 258 NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE 337
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 338 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 415
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 416 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNG-REMGEFGLREYSEVKTV 488
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-489 |
6.34e-171 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 491.17 E-value: 6.34e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 12 SPIKLKLIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFS--LGSVWRRMDASERGRLLDKLA 89
Cdd:PLN02467 3 IPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTGAVRAKYLRAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 90 DLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHG-----MTIPVDgDYFTFTRHEPIGVCGQIIP 164
Cdd:PLN02467 83 AKITERKSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAkqkapVSLPME-TFKGYVLKEPLGVVGLITP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 165 WNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGST 244
Cdd:PLN02467 161 WNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 245 EVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAK 324
Cdd:PLN02467 241 ATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 325 RRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQ 402
Cdd:PLN02467 320 NIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 403 EILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREY 482
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENY 479
|
....*..
gi 332634711 483 SEVKTVT 489
Cdd:PLN02467 480 LSVKQVT 486
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
19-490 |
5.18e-170 |
|
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: 487.47 E-value: 5.18e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAG------WADKIHGMTIpvdGDyfTFTRHEPIGVCGQIIPWNFPLLMF 172
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAAlardfpFEERRPGSGG---GH--VLVRREPVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 173 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQE 252
Cdd:cd07139 155 ALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 253 AAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 332
Cdd:cd07139 234 VCGE-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 333 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK---GLGRkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 409
Cdd:cd07139 313 DPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpaGLDR-GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 410 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYnALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 489
Cdd:cd07139 392 EDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
.
gi 332634711 490 V 490
Cdd:cd07139 471 L 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
20-488 |
2.97e-167 |
|
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: 480.61 E-value: 2.97e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:cd07088 78 AKLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsN 258
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERA 417
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332634711 418 NNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
20-490 |
1.31e-165 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 476.84 E-value: 1.31e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQ-VCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFP---EWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 177
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 178 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRS 257
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 258 NlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE 337
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 338 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNAlNAQSPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 490
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
20-494 |
1.62e-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: 469.29 E-value: 1.62e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWA-DKIHGMTIPVDgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 175
Cdd:TIGR02299 81 AVLECLDCGQPLRQT----RQQVIRAaenFRFFADKCeEAMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 176 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQeAAG 255
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIM-RNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 256 RSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 335
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 336 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG-------RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 408
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 409 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
490
....*....|.
gi 332634711 489 TV-----KIPQ 494
Cdd:TIGR02299 475 ALalgphHIPK 485
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
36-492 |
1.49e-161 |
|
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: 465.70 E-value: 1.49e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAF 115
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 195
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 196 LSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIF 275
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 276 ADADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELI 354
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 355 QSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 430
Cdd:cd07107 315 DSAKREGARLVTGGGrpegPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332634711 431 NDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 492
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
36-490 |
6.80e-161 |
|
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: 464.14 E-value: 6.80e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 115
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 195
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 196 LSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLI-QEAAGRsnLKRVTLELGGKSPNII 274
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 275 FADADLDYAVEQAHQGV-FFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILEL 353
Cdd:cd07108 235 FPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 354 IQSGVAE-GAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 428
Cdd:cd07108 315 IDLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332634711 429 FTNDINKALTVSSAMQAGTVWIN-CYNALNAQSpFGGFKMSGNGREMG-EFGLREYSEVKTVTV 490
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNqGGGQQPGQS-YGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
34-490 |
1.25e-157 |
|
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: 455.52 E-value: 1.25e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 34 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 113
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 114 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-----DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 188
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 189 KPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGG 268
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 269 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 348
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 349 KILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 428
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332634711 429 FTNDINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-488 |
3.04e-153 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 445.88 E-value: 3.04e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 7 TVWLKSPIKLKL---IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGR 83
Cdd:PRK09847 7 AYWQDKALSLAIenrLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERG-DWSLSSPAKRKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 84 LLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQII 163
Cdd:PRK09847 86 VLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 164 PWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGS 243
Cdd:PRK09847 166 PWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 244 TEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVER 322
Cdd:PRK09847 246 TRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 323 AKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGfFIEPTVFSNVTDDMRIAKEEIFGPVQ 402
Cdd:PRK09847 326 AQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 403 EILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREY 482
Cdd:PRK09847 404 VVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKF 483
|
....*.
gi 332634711 483 SEVKTV 488
Cdd:PRK09847 484 TELKTI 489
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
34-490 |
7.59e-153 |
|
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: 443.31 E-value: 7.59e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 34 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 113
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 114 AFYvDLQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAE 192
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 193 QTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPN 272
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 273 IIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILE 352
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 353 LIQSGVAEGAKLECGGKGLGRkgfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 432
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 332634711 433 INKALTVSSAMQAGTVWINCYNAL-NAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
20-491 |
1.43e-152 |
|
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: 443.42 E-value: 1.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTI------PVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 173
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 174 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEA 253
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 254 AGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 333
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 334 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 491
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
20-488 |
1.74e-152 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 444.13 E-value: 1.74e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:PLN02278 105 AQLMTLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSn 258
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERAN 418
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 419 NSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
55-490 |
7.34e-152 |
|
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: 440.04 E-value: 7.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 55 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWAD 134
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 135 KIHGMTIPVDGD-YFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI-KEAGFPP 212
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIfEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 213 GVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF 292
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 293 FNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglg 372
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 373 RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINC 452
Cdd:cd07104 313 YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 332634711 453 YNALN-AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07104 393 QTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
34-490 |
9.14e-151 |
|
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: 438.32 E-value: 9.14e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 34 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 113
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD---VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 114 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-DY----FTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 188
Cdd:cd07145 78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyEYnerrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 189 KPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGG 268
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 269 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 348
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 349 KILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 428
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332634711 429 FTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
20-490 |
1.92e-150 |
|
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: 438.04 E-value: 1.92e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 179
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 180 LCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNL 259
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 260 KRVTLELGGKSPNIIFA------DADLDYAVEQAhqGVF-FNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 332
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 333 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNvTDDMRIAKEEIFGPVQEILRFK 408
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 409 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
..
gi 332634711 489 TV 490
Cdd:cd07116 476 LV 477
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
20-492 |
2.21e-146 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 427.99 E-value: 2.21e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWqnSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfsLGSVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:TIGR03216 4 FINGAF--VESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA--LKGPWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHG----MTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 175
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTecfeMATPDGKGALNYAVRKPLGVVGVISPWNLPLLLMTWK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 176 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGP-TAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 254
Cdd:TIGR03216 160 VGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSAIMKAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 255 GRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 334
Cdd:TIGR03216 240 ADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 335 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGG-----KGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 409
Cdd:TIGR03216 319 ATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 410 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 489
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
...
gi 332634711 490 VKI 492
Cdd:TIGR03216 479 IKL 481
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
20-490 |
1.62e-143 |
|
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: 420.43 E-value: 1.62e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGrVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07086 2 VIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK---EWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGYGPtAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 254
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 255 GRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 334
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 335 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 412
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 413 VIERANNSDFGLVAAVFTNDINKALTVSSAM--QAGTVWIN--CYNAlNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
..
gi 332634711 489 TV 490
Cdd:cd07086 474 TI 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-492 |
9.05e-141 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 414.70 E-value: 9.05e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQnsESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 97
Cdd:cd07124 35 LVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 98 VLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 177
Cdd:cd07124 110 ELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 178 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGR- 256
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 257 ----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 332
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 333 DPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 410
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 411 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSG-NGREMGEFGLREYSEVKT 487
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507
|
....*
gi 332634711 488 VTVKI 492
Cdd:cd07124 508 VTENF 512
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
37-490 |
2.35e-136 |
|
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: 401.34 E-value: 2.35e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 37 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRmDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfY 116
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 117 VDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPL 196
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 197 SALYMGALIKEA-GFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIF 275
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 276 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 355
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 356 SGVAEGAK-LECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 432
Cdd:cd07120 318 RAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 433 INKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
56-490 |
1.21e-133 |
|
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: 393.36 E-value: 1.21e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 56 IDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY-VDLQGVIktFRYYAgwaD 134
Cdd:cd07100 1 IEAALDRAHAAFL---AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEKCAWI--CRYYA---E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 135 KIHGM----TIPVDGDYfTFTRHEPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVIKPAEQTPLSALYMGALIKE 207
Cdd:cd07100 73 NAEAFladePIETDAGK-AYVRYEPLGVVLGIMPWNFPFwqvFRFA---APNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 208 AGFPPGVINILPGYGPTAGAAIASHIgIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQA 287
Cdd:cd07100 149 AGFPEGVFQNLLIDSDQVEAIIADPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 288 HQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECG 367
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 368 GKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGT 447
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 332634711 448 VWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
36-490 |
2.58e-131 |
|
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: 388.33 E-value: 2.58e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 115
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAE---NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:cd07094 80 V-EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGGKS 270
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 271 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 350
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 351 LELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 430
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332634711 431 NDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
23-491 |
3.07e-131 |
|
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: 388.59 E-value: 3.07e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 23 NEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATM 102
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 103 ESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP--VDGDYFTFTRhEPIGVCGQIIPWNFPLLMFAWKIAPAL 180
Cdd:cd07151 78 LIRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPsdVPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 181 CCGNTVVIKPAEQTPLSA-LYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNL 259
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 260 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 339
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 340 PQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANN 419
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGE---AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332634711 420 SDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALN--AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 491
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVNdePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
37-490 |
7.19e-131 |
|
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: 387.35 E-value: 7.19e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 37 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFY 116
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR---AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 117 VDLQGVIKTFRYYAGWADKI-------HGMTIPVdgdyFTFT-RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 188
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVlaprkvpTGLLMPN----KKATvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 189 KPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIAShiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGG 268
Cdd:cd07099 153 KPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 269 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 348
Cdd:cd07099 230 KDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 349 KILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 428
Cdd:cd07099 310 IVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332634711 429 FTNDINKALTVSSAMQAGTVWINC--YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
34-486 |
1.74e-127 |
|
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: 378.51 E-value: 1.74e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 34 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 113
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 114 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGD-----YFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 188
Cdd:cd07147 78 A-RGEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 189 KPAEQTPLSALYMGALIKEAGFPPGVINILPGygPTAGAAI-ASHIGIDKIAFTGSTEVGKLIQEAAGRsnlKRVTLELG 267
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 268 GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQY 347
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 348 NKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 427
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 428 VFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVK 486
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINDVPTFRVDHmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
28-490 |
3.63e-127 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 380.38 E-value: 3.63e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 28 SESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNG 107
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA---QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 108 GKPFLQAFYvDLQGVIKTFRYYAGWADKI-----HGMTIPVDGDyfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCC 182
Cdd:PRK09407 105 GKARRHAFE-EVLDVALTARYYARRAPKLlaprrRAGALPVLTK--TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 183 GNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHigIDKIAFTGSTEVGKLIQEAAGRsNLKRV 262
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-RLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 263 TLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQI 342
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 343 DKKQYNKILELIQSGVAEGAKLECGGKG---LGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANN 419
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAGGKArpdLG--PLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAND 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332634711 420 SDFGLVAAVFTNDINKALTVSSAMQAGTVWIN-CYNALNA--QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:PRK09407 417 TPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
19-491 |
2.77e-125 |
|
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: 373.83 E-value: 2.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWQNSeSGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRAV 98
Cdd:cd07082 4 YLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 99 LATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWADKIHGMTIPVDGDYFT-----FTRHEPIGVCGQIIPWNFPLL 170
Cdd:cd07082 81 VANLLMWEIGKTLKDA----LKEVDRTidyIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 171 MFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLI 250
Cdd:cd07082 157 LTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 251 QEAAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGS 330
Cdd:cd07082 237 KKQHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 331 PFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 410
Cdd:cd07082 314 PWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 411 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTVT 489
Cdd:cd07082 392 EEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMTRRKGIV 471
|
..
gi 332634711 490 VK 491
Cdd:cd07082 472 IN 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
20-491 |
9.24e-124 |
|
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: 369.92 E-value: 9.24e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:cd07085 81 ARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSN 258
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 lKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:cd07085 239 -KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 414
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 415 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKMS--GNGREMGEFGLREYSEVKTVTVK 491
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPlAFFSFGGWKGSffGDLHFYGKDGVRFYTQTKTVTSR 477
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
42-490 |
1.89e-122 |
|
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: 365.46 E-value: 1.89e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 42 GEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATM---ESlnGGKPFLQAFYVD 118
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA---QRAWAATPPRERAAVLRRAADLLEEHADEIADWivrES--GSIRPKAGFEVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 119 LqgVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSA 198
Cdd:cd07152 76 A--AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 199 LYMGALI-KEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFAD 277
Cdd:cd07152 154 GVVIARLfEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 278 ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSG 357
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 358 VAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKAL 437
Cdd:cd07152 312 VAAGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 438 TVSSAMQAGTVWINCYNALN-AQSPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 490
Cdd:cd07152 389 ALADRLRTGMLHINDQTVNDePHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
21-489 |
4.10e-122 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 366.95 E-value: 4.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 21 INNEWQNSEsgRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PRK03137 41 IGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYA----GWADKIHgmTIPVDGDYFTFtRHEPIGVCGQIIPWNFPLLMFAWK 175
Cdd:PRK03137 116 SAWLVKEAGKPWAEA-DADTAEAIDFLEYYArqmlKLADGKP--VESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 176 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAG 255
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 256 RSN-----LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGS 330
Cdd:PRK03137 272 KVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 331 PFDPtTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 410
Cdd:PRK03137 352 PEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 411 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSG-NGREMGEFGLREYSEVKT 487
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGtDSKAGGPDYLLLFLQAKT 509
|
..
gi 332634711 488 VT 489
Cdd:PRK03137 510 VS 511
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
55-490 |
2.21e-121 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 362.28 E-value: 2.21e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 55 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL-ATMESLNGGKPFLQAFYVDLqgVIKTFRYYAGWA 133
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFiEAMMEETGATAAWAGFNVDL--AAGMLREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 134 DKIHGMTIPVD--GDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFP 211
Cdd:cd07105 76 TQIIGGSIPSDkpGTL-AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 212 PGVINIL---PGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAH 288
Cdd:cd07105 155 KGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 289 QGVFFNQGQCCTAGSRIFVEESIYEEFVrrsvERAKRRVVGSPFDPTTEqGPQIDKKQYNKILELIQSGVAEGAKLECGG 368
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFV----EKLKAAAEKLFAGPVVL-GSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 369 KG-LGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGT 447
Cdd:cd07105 309 LAdESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 332634711 448 VWINCYNALN-AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07105 389 VHINGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
39-490 |
3.28e-121 |
|
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: 362.40 E-value: 3.28e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 39 PATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvD 118
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA---QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 119 LQGVIKTFRYYAGWADKI-----HGMTIPVdgdyFTFTR--HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 191
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPV----LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 192 EQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 271
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNA--DYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 272 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 351
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 352 ELIQSGVAEGAKLECGGKG---LGRkgFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 428
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRArpdLGP--YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 429 FTNDINKALTVSSAMQAGTVWIN-CYNAL--NAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
37-488 |
6.50e-114 |
|
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: 343.84 E-value: 6.50e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 37 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfy 116
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK---GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 117 vdlQGVIKTF----RYYAGWADKIHGMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 191
Cdd:cd07102 76 ---GGEIRGMleraRYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 192 EQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIgIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 271
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPR-IDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 272 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 351
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 352 ELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 428
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 429 FTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
20-492 |
2.77e-113 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 343.43 E-value: 2.77e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP---AWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfyvdlQGVIKTFRYYAGW----ADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAW 174
Cdd:PRK11241 91 ARLMTLEQGKPLAEA-----KGEISYAASFIEWfaeeGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 175 KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 254
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 255 GRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 334
Cdd:PRK11241 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 335 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 414
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 415 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 492
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
36-490 |
3.58e-113 |
|
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: 342.03 E-value: 3.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAArlafslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 115
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:cd07146 77 Y-EVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGGKS 270
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 271 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 350
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 351 LELIQSGVAEGAKLECGGkglGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 430
Cdd:cd07146 313 ENRVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332634711 431 NDINKALTVSSAMQAGTVWINCYNALNAQ-SPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 490
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
37-490 |
1.18e-106 |
|
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: 325.79 E-value: 1.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 37 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY 116
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQR---EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 117 vdlqGVIKTFryyagwADKI-----HG----MTIPVDGDYFTFTR-----HEPIGVCGQIIPWNFPLLMFAWKIAPALCC 182
Cdd:cd07098 78 ----GEILVT------CEKIrwtlkHGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 183 GNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSn 258
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 338
Cdd:cd07098 226 LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 339 GPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 414
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 415 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCY--NALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 490
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
85-488 |
8.54e-105 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 318.99 E-value: 8.54e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 85 LDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD---GDYFTFTRhePIGVCGQ 161
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 162 IIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFT 241
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 242 GSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVE 321
Cdd:PRK10090 158 GSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 322 RAKRRVVGSPFD-PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGP 400
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 401 VQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLR 480
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 332634711 481 EYSEVKTV 488
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
38-488 |
9.52e-100 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 307.43 E-value: 9.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 38 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYV 117
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-KA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 118 DLQGVIKTFRYYAgwaDKIHGMTIPVDGDYFT------FTRHEPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVI 188
Cdd:PRK09406 83 EALKCAKGFRYYA---EHAEALLADEPADAAAvgasraYVRYQPLGVVLAVMPWNFPLwqvVRFA---APALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 189 KPAEQTPLSALYMGALIKEAGFPPGVINILPgYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGG 268
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 269 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 348
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 349 KILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 428
Cdd:PRK09406 315 EVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 429 FTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-489 |
3.77e-92 |
|
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: 289.48 E-value: 3.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 19 IFINNEWqnSESGRVFPVYNP-ATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 97
Cdd:cd07083 21 LVIGGEW--VDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 98 VLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADKIHG---MTIPVDG-DYFTFTRhePIGVCGQIIPWNFPLLMFA 173
Cdd:cd07083 96 ELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYpavEVVPYPGeDNESFYV--GLGAGVVISPWNFPVAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 174 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 253
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 254 AGR-----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVV 328
Cdd:cd07083 253 AARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 329 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 408
Cdd:cd07083 333 GPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 409 TMD--EVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFG-LREYS 483
Cdd:cd07083 412 DDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNAKTGGPHyLRRFL 491
|
....*.
gi 332634711 484 EVKTVT 489
Cdd:cd07083 492 EMKAVA 497
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
22-490 |
2.01e-88 |
|
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: 278.71 E-value: 2.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 22 NNEWQnsESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLAT 101
Cdd:cd07130 4 DGEWG--GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK---EWRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 102 MESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPAL 180
Cdd:cd07130 79 LVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 181 CCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLI-QEAAG 255
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVgQAVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 256 RsnLKRVTLELGGKSPNIIFADADLDYAVeqahQGVFF----NQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSP 331
Cdd:cd07130 237 R--FGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 332 FDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSnVTDDMRIAKEEIFGPVQEILRFKTMD 411
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 412 EVIERANNSDFGLVAAVFTNDINKALTVSSAMQA--GTVWINC-YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 469
|
..
gi 332634711 489 TV 490
Cdd:cd07130 470 TI 471
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
35-495 |
1.02e-85 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 273.30 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 35 PVYNPATGEQV-CEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 113
Cdd:cd07125 49 PVIDPADHERTiGEVSLADAEDVDAALAIAAAAFA---GWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 114 AFyVDLQGVIKTFRYYAGWADK-IHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAE 192
Cdd:cd07125 126 AD-AEVREAIDFCRYYAAQARElFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 193 QTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAagRSNLKRVTL----ELGG 268
Cdd:cd07125 205 QTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRA--LAERDGPILpliaETGG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 269 KspNIIFAD--ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQ 346
Cdd:cd07125 283 K--NAMIVDstALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 347 YNKILELIQSGVAEgAKLECGGKGLGRKGFFIEPTVFSNVTDDMRiaKEEIFGPVQEILRFK--TMDEVIERANNSDFGL 424
Cdd:cd07125 361 GKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFKaeDLDEAIEDINATGYGL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 425 VAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----QsPFGGFKMSGNGREMGefG---LREYSEVKTVTVKIPQK 495
Cdd:cd07125 438 TLGIHSRDEREIEYWRERVEAGNLYIN-RNITGAivgrQ-PFGGWGLSGTGPKAG--GpnyLLRFGNEKTVSLNTTAA 511
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-488 |
1.53e-83 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 265.96 E-value: 1.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 38 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGrllDKLADLVE--RDRA-VLATMESLNGGKPFLQA 114
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRA---QKLRDIGKalRARSeEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 115 fyvdLQGVIKTFRYYAGWADKIHGMTIP----VDGDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:PRK13968 87 ----RAEVAKSANLCDWYAEHGPAMLKAeptlVENQQ-AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAGFPPGVInilpGYGPTAGAAIASHIGIDKIA---FTGSTEVGKLIQEAAGRSnLKRVTLELG 267
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVY----GWLNADNDGVSQMINDSRIAavtVTGSVRAGAAIGAQAGAA-LKKCVLELG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 268 GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQY 347
Cdd:PRK13968 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 348 NKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 427
Cdd:PRK13968 317 DELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332634711 428 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
36-471 |
2.58e-81 |
|
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: 260.04 E-value: 2.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWrrMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 115
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 YVDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 190
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 191 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHigidKIA---FTGSTEVGKLIqeaagRSNLK---RVTL 264
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDP----RVAffsFIGSARVGWML-----RSKLApgtRCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 265 ELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDK 344
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 345 KQYNKILELIQSGVAEGAKLECGGKGLGRKGFfiEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGL 424
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 332634711 425 VAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQ-SPFGGFKMSGNG 471
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
152-488 |
2.98e-79 |
|
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: 253.69 E-value: 2.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 152 RHEPIGVCGQIIPWNFPL-LMFAwKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGygptaGAAIA 230
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFnLAFG-PLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DAEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 231 SHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 307
Cdd:cd07134 170 QALlelPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 308 EESIYEEFVRRsVERAKRRVVGSpfDPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKLECGGKgLGRKGFFIEPTVF 383
Cdd:cd07134 249 HESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 384 SNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKALTVSSamqAGTVWIN--CYNALNA 458
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDkanVNKVLARTS---SGGVVVNdvVLHFLNP 401
|
330 340 350
....*....|....*....|....*....|
gi 332634711 459 QSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
55-472 |
1.60e-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: 249.11 E-value: 1.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 55 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY--------VDLQgvIKTF 126
Cdd:cd07095 1 QVDAAVAAARAAFP---GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 127 RYYAGwaDKIHGMtipvdGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIK 206
Cdd:cd07095 76 HERTG--ERATPM-----AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 207 EAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLI-QEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVE 285
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPG-KILALEMGGNNPLVVWDVADIDAAAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 286 QAHQGVFFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL 364
Cdd:cd07095 227 LIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 365 ECGGKGLGRKGFFIEPTVFsNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQ 444
Cdd:cd07095 307 LLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420 430
....*....|....*....|....*....|.
gi 332634711 445 AGTVWINcyNALNAQS---PFGGFKMSGNGR 472
Cdd:cd07095 386 AGIVNWN--RPTTGASstaPFGGVGLSGNHR 414
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
20-491 |
6.87e-76 |
|
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: 246.33 E-value: 6.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFL---TWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFYVDLQGvIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARG-LEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSN 258
Cdd:TIGR01722 160 AIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 lKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR-IFVEESiyEEFVRRSVERAKRRVVGSPFDPTTE 337
Cdd:TIGR01722 239 -KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAaVLVGAA--DEWVPEIRERAEKIRIGPGDDPGAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 338 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGF----FIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:TIGR01722 316 MGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSP---FGGFKMS--GNGREMGEFGLREYSEVKTV 488
Cdd:TIGR01722 396 IALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYTRGKTV 473
|
...
gi 332634711 489 TVK 491
Cdd:TIGR01722 474 TTR 476
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
20-472 |
1.05e-75 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 246.02 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQnSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP---AWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAFY--------VDLQgvIKTFRYYAGwaDKIHGMtipvdGDYFTFTRHEPIGVCGQIIPWNFPLLM 171
Cdd:PRK09457 80 AEVIARETGKPLWEAATevtaminkIAIS--IQAYHERTG--EKRSEM-----ADGAAVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 172 FAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLI- 250
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 251 QEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVVG 329
Cdd:PRK09457 230 RQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 330 SPF-DPTTEQGPQIDKKQYNKILELIQSGVAEGAK----LECGGKGLGrkgfFIEPTVFsNVTDDMRIAKEEIFGPVQEI 404
Cdd:PRK09457 309 RWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKslleMTQLQAGTG----LLTPGII-DVTGVAELPDEEYFGPLLQV 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332634711 405 LRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTV-WINCYNALNAQSPFGGFKMSGNGR 472
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
20-471 |
3.24e-75 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 245.05 E-value: 3.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAF-----------YVDLQGViktfrYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPWNF 167
Cdd:PLN00412 96 AECLVKEIAKPAKDAVtevvrsgdlisYTAEEGV-----RILGEGKFLVSDSFPGNErNKYCLTSKIPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 168 PLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGStEVG 247
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 248 KLIQEAAGRSNLKrvtLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRV 327
Cdd:PLN00412 250 IAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 328 VGSPFDpTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRF 407
Cdd:PLN00412 327 VGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 408 KTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNG 471
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIG 467
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
73-488 |
2.69e-72 |
|
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: 235.50 E-value: 2.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 73 WRRmdasergRLLDKLADLV-ERDRAVLATMES-LngGKPFLQAFYVDLQGVIKTFRYY----AGWADKIHGMTIPVDGD 146
Cdd:cd07087 21 WRK-------AQLKALKRMLtENEEEIAAALYAdL--GKPPAEAYLTEIAVVLGEIDHAlkhlKKWMKPRRVSVPLLLQP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 147 YFTFTRHEPIGVCGQIIPWNFPLLMfawKIAP---ALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGygp 223
Cdd:cd07087 92 AKAYVIPEPLGVVLIIGPWNYPLQL---ALAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 224 taGAAIASHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCT 300
Cdd:cd07087 165 --GVEVATALlaePFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 301 AGSRIFVEESIYEEFvrrsVERAKRRVV---GSPFDPTTEQGPQIDKKQYNKILELIQSGvaegaKLECGGkGLGRKGFF 377
Cdd:cd07087 242 APDYVLVHESIKDEL----IEELKKAIKefyGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-QVDKEERY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 378 IEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNA 455
Cdd:cd07087 312 IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHA 391
|
410 420 430
....*....|....*....|....*....|...
gi 332634711 456 LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07087 392 AIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
31-475 |
1.93e-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: 1.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 31 GRVFPVYNPAT-GEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGK 109
Cdd:TIGR01238 50 GEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFP---TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 110 PFLQAFyVDLQGVIKTFRYYAGWADkihgmtipvdgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIK 189
Cdd:TIGR01238 127 TIHNAI-AEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 190 PAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTL--ELG 267
Cdd:TIGR01238 195 PAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 268 GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQY 347
Cdd:TIGR01238 275 GQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 348 NKILELIQSGVAEG---AKLECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDF 422
Cdd:TIGR01238 355 QNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGY 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 423 GLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSGNGREMG 475
Cdd:TIGR01238 433 GLTMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
20-492 |
3.56e-70 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 241.64 E-value: 3.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQN----SESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVER 94
Cdd:PRK11904 546 FLEKQWQAgpiiNGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFP---AWSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 95 DRAVLATMESLNGGKPfLQ--------AfyVDlqgviktF-RYYAGWADKIHGMTIPVDGdyftFT------RHEPIGV- 158
Cdd:PRK11904 623 NRAELIALCVREAGKT-LQdaiaevreA--VD-------FcRYYAAQARRLFGAPEKLPG----PTgesnelRLHGRGVf 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 159 -CgqIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDK 237
Cdd:PRK11904 689 vC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAG 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 238 IAFTGSTEVGKLIQEA-AGRSNlKRVTL--ELGGKspNIIFADAD------LDYAVEQAhqgvFFNQGQCCTAGSRIFVE 308
Cdd:PRK11904 767 VAFTGSTETARIINRTlAARDG-PIVPLiaETGGQ--NAMIVDSTalpeqvVDDVVTSA----FRSAGQRCSALRVLFVQ 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 309 ESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEG---AKLECGgkGLGRKGFFIEPTVFSn 385
Cdd:PRK11904 840 EDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP--AGTENGHFVAPTAFE- 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 386 vTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----Q 459
Cdd:PRK11904 917 -IDSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ 994
|
490 500 510
....*....|....*....|....*....|....*.
gi 332634711 460 sPFGGFKMSGNGREMGefG---LREYSEVKTVTVKI 492
Cdd:PRK11904 995 -PFGGQGLSGTGPKAG--GphyLLRFATEKTVTVNT 1027
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
27-471 |
7.51e-70 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 241.77 E-value: 7.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 27 NSESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESL 105
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFP---AWSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 106 NGGKPFL-------QAfyVDlqgviktF-RYYAGWADKIHGMTipvdgdyftfTRHEPIGVCGQIIPWNFPLLMFAWKIA 177
Cdd:COG4230 642 EAGKTLPdaiaevrEA--VD-------FcRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAIFTGQVA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 178 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA-AGR 256
Cdd:COG4230 703 AALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTlAAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 257 SNlKRVTL--ELGGKspNIIFADADldyA-VEQAHQGV----FFNQGQCCTAgSRI-FVEESIYEEFVRRSVERAKRRVV 328
Cdd:COG4230 783 DG-PIVPLiaETGGQ--NAMIVDSS---AlPEQVVDDVlasaFDSAGQRCSA-LRVlCVQEDIADRVLEMLKGAMAELRV 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 329 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRF 407
Cdd:COG4230 856 GDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVRY 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332634711 408 K--TMDEVIERANNSDFGLVAAVFT-NDiNKALTVSSAMQAGTVWINcYNALNA----QsPFGGFKMSGNG 471
Cdd:COG4230 934 KadELDKVIDAINATGYGLTLGVHSrID-ETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
77-488 |
8.32e-67 |
|
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: 221.20 E-value: 8.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 77 DASERGRLLDKLADLVERDRAVLAtmESLN---GGKPFLQAFYVDLQGVIKTFRYY----AGW--ADKIHGMtipvdgdy 147
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALA--EAISadfGHRSRHETLLAEILPSIAGIKHArkhlKKWmkPSRRHVG-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 148 FTFT------RHEPIGVCGQIIPWNFPL-LMFAWKIApALCCGNTVVIKPAEQTP-LSALyMGALIKEAgFPPGVINILP 219
Cdd:cd07133 88 LLFLpakaevEYQPLGVVGIIVPWNYPLyLALGPLIA-ALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 220 GyGPTAGAAIaSHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 299
Cdd:cd07133 165 G-GADVAAAF-SSLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 300 TAGSRIFVEESIYEEFVRRSVERAKRRVvgspfdPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKL-ECGGKG---- 370
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKMY------PTLADNPDytsiINERHYARLQGLLEDARAKGARViELNPAGedfa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 371 LGRKgffIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKAL--TVSsamqa 445
Cdd:cd07133 316 ATRK---LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDkaeQDRVLrrTHS----- 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 332634711 446 GTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07133 388 GGVTINdtLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
20-489 |
2.74e-66 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 224.63 E-value: 2.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:PLN02419 194 AMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGaAIASHIGIDKIAFTGSTEVGKLIQEAAGRSN 258
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 259 lKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR-IFVEESiyEEFVRRSVERAKRRVVGSPFDPTTE 337
Cdd:PLN02419 352 -KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERAKALKVTCGSEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 338 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 413
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 414 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSPFGGF-----KMSGNGREMGEFGLREYSEVKTV 488
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgnkaSFAGDLNFYGKAGVDFFTQIKLV 586
|
.
gi 332634711 489 T 489
Cdd:PLN02419 587 T 587
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
54-488 |
4.18e-66 |
|
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: 219.40 E-value: 4.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 54 ADIDKAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAG-- 131
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKnl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 132 --WA--DKIHGMTIPvdgdYF---TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGAL 204
Cdd:cd07135 82 kkWAkdEKVKDGPLA----FMfgkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 205 IKEAgFPPGVINILPGYGPTAGAAIASHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAV 284
Cdd:cd07135 158 VPKY-LDPDAFQVVQGGVPETTALLEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 285 EQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSvERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKL 364
Cdd:cd07135 234 KRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 365 ECGGKgLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQ 444
Cdd:cd07135 310 VIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTR 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 332634711 445 AGTVWIN-------CYNAlnaqsPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07135 389 SGGVVINdtlihvgVDNA-----PFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
154-488 |
5.82e-65 |
|
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: 216.99 E-value: 5.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 154 EPIGVCGQIIPWNFPLLMfawKIAP---ALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIA 230
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 231 SHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 310
Cdd:cd07136 175 QKF--DYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 311 IYEEFVRRSVERAKRRVVGSPFDptTEQGPQI-DKKQYNKILELIQSGvaegaKLECGGKGlGRKGFFIEPTVFSNVTDD 389
Cdd:cd07136 252 VKEKFIKELKEEIKKFYGEDPLE--SPDYGRIiNEKHFDRLAGLLDNG-----KIVFGGNT-DRETLYIEPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 390 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcyNAL----NAQSPFGGF 465
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTImhlaNPYLPFGGV 401
|
330 340
....*....|....*....|...
gi 332634711 466 KMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07136 402 GNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
36-469 |
8.96e-65 |
|
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: 218.22 E-value: 8.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 36 VYNPATGEQVC---------EVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVE---RDRAVLATMe 103
Cdd:cd07123 42 VRTGNTGKQVMphdhahvlaTYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAATM- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 104 sLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTiPVDGDYFTFTR--HEPI-GVCGQIIPWNFPLLMFAWKIAPAL 180
Cdd:cd07123 118 -LGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRleYRPLeGFVYAVSPFNFTAIGGNLAGAPAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 181 CcGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRS--- 257
Cdd:cd07123 196 M-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 258 --NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 335
Cdd:cd07123 275 yrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 336 TEQGPQIDKKQYNKILELIQSGVAE-GAKLECGGKGLGRKGFFIEPTVFsnVTDD--MRIAKEEIFGPVQEILRFKTMD- 411
Cdd:cd07123 355 NFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI--ETTDpkHKLMTEEIFGPVLTVYVYPDSDf 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 412 -EVIERANN-SDFGLVAAVFTND---INKALTVSSaMQAGTVWIN--CYNALNAQSPFGGFKMSG 469
Cdd:cd07123 433 eETLELVDTtSPYALTGAIFAQDrkaIREATDALR-NAAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
28-471 |
5.61e-64 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 225.13 E-value: 5.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 28 SESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLN 106
Cdd:PRK11905 563 DVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP---EWSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 107 GGKPFLQAF-----YVDlqgviktF-RYYAGWADkihgmtipvdgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPAL 180
Cdd:PRK11905 640 AGKTLANAIaevreAVD-------FlRYYAAQAR-----------RLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAAL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 181 CCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA-AGRSNl 259
Cdd:PRK11905 702 VAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTlAKRSG- 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 260 KRVTL--ELGGKSPNIIFADAdldyAVEQAHQGV----FFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 333
Cdd:PRK11905 781 PPVPLiaETGGQNAMIVDSSA----LPEQVVADViasaFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWR 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 334 PTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRFKT--M 410
Cdd:PRK11905 857 LSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKAdeL 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 411 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----QsPFGGFKMSGNG 471
Cdd:PRK11905 935 DRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
20-490 |
2.10e-56 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 195.82 E-value: 2.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQnsESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAArlaFSLGSVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRAC---EEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKpFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 178
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 179 ALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 254
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 255 gRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 334
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 335 TTEQGP---QIDKKQYNKILELIQSgvaEGAKLECGGKGLGRKGFFIEPTVFSnVTDDMRIAKEEIFGPVQEILRFKTMD 411
Cdd:PLN02315 336 GTLLGPlhtPESKKNFEKGIEIIKS---QGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 412 EVIERANNSDFGLVAAVFTND---INKALTVSSAmQAGTVWINC-YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKT 487
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNpetIFKWIGPLGS-DCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
|
...
gi 332634711 488 VTV 490
Cdd:PLN02315 491 CTI 493
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
28-471 |
3.31e-56 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 202.51 E-value: 3.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 28 SESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVErdravlATMESLN 106
Cdd:PRK11809 655 VAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLME------AQMQTLM 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 107 G------GKPFLQAF-----YVDLqgviktFRYYAGWADkihgmtipvdgDYFTFTRHEPIG--VCgqIIPWNFPLLMFA 173
Cdd:PRK11809 726 GllvreaGKTFSNAIaevreAVDF------LRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFT 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 174 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 253
Cdd:PRK11809 787 GQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRN 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 254 -AGR-SNLKRVT---LELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEefvrRSVERAK---- 324
Cdd:PRK11809 867 lAGRlDPQGRPIpliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVAD----RTLKMLRgama 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 325 RRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAK---LECGGKGLGRKGFFIEPTVFS-NVTDDMriaKEEIFGP 400
Cdd:PRK11809 943 ECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLIElDSFDEL---KREVFGP 1019
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332634711 401 VQEILRFK--TMDEVIERANNSDFGLVAAVFTN-DINKALTVSSAmQAGTVWINcYNALNA----QsPFGGFKMSGNG 471
Cdd:PRK11809 1020 VLHVVRYNrnQLDELIEQINASGYGLTLGVHTRiDETIAQVTGSA-HVGNLYVN-RNMVGAvvgvQ-PFGGEGLSGTG 1094
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
149-491 |
2.52e-55 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 192.55 E-value: 2.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 149 TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGyGPTAGAA 228
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 229 IASHiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVE 308
Cdd:PTZ00381 181 LLKE-PFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 309 ESIYEEFVrRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKLECGGKgLGRKGFFIEPTVFSNVTD 388
Cdd:PTZ00381 259 RSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVNPDL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 389 DMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFK 466
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGVG 413
|
330 340
....*....|....*....|....*
gi 332634711 467 MSGNGREMGEFGLREYSEVKTVTVK 491
Cdd:PTZ00381 414 NSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
58-491 |
1.50e-46 |
|
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: 167.78 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 58 KAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVE--RDRAVLATMESLNggKPFLQAFYVDLQGVIKTFRY----YAG 131
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEenEDEIVEALAKDLR--KPKFEAVLSEILLVKNEIKYaisnLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 132 WADkihgmTIPVDGDYFT-----FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI- 205
Cdd:cd07132 77 WMK-----PEPVKKNLATllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 206 ----KEAgFPpgVInilpgygpTAGAAIASHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADA 278
Cdd:cd07132 152 kyldKEC-YP--VV--------LGGVEETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 279 DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFvrrsVERAKRRVV---GSpfDPTTEQ--GPQIDKKQYNKILEL 353
Cdd:cd07132 220 DIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKF----VEALKKTLKefyGE--DPKESPdyGRIINDRHFQRLKKL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 354 IQSG-VA---EGAKLECggkglgrkgfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 429
Cdd:cd07132 294 LSGGkVAiggQTDEKER----------YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVF 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 430 TND---INKALTVSSamqAGTVwinCYNALNAQS-----PFGGFKMSGNGREMGEFGLREYSEVKTVTVK 491
Cdd:cd07132 364 SNNkkvINKILSNTS---SGGV---CVNDTIMHYtldslPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
60-488 |
5.09e-41 |
|
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: 152.57 E-value: 5.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 60 VQAARLAFSLGsvwRRMDASERGRLLDKLADLV-ERDRAVLATMESlNGGKPFLQAFYVDLQGVIKT----FRYYAGWAD 134
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSScklaIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 135 ----KIHGMTIPVDGDYFTftrhEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgF 210
Cdd:cd07137 81 pekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 211 PPGVINILPGyGPTAGAAIASHiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQG 290
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 291 VF-FNQGQCCTAGSRIFVEESIYEEFVRrsverAKRRVVGSPF--DP-TTEQGPQIDKKQYNKILELIQSGVAEGAKLEC 366
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLID-----ALKNTLEKFFgeNPkESKDLSRIVNSHHFQRLSRLLDDPSVADKIVH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 367 GGkGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNdiNKALT--VSSAMQ 444
Cdd:cd07137 308 GG-ERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK--NKELKrrIVAETS 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 332634711 445 AGTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 488
Cdd:cd07137 385 SGGVTFNdtVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
20-480 |
6.05e-38 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 145.62 E-value: 6.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQnSESGRVFPVYNPATGEQVCEVqEADKADIDKAVQAARLafSLGSVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:PRK11903 8 YVAGRWQ-AGSGAGTPLFDPVTGEELVRV-SATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI----------GVCGQIIPWNFPl 169
Cdd:PRK11903 84 YDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFNFP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 170 lmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGVINILPGygptAGAAIASHIG-IDKIAFTGS 243
Cdd:PRK11903 162 ---AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHLQpFDVVSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 244 TEVGKLIQE--AAGRSNLkRVTLELGGKSPNIIFADAD-----LDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 316
Cdd:PRK11903 235 AETAAVLRShpAVVQRSV-RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 317 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQsGVAEGAKLECGGKGLG------RKGFFIEPTVF-SNVTDD 389
Cdd:PRK11903 314 EALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgASDPDA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 390 MRIAKE-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI--------------NKALTVSSAMQA-----GTVW 449
Cdd:PRK11903 393 ATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshGRVHVISPDVAAlhtghGNVM 472
|
490 500 510
....*....|....*....|....*....|.
gi 332634711 450 incynalnAQSPFGGFKMSGNGREMGefGLR 480
Cdd:PRK11903 473 --------PQSLHGGPGRAGGGEELG--GLR 493
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
61-471 |
1.30e-36 |
|
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: 140.45 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 61 QAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyvDLQGVIKTFRYYA--GWADKIHG 138
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE--NICGDQVQLRARAfvIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 139 MTIPVDGDYFTFTRHE---PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGV 214
Cdd:cd07084 81 EPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 215 INILPGYGPTaGAAIASHIGIDKIAFTGSTEVGkliqeAAGRSNLK--RVTLELGGKSPNIIFADAD-LDYAVEQAHQGV 291
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQaVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 292 FFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVVGspfdpTTEQGPQidkkQYNKILELIQSGVAE-GAKLECGGK 369
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGPV----QTFTTLAMIAHMENLlGSVLLFSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 370 GLGRK------GFFIEPTVFSNVTDDMRIAK---EEIFGPVQEILRFK-----TMDEVIERANNSdfgLVAAVFTNDInk 435
Cdd:cd07084 306 ELKNHsipsiyGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSNDP-- 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 332634711 436 alTVSSAMqAGTVWINCYNALNAQSPFGGFKMSGNG 471
Cdd:cd07084 381 --IFLQEL-IGNLWVAGRTYAILRGRTGVAPNQNHG 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
20-480 |
7.67e-35 |
|
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: 136.63 E-value: 7.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQnSESGRVFPVYNPATGEQVCEVQeADKADIDKAVQAARLAFslGSVWRRMDASERGRLLDKLADLVERDRAVL 99
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREKG--GPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 100 ATMESLNGGKpfLQAFYVDLQGVIKTFRYYAGWADK--------IHGMTIPVDGDYFTFTRH--EPI-GVCGQIIPWNFP 168
Cdd:cd07128 80 YALSAATGAT--RRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDGTFVGQHilTPRrGVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 169 llmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGVINILPGygptAGAAIASHIGI-DKIAFTG 242
Cdd:cd07128 158 ----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGDLLDHLGEqDVVAFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 243 STEVG-KL-----IQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 316
Cdd:cd07128 230 SAATAaKLrahpnIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 317 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN----KILELIQSG-VAEGAKLECGGKGLGR-KGFFIEPTVF-SNVTDD 389
Cdd:cd07128 310 EALKARLAKVVVGDPRLEGVRMGPLVSREQREdvraAVATLLAEAeVVFGGPDRFEVVGADAeKGAFFPPTLLlCDDPDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 390 MRIAKE-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQA--GTVWINcyNALNAQ------S 460
Cdd:cd07128 390 ATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVL--NRDSAKestghgS 467
|
490 500
....*....|....*....|....*
gi 332634711 461 PF-----GGFKMSGNGREMGefGLR 480
Cdd:cd07128 468 PLpqlvhGGPGRAGGGEELG--GLR 490
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
154-489 |
5.78e-30 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 122.14 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 154 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKeAGFPPGVINILPGyGPTAGAAIASHi 233
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 234 GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNI---IFADADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEE 309
Cdd:PLN02203 184 KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 310 siyeEFVRRSVERAK---RRVVGSPFDPTTEQGPQIDKKQYNKILEL-----IQSGVAEGAKLEcggkglgRKGFFIEPT 381
Cdd:PLN02203 263 ----RFAPILIELLKstiKKFFGENPRESKSMARILNKKHFQRLSNLlkdprVAASIVHGGSID-------EKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 382 VFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNA 458
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaiIQYACDS 411
|
330 340 350
....*....|....*....|....*....|.
gi 332634711 459 qSPFGGFKMSGNGREMGEFGLREYSEVKTVT 489
Cdd:PLN02203 412 -LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
154-488 |
1.55e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 118.22 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 154 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIkEAGFPPGVINILPGYGPTAGAAIASHi 233
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQK- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 234 gIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF-FNQGQCCTAGSRIFVEESiY 312
Cdd:PLN02174 189 -WDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKE-Y 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 313 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELI-QSGVAEgaKLECGGKGlGRKGFFIEPTVFSNVTDDMR 391
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLdEKEVSD--KIVYGGEK-DRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 392 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNAQsPFGGFKMS 468
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALHTL-PFGGVGES 421
|
330 340
....*....|....*....|
gi 332634711 469 GNGREMGEFGLREYSEVKTV 488
Cdd:PLN02174 422 GMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
56-418 |
8.14e-17 |
|
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: 82.59 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 56 IDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPflQAfyvDLQGVI-KT---FRYYA- 130
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP--EA---RLQGELgRTtgqLRLFAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 131 -----GWadkiHGMTI-PVDGDYFTFTR------HEPIGVCGQIIPWNFPllmFAWKI-----APALCCGNTVVIK---- 189
Cdd:cd07129 73 lvregSW----LDARIdPADPDRQPLPRpdlrrmLVPLGPVAVFGASNFP---LAFSVaggdtASALAAGCPVVVKahpa 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 190 -PAeqtpLSALYMGAL---IKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGK-LIQEAAGRSNLKRVTL 264
Cdd:cd07129 146 hPG----TSELVARAIraaLRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 265 ELGGKSPNIIFADAdLDYAVEQAHQG----VFFNQGQCCTAGSRIFVEESiyEEFvRRSVERAKRRVVGSPFDPTTEQGp 340
Cdd:cd07129 222 ELGSVNPVFILPGA-LAERGEAIAQGfvgsLTLGAGQFCTNPGLVLVPAG--PAG-DAFIAALAEALAAAPAQTMLTPG- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 341 qidkkqynkILELIQSGVAE----GAKLECGGKGLGRKGFFIEPTVFSNVTDDMR---IAKEEIFGPVQEILRFKTMDEV 413
Cdd:cd07129 297 ---------IAEAYRQGVEAlaaaPGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAEL 367
|
....*
gi 332634711 414 IERAN 418
Cdd:cd07129 368 LAVAE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
20-434 |
2.21e-16 |
|
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: 81.39 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 20 FINNEWQNSESGRVFPvyNPATGEQVCEVQEADKADIDKAVQAARlAFSLGSVWRRMDASER----GRLLDKLADLVERD 95
Cdd:cd07126 2 LVAGKWKGASNYTTLL--DPLNGDKFISVPDTDEDEINEFVDSLR-QCPKSGLHNPLKNPERyllyGDVSHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 96 RA--VLATMESLNGGKPFLQAfyvdLQGVIKTFRYYAGWA-DKIHGMT--IPVDGDYFTFTRHE---PIGVCGQIIPWNF 167
Cdd:cd07126 79 EVedFFARLIQRVAPKSDAQA----LGEVVVTRKFLENFAgDQVRFLArsFNVPGDHQGQQSSGyrwPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 168 PLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGaAIASHIGIDKIAFTGSTEVG 247
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 248 -KLIQEAAGrsnlkRVTLELGGKSPNIIFAD-ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES-IYEEFVRRSVERAK 324
Cdd:cd07126 234 eRLALELHG-----KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 325 RR-----VVGSPFDPTTEqgpqidkkqynKILELIQSGVA-EGAKLECGGKGLGRKGF-----FIEPT-VF-----SNVT 387
Cdd:cd07126 309 QRkledlTIGPVLTWTTE-----------RILDHVDKLLAiPGAKVLFGGKPLTNHSIpsiygAYEPTaVFvpleeIAIE 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 332634711 388 DDMRIAKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTNDIN 434
Cdd:cd07126 378 ENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSNDIR 426
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
57-451 |
1.68e-12 |
|
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: 69.17 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 57 DKAVQAARLA-FSLGSVWRRMDASERGRLLDKLAdlverdrAVLATMESLNGGKpflqafyvdLQGVIKTFRYYAGWADK 135
Cdd:cd07077 19 DLIINAIANAlYDTRQRLASEAVSERGAYIRSLI-------ANWIAMMGCSESK---------LYKNIDTERGITASVGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 136 IHGMTIPVDGDyfTFTRHEPIGVCGQIIPWNFPLLMFAwKIAPALCCGNTVVIKPAEQTPLSALYMgALIKEAGFPPGVI 215
Cdd:cd07077 83 IQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL-ALLFQAADAAHGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 216 NILPGYGPTAGAAIA----SHIGIDKIAFTGSTEVGKLIQEAagrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGV 291
Cdd:cd07077 159 KILVLYVPHPSDELAeellSHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 292 FFNQGQCctagsriFVEESIYeefvrrsverakrrVVGSPFDPTTEQgpqidkkqynkileLIQSGVAEGAKLECGGKGL 371
Cdd:cd07077 236 FFDQNAC-------ASEQNLY--------------VVDDVLDPLYEE--------------FKLKLVVEGLKVPQETKPL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 372 grkgffieptvFSNVTDDMRIAKEEIFGPVQeiLRFKTMDEVIERANNSDF------GLVAAVFTNDINKALTVSSAMQA 445
Cdd:cd07077 281 -----------SKETTPSFDDEALESMTPLE--CQFRVLDVISAVENAWMIiesgggPHTRCVYTHKINKVDDFVQYIDT 347
|
....*.
gi 332634711 446 GTVWIN 451
Cdd:cd07077 348 ASFYPN 353
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
144-451 |
1.68e-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: 56.51 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 144 DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP----AEQTPLSALYMGALIKEAGFPPGVINILP 219
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 220 GYGPTAGAAIASHIGIDKIAFTGSTEVGKliqeaAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 299
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 300 TAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE-------QGPQIDKKQYNKILELIQSGVAEGAKLecggkglg 372
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPvilkngdVNRDIVGQDAYKIAAAAGLKVPQETRI-------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 373 rkgFFIEPTVFsnvtDDMRIAKEEIFGPVQEILRFKTMDEVIERA----NNSDFGLVAAVFTNDINKALTV---SSAMQA 445
Cdd:cd07081 311 ---LIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENMnqfANAMKT 383
|
....*.
gi 332634711 446 GTVWIN 451
Cdd:cd07081 384 SRFVKN 389
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
154-452 |
8.01e-07 |
|
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: 51.34 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 154 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP---AEQTPLSAL-YMGALIKEAGFPPGVINILPGygPT--AGA 227
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAkIMREAAVAAGAPEGLIQWIEE--PSieLTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 228 AIASHIGIDKIAFTGSTEVGKliqeAAGRSNlkrvTLELG---GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR 304
Cdd:cd07122 172 ELMKHPDVDLILATGGPGMVK----AAYSSG----KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 305 IFVEESIYEEFVRRSVER--------AKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL---ECGGKGLGr 373
Cdd:cd07122 244 VIVDDEIYDEVRAELKRRgayflneeEKEKLEKALFDDGGTLNPDIVGKSAQKIAELAGIEVPEDTKVlvaEETGVGPE- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 374 kgffiEPtvFSNvtddmriakeEIFGPVQEILRFKTMDEVIERA----NNSDFGLVAAVFTNDINKALTVSSAMQAGTVW 449
Cdd:cd07122 323 -----EP--LSR----------EKLSPVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPVSRIL 385
|
...
gi 332634711 450 INC 452
Cdd:cd07122 386 VNT 388
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
54-417 |
5.86e-06 |
|
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: 48.77 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 54 ADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGViktfryyagwA 133
Cdd:cd07121 4 ATVDDAVAAAKAAQK---QYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLA----------A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 134 DKIHGM----TIPVDGDY-FTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP---AEQTPLSALYM-GAL 204
Cdd:cd07121 71 EKTPGTedltTTAWSGDNgLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELiNKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 205 IKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKliqeaAGRSNLKRVTLELGGKSPNIIFADADLDYAV 284
Cdd:cd07121 151 IAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVK-----AALSSGKKAIGAGAGNPPVVVDETADIEKAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 285 EQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRR------------SVERAKRRVVgspfdpTTEQGPQIDK----KQYN 348
Cdd:cd07121 226 RDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAmqrngayvlndeQAEQLLEVVL------LTNKGATPNKkwvgKDAS 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332634711 349 KILELIqsGVAEGAKLECggkglgrkgffieptVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERA 417
Cdd:cd07121 300 KILKAA--GIEVPADIRL---------------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
52-307 |
4.45e-05 |
|
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: 45.93 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 52 DKADIDKAVQAARLAFSlgsVWRrmDASERGR------LLDKLADLV-ERDRAVLATmeslnGGKPFLQAF--------- 115
Cdd:cd07127 82 PQCDPDALLAAARAAMP---GWR--DAGARARagvcleILQRLNARSfEMAHAVMHT-----TGQAFMMAFqaggphaqd 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 116 ---------YVDLQGVIKTFRYyagwaDKIHGMTIPVDGDYfTFTRhEPIGV-----CGQIIPWNFPLLMFAwkiapALC 181
Cdd:cd07127 152 rgleavayaWREMSRIPPTAEW-----EKPQGKHDPLAMEK-TFTV-VPRGValvigCSTFPTWNGYPGLFA-----SLA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332634711 182 CGNTVVIKPAeqtPLSALYMG-------ALIKEAGFPPGVInILPGYGPTAGAA--IASHIGIDKIAFTGSTEVGKLIQE 252
Cdd:cd07127 220 TGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFDPNLV-TLAADTPEEPIAqtLATRPEVRIIDFTGSNAFGDWLEA 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 332634711 253 AAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 307
Cdd:cd07127 296 NARQ---AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYV 347
|
|
| |
