|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-498 |
0e+00 |
|
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: 649.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 22 GLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARvWSGLRPADRERILLKLADLIERDAET 101
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSA-WAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 102 LAQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIA 181
Cdd:cd07113 80 LAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 182 VWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTA 261
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 262 AVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDP 341
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 342 SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTpADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADA 421
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE-ALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 422 VRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
18-500 |
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: 647.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 18 ARDFGLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIER 97
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA--WAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 98 DAETLAQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTLDVSIPfppgtRYTAYTRKEPVGVVAAIVPWNFP 177
Cdd:COG1012 81 RREELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDAP-----GTRAYVRREPLGVVGAITPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 178 LMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGK 256
Cdd:COG1012 155 LALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 257 LVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLG 336
Cdd:COG1012 235 RIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 337 AGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFD 416
Cdd:COG1012 315 DPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 417 DAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIP-LDPSMPFGGYKQSGIGREFGQYAIEGFTETKS 495
Cdd:COG1012 395 DEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
....*
gi 981295204 496 VCIAH 500
Cdd:COG1012 475 VTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
37-496 |
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: 599.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 37 RLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHV 116
Cdd:pfam00171 8 TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 117 SRAiEVGASVEYARYMAGWATKITGQTldvsIPFPPGtrYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIV 196
Cdd:pfam00171 86 ARG-EVDRAIDVLRYYAGLARRLDGET----LPSDPG--RLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 197 LKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGG 275
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 276 KNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRD 355
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 356 KVVQHIERARRDGLTFLAGGtPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAAS 435
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGG-EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981295204 436 IWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSM-PFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-496 |
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: 586.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 22 GLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAET 101
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 102 LAQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTldvsipFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIA 181
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKT------IPIDGNFLAYTRREPIGVCGQIIPWNFPLLML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 182 VWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGT 260
Cdd:cd07091 159 AWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQ-NMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGL 339
Cdd:cd07091 239 AAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 340 DPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGS-KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
40-498 |
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: 556.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 IEVGASVEYARYMAGWATKITGQTldvsipFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGES------YPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07093 153 SEWTPLTAWLLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVV 358
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRDGLTFLAGGTPADDLP---GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAAS 435
Cdd:cd07093 313 GYVELARAEGATILTGGGRPELPDlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981295204 436 IWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
40-498 |
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: 552.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 iEVGASVEYARYMAGWATKITGQTLDVSIPfppgtRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAVIPVDKG-----DYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVV 358
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRDGLTFLAGGTPADDLP---GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAAS 435
Cdd:cd07114 315 RYVARAREEGARVLTGGERPSGADlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981295204 436 IWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
38-498 |
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: 546.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVS 117
Cdd:cd07112 4 FATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RAIEVGASVEYARYMAGWATKITGQTLdvsipfPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVL 197
Cdd:cd07112 84 LAVDVPSAANTFRWYAEAIDKVYGEVA------PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 198 KPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGK-LVGTAAVQNMTRFSLELGG 275
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRrFLEYSGQSNLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 276 KNPIVMLDDV-DVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHR 354
Cdd:cd07112 238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 355 DKVVQHIERARRDGLTFLAGGTPAD-DLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLA 433
Cdd:cd07112 318 DKVLGYIESGKAEGARLVAGGKRVLtETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981295204 434 ASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07112 398 ASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-498 |
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: 546.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 61 EQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKIT 140
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 141 GQTLdvsIPFPPGTRytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVP 220
Cdd:cd07078 78 GEVI---PSPDPGEL--AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 221 PGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAF 299
Cdd:cd07078 153 PGVLNVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 300 FNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAD 379
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 380 DLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN 459
Cdd:cd07078 313 GGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 981295204 460 CHIP-LDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07078 393 DYSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
23-500 |
0e+00 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 542.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAvARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETL 102
Cdd:PRK13473 5 LLINGELVAGEG-EKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQtldVSIPFPPGtrYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:PRK13473 82 ARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGK---AAGEYLEG--HTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAgVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTA 261
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 262 AVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDP 341
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 342 SAQINPLVSAHHRDKVVQHIERARRDG-LTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAAD 420
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG-KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 421 AVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCIAH 500
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKH 474
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-496 |
0e+00 |
|
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: 532.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 iEVGASVEYARYMAGwatkitgQTLDVSIPFPPGTRYTAYTRKePVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07106 79 -EVGGAVAWLRYTAS-------LDLPDEVIEDDDTRRVELRRK-PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAgVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPI 279
Cdd:cd07106 150 SPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 280 VMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQ 359
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 360 HIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSN 439
Cdd:cd07106 309 LVEDAKAKGAKVLAGGEPLDG-PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 440 DLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07106 388 DLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
42-499 |
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: 531.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 42 DPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAIE 121
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 122 VGASVEYARYMAGWATKITGQTLDVSIPFppgtryTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSP 201
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPF------LNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 202 ETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIV 280
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 281 MLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQH 360
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 361 IERARRDGLTFLAGGTpADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSND 440
Cdd:cd07115 315 VDVGREEGARLLTGGK-RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 441 LKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCIA 499
Cdd:cd07115 394 LGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-498 |
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: 526.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIHVSRaIEVGASVEYARYMAGWATKITGQTLDVsipfPPGTRytAYTRKEPVGVVAAIVPWNFPLMIAVW 183
Cdd:cd07119 81 RLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDV----PPHVI--SRTVREPVGVCGLITPWNYPLLQAAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 184 KLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAA 262
Cdd:cd07119 154 KLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 263 VQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPS 342
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 343 AQINPLVSAHHRDKVVQHIERARRDGLTFLAGGT-PADDL--PGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKrPTGDElaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07119 394 EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
22-498 |
1.38e-180 |
|
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: 515.03 E-value: 1.38e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 22 GLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArVWSGLRPADRERILLKLADLIERDAET 101
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 102 LAQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTldvsipFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIA 181
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKT------IPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 182 VWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGT 260
Cdd:cd07144 162 AWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGL-ADVAQSMKLGAGL 339
Cdd:cd07144 242 AAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFvEHVKQNYKVGSPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 340 DPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLP--GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDD 417
Cdd:cd07144 322 DDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 418 AADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVC 497
Cdd:cd07144 402 YEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVH 481
|
.
gi 981295204 498 I 498
Cdd:cd07144 482 I 482
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-496 |
5.97e-180 |
|
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: 512.89 E-value: 5.97e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTldvsiPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEE-----RRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAA 262
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 263 VQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPS 342
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 343 AQINPLVSAHHRDKVVQHIERARRDGLTFLAGG-TPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADA 421
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGgRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981295204 422 VRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNcHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-496 |
1.40e-177 |
|
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: 506.09 E-value: 1.40e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 IEVGASVEYARYMAGWATKITGQtldVSIPFPPGtrYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGP---AAGEYLPG--HTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDaGVPPGVFNVVTGGR-VCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07092 154 SETTPLTTLLLAELAAE-VLPPGVVNVVCGGGaSAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVV 358
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRdGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWS 438
Cdd:cd07092 313 GFVERAPA-HARVLTGGRRAEG-PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 981295204 439 NDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-498 |
6.50e-176 |
|
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: 501.96 E-value: 6.50e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 iEVGASVEYARYMAGWATKITGQTLDVSIPfppGTRYTayTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07103 79 -EVDYAASFLEWFAEEARRIYGRTIPSPAP---GKRIL--VIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07103 153 AEETPLSALALAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVV 358
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRDGLTFLAGGTpADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWS 438
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGK-RLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 439 NDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07103 392 RDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
23-496 |
5.84e-175 |
|
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: 500.11 E-value: 5.84e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAgwatkitgQTLDvSIPFPPgTRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAA--------DALK-DFEFEE-RRGNSLVVREPIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTA 261
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 262 AVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDP 341
Cdd:cd07138 229 AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 342 SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGT--PADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgrPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNcHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
23-498 |
2.80e-168 |
|
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: 483.77 E-value: 2.80e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFD-ARVWSGLRPADRERILLKLADLIERDAET 101
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlGSPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 102 LAQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLdvsipfPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIA 181
Cdd:cd07141 89 LASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTI------PMDGDFFTYTRHEPVGVCGQIIPWNFPLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 182 VWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLV-G 259
Cdd:cd07141 163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIqQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 260 TAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGL 339
Cdd:cd07141 243 AAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 340 DPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:cd07141 323 DPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGD-KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-496 |
6.81e-168 |
|
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: 482.13 E-value: 6.81e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSgLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 IEVGASVEYARYMAGWATKITGQTlDVSIPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEF-DLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTGG-RVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSdNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVV 358
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRDGLTFLAGGTPADDLP-GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIW 437
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGLDkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 438 SNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-498 |
1.04e-167 |
|
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: 482.41 E-value: 1.04e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 22 GLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAET 101
Cdd:cd07143 8 GLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 102 LAQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIpfppgtRYTAYTRKEPVGVVAAIVPWNFPLMIA 181
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDI------KKLTYTRHEPIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 182 VWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGT 260
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQ-NMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGL 339
Cdd:cd07143 242 AAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 340 DPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLpGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
41-498 |
1.59e-165 |
|
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: 475.67 E-value: 1.59e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 41 HDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAi 120
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 121 EVGASVEYARYMAGWATKITGQTLDVSipfppGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPS 200
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGDSYNNL-----GDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 201 PETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPI 279
Cdd:cd07118 156 EFTSGTTLMLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 280 VMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQ 359
Cdd:cd07118 236 IVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 360 HIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSN 439
Cdd:cd07118 316 YVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 440 DLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07118 396 DIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
40-498 |
3.53e-165 |
|
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: 474.87 E-value: 3.53e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQ--KEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 iEVGASVEYARYMAGWATKITGQTLDVsipfpPGTRYtAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07090 79 -DIDSSADCLEYYAGLAPTLSGEHVPL-----PGGSF-AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPI 279
Cdd:cd07090 152 SPFTPLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 280 VMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQ 359
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 360 HIERARRDGLTFLAGGTPADDLP----GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAAS 435
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVPEDglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981295204 436 IWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07090 392 VFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
23-496 |
6.67e-165 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 475.52 E-value: 6.67e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLI-ERDAEt 101
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 102 LAQLETLNQGKSIHVSRAIEV--GASVeyARYMAGWATKITGQtldvSIPFPPGTRYtaYTRKEPVGVVAAIVPWNFPLM 179
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIvtGADV--LEYYAGLAPALEGE----QIPLRGGSFV--YTRREPLGVCAGIGAWNYPIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 180 IAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVcGAALASHPSISKISFTGSTATGKLV 258
Cdd:PRK13252 158 IACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGdGRV-GAWLTEHPDIAKVSFTGGVPTGKKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 259 GTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAG 338
Cdd:PRK13252 237 MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 339 LDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGG---TPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPF 415
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGerlTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 416 DDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKS 495
Cdd:PRK13252 397 DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
.
gi 981295204 496 V 496
Cdd:PRK13252 477 V 477
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-498 |
8.95e-163 |
|
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: 468.64 E-value: 8.95e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDARvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 iEVGASVEYARYMAGWATKITGQTldvsIPFPPGtrYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07109 80 -DVEAAARYFEYYGGAADKLHGET----IPLGPG--YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07109 153 AEDAPLTALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDpSAQINPLVSAHHRDKVV 358
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRDGLTFLAGGTPADDLP--GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASI 436
Cdd:cd07109 312 GFVARARARGARIVAGGRIAEGAPagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981295204 437 WSNDLKRVMNLVPQIEAGTVWVNCHIPLDP-SMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
40-496 |
3.13e-162 |
|
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: 467.60 E-value: 3.13e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSrA 119
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 IEVGASVEYARYMAGWATKITgQTLDVSIPFPpGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLD-AKAERAVPLP-SEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07110 156 SELTSLTELELAEIAAEAGLPPGVLNVVTGtGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVV 358
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRDGLTFLAGGTPADDLP-GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIW 437
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAHLEkGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 438 SNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
23-496 |
3.29e-157 |
|
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: 455.42 E-value: 3.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIPfppgtrYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:cd07142 86 AALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGP------HHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLV-GT 260
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIImQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLD 340
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 341 PSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAAD 420
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGS-KGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981295204 421 AVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
21-498 |
5.44e-156 |
|
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: 452.57 E-value: 5.44e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 21 FGLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAE 100
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 101 TLAQLETLNQGKSIHVSRAIEVGASVEYARYMA-------GWATKITGQTLdvsipfppgtrytAYTRKEPVGVVAAIVP 173
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAgviraqeGSLSEIDEDTL-------------SYHFHEPLGVVGQIIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 174 WNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAgVPPGVFNVVTG-GRVCGAALASHPSISKISFTGST 252
Cdd:cd07559 146 WNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 253 ATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQ-----ALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLA 327
Cdd:cd07559 225 TVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDADddfddKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 328 DVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGG---TPADDLPGYFVKPAVIADPRPDSAIVRDE 404
Cdd:cd07559 305 ERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGerlTLGGLDKGYFYEPTLIKGGNNDMRIFQEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 405 VFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQ 484
Cdd:cd07559 385 IFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHK 464
|
490
....*....|....
gi 981295204 485 YAIEGFTETKSVCI 498
Cdd:cd07559 465 MMLDHYQQTKNILV 478
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
24-494 |
4.29e-152 |
|
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: 441.94 E-value: 4.29e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIPfppgtrYTAYTRKEPVGVVAAIVPWNFPLMIAVW 183
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGP------SFAYTIREPLGVCVGIGAWNYPLQIASW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 184 KLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAA 262
Cdd:TIGR01804 153 KIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGdGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 263 VQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPS 342
Cdd:TIGR01804 233 AGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 343 AQINPLVSAHHRDKVVQHIERARRDGLTFLAGG-TPADDLP--GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:TIGR01804 313 TEMGPLISAAHRDKVLSYIEKGKAEGATLATGGgRPENVGLqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDED 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETK 494
Cdd:TIGR01804 393 EVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-496 |
1.61e-150 |
|
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: 438.24 E-value: 1.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIHVSRaIEVGASVEYARYMAGWATKITGQTLDVSIPfppgtRYTAYTRKEPVGVVAAIVPWNFPLMIAVW 183
Cdd:cd07088 79 KLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRP-----NENIFIFKVPIGVVAGILPWNFPFFLIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 184 KLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAA 262
Cdd:cd07088 153 KLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 263 VQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPS 342
Cdd:cd07088 233 AENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 343 AQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAV 422
Cdd:cd07088 313 TDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981295204 423 RLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPlDPSMPF-GGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENF-EAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
23-496 |
2.64e-150 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 438.87 E-value: 2.64e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETL 102
Cdd:PLN02766 23 LFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIPfppgtrYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:PLN02766 103 AALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQ------LQGYTLKEPIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLV-GT 260
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKImQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLD 340
Cdd:PLN02766 257 AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 341 PSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAAD 420
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGD-KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981295204 421 AVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
18-492 |
1.79e-149 |
|
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: 435.67 E-value: 1.79e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 18 ARDFGLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIER 97
Cdd:cd07111 19 DRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 98 DAETLAQLETLNQGKSIHVSRAIEVGASVEYARYMAGWAtkitgQTLDvsipfppgtryTAYTRKEPVGVVAAIVPWNFP 177
Cdd:cd07111 97 HQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWA-----QLLD-----------TELAGWKPVGVVGQIVPWNFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 178 LMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKL 257
Cdd:cd07111 161 LLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 258 VGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGA 337
Cdd:cd07111 241 LRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 338 GLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLaggTPADDLP--GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPF 415
Cdd:cd07111 321 PLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVF---QPGADLPskGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 416 DDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQyaiEGFTE 492
Cdd:cd07111 398 RTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGK---EGLYE 471
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-496 |
8.74e-148 |
|
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: 431.29 E-value: 8.74e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAvaRLDVHDPA-TGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTLDVSipfPPGTRytAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:cd07097 80 ARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPST---RPGVE--VETTREPLGVVGLITPWNFPIAIPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTA 261
Cdd:cd07097 154 WKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 262 AVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDP 341
Cdd:cd07097 234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 342 SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAD-DLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAAD 420
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981295204 421 AVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNC-HIPLDPSMPFGGYKQSGIG-REFGQYAIEGFTETKSV 496
Cdd:cd07097 394 ALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLpTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-498 |
3.67e-147 |
|
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: 429.09 E-value: 3.67e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPE--WAATPARERGKLLARIADALEARSEELARLLALETGNALRTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 IEVGASVEYARYMAGWATKITGQTLdvsiPFPPGTryTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETL----PFGPDV--LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAgVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07108 153 AEDAPLAVLLLAEILAQV-LPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGA-FFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKV 357
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 358 VQHIERARR-DGLTFLAGGTP---ADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLA 433
Cdd:cd07108 312 CGYIDLGLStSGATVLRGGPLpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 434 ASIWSNDLKRVMNLVPQIEAGTVWVN-CHIPLdPSMPFGGYKQSGIGREFG-QYAIEGFTETKSVCI 498
Cdd:cd07108 392 AYVWTRDLGRALRAAHALEAGWVQVNqGGGQQ-PGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
65-498 |
5.69e-147 |
|
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: 425.10 E-value: 5.69e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 65 ASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGqtL 144
Cdd:cd06534 1 AAARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGG--P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 145 DVSIPFPPGTrytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVF 224
Cdd:cd06534 76 ELPSPDPGGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 225 NVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQG 303
Cdd:cd06534 153 NVVPGgGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 304 QVCAAASRIYVHRSKFAQLANGLAdvaqsmklgagldpsaqinplvsahhrdkvvqhierarrdgltflaggtpaddlpg 383
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 384 yfvkpAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIP 463
Cdd:cd06534 257 -----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSI 331
|
410 420 430
....*....|....*....|....*....|....*.
gi 981295204 464 L-DPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd06534 332 GvGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
22-496 |
5.77e-146 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 427.61 E-value: 5.77e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 22 GLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAF---DARVWSGLRPADRERILLKLADLIERD 98
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 99 AETLAQLETLNQGKSIH--VSRAIEVGASVEYaryMAGWATKITG-QTLDVSIPFppgTRYTAYTRKEPVGVVAAIVPWN 175
Cdd:PLN02467 89 KSELAKLETLDCGKPLDeaAWDMDDVAGCFEY---YADLAEALDAkQKAPVSLPM---ETFKGYVLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 176 FPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTAT 254
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 255 GKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMK 334
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 335 LGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGT-PADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVL 413
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 414 PFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTET 493
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSV 482
|
...
gi 981295204 494 KSV 496
Cdd:PLN02467 483 KQV 485
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-498 |
6.83e-146 |
|
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: 426.49 E-value: 6.83e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 21 FGLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAE 100
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 101 TLAQLETLNQGKSIHVSRAIEVGASVEYARYMA-------GWATKITGQTLDVsipfppgtrytayTRKEPVGVVAAIVP 173
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAgviraeeGSANMIDEDTLSI-------------VLREPIGVVGQIIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 174 WNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAgVPPGVFNVVTG-GRVCGAALASHPSISKISFTGST 252
Cdd:cd07117 146 WNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 253 ATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQS 332
Cdd:cd07117 225 EVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFEN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 333 MKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGG---TPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPV 409
Cdd:cd07117 305 VKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrlTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 410 IVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEG 489
Cdd:cd07117 385 ATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDA 464
|
....*....
gi 981295204 490 FTETKSVCI 498
Cdd:cd07117 465 YTQMKNIYI 473
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
38-498 |
3.26e-144 |
|
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: 421.35 E-value: 3.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLeTLNQGKSIHVS 117
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDL-LIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RAIEVGASVEYARYMAGWATKITGQTLDvsiPFPPGTryTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVL 197
Cdd:cd07150 78 AWFETTFTPELLRAAAGECRRVRGETLP---SDSPGT--VSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 198 KPSPETPLTALRLAELARDAGVPPGVFNVVTGGR-VCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGK 276
Cdd:cd07150 153 KPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGaEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 277 NPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDK 356
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 357 VVQHIERARRDGLTFLAGGTPAddlpGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASI 436
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGGKYD----GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981295204 437 WSNDLKRVMNLVPQIEAGTVWVNCHIPLD-PSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07150 389 LTNDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
59-498 |
3.73e-143 |
|
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: 417.70 E-value: 3.73e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 59 DVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLeTLNQGKSIHVSRAIEVGASVEYARYMAGWATK 138
Cdd:cd07104 1 DVDRAYAAAAAAQKA--WAATPPQERAAILRKAAEILEERRDEIADW-LIRESGSTRPKAAFEVGAAIAILREAAGLPRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 139 ITGQTLDVSIPfppGTryTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLT-ALRLAELARDA 217
Cdd:cd07104 78 PEGEILPSDVP---GK--ESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 218 GVPPGVFNVVTGGR-VCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAA 296
Cdd:cd07104 153 GLPKGVLNVVPGGGsEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 297 GAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGT 376
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 377 PAddlpGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTV 456
Cdd:cd07104 313 YE----GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 981295204 457 WVNCHIPLD-PSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07104 389 HINDQTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
42-497 |
8.80e-143 |
|
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: 417.90 E-value: 8.80e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 42 DPATGERLASVADADEHDVEQAVASAKRAFDARVWSGlRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRaIE 121
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-FE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 122 VGASVEYARYMAGWATKITGQTLDVSipfpPGTryTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSP 201
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPE----PGS--FSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 202 ETPLTALRLAE-LARDAGVPPGVFNVVTGGRVCGAA-LASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPI 279
Cdd:cd07120 155 QTAQINAAIIRiLAEIPSLPAGVVNLFTESGSEGAAhLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 280 VMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQ 359
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 360 HIERARRDGLT-FLAGGTPADDLP-GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIW 437
Cdd:cd07120 315 MVERAIAAGAEvVLRGGPVTEGLAkGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 438 SNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVC 497
Cdd:cd07120 395 TRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
23-496 |
3.88e-140 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 414.20 E-value: 3.88e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETL 102
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLdvsipfPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTV------PADGPHHVQTLHEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLV-GT 260
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRS---KFAQLANgladvAQSMKLGA 337
Cdd:PLN02466 294 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERvydEFVEKAK-----ARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 338 GlDP---SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLP 414
Cdd:PLN02466 369 G-DPfkkGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGS-KGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILK 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 415 FDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETK 494
Cdd:PLN02466 447 FKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
..
gi 981295204 495 SV 496
Cdd:PLN02466 527 AV 528
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-498 |
7.02e-139 |
|
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: 407.92 E-value: 7.02e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF--PEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 iEVGASVEYARYMAGWATKITGQTLdvsipfPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07107 79 -DVMVAAALLDYFAGLVTELKGETI------PVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAgVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07107 152 PEQAPLSALRLAELAREV-LPPGVFNILPGdGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFN-QGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKV 357
Cdd:cd07107 231 LIVFPDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 358 VQHIERARRDGLTFLAGGTPADDLP---GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAA 434
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981295204 435 SIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-498 |
3.19e-137 |
|
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: 403.51 E-value: 3.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVS 117
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGA--KEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RAiEVGASVEYARYMAGWATKITGQTldvsIPF---PPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCT 194
Cdd:cd07149 79 RK-EVDRAIETLRLSAEEAKRLAGET----IPFdasPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 195 IVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAvqNMTRFSLEL 273
Cdd:cd07149 154 VVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGsGETVGDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 274 GGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHH 353
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 354 RDKVVQHIERARRDGLTFLAGGTPAddlpGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLA 433
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLTGGKRD----GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981295204 434 ASIWSNDLKRVMNLVPQIEAGTVWVNchiplDPS------MPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGVMIN-----DSStfrvdhMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
19-499 |
4.60e-137 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 404.84 E-value: 4.60e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 19 RDFGLF-----IDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLAD 93
Cdd:PLN02278 18 RNAGLLrtqglIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAF--PSWSKLTASERSKILRRWYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 94 LIERDAETLAQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGqtlDVsIPFP-PGTRYTAYtrKEPVGVVAAIV 172
Cdd:PLN02278 96 LIIANKEDLAQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYG---DI-IPSPfPDRRLLVL--KQPVGVVGAIT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 173 PWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRV-CGAALASHPSISKISFTGS 251
Cdd:PLN02278 169 PWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPeIGDALLASPKVRKITFTGS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 252 TATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQ 331
Cdd:PLN02278 249 TAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 332 SMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAdDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIV 411
Cdd:PLN02278 329 KLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRH-SLGGTFYEPTVLGDVTEDMLIFREEVFGPVAP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 412 VLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFT 491
Cdd:PLN02278 408 LTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYL 487
|
....*...
gi 981295204 492 ETKSVCIA 499
Cdd:PLN02278 488 EIKYVCLG 495
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
23-498 |
4.71e-137 |
|
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: 404.57 E-value: 4.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07140 8 LFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIPFPpgTRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:cd07140 88 ATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARP--NRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGK-LVGT 260
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGsGSLVGQRLSDHPDVRKLGFTGSTPIGKhIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLD 340
Cdd:cd07140 246 CAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 341 PSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAdDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDA-A 419
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQV-DRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 420 DAV-RLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07140 405 DGVlQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-500 |
1.15e-136 |
|
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: 403.27 E-value: 1.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAVARLDVHDPATGERL-ASVADADEHDVEQAVASAKRAFDarVWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFP--EWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTLDVSIPfppgtRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:cd07131 80 ARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSELP-----NKDAMTRRQPIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTA 261
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 262 AVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDP 341
Cdd:cd07131 234 CARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 342 SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADD---LPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDA 418
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 419 ADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNC-HIPLDPSMPFGGYKQSGIG-REFGQYAIEGFTETKSV 496
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNApTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
....
gi 981295204 497 CIAH 500
Cdd:cd07131 474 YVDY 477
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
23-499 |
1.64e-132 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 393.11 E-value: 1.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSGLRPADRERILLKLADLIERDAETL 102
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLdvsipfPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVA------TTSSHELAMIVREPVGVIAAIVPWNFPLLLTC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGK-LVGT 260
Cdd:PRK09847 176 WKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKqLLKD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNP-IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGL 339
Cdd:PRK09847 256 AGDSNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 340 DPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAddLPGYfVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAG--LAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCIA 499
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
38-498 |
3.81e-132 |
|
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: 390.56 E-value: 3.81e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAFDarVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVS 117
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RaIEVGASVEYARYMAGWATKITGQTLDVSiPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVL 197
Cdd:cd07145 79 R-VEVERTIRLFKLAAEEAKVLRGETIPVD-AYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 198 KPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGK 276
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGyGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 277 NPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDK 356
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 357 VVQHIERARRDGLTFLAGGtpaDDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASI 436
Cdd:cd07145 317 MENLVNDAVEKGGKILYGG---KRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981295204 437 WSNDLKRVMNLVPQIEAGTVWVNCHIPLDP-SMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWdNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
40-494 |
1.83e-128 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 381.01 E-value: 1.83e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRA 119
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT--WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 iEVGASVEYARYMAGWATKITGQTldvsIPfPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:TIGR01780 79 -EILYAASFLEWFAEEAKRVYGDT----IP-SPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTGGRV--CGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKN 277
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGSRAkeVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 278 PIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKV 357
Cdd:TIGR01780 233 PFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 358 VQHIERARRDGLTFLAGGTpADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIW 437
Cdd:TIGR01780 313 EKHIADAVEKGAKVVTGGK-RHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 438 SNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETK 494
Cdd:TIGR01780 392 SRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
38-498 |
1.23e-124 |
|
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: 371.38 E-value: 1.23e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVS 117
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAG--AENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RaIEVGASVEYARYMAGWATKITGqtldVSIPFPPGTRYT---AYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCT 194
Cdd:cd07094 79 R-VEVDRAIDTLRLAAEEAERIRG----EEIPLDATQGSDnrlAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 195 IVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAvqNMTRFSLEL 273
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEALRANA--GGKRIALEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 274 GGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHH 353
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 354 RDKVVQHIERARRDGLTFLAGGTPADDLpgyfVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLA 433
Cdd:cd07094 312 AERVERWVEEAVEAGARLLCGGERDGAL----FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981295204 434 ASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLD-PSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRtDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-496 |
2.61e-124 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 373.06 E-value: 2.61e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 31 PAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLA---QLET 107
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLdlvQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 108 lnqGKSihvsRAI---EVGASVEYARYMAGWATKITGQTlDVSIPFPPGTRYTayTRKEPVGVVAAIVPWNFPLMIAVWK 184
Cdd:PRK09407 105 ---GKA----RRHafeEVLDVALTARYYARRAPKLLAPR-RRAGALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 185 LIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHpsISKISFTGSTATGKLVGTAAV 263
Cdd:PRK09407 175 AIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGpGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 264 QNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSA 343
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 344 QINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVR 423
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 424 LANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNchiplDP--------SMPFGGYKQSGIGREFGQYAIEGFTETKS 495
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN-----EGyaaawgsvDAPMGGMKDSGLGRRHGAEGLLKYTESQT 487
|
.
gi 981295204 496 V 496
Cdd:PRK09407 488 I 488
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-500 |
6.13e-124 |
|
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: 370.10 E-value: 6.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 27 GEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLI-ERDAETLAQL 105
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILeERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 106 etLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIPfppGTRYTAYtrKEPVGVVAAIVPWNFPLMIAVWKL 185
Cdd:cd07151 79 --IRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVP---GKENRVY--REPLGVVGVISPWNFPLHLSMRSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 186 IPALAAGCTIVLKPSPETPLTA-LRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAV 263
Cdd:cd07151 152 APALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 264 QNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSA 343
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 344 QINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAddlpGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVR 423
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE----GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981295204 424 LANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLD-PSMPFGGYKQSGIGREFGQYAIEGFTETKSVCIAH 500
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
41-496 |
5.49e-122 |
|
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: 364.62 E-value: 5.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 41 HDPATGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRaI 120
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA--QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 121 EVGASVEYARYMAGWATKITGQTldvSIPFPPGTRY-TAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLAPR---KVPTGLLMPNkKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPI 279
Cdd:cd07099 155 SEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 280 VMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQ 359
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 360 HIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSN 439
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNG-GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 440 DLKRVMNLVPQIEAGTVWVNCHI--PLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINDVLltAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-500 |
2.63e-121 |
|
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: 363.81 E-value: 2.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAhAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTLDVSIPfppGTRytAYTRKEPVGVVAAIVPWNFPLMIAVW 183
Cdd:cd07086 79 RLVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSERP---GHR--LMEQWNPLGVVGVITAFNFPVAVPGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 184 KLIPALAAGCTIVLKPSPETPLTALRLAELARDA----GVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVG 259
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 260 TAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGL 339
Cdd:cd07086 233 ETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 340 DPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAD-DLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDA 418
Cdd:cd07086 313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 419 ADAVRLANASPYGLAASIWSNDLKRVMNLV--PQIEAGTVWVNchIPldPS-----MPFGGYKQSGIGREFGQYAIEGFT 491
Cdd:cd07086 393 EEAIAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVN--IP--TSgaeigGAFGGEKETGGGRESGSDAWKQYM 468
|
....*....
gi 981295204 492 ETKSVCIAH 500
Cdd:cd07086 469 RRSTCTINY 477
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
23-496 |
2.77e-121 |
|
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: 363.76 E-value: 2.77e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIH-----VSRAIEVgasVEYArymAGWATKITGQTLDVSipfppGTRYTAYTRKEPVGVVAAIVPWNFP 177
Cdd:cd07085 81 ARLITLEHGKTLAdargdVLRGLEV---VEFA---CSIPHLLKGEYLENV-----ARGIDTYSYRQPLGVVAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 178 LMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKL 257
Cdd:cd07085 150 AMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 258 VGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGA 337
Cdd:cd07085 230 IYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 338 GLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGG---TPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLP 414
Cdd:cd07085 310 GDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 415 FDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLD-PSMPFGGYKQS--GIGREFGQYAIEGFT 491
Cdd:cd07085 390 VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPlAFFSFGGWKGSffGDLHFYGKDGVRFYT 469
|
....*
gi 981295204 492 ETKSV 496
Cdd:cd07085 470 QTKTV 474
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
38-498 |
1.57e-118 |
|
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: 355.78 E-value: 1.57e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVS 117
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAF--RPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RAiEVGASVEYARYMAGWATKITGQTLDVSIpFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVL 197
Cdd:cd07147 79 RG-EVARAIDTFRIAAEEATRIYGEVLPLDI-SARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 198 KPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATG-KLVGTAAVQNMTrfsLELGGK 276
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGwDLKARAGKKKVV---LELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 277 NPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDK 356
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 357 VVQHIERARRDGLTFLAGGTpaddLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASI 436
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGK----RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981295204 437 WSNDLKRVMNLVPQIEAGTVWVNcHIP---LDpSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVIN-DVPtfrVD-HMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
43-496 |
3.43e-118 |
|
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: 355.02 E-value: 3.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 43 PATGERLASVADADEhdvEQAVASAKRAFDA-RVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAiE 121
Cdd:cd07102 3 PIDGSVIAERPLASL---EAVRAALERARAAqKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 122 VGASVEYARYMAGWATKITGqtldvSIPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSP 201
Cdd:cd07102 79 IRGMLERARYMISIAEEALA-----DIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 202 ETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVM 281
Cdd:cd07102 154 QTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 282 LDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHI 361
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 362 ERARRDGLTFLAGG--TPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSN 439
Cdd:cd07102 314 ADAIAKGARALIDGalFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 440 DLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
24-500 |
2.82e-117 |
|
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: 353.68 E-value: 2.82e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIHVSRAIEVGASVEYARYMA-------GWATKITGQTLdvsipfppgtrytAYTRKEPVGVVAAIVPWNF 176
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAgciraqeGSISEIDENTV-------------AYHFHEPLGVVGQIIPWNF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 177 PLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAgVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATG 255
Cdd:cd07116 149 PLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 256 KLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQ------ALDGVAAGAfFNQGQVCAAASRIYVHRSKFAQLANGLADV 329
Cdd:cd07116 228 RLIMQYASENIIPVTLELGGKSPNIFFADVMDADdaffdkALEGFVMFA-LNQGEVCTCPSRALIQESIYDRFMERALER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 330 AQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPA---DDLPGYFVKPAVIADPRpDSAIVRDEVF 406
Cdd:cd07116 307 VKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelgGLLGGGYYVPTTFKGGN-KMRIFQEEIF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 407 GPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYA 486
Cdd:cd07116 386 GPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMM 465
|
490
....*....|....
gi 981295204 487 IEGFTETKSVCIAH 500
Cdd:cd07116 466 LDHYQQTKNLLVSY 479
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
60-498 |
2.84e-117 |
|
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: 351.76 E-value: 2.84e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 60 VEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAiEVGASVEYARYMAgwaTKI 139
Cdd:cd07100 1 IEAALDRAHAAF--LAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYA---ENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 140 TGQTLDVSIPFPPGTrytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGV 219
Cdd:cd07100 75 EAFLADEPIETDAGK---AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 220 PPGVFN--VVTGGRVcgAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAG 297
Cdd:cd07100 152 PEGVFQnlLIDSDQV--EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 298 AFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTP 377
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 378 aDDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVW 457
Cdd:cd07100 310 -PDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 981295204 458 VNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07100 389 INGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-496 |
5.75e-117 |
|
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: 352.00 E-value: 5.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 41 HDPATGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKS-IHVSRA 119
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKArRHAFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 120 IEVGASVeyARYMAGWATKITGQTLDVSiPFPPGTRYTAYTRkePVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:cd07101 79 VLDVAIV--ARYYARRAERLLKPRRRRG-AIPVLTRTTVNRR--PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSIskISFTGSTATGKLVGTAAVQNMTRFSLELGGKNP 278
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGpGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 279 IVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVV 358
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 359 QHIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWS 438
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981295204 439 NDLKRVMNLVPQIEAGTVWVN-CHIPLDPSM--PFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNeGYAAAWASIdaPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
59-498 |
5.83e-116 |
|
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: 348.41 E-value: 5.83e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 59 DVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRaIEVGASVEYARYMAGWATK 138
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 139 ITGQTLDVSIPfppGTryTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAG 218
Cdd:cd07105 78 IIGGSIPSDKP---GT--LAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 219 VPPGVFNVVT------GGRVcgAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALD 292
Cdd:cd07105 153 LPKGVLNVVThspedaPEVV--EALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 293 GVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPsaqinPLVSAHHRDKVVQHIERARRDGLTFL 372
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLG-----SLVSAAAADRVKELVDDALSKGAKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 373 AGGTPADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIE 452
Cdd:cd07105 306 VGGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 981295204 453 AGTVWVN-CHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07105 386 SGAVHINgMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-497 |
1.04e-114 |
|
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: 348.06 E-value: 1.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 11 DTVRTFVARDFGLFIDGEmqPAHAVARLDVHDPA-TGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILL 89
Cdd:cd07124 23 ARVREELGREYPLVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 90 KLADLIERDAETLAQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTLDVSIPFPPGTRYtaytrkEPVGVVA 169
Cdd:cd07124 99 RAAALLRRRRFELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVY------RPLGVGA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 170 AIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISF 248
Cdd:cd07124 172 VISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGpGEEVGDYLVEHPDVRFIAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 249 TGSTATG-KLVGTAAV-----QNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQL 322
Cdd:cd07124 252 TGSREVGlRIYERAAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 323 ANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSAIVR 402
Cdd:cd07124 332 LERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 403 DEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN--CHIPLDPSMPFGGYKQSGIG- 479
Cdd:cd07124 412 EEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTGs 491
|
490
....*....|....*...
gi 981295204 480 REFGQYAIEGFTETKSVC 497
Cdd:cd07124 492 KAGGPDYLLQFMQPKTVT 509
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
23-499 |
3.24e-114 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 345.60 E-value: 3.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAvARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARVWSgLRPADRERILLKLADLIERDAETL 102
Cdd:TIGR04284 3 LLIDGKLVAGSA-GTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDETDWS-RDTALRVRCLRQLRDALRAHVEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITGQTlDVSIPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:TIGR04284 81 RELTIAEVGAPRMLTAGAQLEGPVDDLGFAADLAESYAWTT-DLGVASPMGIPTRRTLRREAVGVVGAITPWNFPHQINL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAEL-ARDAGVPPGVFNVVTGGR-VCGAALASHPSISKISFTGSTATGKLVGT 260
Cdd:TIGR04284 160 AKLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDhRLGALLAKDPRVDMVSFTGSTATGRAVMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLD 340
Cdd:TIGR04284 240 DAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 341 PSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGT-PADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAA 419
Cdd:TIGR04284 320 PGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGrPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 420 DAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCIA 499
Cdd:TIGR04284 400 DAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLIATA 479
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
38-498 |
6.92e-114 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 343.96 E-value: 6.92e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAkrafdARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVS 117
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALA-----ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RaIEVGASVEYARYMAGWATKITGQTLDVSIPFPPGTRyTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVL 197
Cdd:cd07146 76 R-YEVGRAADVLRFAAAEALRDDGESFSCDLTANGKAR-KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 198 KPSPETPLTALRLAELARDAGVPPGVFNVVTGG-RVCGAALASHPSISKISFTGSTATGKLVgtAAVQNMTRFSLELGGK 276
Cdd:cd07146 154 KPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 277 NPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDK 356
Cdd:cd07146 232 DPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 357 VVQHIERARRDGLTFLAGGtpadDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASI 436
Cdd:cd07146 312 IENRVEEAIAQGARVLLGN----QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981295204 437 WSNDLKRVMNLVPQIEAGTVWVNcHIP--LDPSMPFGGYKQSGIG-REFGQYAIEGFTETKSVCI 498
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVN-EVPgfRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
46-492 |
1.17e-112 |
|
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: 340.43 E-value: 1.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 46 GERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLAQLeTLNQGKSIHVSRAIEVGAS 125
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADW-IVRESGSIRPKAGFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 126 VEYARYMAGWATKITGQTLdvsiPFPPGTryTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPL 205
Cdd:cd07152 78 IGELHEAAGLPTQPQGEIL----PSAPGR--LSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 206 TA-LRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDD 284
Cdd:cd07152 152 SGgVVIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 285 VDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERA 364
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 365 RRDGLTFLAGGTpADDLpgyFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRV 444
Cdd:cd07152 312 VAAGARLEAGGT-YDGL---FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 981295204 445 MNLVPQIEAGTVWVNCHIPLD-PSMPFGGYKQSGIGREFGQYA-IEGFTE 492
Cdd:cd07152 388 MALADRLRTGMLHINDQTVNDePHNPFGGMGASGNGSRFGGPAnWEEFTQ 437
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
24-499 |
2.06e-108 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 330.72 E-value: 2.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTldvsIP-FPPGTRYTAYtrKEPVGVVAAIVPWNFPLMIAV 182
Cdd:PRK11241 92 RLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDT----IPgHQADKRLIVI--KQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG--GRVcGAALASHPSISKISFTGSTATGKLVGT 260
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGsaGAV-GGELTSNPLVRKLSFTGSTEIGRQLME 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLD 340
Cdd:PRK11241 244 QCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 341 PSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPaDDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAAD 420
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKA-HELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 421 AVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCIA 499
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
37-498 |
5.48e-107 |
|
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: 326.84 E-value: 5.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 37 RLDVHDPATGERLASVADADEHDVEQAVASAKRAFDARvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSiHV 116
Cdd:cd07082 17 TIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGW-WPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT-LK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 117 SRAIEVGASVEYARYMAGWATKITGQtldvSIPFP--PGTRYT-AYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGC 193
Cdd:cd07082 95 DALKEVDRTIDYIRDTIEELKRLDGD----SLPGDwfPGTKGKiAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 194 TIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVqnMTRFSLE 272
Cdd:cd07082 171 TVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 273 LGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAH 352
Cdd:cd07082 249 LGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 353 HRDKVVQHIERARRDGLTFLAGGtpaDDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGL 432
Cdd:cd07082 329 SADFVEGLIDDAVAKGATVLNGG---GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGL 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 433 AASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDP-SMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07082 406 QASIFTKDINKARKLADALEVGTVNINSKCQRGPdHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVI 472
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
88-496 |
1.60e-93 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 290.10 E-value: 1.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 88 LLKLADLIERDAETLAQLETLNQGKSIHVSRaIEVGASVEYARYMAGWATKITGQTLDVSIPfppgtRYTAYTRKEPVGV 167
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSDRP-----GENILLFKRALGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 168 VAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKI 246
Cdd:PRK10090 75 TTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGrGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 247 SFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGL 326
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 327 ADVAQSMKLGAGLDPSA-QINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEV 405
Cdd:PRK10090 235 GEAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEG-KGYYYPPTLLLDVRQEMSIMHEET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 406 FGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNcHIPLDPSMPF-GGYKQSGIGREFGQ 484
Cdd:PRK10090 314 FGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN-RENFEAMQGFhAGWRKSGIGGADGK 392
|
410
....*....|..
gi 981295204 485 YAIEGFTETKSV 496
Cdd:PRK10090 393 HGLHEYLQTQVV 404
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-497 |
5.26e-91 |
|
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: 285.35 E-value: 5.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 41 HDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAI 120
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ--REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 121 EVGASVEYARYMAGWATKiTGQTLDVSIPFPPGTRyTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPS 200
Cdd:cd07098 79 EILVTCEKIRWTLKHGEK-ALRPESRPGGLLMFYK-RARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 201 PETPLTALRLAELARDA----GVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGK 276
Cdd:cd07098 157 EQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 277 NPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDK 356
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 357 VVQHIERARRDGLTFLAGGT--PADDLP-GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLA 433
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKryPHPEYPqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981295204 434 ASIWSNDLKRVMNLVPQIEAGTVWVN-------CHipldpSMPFGGYKQSGIGREFGQYAIEGFTETKSVC 497
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINdfgvnyyVQ-----QLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
42-499 |
1.64e-88 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 278.54 E-value: 1.64e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 42 DPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAiE 121
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARF--RDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA-E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 122 VGASVEYARYMAGWATK-ITGQTLDVSipfPPGTRyTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPS 200
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEAlLADEPADAA---AVGAS-RAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 201 PETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIV 280
Cdd:PRK09406 160 SNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 281 MLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQH 360
Cdd:PRK09406 240 VMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 361 IERARRDGLTFLAGGTPADDlPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSND 440
Cdd:PRK09406 320 VDDAVAAGATILCGGKRPDG-PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 441 LKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCIA 499
Cdd:PRK09406 399 EAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
23-496 |
5.58e-88 |
|
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: 277.92 E-value: 5.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 23 LFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETL 102
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT--WGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSI-----HVSRAIEVgasVEYArymAGWATKITGQTLDvSIpfppGTRYTAYTRKEPVGVVAAIVPWNFP 177
Cdd:TIGR01722 81 AELITAEHGKTHsdalgDVARGLEV---VEHA---CGVNSLLKGETST-QV----ATRVDVYSIRQPLGVCAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 178 LMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKL 257
Cdd:TIGR01722 150 AMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 258 VGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASrIYVHRSKFAQLANGLADVAQSMKLGA 337
Cdd:TIGR01722 230 IHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 338 GLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGT--PADDLP-GYFVKPAVIADPRPDSAIVRDEVFGPVIVVLP 414
Cdd:TIGR01722 309 GDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRgyKVDGYEeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 415 FDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLD-PSMPFGGYKQSGIG--REFGQYAIEGFT 491
Cdd:TIGR01722 389 ADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPlPYFSFTGWKDSFFGdhHIYGKQGTHFYT 468
|
....*
gi 981295204 492 ETKSV 496
Cdd:TIGR01722 469 RGKTV 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
13-496 |
9.87e-86 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 273.35 E-value: 9.87e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 13 VRTFVARDFGLFIDGEmqPAHAVARLDVHDPA-TGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKL 91
Cdd:PRK03137 29 VEKELGQDYPLIIGGE--RITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 92 ADLIERDAETLAQLETLNQGK-----SIHVSRAI---EVgasveYARYMAGWATkitGQTLdvsIPFPPGTRYTAYtrkE 163
Cdd:PRK03137 105 AAIIRRRKHEFSAWLVKEAGKpwaeaDADTAEAIdflEY-----YARQMLKLAD---GKPV---ESRPGEHNRYFY---I 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 164 PVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPS 242
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGsGSEVGDYLVDHPK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 243 ISKISFTGSTATG-KLVGTAAV-----QNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHR 316
Cdd:PRK03137 251 TRFITFTGSREVGlRIYERAAKvqpgqIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 317 SKFAQLANGLADVAQSMKLGAGLDPSAqINPLVSAHHRDKVVQHIERARRDGLTFLAGGTpaDDLPGYFVKPAVIADPRP 396
Cdd:PRK03137 331 DVYDEVLEKVVELTKELTVGNPEDNAY-MGPVINQASFDKIMSYIEIGKEEGRLVLGGEG--DDSKGYFIQPTIFADVDP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 397 DSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN--CHIPLDPSMPFGGYK 474
Cdd:PRK03137 408 KARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFN 487
|
490 500
....*....|....*....|....
gi 981295204 475 QSGIGREFG--QYAIEgFTETKSV 496
Cdd:PRK03137 488 MSGTDSKAGgpDYLLL-FLQAKTV 510
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
12-483 |
2.22e-85 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 272.12 E-value: 2.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 12 TVRTFVARDFGLFIDGEMqpAHAVARLDVHDPA-TGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLK 90
Cdd:TIGR01237 24 TVKEQLGKTYPLVINGER--VETENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA--WKKTDPEERAAILFK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 91 LADLIERDAETLAQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTLDVSipFPPGTRYTAYTrkePVGVVAA 170
Cdd:TIGR01237 100 AAAIVRRRRHEFSALLVKEVGKPWNEADA-EVAEAIDFMEYYARQMIELAKGKPVNS--REGETNQYVYT---PTGVTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 171 IVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFT 249
Cdd:TIGR01237 174 ISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGsGSEVGDYLVDHPKTSLITFT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 250 GSTATGKLVGTAAV------QNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLA 323
Cdd:TIGR01237 254 GSREVGTRIFERAAkvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 324 NGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLtfLAGGTPADDLPGYFVKPAVIADPRPDSAIVRD 403
Cdd:TIGR01237 334 ERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGR--LVSGGCGDDSKGYFIGPTIFADVDRKARLAQE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 404 EVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN--CHIPLDPSMPFGGYKQSGIGRE 481
Cdd:TIGR01237 412 EIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSK 491
|
..
gi 981295204 482 FG 483
Cdd:TIGR01237 492 AG 493
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
38-479 |
4.78e-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: 259.27 E-value: 4.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAF-DARVWsgLRPADRERILLKLADLIERDAETLAQLETLNQGKSIhv 116
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 117 sraieVGASVEYARYMAG--WATKITGQTLDVSIPF---PPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAA 191
Cdd:cd07148 77 -----VDAKVEVTRAIDGveLAADELGQLGGREIPMgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 192 GCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNmTRFSL 271
Cdd:cd07148 152 GCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 272 ELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSA 351
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 352 HHRDKVVQHIERARRDGLTFLAGGTPADDLpgyFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYG 431
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDT---TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 981295204 432 LAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPS-MPFGGYKQSGIG 479
Cdd:cd07148 388 FQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
44-496 |
3.97e-77 |
|
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: 250.57 E-value: 3.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 44 ATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIhVSRAIEVG 123
Cdd:cd07083 41 APSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNW-VEAIDDVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 124 ASVEYARYMAGWATKITGQTLDVsIPFPPGTRYTAYtrkEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPET 203
Cdd:cd07083 118 EAIDFIRYYARAALRLRYPAVEV-VPYPGEDNESFY---VGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 204 PLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFS------LELGGK 276
Cdd:cd07083 194 VVVGYKVFEIFHEAGFPPGVVQFLPGvGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTwfkrlyVETGGK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 277 NPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDK 356
Cdd:cd07083 274 NAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 357 VVQHIERARRDGlTFLAGGTpADDLPGYFVKPAVIADPRPDSAIVRDEVFGPV--IVVLPFDDAADAVRLANASPYGLAA 434
Cdd:cd07083 354 VLSYIEHGKNEG-QLVLGGK-RLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVlsVIRYKDDDFAEALEVANSTPYGLTG 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981295204 435 SIWSNDLKRVMNLVPQIEAGTVWVNCHI--PLDPSMPFGGYKQSGIG-REFGQYAIEGFTETKSV 496
Cdd:cd07083 432 GVYSRKREHLEEARREFHVGNLYINRKItgALVGVQPFGGFKLSGTNaKTGGPHYLRRFLEMKAV 496
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
24-479 |
1.42e-76 |
|
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: 249.42 E-value: 1.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMqpAHAVARLDVHDPATGER-LASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETL 102
Cdd:cd07125 36 IINGEE--TETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAG--WSATPVEERAEILEKAADLLEANRGEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 103 AQLETLNQGKSihVSRAI-EVGASVEYARYMAGWAtkitgQTLDVSIPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIA 181
Cdd:cd07125 112 IALAAAEAGKT--LADADaEVREAIDFCRYYAAQA-----RELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 182 VWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGT 260
Cdd:cd07125 185 TGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGdGEEIGEALVAHPRIDGVIFTGSTETAKLINR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 261 AAVQNM---TRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGA 337
Cdd:cd07125 265 ALAERDgpiLPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 338 GLDPSAQINPLVSAHHRDKVVQHIERARRDGltFLAGGTPADDLPGYFVKPAVIADPRPDSaiVRDEVFGPVIVVLPFD- 416
Cdd:cd07125 345 PWDLSTDVGPLIDKPAGKLLRAHTELMRGEA--WLIAPAPLDDGNGYFVAPGIIEIVGIFD--LTTEVFGPILHVIRFKa 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981295204 417 -DAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNchipldPSM--------PFGGYKQSGIG 479
Cdd:cd07125 421 eDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN------RNItgaivgrqPFGGWGLSGTG 486
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
38-483 |
1.30e-75 |
|
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: 245.58 E-value: 1.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 38 LDVHDPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVS 117
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAF--KEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 118 RAiEVGASVEYARYMAGWATKITGQTldvsipFP---PGTRYtaYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCT 194
Cdd:cd07130 92 LG-EVQEMIDICDFAVGLSRQLYGLT------IPserPGHRM--MEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 195 IVLKPSPETPLTALR----LAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFS 270
Cdd:cd07130 163 VVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 271 LELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVS 350
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 351 AHHRDKVVQHIERARRDGLTFLAGGtPADDLPGYFVKPAvIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPY 430
Cdd:cd07130 323 KAAVDNYLAAIEEAKSQGGTVLFGG-KVIDGPGNYVEPT-IVEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQ 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 981295204 431 GLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPldPS-----MPFGGYKQSGIGREFG 483
Cdd:cd07130 401 GLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIG--TSgaeigGAFGGEKETGGGRESG 456
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
61-498 |
1.50e-75 |
|
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: 243.97 E-value: 1.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 61 EQAVASAKRAFDARVwsgLRP-ADRERILLKLADLIERDAETLAqlETLNQ--GKSIHVSRAIEVGASVEYARYM----A 133
Cdd:cd07087 1 AELVARLRETFLTGK---TRSlEWRKAQLKALKRMLTENEEEIA--AALYAdlGKPPAEAYLTEIAVVLGEIDHAlkhlK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 134 GWATKitgQTLDVSIPFPPGTrytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAEL 213
Cdd:cd07087 76 KWMKP---RRVSVPLLLQPAK---AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 214 ARDAgVPPGVFNVVTGGRVCGAALASHPsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDG 293
Cdd:cd07087 150 IPKY-FDPEAVAVVEGGVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 294 VAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMkLGAGLDPSAQINPLVSAHHRDKVVQHIERArrdglTFLA 373
Cdd:cd07087 228 IAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 374 GGTpaDDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEA 453
Cdd:cd07087 302 GGQ--VDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 981295204 454 GTVWVN---CHIpLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSVCI 498
Cdd:cd07087 380 GGVCVNdvlLHA-AIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
59-487 |
4.99e-74 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 240.25 E-value: 4.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 59 DVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAiEVGAsveyaryMAGwatK 138
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT-EVAA-------MAG---K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 139 ItgqtlDVSIP-----FPPGTRYT----AYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALR 209
Cdd:cd07095 68 I-----DISIKayherTGERATPMaqgrAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 210 LAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTR-FSLELGGKNPIVMLDDVDVA 288
Cdd:cd07095 143 MVELWEEAGLPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 289 QALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQ-LANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRD 367
Cdd:cd07095 223 AAAYLIVQSAFLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 368 GLTFLAGGTpADDLPGYFVKPAVI----ADPRPDSaivrdEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKR 443
Cdd:cd07095 303 GGEPLLAME-RLVAGTAFLSPGIIdvtdAADVPDE-----EIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEAL 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 981295204 444 VMNLVPQIEAGTVWVNCHIPLDPS-MPFGGYKQSGIGREFGQYAI 487
Cdd:cd07095 377 FERFLARIRAGIVNWNRPTTGASStAPFGGVGLSGNHRPSAYYAA 421
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
42-496 |
6.52e-74 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 240.92 E-value: 6.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 42 DPATGERLASVADADEHDVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAiE 121
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGF--RDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 122 VGASVEYARYMA--GWATKITGQTLDvsipfppgTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKP 199
Cdd:PRK13968 90 VAKSANLCDWYAehGPAMLKAEPTLV--------ENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 200 SPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPI 279
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 280 VMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQ 359
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 360 HIERARRDGLTFLAGGTPADDLPGYFVkPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSN 439
Cdd:PRK13968 322 QVEATLAEGARLLLGGEKIAGAGNYYA-PTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 440 DLKRVMNLVPQIEAGTVWVNCHIPLDPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
152-496 |
9.97e-72 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 234.43 E-value: 9.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 152 PGTRytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFnVVTGGR 231
Cdd:cd07134 90 FGTK--SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEGDA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 232 VCGAALASHPsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASR 311
Cdd:cd07134 167 EVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 312 IYVHRSKFAQLANGL-ADVAQSMKLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPadDLPGYFVKPAV 390
Cdd:cd07134 246 VFVHESVKDAFVEHLkAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF--DAAQRYIAPTV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 391 IADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN---CHIpLDPS 467
Cdd:cd07134 324 LTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdvvLHF-LNPN 402
|
330 340
....*....|....*....|....*....
gi 981295204 468 MPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07134 403 LPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-486 |
5.81e-68 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 225.99 E-value: 5.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 22 GLFIDGEMQPAHAvARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAET 101
Cdd:PRK09457 2 TLWINGDWIAGQG-EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 102 LAQLETLNQGKSIHVSRAiEVGAsveyaryMAGwatKI----------TGQTLDvsiPFPPGTrytAYTRKEPVGVVAAI 171
Cdd:PRK09457 79 LAEVIARETGKPLWEAAT-EVTA-------MIN---KIaisiqayherTGEKRS---EMADGA---AVLRHRPHGVVAVF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 172 VPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGS 251
Cdd:PRK09457 142 GPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 252 TATGKLVGTA-AVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQ-LANGLADV 329
Cdd:PRK09457 222 ANTGYLLHRQfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 330 AQSMKLGAgldPSAQINPLVSAHHRDKVVQHIERARRD-----GLTFLAGGTPADDLPgyFVKPAVI----ADPRPDsai 400
Cdd:PRK09457 302 AKRLTVGR---WDAEPQPFMGAVISEQAAQGLVAAQAQllalgGKSLLEMTQLQAGTG--LLTPGIIdvtgVAELPD--- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 401 vrDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTvwVNCHIPLD---PSMPFGGYKQSG 477
Cdd:PRK09457 374 --EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VNWNKPLTgasSAAPFGGVGASG 449
|
....*....
gi 981295204 478 IGREFGQYA 486
Cdd:PRK09457 450 NHRPSAYYA 458
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
81-490 |
2.58e-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: 222.75 E-value: 2.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 81 PADRERI--LLKLADLIERDAETLAqlETLNQ---GKSIHVSRAIEVGASVEYARY----MAGWATKitgQTLDVSIPFP 151
Cdd:cd07133 17 PSLEERRdrLDRLKALLLDNQDALA--EAISAdfgHRSRHETLLAEILPSIAGIKHarkhLKKWMKP---SRRHVGLLFL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 152 PGTrytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGvPPGVFNVVTGGR 231
Cdd:cd07133 92 PAK---AEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVTGGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 232 VCGAALASHPsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASR 311
Cdd:cd07133 168 DVAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 312 IYVHRSKFAQLANGLADVAQSM--KLGAGLDPSAQINplvsAHHRDKVVQHIERARRDGLTFL-AGGTPADDLPGYFVKP 388
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKMypTLADNPDYTSIIN----ERHYARLQGLLEDARAKGARVIeLNPAGEDFAATRKLPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 389 AVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN---CHIPLD 465
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtlLHVAQD 402
|
410 420
....*....|....*....|....*
gi 981295204 466 pSMPFGGYKQSGIGREFGqyaIEGF 490
Cdd:cd07133 403 -DLPFGGVGASGMGAYHG---KEGF 423
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
59-496 |
1.02e-65 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 218.63 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 59 DVEQAVASAKRAFDARVwsgLRPAD-RERILLKLADLIERDAETLAQLETLNQGKSIHVSRAIEVGASVEYARYMAG--- 134
Cdd:cd07135 6 EIDSIHSRLRATFRSGK---TKDLEyRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKnlk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 135 -WAtkitgQTLDVSIPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAEL 213
Cdd:cd07135 83 kWA-----KDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 214 ARDAgVPPGVFNVVTGG-RVCGAALASHpsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALD 292
Cdd:cd07135 158 VPKY-LDPDAFQVVQGGvPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 293 GVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMkLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDgltFL 372
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLDTTKGK---VV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 373 AGGTpaDDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIE 452
Cdd:cd07135 311 IGGE--MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 981295204 453 AGTVWVN---CHIPLdPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07135 389 SGGVVINdtlIHVGV-DNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-496 |
2.29e-65 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 222.31 E-value: 2.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 24 FIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAFDarVWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTL-DVSipfppgTRYTAYTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:PLN02419 195 MNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLpNVS------NGVDTYSIREPLGVCAGICPFNFPAMIPL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAA 262
Cdd:PLN02419 268 WMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARA 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 263 VQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASR-IYVHRSKfaQLANGLADVAQSMKLGAGLDP 341
Cdd:PLN02419 348 AAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDAK--SWEDKLVERAKALKVTCGSEP 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 342 SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAdDLPGY----FVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDD 417
Cdd:PLN02419 426 DADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDI-VVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 418 AADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLD-PSMPFGGYKQSGIG--REFGQYAIEGFTETK 494
Cdd:PLN02419 505 FDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKASFAGdlNFYGKAGVDFFTQIK 584
|
..
gi 981295204 495 SV 496
Cdd:PLN02419 585 LV 586
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
79-500 |
3.16e-64 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 216.43 E-value: 3.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 79 LRPAD-RERILLKLADLIE--RDAETLAQLETLnqGKSIHVSRAIEVGASVEYARYMAG----WATKitgQTLDVSIPFP 151
Cdd:PTZ00381 25 TRPLEfRKQQLRNLLRMLEenKQEFSEAVHKDL--GRHPFETKMTEVLLTVAEIEHLLKhldeYLKP---EKVDTVGVFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 152 PGTrytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELArDAGVPPGVFNVVTGGR 231
Cdd:PTZ00381 100 PGK---SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 232 VCGAALASHPsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASR 311
Cdd:PTZ00381 176 EVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 312 IYVHRSKFAQLANGLadvAQSMKLGAGLDP--SAQINPLVSAHHRDKVVQHIErarRDGLTFLAGGTPadDLPGYFVKPA 389
Cdd:PTZ00381 255 VLVHRSIKDKFIEAL---KEAIKEFFGEDPkkSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGEV--DIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 390 VIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN-C--HIpLDP 466
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCvfHL-LNP 405
|
410 420 430
....*....|....*....|....*....|....
gi 981295204 467 SMPFGGYKQSGIGREFGQYAIEGFTETKSVCIAH 500
Cdd:PTZ00381 406 NLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
37-477 |
1.87e-61 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 210.03 E-value: 1.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 37 RLDVHDPAT-GERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLI--ERDAETLAQLeTLNQGKS 113
Cdd:TIGR01236 47 RIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDA--KKDWSNLPFYDRAAIFLKAADLLsgPYRYEILAAT-MLGQSKT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 114 IHVSRAIEVGASVEYARYMAGWATKITGQTldvSIPFPPGTRYTAYTRKEpvGVVAAIVPWNFPLMIAVWKLIPALAaGC 193
Cdd:TIGR01236 124 VYQAEIDAVAELIDFFRFNVKYARELYAQQ---PISAPGEWNRTEYRPLE--GFVYAISPFNFTAIAGNLAGAPALM-GN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 194 TIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTRF--- 269
Cdd:TIGR01236 198 TVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGdGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYhnf 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 270 ---SLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQIN 346
Cdd:TIGR01236 278 priVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 347 PLVSAHHRDKVVQHIERARRD--GLTFLAGGTpADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDA-----A 419
Cdd:TIGR01236 358 AVIDEQSFDKIVKYIEDAKKDpeALTILYGGK-YDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDkykeiL 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981295204 420 DAVRlaNASPYGLAASIWSNDLKRVMNLVPQIE--AGTVWVN--CHIPLDPSMPFGGYKQSG 477
Cdd:TIGR01236 437 DLVD--STSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
46-477 |
3.85e-60 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 206.28 E-value: 3.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 46 GERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLI--ERDAETLAqLETLNQGKSIHVSraiEVG 123
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIFLKAADLLsgKYRYELNA-ATMLGQGKNVWQA---EID 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 124 ASVEYA---RYMAGWATKITGQTldvsipfPPGTRYTAYTRKE--PV-GVVAAIVPWNFPLMIAVWKLIPALAaGCTIVL 197
Cdd:cd07123 131 AACELIdflRFNVKYAEELYAQQ-------PLSSPAGVWNRLEyrPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLW 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 198 KPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTAT----GKLVGT--AAVQNMTRFS 270
Cdd:cd07123 203 KPSDTAVLSNYLVYKILEEAGLPPGVINFVPGdGPVVGDTVLASPHLAGLHFTGSTPTfkslWKQIGEnlDRYRTYPRIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 271 LELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSAQINPLVS 350
Cdd:cd07123 283 GETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVID 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 351 AHHRDKVVQHIERARRD-GLTFLAGGTpADDLPGYFVKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDA--ADAVRLAN- 426
Cdd:cd07123 363 EKAFDRIKGYIDHAKSDpEAEIIAGGK-CDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDt 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 427 ASPYGLAASIWSNDLK--RVMNLVPQIEAGTVWVNchiplDPS-------MPFGGYKQSG 477
Cdd:cd07123 442 TSPYALTGAIFAQDRKaiREATDALRNAAGNFYIN-----DKPtgavvgqQPFGGARASG 496
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
84-496 |
2.70e-57 |
|
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: 196.57 E-value: 2.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 84 RERILLKLADLIERDAETLaqLETLNQ--GKSIHVSRAIEVG---ASVEYA-RYMAGWAtkitgQTLDVSIP---FPPGt 154
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEI--LEALKKdlGKSEFEAYMTEIGfvlSEINYAiKHLKKWM-----KPKRVKTPllnFPSK- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 155 rytAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAgVPPGVFNVVTGGRVCG 234
Cdd:cd07136 94 ---SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEEN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 235 AALASHPsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYV 314
Cdd:cd07136 170 QELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 315 HRSKFAQLANGLADVAQSMKlgaGLDPsaQINP----LVSAHHRDKVVQHIErarrDGLTFLAGGTPADDLpgyFVKPAV 390
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFY---GEDP--LESPdygrIINEKHFDRLAGLLD----NGKIVFGGNTDRETL---YIEPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 391 IADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSND---LKRVMNlvpQIEAGTVWVN---CHIpL 464
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDkkvEKKVLE---NLSFGGGCINdtiMHL-A 392
|
410 420 430
....*....|....*....|....*....|..
gi 981295204 465 DPSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07136 393 NPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
40-479 |
1.05e-55 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 200.81 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 40 VHDPATGER-LASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSR 118
Cdd:PRK11904 566 VVSPADRRRvVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 119 AiEVGASVEYARYMAGWATKITGQTldVSIPFPPGTRYTAytRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLK 198
Cdd:PRK11904 644 A-EVREAVDFCRYYAAQARRLFGAP--EKLPGPTGESNEL--RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAK 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 199 PSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVgtaavqNMTR--------- 268
Cdd:PRK11904 719 PAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARII------NRTLaardgpivp 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 269 FSLELGGKNpiVMLddVDvAQAL-----DGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDPSA 343
Cdd:PRK11904 793 LIAETGGQN--AMI--VD-STALpeqvvDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLST 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 344 QINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSaiVRDEVFGPVIVVLPFdDAADAVR 423
Cdd:PRK11904 868 DVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQ--LEREVFGPILHVIRY-KASDLDK 944
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 424 LA---NASPYGLAASIWS-ND--LKRVMNLVPqieAGTVWVNchipldPSM--------PFGGYKQSGIG 479
Cdd:PRK11904 945 VIdaiNATGYGLTLGIHSrIEetADRIADRVR---VGNVYVN------RNQigavvgvqPFGGQGLSGTG 1005
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
18-483 |
3.17e-54 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 190.05 E-value: 3.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 18 ARDFGLFIDGEMQPAHAVarLDVHDPATGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIER 97
Cdd:PLN02315 18 SRNLGCYVGGEWRANGPL--VSSVNPANNQPIAEVVEASLEDYEEGLRACEEA--AKIWMQVPAPKRGEIVRQIGDALRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 98 DAETLAQLETLNQGKsIHVSRAIEVGASVEYARYMAGWATKITGQTLDVSIPfppgtRYTAYTRKEPVGVVAAIVPWNFP 177
Cdd:PLN02315 94 KLDYLGRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERP-----NHMMMEVWNPLGIVGVITAFNFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 178 LMIAVWKLIPALAAGCTIVLKPSPETPLTALRL----AELARDAGVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTA 253
Cdd:PLN02315 168 CAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 254 TGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSM 333
Cdd:PLN02315 248 VGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 334 KLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTpADDLPGYFVKPAVIaDPRPDSAIVRDEVFGPVIVVL 413
Cdd:PLN02315 328 KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGS-AIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVM 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981295204 414 PFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPSM---PFGGYKQSGIGREFG 483
Cdd:PLN02315 406 KFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEiggAFGGEKATGGGREAG 478
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-498 |
3.33e-53 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 186.89 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 21 FGLFIDGEMQPAHAVARLDVHDPATGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAE 100
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 101 TLAQLETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQ-TLDVSIPFPpGTRYTAY--TRKEPVGVVAAIVPWNFP 177
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVT-EVVRSGDLISYTAEEGVRILGEgKFLVSDSFP-GNERNKYclTSKIPLGVVLAIPPFNYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 178 LMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTaTGK 256
Cdd:PLN00412 172 VNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGGD-TGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 257 LVGTAAvqNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLG 336
Cdd:PLN00412 251 AISKKA--GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 337 AGLDpSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLpgyfVKPAVIADPRPDSAIVRDEVFGPVIVVLPFD 416
Cdd:PLN00412 329 PPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNL----IWPLLLDNVRPDMRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 417 DAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHIPLDPS-MPFGGYKQSGIGREFGQYAIEGFTETKS 495
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKS 483
|
...
gi 981295204 496 VCI 498
Cdd:PLN00412 484 TVI 486
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
26-483 |
6.33e-53 |
|
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: 186.27 E-value: 6.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 26 DGEMQPAHAVARldvHDPATGErlasVADADEHDVEQAVASAKRAFDarVWSGLRPADRERILLKLADLIERDAETLAQL 105
Cdd:TIGR01238 49 DGEAQPVTNPAD---RRDIVGQ----VFHANLAHVQAAIDSAQQAFP--TWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 106 ETLNQGKSIHVSRAiEVGASVEYARYMAGWATKITGQTldvsipfppgtrytaytRKEPVGVVAAIVPWNFPLMIAVWKL 185
Cdd:TIGR01238 120 CVREAGKTIHNAIA-EVREAVDFCRYYAKQVRDVLGEF-----------------SVESRGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 186 IPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQ 264
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGrGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 265 ---NMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQLANGLADVAQSMKLGAGLDP 341
Cdd:TIGR01238 262 redAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 342 SAQINPLVSAHHRDKVVQHIERARRDGLTFlAGGTPADDLP---GYFVKPAVIAdpRPDSAIVRDEVFGPVIVVLPF--D 416
Cdd:TIGR01238 342 TTDVGPVIDAEAKQNLLAHIEHMSQTQKKI-AQLTLDDSRAcqhGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYkaR 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981295204 417 DAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHI--PLDPSMPFGGYKQSGIGREFG 483
Cdd:TIGR01238 419 ELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQvgAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
25-479 |
7.67e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 189.76 E-value: 7.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 25 IDGEMQPAHAVArldVHDPATGERLA-SVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLA 103
Cdd:COG4230 562 IAGEAASGEARP---VRNPADHSDVVgTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 104 QLETLNQGKSIhvSRAI-EVGASVEYARYMAGWATKITGQTldvsipfppgtrytayTRKEPVGVVAAIVPWNFPLMIAV 182
Cdd:COG4230 637 ALLVREAGKTL--PDAIaEVREAVDFCRYYAAQARRLFAAP----------------TVLRGRGVFVCISPWNFPLAIFT 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 183 WKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTA 261
Cdd:COG4230 699 GQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRT 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 262 AVQNMTR---FSLELGGKNpiVMLddVD----VAQALDGVAAGAFFNQGQVCAAAsRI-YVHRSKFAQLANGLADVAQSM 333
Cdd:COG4230 779 LAARDGPivpLIAETGGQN--AMI--VDssalPEQVVDDVLASAFDSAGQRCSAL-RVlCVQEDIADRVLEMLKGAMAEL 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 334 KLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPGYFVKPAVIADPRPDSaiVRDEVFGPVIVVL 413
Cdd:COG4230 854 RVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISD--LEREVFGPVLHVV 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981295204 414 PF-----DDAADAVrlaNASPYGLAASIWS-NDlKRVMNLVPQIEAGTVWVNCHI--PLDPSMPFGGYKQSGIG 479
Cdd:COG4230 932 RYkadelDKVIDAI---NATGYGLTLGVHSrID-ETIDRVAARARVGNVYVNRNIigAVVGVQPFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
36-479 |
5.70e-51 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 187.38 E-value: 5.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 36 ARLDVHDPA-TGERLASVADADEHDVEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSi 114
Cdd:PRK11905 567 GTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELFALAVREAGKT- 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 115 hVSRAI-EVGASVEYARYMAGWATkitgqtldvsipfppgtRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGC 193
Cdd:PRK11905 644 -LANAIaEVREAVDFLRYYAAQAR-----------------RLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGN 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 194 TIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGTAAVQNMTR---F 269
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpL 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 270 SLELGGKNpiVMLddVD----VAQALDGVAAGAFFNQGQVCAAASRIYVHRskfaqlanglaDVAQS---MKLGA----- 337
Cdd:PRK11905 786 IAETGGQN--AMI--VDssalPEQVVADVIASAFDSAGQRCSALRVLCLQE-----------DVADRvltMLKGAmdelr 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 338 -GlDP---SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPGYFVKPAVIAdpRPDSAIVRDEVFGPVIVVL 413
Cdd:PRK11905 851 iG-DPwrlSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVV 927
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 414 PFD-DAADAVRLA-NASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHI--PLDPSMPFGGYKQSGIG 479
Cdd:PRK11905 928 RFKaDELDRVIDDiNATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIigAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
157-496 |
1.12e-50 |
|
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: 178.95 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 157 TAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELardagVP----PGVFNVVTGGRV 232
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPkyldKECYPVVLGGVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 233 CGAALASHpSISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRI 312
Cdd:cd07132 168 ETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 313 YVH---RSKFAQLANgladvaQSMKLGAGLDP--SAQINPLVSAHHRDKVVQHIErarrdGLTFLAGGT--PADDlpgyF 385
Cdd:cd07132 247 LCTpevQEKFVEALK------KTLKEFYGEDPkeSPDYGRIINDRHFQRLKKLLS-----GGKVAIGGQtdEKER----Y 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 386 VKPAVIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN---CHI 462
Cdd:cd07132 312 IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtiMHY 391
|
330 340 350
....*....|....*....|....*....|....
gi 981295204 463 PLDpSMPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:cd07132 392 TLD-SLPFGGVGNSGMGAYHGKYSFDTFSHKRSC 424
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
163-496 |
2.94e-47 |
|
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: 169.51 E-value: 2.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 163 EPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELArDAGVPPGVFNVVTGGRVCGAALASHpS 242
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEGGVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 243 ISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAF-FNQGQVCAAASRIYVHRSKFAQ 321
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 322 LANGLADVAQSMklgAGLDP--SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLpgyFVKPAVIADPRPDSA 399
Cdd:cd07137 258 LIDALKNTLEKF---FGENPkeSKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNL---YIEPTILLDPPLDSS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 400 IVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN---CHIpLDPSMPFGGYKQS 476
Cdd:cd07137 332 IMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtvVQY-AIDTLPFGGVGES 410
|
330 340
....*....|....*....|
gi 981295204 477 GIGREFGQYAIEGFTETKSV 496
Cdd:cd07137 411 GFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
30-479 |
3.60e-41 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 158.21 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 30 QPAHAVARLDVHDPA-TGERLASVADADEHDVEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLAQLETL 108
Cdd:PRK11809 653 DPVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNA--APIWFATPPAERAAILERAADLMEAQMQTLMGLLVR 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 109 NQGKSIhvSRAI-EVGASVEYARYMAGwatkitgQTLDvsiPFPPGTRytaytrkEPVGVVAAIVPWNFPLMIAVWKLIP 187
Cdd:PRK11809 731 EAGKTF--SNAIaEVREAVDFLRYYAG-------QVRD---DFDNDTH-------RPLGPVVCISPWNFPLAIFTGQVAA 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 188 ALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGKLVGtaavQNM 266
Cdd:PRK11809 792 ALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGrGETVGAALVADARVRGVMFTGSTEVARLLQ----RNL 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 267 -TRFS---------LELGGKNPIVmlddVDVA----QALDGVAAGAFFNQGQVCAAAsRIYVhrskfaqLANGLADVAQS 332
Cdd:PRK11809 868 aGRLDpqgrpipliAETGGQNAMI----VDSSalteQVVADVLASAFDSAGQRCSAL-RVLC-------LQDDVADRTLK 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 333 MKLGA------GlDP---SAQINPLVSAHHRDKVVQHIERARRDGLTF--LAGGTPADDLPGYFVKPAVIADPRPDSaiV 401
Cdd:PRK11809 936 MLRGAmaecrmG-NPdrlSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqAARENSEDWQSGTFVPPTLIELDSFDE--L 1012
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 402 RDEVFGPVIVVLPF--DDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHI--PLDPSMPFGGYKQSG 477
Cdd:PRK11809 1013 KREVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMvgAVVGVQPFGGEGLSG 1092
|
..
gi 981295204 478 IG 479
Cdd:PRK11809 1093 TG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
163-496 |
1.21e-38 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 146.80 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 163 EPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAelardAGVP----PGVFNVVTGGRVCGAALA 238
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPkyldSKAVKVIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 239 SHPsISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVmLDDVDVAQ----ALDGVAAGAFFN-QGQVCAAASRIY 313
Cdd:PLN02203 182 QHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCI-VDSLSSSRdtkvAVNRIVGGKWGScAGQACIAIDYVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 314 VHRsKFAQLangLADVAQSM-KLGAGLDP--SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLpgyFVKPAV 390
Cdd:PLN02203 260 VEE-RFAPI---LIELLKSTiKKFFGENPreSKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKL---FIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 391 IADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVNCHI---PLDpS 467
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIiqyACD-S 411
|
330 340
....*....|....*....|....*....
gi 981295204 468 MPFGGYKQSGIGREFGQYAIEGFTETKSV 496
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
62-459 |
6.56e-37 |
|
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: 141.22 E-value: 6.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 62 QAVASAKRAfDARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAIEVGASVEYARYMAGWATKITG 141
Cdd:cd07084 2 ERALLAADI-STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 142 QTLDvsiPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAG-VP 220
Cdd:cd07084 81 EPGN---HLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 221 PGVFNVVTGGRVCGAALASHPSISKISFTGSTATGKLVGTAAVQnmTRFSLELGGKNPIVMLDDVD-VAQALDGVAAGAF 299
Cdd:cd07084 158 PEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 300 FNQGQVCAAASRIYVHR--SKFAQLANGLADVAQSMKLGAgldpsaqinpLVSAHHRDKVVQHIERARRDGLTFLAGGT- 376
Cdd:cd07084 236 ACSGQKCTAQSMLFVPEnwSKTPLVEKLKALLARRKLEDL----------LLGPVQTFTTLAMIAHMENLLGSVLLFSGk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 377 -----PADDLPGYFVKPAVIADPRPDSA---IVRDEVFGPVIVVLPFDD--AADAVRLANASPYGLAASIWSNDLKRVMN 446
Cdd:cd07084 306 elknhSIPSIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDPIFLQE 385
|
410
....*....|....
gi 981295204 447 LVPQIE-AGTVWVN 459
Cdd:cd07084 386 LIGNLWvAGRTYAI 399
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
163-496 |
8.61e-34 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 133.25 E-value: 8.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 163 EPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAgVPPGVFNVVTGGRVCGAALASHpS 242
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ-K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 243 ISKISFTGSTATGKLVGTAAVQNMTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAF-FNQGQVCAAASRIYVHRSKFAQ 321
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 322 LANGLadvAQSMKLGAGLDP--SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPADDLPgyfVKPAVIADPRPDSA 399
Cdd:PLN02174 269 VIDAM---KKELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLK---IAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 400 IVRDEVFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQIEAGTVWVN---CHIPLDpSMPFGGYKQS 476
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALH-TLPFGGVGES 421
|
330 340
....*....|....*....|
gi 981295204 477 GIGREFGQYAIEGFTETKSV 496
Cdd:PLN02174 422 GMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
60-459 |
1.03e-27 |
|
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: 115.33 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 60 VEQAVASAKRAFDArvWSGLRPADRERILLKLADLIERDAETL---AQLET-----LNQGksihvsraiEVGASVEYARY 131
Cdd:cd07129 1 VDAAAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELvarAHAETglpeaRLQG---------ELGRTTGQLRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 132 MAgwATKITGQTLDVSIPFPPGTRYTA-----YTRKEPVGVVAAIVPWNFPLMIAVW--KLIPALAAGCTIVLKPSPETP 204
Cdd:cd07129 70 FA--DLVREGSWLDARIDPADPDRQPLprpdlRRMLVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAHPAHP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 205 LTALRLAELARDA----GVPPGVFNVVTG-GRVCGAALASHPSISKISFTGSTATGK-LVGTAAvqnmTR-----FSLEL 273
Cdd:cd07129 148 GTSELVARAIRAAlratGLPAGVFSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAA----ARpepipFYAEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 274 GGKNPIVMLDD---VDVAQALDGVAAGAFFNQGQVCAAASRIYVHRSkfAQLANGLADVAQSMklgAGLDPSAQINPLVS 350
Cdd:cd07129 224 GSVNPVFILPGalaERGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAG--PAGDAFIAALAEAL---AAAPAQTMLTPGIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 351 AHHRDKVVQhieRARRDGLTFLAGGTPADDlpGYFVKPAV--------IADPrpdsaIVRDEVFGPVIVVLPFDDAADAV 422
Cdd:cd07129 299 EAYRQGVEA---LAAAPGVRVLAGGAAAEG--GNQAAPTLfkvdaaafLADP-----ALQEEVFGPASLVVRYDDAAELL 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 981295204 423 RLANASPYGLAASIWS--NDLKRVMNLVPQIE--AGTVWVN 459
Cdd:cd07129 369 AVAEALEGQLTATIHGeeDDLALARELLPVLErkAGRLLFN 409
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
41-440 |
1.72e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 115.57 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 41 HDPATGERLASVaDADEHDVEQAVASAkRAFDARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGK-----SIH 115
Cdd:PRK11903 24 FDPVTGEELVRV-SATGLDLAAAFAFA-REQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTtrndsAVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 116 VSRAI-------EVGASVEYARYMA-GWATKITGQTLDVSIPFPPGTRytaytrkepvGVVAAIVPWNFPLMiAVW-KLI 186
Cdd:PRK11903 102 IDGGIftlgyyaKLGAALGDARLLRdGEAVQLGKDPAFQGQHVLVPTR----------GVALFINAFNFPAW-GLWeKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 187 PALAAGCTIVLKPSPETPLTALRLAELARDAGV-PPGVFNVVTGGrvcGAALASH-PSISKISFTGSTATGKLVGT--AA 262
Cdd:PRK11903 171 PALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGS---SAGLLDHlQPFDVVSFTGSAETAAVLRShpAV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 263 VQNMTRFSLELGGKNPIVMLDDVdvaqALDGVAAGAFFNQ---------GQVCAAASRIYVHRSKFAQLANGLADVAQSM 333
Cdd:PRK11903 248 VQRSVRVNVEADSLNSALLGPDA----APGSEAFDLFVKEvvremtvksGQKCTAIRRIFVPEALYDAVAEALAARLAKT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 334 KLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGT----PADDLPGYFVKPAVIADPRPDSA-IVRD-EVFG 407
Cdd:PRK11903 324 TVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvDADPAVAACVGPTLLGASDPDAAtAVHDvEVFG 403
|
410 420 430
....*....|....*....|....*....|...
gi 981295204 408 PVIVVLPFDDAADAVRLANASPYGLAASIWSND 440
Cdd:PRK11903 404 PVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
39-451 |
1.52e-22 |
|
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: 100.42 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 39 DVHDPATGERLASVaDADEHDVEQAVASAkRAFDARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSR 118
Cdd:cd07128 18 TLHDAVTGEVVARV-SSEGLDFAAAVAYA-REKGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAATGATRRDSWI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 119 AIEVGASVEYArYMAGWATKITGQTL---DVSIPFPPGTRYTA---YTRKEpvGVVAAIVPWNFPlmiaVW----KLIPA 188
Cdd:cd07128 96 DIDGGIGTLFA-YASLGRRELPNAHFlveGDVEPLSKDGTFVGqhiLTPRR--GVAVHINAFNFP----VWgmleKFAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 189 LAAGCTIVLKPSPETPLTALRLAELARDAGV-PPGVFNVVTGGrvCGAALASHPSISKISFTGSTATGKLVGT--AAVQN 265
Cdd:cd07128 169 LLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS--VGDLLDHLGEQDVVAFTGSAATAAKLRAhpNIVAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 266 MTRFSLELGGKNPIVMLDDV------------DVAQALDGVAagaffnqGQVCAAASRIYVHRSKFAQLANGLADVAQSM 333
Cdd:cd07128 247 SIRFNAEADSLNAAILGPDAtpgtpefdlfvkEVAREMTVKA-------GQKCTAIRRAFVPEARVDAVIEALKARLAKV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 334 KLGAGLDPSAQINPLVSAHHRDKVVQHIERARRDGLtfLAGGTP-------ADDLPGYFVKPAVI--ADPRPDSAIVRDE 404
Cdd:cd07128 320 VVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAE--VVFGGPdrfevvgADAEKGAFFPPTLLlcDDPDAATAVHDVE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 981295204 405 VFGPVIVVLPFDDAADAVRLANASPYGLAASIWSNDLKRVMNLVPQI 451
Cdd:cd07128 398 AFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
164-428 |
2.90e-13 |
|
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: 72.13 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 164 PVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELAR----DAGVPPGVFNVV--TGGRVCGAAL 237
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTLAadTPEEPIAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 238 ASHPSISKISFTGSTATGKLVGTAAVQnmTRFSLELGGKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAAASRIYVHRS 317
Cdd:cd07127 273 ATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 318 --KFAQLANGLADVAQSmkLGAGLDP----SAQINPLVSAHHRDKVVQHIERARRDGLTFLAGGTPAD-DLPGYFVK-PA 389
Cdd:cd07127 351 giQTDDGRKSFDEVAAD--LAAAIDGlladPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHpEFPDARVRtPL 428
|
250 260 270
....*....|....*....|....*....|....*....
gi 981295204 390 VIADPRPDSAIVRDEVFGPVIVVLPFDDAADAVRLANAS 428
Cdd:cd07127 429 LLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARES 467
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
164-442 |
3.09e-10 |
|
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: 62.13 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 164 PVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDAGVPPGVFNVVTGGRVCGAALASHPSI 243
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 244 SKISFTGSTATGKlvgtaavqnmtRFSLELGGKnpiVMLDDV---------DVaQALDGVA----AGAFFNQGQVCAAAS 310
Cdd:cd07126 222 RMTLFTGSSKVAE-----------RLALELHGK---VKLEDAgfdwkilgpDV-SDVDYVAwqcdQDAYACSGQKCSAQS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 311 RIYVHRSKF-AQLANGLADVAQSMKLgagldPSAQINPLVSAHHRdKVVQHIER-ARRDGLTFLAGGTPADD-------- 380
Cdd:cd07126 287 ILFAHENWVqAGILDKLKALAEQRKL-----EDLTIGPVLTWTTE-RILDHVDKlLAIPGAKVLFGGKPLTNhsipsiyg 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981295204 381 --LP-GYFVKPAVIADPRpDSAIVRDEVFGPVIVVLPFDDAADAVRLANAS--PYGLAASIWSNDLK 442
Cdd:cd07126 361 ayEPtAVFVPLEEIAIEE-NFELVTTEVFGPFQVVTEYKDEQLPLVLEALErmHAHLTAAVVSNDIR 426
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
65-322 |
1.33e-09 |
|
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: 59.93 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 65 ASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAI----------EVGASVEYARYMAG 134
Cdd:cd07077 1 ESAKNA--QRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANwiammgcsesKLYKNIDTERGITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 135 WATKITGQTLdvsipfppGTRYTAYTRKEPVGVVAAIVPWNFPLMiAVWKLIPALAAGCTIVLKPSPETPLTALRLAELA 214
Cdd:cd07077 79 SVGHIQDVLL--------PDNGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTNRALALLF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 215 RDA----GVPPGVFNVVTGGRVCGAALASHPSISKISFTGSTAtgkLVGTAAVQNMTRFSLELGGKNPIVMLDD-VDVAQ 289
Cdd:cd07077 150 QAAdaahGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRD---AVDAAVKHSPHIPVIGFGAGNSPVVVDEtADEER 226
|
250 260 270
....*....|....*....|....*....|...
gi 981295204 290 ALDGVAAGAFFNQgQVCAAASRIYVHRSKFAQL 322
Cdd:cd07077 227 ASGSVHDSKFFDQ-NACASEQNLYVVDDVLDPL 258
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
60-317 |
1.39e-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: 56.89 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 60 VEQAVASAKRAfdARVWSGLRPADRERILLKLADLIERDAETLAQLETLNQGKSIHVSRAIEvgaSVEYARYMAG-WATK 138
Cdd:cd07081 1 LDDAVAAAKVA--QQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIK---NHFAAEYIYNvYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 139 ITGQTLDVSIPFppGTrytaYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDA- 217
Cdd:cd07081 76 KTCGVLTGDENG--GT----LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 218 ---GVPPGVFNVVTGGRV-CGAALASHPSISKISFTGSTATGKlvgtaAVQNMTRFSLELGGKNPIVMLDD-VDVAQALD 292
Cdd:cd07081 150 vaaGAPENLIGWIDNPSIeLAQRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPAIGVGAGNTPVVIDEtADIKRAVQ 224
|
250 260
....*....|....*....|....*
gi 981295204 293 GVAAGAFFNQGQVCAAASRIYVHRS 317
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDS 249
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
163-347 |
5.26e-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: 52.11 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 163 EPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDA----GVPPGVFNVVTGGRVCGA-AL 237
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEPSIELTqEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 238 ASHPSISKISFTGSTAtgkLV------GTAAvqnmtrfsleLG---GKNPIVMLDDVDVAQALDGVAAGAFFNQGQVCAA 308
Cdd:cd07122 174 MKHPDVDLILATGGPG---MVkaayssGKPA----------IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 981295204 309 ASRIYVHRSKFAQL-----ANG--LADVAQSMKLGAGL-DPSAQINP 347
Cdd:cd07122 241 EQSVIVDDEIYDEVraelkRRGayFLNEEEKEKLEKALfDDGGTLNP 287
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
59-322 |
6.95e-05 |
|
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: 45.31 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 59 DVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQL---ETlnqgksiHVSRaieVGASVEYARYMAgw 135
Cdd:cd07121 5 TVDDAVAAAKAAQ--KQYRKCTLADREKIIEAIREALLSNAEELAEMaveET-------GMGR---VEDKIAKNHLAA-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 136 atKITGQTLDVSIPFPPGTRYTAYTRKEPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAEL-- 213
Cdd:cd07121 71 --EKTPGTEDLTTTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELin 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 214 --ARDAGVPPGVFNVVTGGRV-CGAALASHPSISKISFTGstatGKLVGTAAVQNMTRfSLELGGKNPIVMLDDV-DVAQ 289
Cdd:cd07121 149 kaIAEAGGPDNLVVTVEEPTIeTTNELMAHPDINLLVVTG----GPAVVKAALSSGKK-AIGAGAGNPPVVVDETaDIEK 223
|
250 260 270
....*....|....*....|....*....|...
gi 981295204 290 ALDGVAAGAFFNQGQVCAAASRIYVHRSKFAQL 322
Cdd:cd07121 224 AARDIVQGASFDNNLPCIAEKEVIAVDSVADYL 256
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
151-426 |
3.42e-04 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 43.03 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 151 PPGTryTAYTRKEPVGVVAAIVPWNFPLmIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDagvppgvfnvvtgg 230
Cdd:cd07080 101 PPGR--GGYIRAQPRGLVVHIIAGNVPL-LPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLAD-------------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 231 rvcgaALASHP---SISKISFTGSTAT--GKLV----------GTAAVQNMTRFS------LELGGKNPIVMLDD----- 284
Cdd:cd07080 164 -----VDPNHPltdSISVVYWPGGDAEleERILasadavvawgGEEAVKAIRSLLppgcrlIDFGPKYSFAVIDReales 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 285 VDVAQALDGVAAG-AFFNQgQVCAAASRIYVHRSKFA-------QLANGLADVAqsmKLGAGLDPSAQINPLvsahhrdk 356
Cdd:cd07080 239 EKLAEVADALAEDiCRYDQ-QACSSPQVVFVEKDDDEelrefaeALAAALERLP---RRYPALSLSAAESAK-------- 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981295204 357 vvqhIERARRDG-LTFLAGGTPADDlpGYFVkpaVIADPRPDSAivrdEVFGPVIVVLPFDDAADAVRLAN 426
Cdd:cd07080 307 ----IARARLEAeFYELKGGVSRDL--GWTV---IISDEIGLEA----SPLNRTVNVKPVASLDDVLRPVT 364
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
59-308 |
7.98e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.81 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 59 DVEQAVASAKRAFdaRVWSGLRPADRERILLKLADLIERDAETLAQLEtlnqgksihvsrAIEVGasveyaryMAGWATK 138
Cdd:PRK15398 37 SVDDAVAAAKVAQ--QRYQQKSLAMRQRIIDAIREALLPHAEELAELA------------VEETG--------MGRVEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 139 ItgQTLDVSIPFPPGT---RYTAYTRKE--------PVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTA 207
Cdd:PRK15398 95 I--AKNVAAAEKTPGVedlTTEALTGDNgltlieyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 208 LRLAEL----ARDAGvppGVFNVVTGGRV----CGAALASHPSISKISFTGSTA-------TGKLVGTAavqnmtrfsle 272
Cdd:PRK15398 173 LRAIELlneaIVAAG---GPENLVVTVAEptieTAQRLMKHPGIALLVVTGGPAvvkaamkSGKKAIGA----------- 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 981295204 273 lGGKNPIVMLDD-VDVAQALDGVAAGAFFNQGQVCAA 308
Cdd:PRK15398 239 -GAGNPPVVVDEtADIEKAARDIVKGASFDNNLPCIA 274
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
163-250 |
7.06e-03 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 39.01 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981295204 163 EPVGVVAAIVPWNFPLMIAVWKLIPALAAGCTIVLKPSPETPLTALRLAELARDA----GVPPGVFNVV-------TGgr 231
Cdd:PRK13805 107 EPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAavaaGAPKDIIQWIeepsvelTN-- 184
|
90
....*....|....*....
gi 981295204 232 vcgaALASHPSISKISFTG 250
Cdd:PRK13805 185 ----ALMNHPGIALILATG 199
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