|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
21-497 |
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: 606.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 21 ERPKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMARLADLVNA 99
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 100 NLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLalqGDPFHCYTLRQPLGVAAGIIPWNYPFAQ 179
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPI---DGNFLAYTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 180 ASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIA 259
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 260 QAAT-GNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPG 338
Cdd:cd07091 238 EAAAkSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 339 LDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPD 418
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2734213326 419 KIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
21-499 |
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: 596.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 21 ERPKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFdGVWRDMAPAGRAALMARLADLVNAN 100
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF-PAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 101 LEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSYNLALQGdpFHCYTLRQPLGVAAGIIPWNYPFAQA 180
Cdd:COG1012 82 REELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDAPG--TRAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 181 SFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQ 260
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 261 AATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLD 340
Cdd:COG1012 239 AAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 341 PNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI-GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDK 419
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 420 IPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVF-DPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIR 498
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 2734213326 499 L 499
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
34-495 |
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: 559.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 34 TAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTG 113
Cdd:pfam00171 2 VDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA-WRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 114 KPVSMARAlDIPFAAEIYRYYAGWATKLEGRSynlaLQGDP-FHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGC 192
Cdd:pfam00171 81 KPLAEARG-EVDRAIDVLRYYAGLARRLDGET----LPSDPgRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 193 TVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLE 272
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 273 LGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEA 352
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 353 QQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLA 432
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 433 ASIWTRDLSRAHRLARSINAGAIWINCFGVFDP-NLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
45-497 |
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: 537.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARALDI 124
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG-WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNlalQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPL 204
Cdd:cd07093 82 PRAAANFRFFADYILQLDGESYP---QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 205 TALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFAD 284
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 285 ADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQG 364
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 365 KRDGAHVAVGGARIGNS----GYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDL 440
Cdd:cd07093 319 RAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 441 SRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
26-498 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 534.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAF--DGVWRDMAPAGRAALMARLADLVNANLEE 103
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklGSPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 104 LAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSynLALQGDpFHCYTLRQPLGVAAGIIPWNYPFAQASFK 183
Cdd:cd07141 89 LASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKT--IPMDGD-FFTYTRHEPVGVCGQIIPWNFPLLMAAWK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 184 IAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAA- 262
Cdd:cd07141 166 LAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 263 TGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPN 342
Cdd:cd07141 246 KSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 343 SEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPS 422
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIE 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 423 VANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIR 498
Cdd:cd07141 406 RANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
43-497 |
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: 533.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 43 TEDPATGRTIVEVAEAGAADVDAAVAAARSAF-DGVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARA 121
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 122 LdIPFAAEIYRYYAGWATKLEGRSynLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQ 201
Cdd:cd07114 81 Q-VRYLAEWYRYYAGLADKIEGAV--IPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 202 TPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVI 281
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 282 FADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFV 361
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 362 EQGKRDGAHVAVGGARIG----NSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWT 437
Cdd:cd07114 318 ARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 438 RDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
38-497 |
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: 526.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 38 GKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAF-DGVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPV 116
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 117 SMARALDIPFAAEIYRYYAGWATKLEGrsyNLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLL 196
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYG---EVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 197 KPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQ-AATGNLKRVTLELGG 275
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEySGQSNLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 276 KSPNVIFADA-DLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQ 354
Cdd:cd07112 238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 355 RRVTDFVEQGKRDGAHVAVGG--ARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLA 432
Cdd:cd07112 318 DKVLGYIESGKAEGARLVAGGkrVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2734213326 433 ASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07112 398 ASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
43-499 |
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: 523.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 43 TEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAL 122
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA-WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 123 DIPFAAEIYRYYAGWATKLEGRSYNLAlqgDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQT 202
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVR---GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 203 PLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIF 282
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 283 ADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVE 362
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 363 QGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSR 442
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 443 AHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
71-497 |
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: 519.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 71 RSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSynLAL 150
Cdd:cd07078 8 RAAFKA-WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEV--IPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 151 QGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFG 230
Cdd:cd07078 84 PDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 231 ETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGS 310
Cdd:cd07078 164 DEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 311 RLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNS-GYFMQPTV 389
Cdd:cd07078 244 RLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 390 LTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVF-DPNLP 468
Cdd:cd07078 324 LTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEPSAP 403
|
410 420
....*....|....*....|....*....
gi 2734213326 469 FGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07078 404 FGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
27-499 |
1.14e-179 |
|
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: 512.63 E-value: 1.14e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSYNLalqGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIA 185
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDV---PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 186 PALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGN 265
Cdd:cd07119 157 PALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 266 LKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEI 345
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 346 GPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNS----GYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIP 421
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2734213326 422 SVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
20-499 |
2.69e-178 |
|
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: 509.26 E-value: 2.69e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 20 LERPKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGVWRDMAPAGRAALMARLADLVNA 99
Cdd:cd07144 4 YDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 100 NLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLalqGDPFHCYTLRQPLGVAAGIIPWNYPFAQ 179
Cdd:cd07144 84 NRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPT---SPNKLAYTLHEPYGVCGQIIPWNYPLAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 180 ASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIA 259
Cdd:cd07144 161 AAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 260 QAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAG-IEQVAANLKVGPG 338
Cdd:cd07144 241 KAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKfVEHVKQNYKVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 339 LDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNS---GYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFD 415
Cdd:cd07144 321 FDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 416 DPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:cd07144 401 TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
....
gi 2734213326 496 TIRL 499
Cdd:cd07144 481 HINL 484
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
22-495 |
1.28e-173 |
|
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: 497.02 E-value: 1.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 22 RPKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMARLADLVNAN 100
Cdd:cd07142 2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDeGPWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 101 LEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGrsynLALQGD-PFHCYTLRQPLGVAAGIIPWNYPFAQ 179
Cdd:cd07142 82 ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHG----MTLPADgPHHVYTLHEPIGVVGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 180 ASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIA 259
Cdd:cd07142 158 FAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 260 Q-AATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPG 338
Cdd:cd07142 238 QlAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 339 LDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPD 418
Cdd:cd07142 318 FRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 419 KIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
44-497 |
3.92e-172 |
|
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: 492.52 E-value: 3.92e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 44 EDPATGRTIVEVAEAGAADVDAAVAAARSAFDGVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlD 123
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 124 IPFAAEIYRYYAGWATKLEGRSYNLalqGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTP 203
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPL---GPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 204 LTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFA 283
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 284 DADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDpNSEIGPLMSEAQQRRVTDFVEQ 363
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 364 GKRDGAHVAVGGARIGN---SGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDL 440
Cdd:cd07109 317 ARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2734213326 441 SRAHRLARSINAGAIWINCF----GVfdpNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYgaggGI---ELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
21-499 |
1.85e-170 |
|
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: 489.35 E-value: 1.85e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 21 ERPKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGVW-RDMAPAGRAALMARLADLVNA 99
Cdd:cd07143 4 EQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWgLKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 100 NLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSynlaLQGDPFH-CYTLRQPLGVAAGIIPWNYPFA 178
Cdd:cd07143 84 NLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQV----IETDIKKlTYTRHEPIGVCGQIIPWNFPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 179 QASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKI 258
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 259 AQAAT-GNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGP 337
Cdd:cd07143 240 MEAAAkSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 338 GLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDP 417
Cdd:cd07143 320 PFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 418 DKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07143 400 EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
..
gi 2734213326 498 RL 499
Cdd:cd07143 480 NL 481
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
18-495 |
2.11e-169 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 487.41 E-value: 2.11e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 18 AFLERPK----ALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMAR 92
Cdd:PLN02766 11 SGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhGPWPRMSGFERGRIMMK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 93 LADLVNANLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLALQgdpFHCYTLRQPLGVAAGIIP 172
Cdd:PLN02766 91 FADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQ---LQGYTLKEPIGVVGHIIP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 173 WNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGST 252
Cdd:PLN02766 168 WNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 253 EIGKKIAQ-AATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAA 331
Cdd:PLN02766 248 EVGRKIMQaAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 332 NLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCA 411
Cdd:PLN02766 328 DWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 412 MPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTE 491
Cdd:PLN02766 408 MKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
....
gi 2734213326 492 QKAV 495
Cdd:PLN02766 488 VKSV 491
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
46-497 |
2.11e-163 |
|
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: 470.28 E-value: 2.11e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 46 PATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDI 124
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDkGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNlALqGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPL 204
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYN-NL-GDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 205 TALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFAD 284
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 285 ADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQG 364
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 365 KRDGAHVAVGGARI-GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRA 443
Cdd:cd07118 321 RAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 444 HRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
44-497 |
4.09e-163 |
|
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: 469.22 E-value: 4.09e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 44 EDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlD 123
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT-WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 124 IPFAAEIYRYYAGWATKLEGRSYNLALQGdpFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTP 203
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGRTIPSPAPG--KRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 204 LTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFA 283
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 284 DADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQ 363
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 364 GKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRA 443
Cdd:cd07103 318 AVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 444 HRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07103 398 WRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
25-498 |
3.32e-162 |
|
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: 468.07 E-value: 3.32e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 25 ALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGVWRDMAPAGRAALMARLADLVNANLEEL 104
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 105 AELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLAL---QGDPFHCYTLRQPLGVAAGIIPWNYPFAQAS 181
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIpsmQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 182 FKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETaGAAITAHRGVDKVSFTGSTEIGKKIAQA 261
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 262 ATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDP 341
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 342 NSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIP 421
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 422 SVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIR 498
Cdd:cd07113 400 QLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
26-496 |
5.16e-160 |
|
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: 461.97 E-value: 5.16e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA-WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARALDIPFAAEIYRYYAG------WATKLEGrsynlALQgdpfhcytLRQPLGVAAGIIPWNYPFAQ 179
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGN-----SLV--------VREPIGVCGLITPWNWPLNQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 180 ASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIA 259
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 260 QAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGL 339
Cdd:cd07138 227 EAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 340 DPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIG---NSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDD 416
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPeglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 417 PDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINcFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVT 496
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
26-497 |
2.24e-159 |
|
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: 460.50 E-value: 2.24e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMARLADLVNANLEEL 104
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 105 AELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLALQGDpfHCYTLRQPLGVAAGIIPWNYPFAQASFKI 184
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGG--HVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 185 APALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGfGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATG 264
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 265 NLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSE 344
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 345 IGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIG--NSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPS 422
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2734213326 423 VANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVfDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
26-499 |
4.84e-159 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 460.15 E-value: 4.84e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVtAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:PRK13473 5 LLINGELV-AGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE-WSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLALQGdpFHCYTLRQPLGVAAGIIPWNYPFAQASFKIA 185
Cdd:PRK13473 83 RLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEG--HTSMIRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 186 PALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGN 265
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 266 LKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEI 345
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 346 GPLMSEAQQRRVTDFVEQGKRDG-AHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVA 424
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2734213326 425 NDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKH 474
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
45-496 |
8.98e-158 |
|
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: 456.04 E-value: 8.98e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMArALDI 124
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPR-WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRS-YNLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTP 203
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAeRAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 204 LTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFA 283
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 284 DADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQ 363
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 364 GKRDGAHVAVGGAR--IGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLS 441
Cdd:cd07110 321 GKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2734213326 442 RAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVT 496
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
45-499 |
1.82e-157 |
|
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: 455.23 E-value: 1.82e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDI 124
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQK-EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV-DI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNLAlqGDPFhCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPL 204
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLP--GGSF-AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 205 TALRLAELVAEAGFPKGVVNVLTGFGETaGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFAD 284
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 285 ADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQG 364
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 365 KRDGAHVAVGGARIG-----NSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRD 439
Cdd:cd07090 317 KQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 440 LSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEM 456
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
26-499 |
1.69e-156 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 453.95 E-value: 1.69e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFdGVWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ-KIWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSynLALQGDPFHcYTLRQPLGVAAGIIPWNYPFAQASFKIA 185
Cdd:PRK13252 88 ALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQ--IPLRGGSFV-YTRREPLGVCAGIGAWNYPIQIACWKSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 186 PALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETaGAAITAHRGVDKVSFTGSTEIGKKIAQAATGN 265
Cdd:PRK13252 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 266 LKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEI 345
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 346 GPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGN----SGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIP 421
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2734213326 422 SVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEM 481
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
44-497 |
3.90e-155 |
|
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: 449.08 E-value: 3.90e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 44 EDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARALD 123
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS-WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 124 IPFAAEIYRYYAGWATKLEGRSYNLALQGdpFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTP 203
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPG--HTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 204 LTALRLAELVAEaGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFA 283
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 284 DADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQ 363
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 364 GKRdGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRA 443
Cdd:cd07092 318 APA-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 444 HRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
26-497 |
2.46e-152 |
|
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: 442.94 E-value: 2.46e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT-WGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLALQgdpFHCYTLRQPLGVAAGIIPWNYPFAQASFKIA 185
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDED---TLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 186 PALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGN 265
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 266 LKRVTLELGGKSPNVIFADA-----DLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLD 340
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 341 PNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI----GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDD 416
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 417 PDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVT 496
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
.
gi 2734213326 497 I 497
Cdd:cd07559 478 V 478
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
44-497 |
1.56e-151 |
|
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: 439.66 E-value: 1.56e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 44 EDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlD 123
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG-WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 124 IPFAAEIYRYYAGWATKLEgrsynLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTP 203
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDE-----VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 204 LTALRLAELVAEAgFPKGVVNVLTGFGEtAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFA 283
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 284 DADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQ 363
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 364 GKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRA 443
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 444 HRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
27-493 |
1.58e-151 |
|
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: 440.79 E-value: 1.58e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFdGVWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ-GEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLalqGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAP 186
Cdd:TIGR01804 80 LETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL---GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 187 ALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNL 266
Cdd:TIGR01804 157 ALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 267 KRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIG 346
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 347 PLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGN----SGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPS 422
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2734213326 423 VANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQK 493
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
13-493 |
3.88e-151 |
|
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: 439.91 E-value: 3.88e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 13 SAAAKAFLE---RPKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAAL 89
Cdd:cd07111 8 AACALAWLDahdRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES-WSALPGHVRARH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 90 MARLADLVNANLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGrsynlALQGdpfhcytlRQPLGVAAG 169
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDT-----ELAG--------WKPVGVVGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 170 IIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETaGAAITAHRGVDKVSFT 249
Cdd:cd07111 154 IVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 250 GSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQV 329
Cdd:cd07111 233 GSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 330 AANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVL 409
Cdd:cd07111 313 MSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 410 CAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAF 489
Cdd:cd07111 393 VVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
....
gi 2734213326 490 TEQK 493
Cdd:cd07111 473 LRPS 476
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
11-495 |
9.28e-150 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 438.86 E-value: 9.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 11 RLSAAAKAfLERP---------KALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRD 80
Cdd:PLN02466 37 RFSTAAAA-VEEPitppvqvsyTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDeGPWPK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 81 MAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGrsynLALQGD-PFHCYT 159
Cdd:PLN02466 116 MTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHG----LTVPADgPHHVQT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 160 LRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITA 239
Cdd:PLN02466 192 LHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALAS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 240 HRGVDKVSFTGSTEIGKKIAQ-AATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSA 318
Cdd:PLN02466 272 HMDVDKLAFTGSTDTGKIVLElAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 319 FDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMA 398
Cdd:PLN02466 352 YDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDML 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 399 VHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWG 478
Cdd:PLN02466 432 IAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIG 511
|
490
....*....|....*..
gi 2734213326 479 REMAREGVEAFTEQKAV 495
Cdd:PLN02466 512 REKGIYSLNNYLQVKAV 528
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
45-495 |
1.83e-148 |
|
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: 432.44 E-value: 1.83e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRdMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARALD 123
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDtGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 124 IPFAAEIYRYYAGWATKLEGrSYNL---ALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAE 200
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPW-EFDLpvpALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 201 QTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNV 280
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 281 IFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDF 360
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 361 VEQGKRDGAHVAVGGARI--GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTR 438
Cdd:cd07089 321 IARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 439 DLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
43-497 |
3.95e-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: 3.95e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 43 TEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAL 122
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPE-WAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 123 DIPFAAEIYRYYAGWATKLEGRSYnlalqgdPFH----CYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKP 198
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETL-------PFGpdvlTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 199 AEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSP 278
Cdd:cd07108 153 AEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 279 NVIFADADLDEAIPAAAMAI-FGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRV 357
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 358 TDFVEQGKR-DGAHVAVGG----ARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLA 432
Cdd:cd07108 312 CGYIDLGLStSGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 433 ASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREG-VEAFTEQKAVTI 497
Cdd:cd07108 392 AYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
26-499 |
5.26e-144 |
|
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: 421.86 E-value: 5.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK-TWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLALQgdpFHCYTLRQPLGVAAGIIPWNYPFAQASFKIA 185
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDED---TLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 186 PALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGN 265
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 266 LKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEI 345
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 346 GPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNS----GYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIP 421
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2734213326 422 SVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
71-497 |
3.34e-143 |
|
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: 415.47 E-value: 3.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 71 RSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSynLAL 150
Cdd:cd06534 4 RAAFKA-WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPE--LPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 151 QGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFG 230
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 231 ETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGS 310
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 311 RLYVERSAFDKvmagieqvaanlkvgpgldpnseigplmseaqqrrvtdFVEQGKrdgahvavggarignsgyfmqpTVL 390
Cdd:cd06534 240 RLLVHESIYDE--------------------------------------FVEKLV----------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 391 TGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVF-DPNLPF 469
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGPEAPF 339
|
410 420
....*....|....*....|....*...
gi 2734213326 470 GGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
20-497 |
6.63e-140 |
|
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: 411.50 E-value: 6.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 20 LERPKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMARLADLVN 98
Cdd:cd07140 2 LKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEnGEWGKMNARDRGRLMYRLADLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 99 ANLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLAlQGDPFH--CYTLRQPLGVAAGIIPWNYP 176
Cdd:cd07140 82 EHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPIN-QARPNRnlTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 177 FAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGK 256
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 257 KIAQ-AATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKV 335
Cdd:cd07140 241 HIMKsCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 336 GPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFD 415
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 416 DPDkIPSV---ANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQ 492
Cdd:cd07140 401 DGD-VDGVlqrANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*
gi 2734213326 493 KAVTI 497
Cdd:cd07140 480 KTVTI 484
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
27-497 |
2.40e-138 |
|
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: 407.04 E-value: 2.40e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA-WERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMARaLDIPFAAEIYRYYAGWATKLEGRsynlALQGDPF--HCYTLRQPLGVAAGIIPWNYPFAQASFKI 184
Cdd:cd07088 80 LIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGE----IIPSDRPneNIFIFKVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 185 APALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATG 264
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 265 NLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSE 344
Cdd:cd07088 235 NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 345 IGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI-GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSV 423
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2734213326 424 ANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGvFDPNLPF-GGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINREN-FEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
78-497 |
4.66e-137 |
|
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: 402.29 E-value: 4.66e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMArALDIPFAAEIYRYYAGWATKLEGRSYNLALQGDPFHC 157
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPRRPEGEILPSDVPGKESMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 158 YtlRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLT-ALRLAELVAEAGFPKGVVNVLTGFGETAGAA 236
Cdd:cd07104 95 R--RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 237 ITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVER 316
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 317 SAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNsgyFMQPTVLTGTTPD 396
Cdd:cd07104 253 SVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGL---FYQPTVLSDVTPD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 397 MAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFD-PNLPFGGMRES 475
Cdd:cd07104 330 MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDePHVPFGGVKAS 409
|
410 420
....*....|....*....|..
gi 2734213326 476 GWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07104 410 GGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
43-499 |
6.99e-136 |
|
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: 400.21 E-value: 6.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 43 TEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAl 122
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE-WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 123 DIPFAAEIYRYYAGWATKLEGRSynLALQGDPFHcYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQT 202
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGET--IPVGGRNLH-YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 203 PLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIF 282
Cdd:cd07107 156 PLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 283 ADADLDEAIPAAAMAI-FGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFV 361
Cdd:cd07107 235 PDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 362 EQGKRDGAHVAVGGAR----IGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWT 437
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2734213326 438 RDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
71-495 |
1.31e-135 |
|
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: 400.09 E-value: 1.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 71 RSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGrsYNLAL 150
Cdd:cd07097 47 AAAFPA-WRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSG--ETLPS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 151 QGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFG 230
Cdd:cd07097 123 TRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 231 ETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGS 310
Cdd:cd07097 203 SEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 311 RLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI--GNSGYFMQPT 388
Cdd:cd07097 283 RLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 389 VLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINC--FGVfDPN 466
Cdd:cd07097 363 LFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptAGV-DYH 441
|
410 420 430
....*....|....*....|....*....|
gi 2734213326 467 LPFGGMRESGWG-REMAREGVEAFTEQKAV 495
Cdd:cd07097 442 VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
23-496 |
7.68e-135 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 399.11 E-value: 7.68e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 23 PKALFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAF----DGVWRDMAPAGRAALMARLADLVN 98
Cdd:PLN02467 7 RRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkGKDWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 99 ANLEELAELEALDTGKPVSMArALDIPFAAEIYRYYAGWATKLEGRSYN-LALQGDPFHCYTLRQPLGVAAGIIPWNYPF 177
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKQKApVSLPMETFKGYVLKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 178 AQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKK 257
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 258 IAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGP 337
Cdd:PLN02467 246 IMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 338 GLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIG--NSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFD 415
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 416 DPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
.
gi 2734213326 496 T 496
Cdd:PLN02467 486 T 486
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
27-497 |
2.00e-132 |
|
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: 392.10 E-value: 2.00e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIV-EVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVgTFPLSTASDVDAAVEAAREAFPE-WRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARAlDIPFAAEIYRYYAGwatklEGRSynlaLQGDPF-------HCYTLRQPLGVAAGIIPWNYPFA 178
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAG-----EGRR----LFGETVpselpnkDAMTRRQPIGVVALITPWNFPVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 179 QASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKI 258
Cdd:cd07131 151 IPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 259 AQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPG 338
Cdd:cd07131 231 GETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 339 LDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI----GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPF 414
Cdd:cd07131 311 LDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 415 DDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVfDPNLPFGGMRESGWG-REMAREGVEAFTE 491
Cdd:cd07131 391 SSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTE 469
|
....*.
gi 2734213326 492 QKAVTI 497
Cdd:cd07131 470 WKAVYV 475
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
26-499 |
7.57e-132 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 391.18 E-value: 7.57e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFD-GVWRDMAPAGRAALMARLADLVNANLEEL 104
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 105 AELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRsynLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKI 184
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGE---VATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 185 APALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQ-AAT 263
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 264 GNLKRVTLELGGKSPNVIFADA-DLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPN 342
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 343 SEIGPLMSEAQQRRVTDFVEQGKRDGAhVAVGGARIGNSGYfMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPS 422
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQ-LLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 423 VANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
45-497 |
1.81e-130 |
|
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: 386.30 E-value: 1.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMArALDI 124
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPA-WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNLALQGDpfHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPL 204
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGT--VSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 205 TALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFAD 284
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 285 ADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQG 364
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 365 KRDGAHVAVGGARIGNsgyFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAH 444
Cdd:cd07150 321 VAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 445 RLARSINAGAIWINCFGVFD-PNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07150 398 KLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
45-497 |
5.45e-129 |
|
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: 382.47 E-value: 5.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARaLDI 124
Cdd:cd07145 5 NPANGEVIDTVPSLSREEVREAIEVAEKAKD-VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR-VEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNL--ALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQT 202
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLRGETIPVdaYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 203 PLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIF 282
Cdd:cd07145 163 PLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 283 ADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVE 362
Cdd:cd07145 243 KDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 363 QGKRDGAHVAVGGARIGnsGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSR 442
Cdd:cd07145 323 DAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 443 AHRLARSINAGAIWINCFGVFDP-NLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07145 401 ALKVARELEAGGVVINDSTRFRWdNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
78-497 |
9.18e-128 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 378.34 E-value: 9.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLegrsynLA---LQGDP 154
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAENAEAF------LAdepIETDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 155 FHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGV-VNVLTGFGETA 233
Cdd:cd07100 88 GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQNLLIDSDQVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 234 gaAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLY 313
Cdd:cd07100 168 --AIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 314 VERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGT 393
Cdd:cd07100 246 VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 394 TPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMR 473
Cdd:cd07100 326 TPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVK 405
|
410 420
....*....|....*....|....
gi 2734213326 474 ESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07100 406 RSGYGRELGRFGIREFVNIKTVWV 429
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
27-495 |
5.79e-125 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 373.64 E-value: 5.79e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP-SWSKLTASERSKILRRWYDLIIANKEDLAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMARAlDIPFAAEIYRYYAGWATklegRSYnlalqGD----PF---HCYTLRQPLGVAAGIIPWNYPFAQ 179
Cdd:PLN02278 107 LMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAK----RVY-----GDiipsPFpdrRLLVLKQPVGVVGAITPWNFPLAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 180 ASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIA 259
Cdd:PLN02278 177 ITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 260 QAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGL 339
Cdd:PLN02278 257 AGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 340 DPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDK 419
Cdd:PLN02278 337 EEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 420 IPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
45-496 |
2.39e-124 |
|
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: 370.91 E-value: 2.39e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDGV-WRDmAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARaLD 123
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDETdWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-FE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 124 IPFAAEIYRYYAGWATKLEGRSynLALQGDPFHCYtLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTP 203
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRM--IEPEPGSFSLV-LREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 204 LTALRLAELVAEA-GFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIF 282
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 283 ADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVE 362
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 363 QGKRDGAHVAVGGARIG---NSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRD 439
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTeglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 440 LSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVT 496
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
45-497 |
6.54e-121 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 361.92 E-value: 6.54e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFdGVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARaLDI 124
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQ-RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKL---EGRSYNLALqgdPFHCYTL-RQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAE 200
Cdd:cd07099 80 LLALEAIDWAARNAPRVlapRKVPTGLLM---PNKKATVeYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 201 QTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAhrGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNV 280
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 281 IFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDF 360
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 361 VEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDL 440
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2734213326 441 SRAHRLARSINAGAIWINCFGVFD--PNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDVLLTAgiPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
45-497 |
1.43e-118 |
|
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: 355.75 E-value: 1.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDI 124
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAK-EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK-EV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNLalQGDPFH----CYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAE 200
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPF--DASPGGegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 201 QTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAAtgNLKRVTLELGGKSPNV 280
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 281 IFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDF 360
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 361 VEQGKRDGAHVAVGGARIGNsgyFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDL 440
Cdd:cd07149 319 VEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2734213326 441 SRAHRLARSINAGAIWINcfgvfDP------NLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07149 396 QKALKAARELEVGGVMIN-----DSstfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
27-480 |
3.54e-118 |
|
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: 355.61 E-value: 3.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA-WGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLALQGDPFHCYtlrQPLGVAAGIIPWNYPFAQASFKIAP 186
Cdd:cd07116 83 AETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFH---EPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 187 ALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNL 266
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 267 KRVTLELGGKSPNVIFA------DADLDEAIPAAAMAIFgNSGQVCNAGSRLYVERSAFDKVMA-GIEQVAAnLKVGPGL 339
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMErALERVKA-IKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 340 DPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGAR-----IGNSGYFMQPTVLTGTtpDMAVHTEEIFGPVLCAMPF 414
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelggLLGGGYYVPTTFKGGN--KMRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 415 DDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGRE 480
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRE 460
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
27-497 |
4.28e-117 |
|
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: 353.02 E-value: 4.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVtAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDM-APAgRAALMARLADLVNANLEELA 105
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK-EWRKVpAPR-RGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARAlDIPFAAEIYRYYAGwatklEGRSynlaLQGDPFHC-------YTLRQPLGVAAGIIPWNYPFA 178
Cdd:cd07086 79 RLVSLEMGKILPEGLG-EVQEMIDICDYAVG-----LSRM----LYGLTIPSerpghrlMEQWNPLGVVGVITAFNFPVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 179 QASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEA----GFPKGVVNVLTGFGEtAGAAITAHRGVDKVSFTGSTEI 254
Cdd:cd07086 149 VPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 255 GKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLK 334
Cdd:cd07086 228 GRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 335 VGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI--GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAM 412
Cdd:cd07086 308 IGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 413 PFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRL--ARSINAGAIWIN--CFGVfDPNLPFGGMRESGWGREMAREGVEA 488
Cdd:cd07086 388 KFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQ 466
|
....*....
gi 2734213326 489 FTEQKAVTI 497
Cdd:cd07086 467 YMRRSTCTI 475
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
45-493 |
3.35e-115 |
|
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: 347.11 E-value: 3.35e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDI 124
Cdd:TIGR01780 3 NPATGEIIGSVPDQGVDETEAAIRAAYEAFK-TWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKG-EI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNlALQGDPFhCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPL 204
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIP-SPQSDKR-LIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 205 TALRLAELVAEAGFPKGVVNVLTG-FGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFA 283
Cdd:TIGR01780 159 SALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 284 DADLDEAIpAAAMAI-FGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVE 362
Cdd:TIGR01780 239 DADLDQAV-EGAMASkFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 363 QGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSR 442
Cdd:TIGR01780 318 DAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2734213326 443 AHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQK 493
Cdd:TIGR01780 398 IWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
72-497 |
5.60e-114 |
|
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: 343.41 E-value: 5.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 72 SAFdGVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARaLDIPFAAEIYRYYAGWATKLEGRSYNLALQ 151
Cdd:cd07105 11 AAF-PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQIIGGSIPSDKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 152 GDpfHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGE 231
Cdd:cd07105 89 GT--LAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 232 TAGA---AITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNA 308
Cdd:cd07105 167 DAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 309 GSRLYVERSAFDKVMAGIEQVAANLKVGPgldpnSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGG-ARIGNSGYFMQP 387
Cdd:cd07105 247 TERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADESPSGTSMPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 388 TVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFD-PN 466
Cdd:cd07105 322 TILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDePT 401
|
410 420 430
....*....|....*....|....*....|.
gi 2734213326 467 LPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07105 402 LPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
30-497 |
4.19e-112 |
|
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: 339.67 E-value: 4.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 30 GDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAfDGVWRDMAPAGRAALMARLADLVNANLEELAELEA 109
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 110 LDTGKPVSMArALDIPFAAEIYRYYAGWATKLEGRSYNLALQGDPFHCYtlRQPLGVAAGIIPWNYPFAQASFKIAPALA 189
Cdd:cd07151 80 RESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVY--REPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 190 AGCTVLLKPAEQTPLTA-LRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKR 268
Cdd:cd07151 157 LGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 269 VTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPL 348
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 349 MSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNsgyFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTR 428
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 429 FGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFD-PNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
5-496 |
7.27e-110 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 336.08 E-value: 7.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 5 TPIIDERLSAAAKAFLERPKALfidgdfVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAfDGVWRDMAPA 84
Cdd:PRK09407 4 TALPMPAPSALTFERLRRLTAR------VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRAWAATPVR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 85 GRAALMARLADLVNANLEELAELEALDTGKPVSMA--RALDIPFAAeiyRYYAGWATK-LEGRSYNLALqgdPFHCYT-- 159
Cdd:PRK09407 77 ERAAVLLRFHDLVLENREELLDLVQLETGKARRHAfeEVLDVALTA---RYYARRAPKlLAPRRRAGAL---PVLTKTte 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 160 LRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITA 239
Cdd:PRK09407 151 LRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 240 HrgVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAF 319
Cdd:PRK09407 231 N--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 320 DKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGG-AR--IGNsgYFMQPTVLTGTTPD 396
Cdd:PRK09407 309 DEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGkARpdLGP--LFYEPTVLTGVTPD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 397 MAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN-----CFGVFDPnlPFGG 471
Cdd:PRK09407 387 MELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVDA--PMGG 464
|
490 500
....*....|....*....|....*
gi 2734213326 472 MRESGWGREMAREGVEAFTEQKAVT 496
Cdd:PRK09407 465 MKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
42-497 |
7.68e-106 |
|
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: 323.23 E-value: 7.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 42 ATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARA 121
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN-RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 122 lDIPFAAEIYRYYAGWATKLEGRSYNLALQ--GDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPA 199
Cdd:cd07094 81 -EVDRAIDTLRLAAEEAERIRGEEIPLDATqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 200 EQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGnlKRVTLELGGKSPN 279
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 280 VIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTD 359
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 360 FVEQGKRDGAHVAVGGARignSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRD 439
Cdd:cd07094 318 WVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2734213326 440 LSRAHRLARSINAGAIWINCFGVFD-PNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRtDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
44-496 |
1.83e-103 |
|
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: 316.94 E-value: 1.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 44 EDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMA--RA 121
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRA-WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAfeEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 122 LDIPFAAeiyRYYAGWATK-LEGRSYNLALqgdPFHCYT--LRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKP 198
Cdd:cd07101 80 LDVAIVA---RYYARRAERlLKPRRRRGAI---PVLTRTtvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 199 AEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHrgVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSP 278
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 279 NVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVT 358
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 359 DFVEQGKRDGAHVAVGG-ARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWT 437
Cdd:cd07101 312 AHVDDAVAKGATVLAGGrARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 438 RDLSRAHRLARSINAGAIWIN-----CFGVFDPnlPFGGMRESGWGREMAREGVEAFTEQKAVT 496
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
27-499 |
6.67e-103 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 316.85 E-value: 6.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP-AWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSYNlALQGDPfHCYTLRQPLGVAAGIIPWNYPFAQASFKIAP 186
Cdd:PRK11241 93 LMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIP-GHQADK-RLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 187 ALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNL 266
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 267 KRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIG 346
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 347 PLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVAND 426
Cdd:PRK11241 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAND 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2734213326 427 TRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTIRL 499
Cdd:PRK11241 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
26-498 |
1.43e-102 |
|
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: 315.61 E-value: 1.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA-WSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGR-SYNLALQGDpfhCYTLRQPLGVAAGIIPWNYPFAQASFKI 184
Cdd:cd07085 82 RLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEyLENVARGID---TYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 185 APALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGfGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATG 264
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 265 NLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSE 344
Cdd:cd07085 237 NGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 345 IGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI----GNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKI 420
Cdd:cd07085 317 MGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 421 PSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINcFGVFDP--NLPFGGMRESGWG--REMAREGVEAFTEQKAVT 496
Cdd:cd07085 397 IAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN-VPIPVPlaFFSFGGWKGSFFGdlHFYGKDGVRFYTQTKTVT 475
|
..
gi 2734213326 497 IR 498
Cdd:cd07085 476 SR 477
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-496 |
6.56e-102 |
|
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: 314.93 E-value: 6.56e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 5 TPIIDERLSAAAKAF---LERPKA-------LFIDGDFVtaKDGKTFATEDPA-TGRTIVEVAEAGAADVDAAVAAARSA 73
Cdd:cd07124 4 EPFTDFADEENRAAFraaLARVREelgreypLVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 74 FDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSynlALQGD 153
Cdd:cd07124 82 FPT-WRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFP---VEMVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 154 PFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETA 233
Cdd:cd07124 157 GEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 234 GAAITAHRGVDKVSFTGSTEIGKKI-AQAATG-----NLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCN 307
Cdd:cd07124 237 GDYLVEHPDVRFIAFTGSREVGLRIyERAAKVqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 308 AGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGaHVAVGGARIGN--SGYFM 385
Cdd:cd07124 317 ACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 386 QPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVF 463
Cdd:cd07124 396 QPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGAL 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 2734213326 464 DPNLPFGGMRESGWGremAREG----VEAFTEQKAVT 496
Cdd:cd07124 476 VGRQPFGGFKMSGTG---SKAGgpdyLLQFMQPKTVT 509
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
46-495 |
2.84e-101 |
|
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: 311.49 E-value: 2.84e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 46 PATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIP 125
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKG-WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 126 FAAEIYRYYAGWATKlegrsynlALQGDP------FHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPA 199
Cdd:cd07102 81 GMLERARYMISIAEE--------ALADIRvpekdgFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 200 EQTPLTALRLAELVAEAGFPKGVVNVLTGFGETaGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPN 279
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 280 VIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTD 359
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 360 FVEQGKRDGAHVAVGGARIGNS---GYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIW 436
Cdd:cd07102 312 QIADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2734213326 437 TRDLSRAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
27-498 |
3.55e-99 |
|
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: 306.81 E-value: 3.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAkDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGVWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMA-----RALD-IPFAAEIYRyyagwatKLEGRSynlaLQGDPFH------CYTLRQPLGVAAGIIPWN 174
Cdd:cd07082 84 LLMWEIGKTLKDAlkevdRTIDyIRDTIEELK-------RLDGDS----LPGDWFPgtkgkiAQVRREPLGVVLAIGPFN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 175 YPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEI 254
Cdd:cd07082 153 YPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 255 GKKIAQAATgnLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLK 334
Cdd:cd07082 233 GNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 335 VGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSgyFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPF 414
Cdd:cd07082 311 VGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 415 DDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCF-----GVFdpnlPFGGMRESGWGREMAREGVEAF 489
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHF----PFLGRKDSGIGTQGIGDALRSM 464
|
....*....
gi 2734213326 490 TEQKAVTIR 498
Cdd:cd07082 465 TRRKGIVIN 473
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
86-497 |
8.25e-99 |
|
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: 305.05 E-value: 8.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 86 RAALMARLADLVNANLEELAELEALDTGKPVSMARaLDIPFAAEIYRYYAGWATKLEGRSY--NLALQGDPFHCYTLRQP 163
Cdd:cd07146 42 RSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVGRAADVLRFAAAEALRDDGESFscDLTANGKARKIFTLREP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 164 LGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGV 243
Cdd:cd07146 121 LGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 244 DKVSFTGSTEIGKKIAQAATGnlKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVM 323
Cdd:cd07146 201 DLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 324 AGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARignSGYFMQPTVLTGTTPDMAVHTEE 403
Cdd:cd07146 279 DLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 404 IFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFD-PNLPFGGMRESGWG-REM 481
Cdd:cd07146 356 TFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRsELSPFGGVKDSGLGgKEG 435
|
410
....*....|....*.
gi 2734213326 482 AREGVEAFTEQKAVTI 497
Cdd:cd07146 436 VREAMKEMTNVKTYSL 451
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
113-495 |
3.73e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 302.04 E-value: 3.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 113 GKPVSMARaLDIPFAAEIYRYYAGWATKLEGRsynlALQGDPF--HCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAA 190
Cdd:PRK10090 24 GKIQQLAE-VEVAFTADYIDYMAEWARRYEGE----IIQSDRPgeNILLFKRALGVTTGILPWNFPFFLIARKMAPALLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 191 GCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVT 270
Cdd:PRK10090 99 GNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 271 LELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVG-PGLDPNSEIGPLM 349
Cdd:PRK10090 179 LELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGnPAERNDIAMGPLI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 350 SEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRF 429
Cdd:PRK10090 259 NAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDY 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2734213326 430 GLAASIWTRDLSRAHRLARSINAGAIWINCFGvFDPNLPF-GGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:PRK10090 339 GLTSSIYTQNLNVAMKAIKGLKFGETYINREN-FEAMQGFhAGWRKSGIGGADGKHGLHEYLQTQVV 404
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
78-497 |
2.47e-97 |
|
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: 301.13 E-value: 2.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNANLEELAELEALDTGKpVSMARALDIPFAAEIYRYYAGWATKLEGRsynLALQGDPFHC 157
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGAAIGELHEAAGLPTQPQGE---ILPSAPGRLS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 158 YTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTA-LRLAELVAEAGFPKGVVNVLTGFGEtAGAA 236
Cdd:cd07152 105 LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPGGAD-AGEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 237 ITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVER 316
Cdd:cd07152 184 LVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 317 SAFDKVMAGIEQVAANLKVGpglDPNSE---IGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARignSGYFMQPTVLTGT 393
Cdd:cd07152 264 SVADAYTAKLAAKAKHLPVG---DPATGqvaLGPLINARQLDRVHAIVDDSVAAGARLEAGGTY---DGLFYRPTVLSGV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 394 TPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFD-PNLPFGGM 472
Cdd:cd07152 338 KPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGM 417
|
410 420
....*....|....*....|....*.
gi 2734213326 473 RESGWG-REMAREGVEAFTEQKAVTI 497
Cdd:cd07152 418 GASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
79-497 |
1.02e-94 |
|
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: 294.54 E-value: 1.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 79 RDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSYNLAL--QGDPFH 156
Cdd:cd07147 38 RALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG-EVARAIDTFRIAAEEATRIYGEVLPLDIsaRGEGRQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 157 CYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAA 236
Cdd:cd07147 117 GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 237 ITAHRgVDKVSFTGSTEIGKKIaQAATGNlKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVER 316
Cdd:cd07147 197 VTDER-IKLLSFTGSPAVGWDL-KARAGK-KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 317 SAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSgyfMQPTVLTGTTPD 396
Cdd:cd07147 274 SVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKRDGAL---LEPTILEDVPPD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 397 MAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVF--DpNLPFGGMRE 474
Cdd:cd07147 351 MEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFrvD-HMPYGGVKD 429
|
410 420
....*....|....*....|...
gi 2734213326 475 SGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07147 430 SGIGREGVRYAIEEMTEPRLLVI 452
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
42-497 |
1.40e-89 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 281.24 E-value: 1.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 42 ATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARA 121
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFR-DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 122 lDIPFAAEIYRYYAGWATKLEGRSYNLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQ 201
Cdd:PRK09406 83 -EALKCAKGFRYYAEHAEALLADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 202 TPLTALRLAELVAEAGFPKGVVNVLTgFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVI 281
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 282 FADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFV 361
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 362 EQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLS 441
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 442 RAHRLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
162-496 |
1.03e-87 |
|
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: 276.87 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEA----GFPKGVVNVLTGFGETaGAAI 237
Cdd:cd07098 119 EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 238 TAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERS 317
Cdd:cd07098 198 TSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEK 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 318 AFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGN----SGYFMQPTVLTGT 393
Cdd:cd07098 278 IYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 394 TPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPN--LPFGG 471
Cdd:cd07098 358 TPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVqqLPFGG 437
|
330 340
....*....|....*....|....*
gi 2734213326 472 MRESGWGREMAREGVEAFTEQKAVT 496
Cdd:cd07098 438 VKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
6-476 |
3.91e-85 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 271.81 E-value: 3.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 6 PIIDERLSAAAKAF---LERPKA-------LFIDGDFVTAKDgkTFATEDPA-TGRTIVEVAEAGAADVDAAVAAARSAF 74
Cdd:PRK03137 9 PFTDFSVEENVEAFeeaLKKVEKelgqdypLIIGGERITTED--KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 75 DgVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSYNLALQGDp 154
Cdd:PRK03137 87 E-TWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADA-DTAEAIDFLEYYARQMLKLADGKPVESRPGE- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 155 fHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAG 234
Cdd:PRK03137 164 -HNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 235 AAITAHRGVDKVSFTGSTEIGKKI----AQAATGN--LKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNA 308
Cdd:PRK03137 243 DYLVDHPKTRFITFTGSREVGLRIyeraAKVQPGQiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 309 GSRLYVERSAFDKVMAGIEQVAANLKVGPGLDpNSEIGPLMSEAQQRRVTDFVEQGKRDGaHVAVGGARIGNSGYFMQPT 388
Cdd:PRK03137 323 CSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 389 VLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPN 466
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGY 480
|
490
....*....|
gi 2734213326 467 LPFGGMRESG 476
Cdd:PRK03137 481 HPFGGFNMSG 490
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-476 |
5.08e-81 |
|
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: 260.95 E-value: 5.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 5 TPIIDERLSAAAKAFLERPKA-------LFIDGDFVTAkDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGv 77
Cdd:TIGR01237 7 TDFADEENRQAFFKALATVKEqlgktypLVINGERVET-ENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSYNLALQGDPFHC 157
Cdd:TIGR01237 85 WKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADA-EVAEAIDFMEYYARQMIELAKGKPVNSREGETNQY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 158 YTlrQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAI 237
Cdd:TIGR01237 164 VY--TPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 238 TAHRGVDKVSFTGSTEIGKKI------AQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSR 311
Cdd:TIGR01237 242 VDHPKTSLITFTGSREVGTRIferaakVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 312 LYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGaHVAVGGARIGNSGYFMQPTVLT 391
Cdd:TIGR01237 322 AVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 392 GTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPNLPF 469
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPF 480
|
....*..
gi 2734213326 470 GGMRESG 476
Cdd:TIGR01237 481 GGFKMSG 487
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
111-497 |
2.52e-76 |
|
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: 245.90 E-value: 2.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 111 DTGKPVSMARALDI-PFAAEIY---RYYAGWATKlegRSYNLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQAsfkIAP 186
Cdd:cd07087 47 DLGKPPAEAYLTEIaVVLGEIDhalKHLKKWMKP---RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 187 ---ALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAgAAITAHRgVDKVSFTGSTEIGKKIAQAAT 263
Cdd:cd07087 121 ligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVA-TALLAEP-FDHIFFTGSPAVGKIVMEAAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 264 GNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQvAANLKVGPGLDPNS 343
Cdd:cd07087 198 KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKK-AIKEFYGEDPKESP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 344 EIGPLMSEAQQRRVTDFVEQGKrdgahVAVGGaRIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSV 423
Cdd:cd07087 277 DYGRIINERHFDRLASLLDDGK-----VVIGG-QVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEF 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 424 ANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:cd07087 351 INSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
81-484 |
5.27e-73 |
|
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: 238.09 E-value: 5.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 81 MAPAGRAALMARLADLVNANLEELAELEALDTGKP-----VSMARALD-IPFAAEIYRyyagwatKLEGRSYNLALQ--G 152
Cdd:cd07148 41 LPAHERIAILERLADLMEERADELALLIAREGGKPlvdakVEVTRAIDgVELAADELG-------QLGGREIPMGLTpaS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 153 DPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGET 232
Cdd:cd07148 114 AGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 233 AGAAITAHRgVDKVSFTGSTEIGKKI-AQAATGNlkRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSR 311
Cdd:cd07148 194 AEKLVTDPR-VAFFSFIGSARVGWMLrSKLAPGT--RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 312 LYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYfmQPTVLT 391
Cdd:cd07148 271 VFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 392 GTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPN-LPFG 470
Cdd:cd07148 349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFA 428
|
410 420
....*....|....*....|..
gi 2734213326 471 GMRESGWG--------REMARE 484
Cdd:cd07148 429 GRRQSGYGtggipytmHDMTQE 450
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-478 |
3.97e-70 |
|
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: 232.47 E-value: 3.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 4 MTPIIDERLSAAA------KAFLERPKAL-FIDGDFvtAKDGKTFATEDPA-TGRTIVEVAEAGAADVDAAVAAARSAFD 75
Cdd:cd07125 6 VNRIFDLEVPLEAladalkAFDEKEWEAIpIINGEE--TETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 76 GvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMA-----RALDipFAaeiyRYYAGWATKLEGRSynlAL 150
Cdd:cd07125 84 G-WSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAdaevrEAID--FC----RYYAAQARELFSDP---EL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 151 QGDPFHCYTLR-QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGF 229
Cdd:cd07125 154 PGPTGELNGLElHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 230 GETAGAAITAHRGVDKVSFTGSTEIGKKIAQA-ATGNLKRVTL--ELGGKspNVIFAD--ADLDEAIPAAAMAIFGNSGQ 304
Cdd:cd07125 234 GEEIGEALVAHPRIDGVIFTGSTETAKLINRAlAERDGPILPLiaETGGK--NAMIVDstALPEQAVKDVVQSAFGSAGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 305 VCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNsGYF 384
Cdd:cd07125 312 RCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGN-GYF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 385 MQPTVLTGTTPDmaVHTEEIFGPVLCAMPFD--DPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN---- 458
Cdd:cd07125 391 VAPGIIEIVGIF--DLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnit 468
|
490 500
....*....|....*....|..
gi 2734213326 459 --CFGVfdpnLPFGGMRESGWG 478
Cdd:cd07125 469 gaIVGR----QPFGGWGLSGTG 486
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
162-495 |
1.59e-69 |
|
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: 228.65 E-value: 1.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITahR 241
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQALLE--L 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 242 GVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDK 321
Cdd:cd07134 176 PFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 322 VMAG-IEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFmQPTVLTGTTPDMAVH 400
Cdd:cd07134 256 FVEHlKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYI-APTVLTNVTPDMKIM 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 401 TEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN-CFGVF-DPNLPFGGMRESGWG 478
Cdd:cd07134 335 QEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdVVLHFlNPNLPFGGVNNSGIG 414
|
330
....*....|....*..
gi 2734213326 479 REMAREGVEAFTEQKAV 495
Cdd:cd07134 415 SYHGVYGFKAFSHERAV 431
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
162-480 |
7.46e-69 |
|
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: 227.86 E-value: 7.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEA----GFPKGVVNVLTGfGETAGAAI 237
Cdd:cd07130 131 NPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 238 TAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERS 317
Cdd:cd07130 210 VKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHES 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 318 AFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGtTPDM 397
Cdd:cd07130 290 IYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEG-LSDA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 398 AVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRlarsinagaiWI-----NCfGVFDPNLP---- 468
Cdd:cd07130 369 PIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFR----------WLgpkgsDC-GIVNVNIGtsga 437
|
330
....*....|....*..
gi 2734213326 469 -----FGGMRESGWGRE 480
Cdd:cd07130 438 eiggaFGGEKETGGGRE 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
26-496 |
1.01e-66 |
|
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: 223.22 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 26 LFIDGDFVTAKDGKTFATEDpATGRTIVEVAEAGAADVDAAVAAARSAFdGVWRDMAPAGRAALMARLADLVNANLEELA 105
Cdd:cd07083 21 LVIGGEWVDTKERMVSVSPF-APSEVVGTTAKADKAEAEAALEAAWAAF-KTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 106 ELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSyNLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIA 185
Cdd:cd07083 99 ATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPA-VEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 186 PALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGN 265
Cdd:cd07083 177 APVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 266 L------KRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGL 339
Cdd:cd07083 257 ApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 340 DPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAvGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAM--PFDDP 417
Cdd:cd07083 337 ENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVL-GGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIryKDDDF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 418 DKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPNLPFGGMRESGWG-REMAREGVEAFTEQKA 494
Cdd:cd07083 416 AEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNaKTGGPHYLRRFLEMKA 495
|
..
gi 2734213326 495 VT 496
Cdd:cd07083 496 VA 497
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
45-495 |
1.79e-66 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 221.27 E-value: 1.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDI 124
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRD-WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 PFAAEIYRYYAGWATKLEGRSYNLALQGDPFHCYtlrQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPL 204
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 205 TALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRgVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFAD 284
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 285 ADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQG 364
Cdd:PRK13968 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 365 KRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAH 444
Cdd:PRK13968 327 LAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQAR 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2734213326 445 RLARSINAGAIWINCFGVFDPNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:PRK13968 407 QMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
162-495 |
1.41e-64 |
|
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: 215.43 E-value: 1.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPLGVAaGII-PWNYPFAQAsfkIAP---ALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAgAAI 237
Cdd:cd07133 100 QPLGVV-GIIvPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGGADVA-AAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 238 TAHRgVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERs 317
Cdd:cd07133 174 SSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPE- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 318 afDKVMAGIEQVAANL-KVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHV--AVGGARIGNSGYFMQPTVLTGTT 394
Cdd:cd07133 252 --DKLEEFVAAAKAAVaKMYPTLADNPDYTSIINERHYARLQGLLEDARAKGARVieLNPAGEDFAATRKLPPTLVLNVT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 395 PDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPNLPFGGM 472
Cdd:cd07133 330 DDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtLLHVAQDDLPFGGV 409
|
330 340
....*....|....*....|...
gi 2734213326 473 RESGWGREMAREGVEAFTEQKAV 495
Cdd:cd07133 410 GASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
161-495 |
1.16e-63 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 213.24 E-value: 1.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 161 RQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFGETAGAAITah 240
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLE-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 241 RGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFD 320
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 321 KVMAGIEQVaANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDgahVAVGGARIGNSgYFMQPTVLTGTTPDMAVH 400
Cdd:cd07135 263 EFVEELKKV-LDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGK---VVIGGEMDEAT-RFIPPTIVSDVSWDDSLM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 401 TEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN-CF---GVfdPNLPFGGMRESG 476
Cdd:cd07135 338 SEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLihvGV--DNAPFGGVGDSG 415
|
330
....*....|....*....
gi 2734213326 477 WGREMAREGVEAFTEQKAV 495
Cdd:cd07135 416 YGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
71-483 |
1.25e-62 |
|
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: 210.21 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 71 RSAFDGvWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPV--------SMARALDIPFAAeiYRYYAGwatklE 142
Cdd:cd07095 10 RAAFPG-WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqtevaAMAGKIDISIKA--YHERTG-----E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 143 GRSYNlalqgdPFHCYTLRQ-PLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKG 221
Cdd:cd07095 82 RATPM------AQGRAVLRHrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 222 VVNVLTGFGETaGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNL-KRVTLELGGKSPNVIFADADLDEAIPAAAMAIFG 300
Cdd:cd07095 156 VLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 301 NSGQVCNAGSRLYVERSAF-DKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIG 379
Cdd:cd07095 235 TAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 380 NSGYFMQPTVLTGTtpDMAVHT-EEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN 458
Cdd:cd07095 315 AGTAFLSPGIIDVT--DAADVPdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN 392
|
410 420
....*....|....*....|....*.
gi 2734213326 459 CFGVFDPN-LPFGGMRESGWGREMAR 483
Cdd:cd07095 393 RPTTGASStAPFGGVGLSGNHRPSAY 418
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
27-496 |
2.98e-62 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 213.84 E-value: 2.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDgVWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP-LWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGRSYNLALQGdpFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAP 186
Cdd:PLN02419 196 NITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNG--VDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 187 ALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGaAITAHRGVDKVSFTGSTEIGKKIAQAATGNL 266
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 267 KRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYV---ERSAFDKVMagieQVAANLKVGPGLDPNS 343
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLV----ERAKALKVTCGSEPDA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 344 EIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGY----FMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDK 419
Cdd:PLN02419 428 DLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 420 IPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINC-FGVFDPNLPFGGMRESGWG--REMAREGVEAFTEQKAVT 496
Cdd:PLN02419 508 AISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVpIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLVT 587
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
154-498 |
1.25e-58 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 201.41 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 154 PFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGfGETA 233
Cdd:PTZ00381 100 PGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 234 GAAITAHRgVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLY 313
Cdd:PTZ00381 178 TTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 314 VERSAFDKVmagIEQVAANLKVGPGLDP-NSE-IGPLMSEAQQRRVTDFVEQgkrDGAHVAVGGaRIGNSGYFMQPTVLT 391
Cdd:PTZ00381 257 VHRSIKDKF---IEALKEAIKEFFGEDPkKSEdYSRIVNEFHTKRLAELIKD---HGGKVVYGG-EVDIENKYVAPTIIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 392 GTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPNLPF 469
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPF 409
|
330 340
....*....|....*....|....*....
gi 2734213326 470 GGMRESGWGREMAREGVEAFTEQKAVTIR 498
Cdd:PTZ00381 410 GGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
154-495 |
2.60e-58 |
|
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: 199.27 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 154 PFHCYTLRQPLGVAAGIIPWNYPFAQAsfkIAP---ALAAGCTVLLKPAEQTPLTALRLAELVAEAgFPKGVVNVLTGFG 230
Cdd:cd07136 91 PSKSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 231 ETAgAAITAHRgVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEaipAAAMAIFG---NSGQVCN 307
Cdd:cd07136 167 EEN-QELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKL---AAKRIVWGkflNAGQTCV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 308 AGSRLYVERSAFDKVmagIEQVAANLKVGPGLDP--NSEIGPLMSEAQQRRVTDFVEQGKrdgahVAVGGaRIGNSGYFM 385
Cdd:cd07136 242 APDYVLVHESVKEKF---IKELKEEIKKFYGEDPleSPDYGRIINEKHFDRLAGLLDNGK-----IVFGG-NTDRETLYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 386 QPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINcfgvfD- 464
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN-----Dt 387
|
330 340 350
....*....|....*....|....*....|....*..
gi 2734213326 465 ------PNLPFGGMRESGWGREMAREGVEAFTEQKAV 495
Cdd:cd07136 388 imhlanPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
27-499 |
1.90e-55 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 193.05 E-value: 1.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 27 FIDGDFVTAKDGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAfDGVWRDMAPAGRAALMARLADLVNANLEELAE 106
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 107 LEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKL--EGRsynlALQGDPF-------HCYTLRQPLGVAAGIIPWNYPF 177
Cdd:PLN00412 98 CLVKEIAKPAKDAVT-EVVRSGDLISYTAEEGVRIlgEGK----FLVSDSFpgnernkYCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 178 AQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGStEIGKK 257
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 258 IAQAAtgNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGP 337
Cdd:PLN00412 252 ISKKA--GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 338 GLDpNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNsgyFMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDP 417
Cdd:PLN00412 330 PED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 418 DKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDPN-LPFGGMRESGWGREMAREGVEAFTEQKAVT 496
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKSTV 485
|
...
gi 2734213326 497 IRL 499
Cdd:PLN00412 486 INL 488
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
24-476 |
5.00e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 180.92 E-value: 5.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 24 KALFIDGDFVTAKdGKTFATEDPATGRTIVEVAEAGAADVDAAVAAARSAFDGvWRDMAPAGRAALMARLADLVNANLEE 103
Cdd:PRK09457 1 MTLWINGDWIAGQ-GEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA-WARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 104 LAELEALDTGKPV--------SMARALDIPFAAeiYRyyagwatKLEGRSYNLALQGDPFhcytLR-QPLGVAAGIIPWN 174
Cdd:PRK09457 79 LAEVIARETGKPLweaatevtAMINKIAISIQA--YH-------ERTGEKRSEMADGAAV----LRhRPHGVVAVFGPYN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 175 YPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETaGAAITAHRGVDKVSFTGSTEI 254
Cdd:PRK09457 146 FPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 255 GKKIAQAATGNL-KRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAF-DKVMAGIEQVAAN 332
Cdd:PRK09457 225 GYLLHRQFAGQPeKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 333 LKVG-PGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTGTT----PDmavhtEEIFGP 407
Cdd:PRK09457 305 LTVGrWDAEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIDVTGvaelPD-----EEYFGP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 408 VLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAI-WINCFGVFDPNLPFGGMRESG 476
Cdd:PRK09457 380 LLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
162-476 |
2.32e-50 |
|
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: 179.70 E-value: 2.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPL-GVAAGIIPWNYPFAQASFKIAPALAaGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAH 240
Cdd:cd07123 168 RPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLAS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 241 RGVDKVSFTGSTEIGKKIAQAATGNLK------RVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYV 314
Cdd:cd07123 247 PHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 315 ERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAH-VAVGGARIGNSGYFMQPTVLTGT 393
Cdd:cd07123 327 PESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAeIIAGGKCDDSVGYFVEPTVIETT 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 394 TPDMAVHTEEIFGPVLCAMPFDDPD--KIPSVANDT-RFGLAASIWTRD------LSRAHRLArsinAGAIWIN--CFGV 462
Cdd:cd07123 407 DPKHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTTsPYALTGAIFAQDrkaireATDALRNA----AGNFYINdkPTGA 482
|
330
....*....|....
gi 2734213326 463 FDPNLPFGGMRESG 476
Cdd:cd07123 483 VVGQQPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
10-478 |
1.04e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 183.09 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 10 ERLSAAAKAFLERPK--ALFIDGDfvtakdGKTFATEDPATGRTIV-EVAEAGAADVDAAVAAARSAFDGvWRDMAPAGR 86
Cdd:PRK11904 537 EPLAAAIAAFLEKQWqaGPIINGE------GEARPVVSPADRRRVVgEVAFADAEQVEQALAAARAAFPA-WSRTPVEER 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 87 AALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATKLEGrsynlalQGDPFHCYT-----LR 161
Cdd:PRK11904 610 AAILERAADLLEANRAELIALCVREAGKTLQDAIA-EVREAVDFCRYYAAQARRLFG-------APEKLPGPTgesneLR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 -QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAH 240
Cdd:PRK11904 682 lHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTAD 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 241 RGVDKVSFTGSTEIGKKIAQA-ATGNLKRVTL--ELGGKspNVIFADAD------LDEAIPAAamaiFGNSGQVCNAGSR 311
Cdd:PRK11904 762 PRIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQ--NAMIVDSTalpeqvVDDVVTSA----FRSAGQRCSALRV 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 312 LYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIG-NSGYFMQPTVL 390
Cdd:PRK11904 836 LFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGtENGHFVAPTAF 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 391 tgTTPDMAVHTEEIFGPVLCAMPF--DDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN------CFGV 462
Cdd:PRK11904 916 --EIDSISQLEREVFGPILHVIRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNrnqigaVVGV 993
|
490
....*....|....*.
gi 2734213326 463 fdpnLPFGGMRESGWG 478
Cdd:PRK11904 994 ----QPFGGQGLSGTG 1005
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
78-476 |
1.08e-44 |
|
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: 164.57 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNAN-LEELAELEALDTGKPVSMAralDIPFAAEI---YRYYAGWATKLEGRSynlALQGD 153
Cdd:TIGR01236 85 WSNLPFYDRAAIFLKAADLLSGPyRYEILAATMLGQSKTVYQA---EIDAVAELidfFRFNVKYARELYAQQ---PISAP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 154 PFHCYTLRQPL-GVAAGIIPWNYPFAQASFKIAPALAaGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGET 232
Cdd:TIGR01236 159 GEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 233 AGAAITAHRGVDKVSFTGST----EIGKKIAQAATG--NLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVC 306
Cdd:TIGR01236 238 VSDQVLADPDLAGIHFTGSTntfkHLWKKVAQNLDRyhNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKC 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 307 NAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAH--VAVGGARIGNSGYF 384
Cdd:TIGR01236 318 SAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEAltILYGGKYDDSQGYF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 385 MQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDpDKIPS----VANDTRFGLAASIWTRD---LSRAHRLARsINAGAIWI 457
Cdd:TIGR01236 398 VEPTVVESKDPDHPLMSEEIFGPVLTVYVYPD-DKYKEildlVDSTSQYGLTGAVFAKDrkaILEADKKLR-FAAGNFYI 475
|
410 420
....*....|....*....|.
gi 2734213326 458 N--CFGVFDPNLPFGGMRESG 476
Cdd:TIGR01236 476 NdkCTGAVVGQQPFGGARMSG 496
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
77-478 |
1.69e-44 |
|
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: 163.54 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 77 VWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATklegrsynlalqgDPFH 156
Cdd:TIGR01238 89 TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVR-------------DVLG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 157 CYTLRqPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAA 236
Cdd:TIGR01238 155 EFSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 237 ITAHRGVDKVSFTGSTEIGKKIAQAATGNLK---RVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLY 313
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLC 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 314 VERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDG---AHVAVGGARIGNSGYFMQPTVL 390
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 391 tgTTPDMAVHTEEIFGPVLCAMPF--DDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPN 466
Cdd:TIGR01238 394 --ELDDIAELSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGV 471
|
410
....*....|..
gi 2734213326 467 LPFGGMRESGWG 478
Cdd:TIGR01238 472 QPFGGQGLSGTG 483
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
78-478 |
1.13e-43 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 165.50 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNANLEELAELEALDTGKpvSMARALdipfaAEIY------RYYAGWATKLegrsynlalq 151
Cdd:COG4230 609 WSATPVEERAAILERAADLLEAHRAELMALLVREAGK--TLPDAI-----AEVReavdfcRYYAAQARRL---------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 152 gdpFHCYTLRQPLGVAAGIIPWNYPFA----QasfkIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLT 227
Cdd:COG4230 672 ---FAAPTVLRGRGVFVCISPWNFPLAiftgQ----VAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLP 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 228 GFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQA-ATGNLKRVTL--ELGGKspNVIFADAdldEAIP--------AAAm 296
Cdd:COG4230 745 GDGETVGAALVADPRIAGVAFTGSTETARLINRTlAARDGPIVPLiaETGGQ--NAMIVDS---SALPeqvvddvlASA- 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 297 aiFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGA 376
Cdd:COG4230 819 --FDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPL 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 377 -RIGNSGYFMQPTVLtgTTPDMAVHTEEIFGPVLCAMPFdDPDKIPSVA---NDTRFGLAASIWTRDLSRAHRLARSINA 452
Cdd:COG4230 897 pEECANGTFVAPTLI--EIDSISDLEREVFGPVLHVVRY-KADELDKVIdaiNATGYGLTLGVHSRIDETIDRVAARARV 973
|
410 420 430
....*....|....*....|....*....|..
gi 2734213326 453 GAIWIN------CFGVfdpnLPFGGMRESGWG 478
Cdd:COG4230 974 GNVYVNrniigaVVGV----QPFGGEGLSGTG 1001
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
157-498 |
2.17e-43 |
|
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: 159.31 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 157 CYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVaeagfPKGVVN-----VLTGFGE 231
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PKYLDKecypvVLGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 232 TAgaAITAHRgVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSR 311
Cdd:cd07132 169 TT--ELLKQR-FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 312 LYVERSAFDKVMAGIEQVaanLKVGPGLDPNS--EIGPLMSEAQQRRVTDFVEQGKrdgahVAVGGaRIGNSGYFMQPTV 389
Cdd:cd07132 246 VLCTPEVQEKFVEALKKT---LKEFYGEDPKEspDYGRIINDRHFQRLKKLLSGGK-----VAIGG-QTDEKERYIAPTV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 390 LTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINcfgvfD----- 464
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN-----Dtimhy 391
|
330 340 350
....*....|....*....|....*....|....*.
gi 2734213326 465 --PNLPFGGMRESGWGREMAREGVEAFTEQKAVTIR 498
Cdd:cd07132 392 tlDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
162-495 |
4.54e-43 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 157.96 E-value: 4.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKgVVNVLTGfGETAGAAITAHR 241
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTK-AIKVIEG-GVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 242 GvDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFG-NSGQVCNAGSRLYVERSAFD 320
Cdd:cd07137 178 W-DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQACIAPDYVLVEESFAP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 321 KVmagIEQVAANLKVGPGLDPNS--EIGPLMSEAQQRRVTDFVEQgKRDGAHVAVGGARIGNSGYfMQPTVLTGTTPDMA 398
Cdd:cd07137 257 TL---IDALKNTLEKFFGENPKEskDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERDEKNLY-IEPTILLDPPLDSS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 399 VHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN--CFGVFDPNLPFGGMRESG 476
Cdd:cd07137 332 IMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtVVQYAIDTLPFGGVGESG 411
|
330
....*....|....*....
gi 2734213326 477 WGREMAREGVEAFTEQKAV 495
Cdd:cd07137 412 FGAYHGKFSFDAFSHKKAV 430
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
78-478 |
1.69e-41 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 159.26 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNANLEELAELEALDTGKpvSMARALD-----IPFAaeiyRYYAGWATKLegrsynlaLQG 152
Cdd:PRK11905 606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGK--TLANAIAevreaVDFL----RYYAAQARRL--------LNG 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 153 DPfhcytlRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGET 232
Cdd:PRK11905 672 PG------HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRT 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 233 AGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKR-VTL--ELGGKspNVIFADAD-LDEAIPAAAMA-IFGNSGQVCN 307
Cdd:PRK11905 746 VGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpVPLiaETGGQ--NAMIVDSSaLPEQVVADVIAsAFDSAGQRCS 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 308 AGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVA-VGGARIGNSGYFMQ 386
Cdd:PRK11905 824 ALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHqLPLPAETEKGTFVA 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 387 PTVLtgTTPDMAVHTEEIFGPVLCAMPF--DDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN------ 458
Cdd:PRK11905 904 PTLI--EIDSISDLEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniiga 981
|
410 420
....*....|....*....|
gi 2734213326 459 CFGVfdpnLPFGGMRESGWG 478
Cdd:PRK11905 982 VVGV----QPFGGEGLSGTG 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
77-478 |
3.23e-38 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 149.35 E-value: 3.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 77 VWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARAlDIPFAAEIYRYYAGWATklegrsynlalqgDPFH 156
Cdd:PRK11809 697 IWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIA-EVREAVDFLRYYAGQVR-------------DDFD 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 157 CYTLRqPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVVNVLTGFGETAGAA 236
Cdd:PRK11809 763 NDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAA 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 237 ITAHRGVDKVSFTGSTEIGKKIAQAATGNL----KRVTL--ELGGKspNVIFADAD-LDEAIPAAAMA-IFGNSGQVCNA 308
Cdd:PRK11809 842 LVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPIPLiaETGGQ--NAMIVDSSaLTEQVVADVLAsAFDSAGQRCSA 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 309 GSRLYVERSAFDKVMAGIEQVAANLKVGpglDP---NSEIGPLMSEAQQRRVTDFVEQGKRDGAHV---AVGGARIGNSG 382
Cdd:PRK11809 920 LRVLCLQDDVADRTLKMLRGAMAECRMG---NPdrlSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaARENSEDWQSG 996
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 383 YFMQPTVLT-GTTPDMavhTEEIFGPVLCAMPF--DDPDKIPSVANDTRFGLAASIWTR-DLSRAHrLARSINAGAIWIN 458
Cdd:PRK11809 997 TFVPPTLIElDSFDEL---KREVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVN 1072
|
410 420
....*....|....*....|....*.
gi 2734213326 459 ------CFGVfdpnLPFGGMRESGWG 478
Cdd:PRK11809 1073 rnmvgaVVGV----QPFGGEGLSGTG 1094
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
163-497 |
6.74e-38 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 145.36 E-value: 6.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 163 PLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEA----GFPKGVVNVLTGfGETAGAAIT 238
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 239 AHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSA 318
Cdd:PLN02315 233 KDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 319 FDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARIGNSGYFMQPTVLTgTTPDMA 398
Cdd:PLN02315 313 YDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDAD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 399 VHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRdlsrahrlarsiNAGAI--WI-----NCfGVFDPNLP--- 468
Cdd:PLN02315 392 VVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTR------------NPETIfkWIgplgsDC-GIVNVNIPtng 458
|
330 340 350
....*....|....*....|....*....|....*
gi 2734213326 469 ------FGGMRESGWGREMAREGVEAFTEQKAVTI 497
Cdd:PLN02315 459 aeiggaFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
76-481 |
1.48e-32 |
|
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: 129.28 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 76 GVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARALDIPFAAEIYRYYAGWATKLEGRSYNLALQGDPF 155
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 156 HCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAG-FPKGVVNVLTGFGETaG 234
Cdd:cd07084 93 QSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-M 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 235 AAITAHRGVDKVSFTGSTEIGKKIAQAAtgNLKRVTLELGGKSPNVIFADAD-LDEAIPAAAMAIFGNSGQVCNAGSRLY 313
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 314 V-ERSAFDKVMAGIEQVAANLKVGPGLdpnseIGPLMSEAQQRRVtdfVEQGKRDGAHVAVGGARIGNS------GYFMQ 386
Cdd:cd07084 250 VpENWSKTPLVEKLKALLARRKLEDLL-----LGPVQTFTTLAMI---AHMENLLGSVLLFSGKELKNHsipsiyGACVA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 387 PTVLTGTTPDMA---VHTEEIFGPVLCAMPFDDpDKIPSVANDTRFG---LAASIWTRD---LSR-AHRLARSINAGAIW 456
Cdd:cd07084 322 SALFVPIDEILKtyeLVTEEIFGPFAIVVEYKK-DQLALVLELLERMhgsLTAAIYSNDpifLQElIGNLWVAGRTYAIL 400
|
410 420
....*....|....*....|....*
gi 2734213326 457 INCFGVFDPNLPFGGMRESGWGREM 481
Cdd:cd07084 401 RGRTGVAPNQNHGGGPAADPRGAGI 425
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
154-498 |
1.11e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 127.47 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 154 PFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVaEAGFPKGVVNVLTGfGETA 233
Cdd:PLN02174 103 PASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEG-AVTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 234 GAAITAHRGvDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFG-NSGQVCNAGSRL 312
Cdd:PLN02174 181 TTALLEQKW-DKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 313 YVERSAFDKVmagIEQVAANLKVGPGLDP--NSEIGPLMSEAQQRRVTDFVEQgKRDGAHVAVGGARiGNSGYFMQPTVL 390
Cdd:PLN02174 260 LTTKEYAPKV---IDAMKKELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE-KEVSDKIVYGGEK-DRENLKIAPTIL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 391 TGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWINCFGVFDP--NLP 468
Cdd:PLN02174 335 LDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLP 414
|
330 340 350
....*....|....*....|....*....|
gi 2734213326 469 FGGMRESGWGREMAREGVEAFTEQKAVTIR 498
Cdd:PLN02174 415 FGGVGESGMGAYHGKFSFDAFSHKKAVLYR 444
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
162-498 |
1.54e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 120.99 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGFPKGVvNVLTGfGETAGAAITAHR 241
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV-KVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 242 GvDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNV---IFADADLDEAIPAAAMAIFGN-SGQVCNAGSRLYVERS 317
Cdd:PLN02203 185 W-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 318 aFDKVMagIEQVAANLKVGPGLDPN--SEIGPLMSEAQQRRVTDFVEQgKRDGAHVAVGGArIGNSGYFMQPTVLTGTTP 395
Cdd:PLN02203 264 -FAPIL--IELLKSTIKKFFGENPResKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGS-IDEKKLFIEPTILLNPPL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 396 DMAVHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSINAGAIWIN----CFGVfdPNLPFGG 471
Cdd:PLN02203 339 DSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaiiQYAC--DSLPFGG 416
|
330 340
....*....|....*....|....*..
gi 2734213326 472 MRESGWGREMAREGVEAFTEQKAVTIR 498
Cdd:PLN02203 417 VGESGFGRYHGKYSFDTFSHEKAVLRR 443
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
79-447 |
5.96e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 114.03 E-value: 5.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 79 RDMAPAGRAALMARLADLVNANLEELAELEALDTGKpVSMARALDIPFAAEIYRYYAGWATKLEGRSY-----NLALQGD 153
Cdd:PRK11903 58 RALTYAQRAALLAAIVKVLQANRDAYYDIATANSGT-TRNDSAVDIDGGIFTLGYYAKLGAALGDARLlrdgeAVQLGKD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 154 P-FHCYTLRQPL-GVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAG-FPKGVVNVLTGfg 230
Cdd:PRK11903 137 PaFQGQHVLVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG-- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 231 etAGAAITAH-RGVDKVSFTGSTEIGKKIAQ--AATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMA-----IFGNS 302
Cdd:PRK11903 215 --SSAGLLDHlQPFDVVSFTGSAETAAVLRShpAVVQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKevvreMTVKS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 303 GQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGpglDPNSE---IGPLMSEAQQRRVTDFVEqGKRDGAHVAVGGARIG 379
Cdd:PRK11903 293 GQKCTAIRRIFVPEALYDAVAEALAARLAKTTVG---NPRNDgvrMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFA 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2734213326 380 ------NSGYFMQPTVLTGTTPDMA--VHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLA 447
Cdd:PRK11903 369 lvdadpAVAACVGPTLLGASDPDAAtaVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
156-450 |
2.93e-24 |
|
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: 105.81 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 156 HCYTLRQplGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAG-FPKGVVNVLTGfgeTAG 234
Cdd:cd07128 139 HILTPRR--GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 235 AAITAHRGVDKVSFTGSTEIGKK-------IAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCN 307
Cdd:cd07128 214 DLLDHLGEQDVVAFTGSAATAAKlrahpniVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 308 AGSRLYVERSAFDKVMAGIEQVAANLKVGpglDPNSE---IGPLMSEAQQRRVTDFVEQGKRDGAHVAVGGARI------ 378
Cdd:cd07128 294 AIRRAFVPEARVDAVIEALKARLAKVVVG---DPRLEgvrMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFevvgad 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 379 GNSGYFMQPTVLTGTTPDMA--VHTEEIFGPVLCAMPFDDPDKIPSVANDTRFGLAASIWTRDLSRAHRLARSI 450
Cdd:cd07128 371 AEKGAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
160-448 |
2.96e-19 |
|
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: 90.29 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 160 LRQ---PLGVAAGIIPWNYPFAqasFKI-----APALAAGCTVLLKPAEQTPLTALRLAELVAEA----GFPKGVVNVLT 227
Cdd:cd07129 99 LRRmlvPLGPVAVFGASNFPLA---FSVaggdtASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 228 GFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAAtgnLKR-----VTLELGGKSPNVIFADAdLDEAIPAAAMAIFG-- 300
Cdd:cd07129 176 GGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA---AARpepipFYAELGSVNPVFILPGA-LAERGEAIAQGFVGsl 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 301 --NSGQVC-NAGSRLYVERSAFDKVmagIEQVAANLKVGPGldpnseiGPLMSEAQQRRVTDFVEQ-GKRDGAHVAVGGA 376
Cdd:cd07129 252 tlGAGQFCtNPGLVLVPAGPAGDAF---IAALAEALAAAPA-------QTMLTPGIAEAYRQGVEAlAAAPGVRVLAGGA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 377 RIGNsGYFMQPTVLTGTTPDMAVH---TEEIFGP----VLCampfDDPDKIPSVANDTRFGLAASIW--TRDLSRAHRLA 447
Cdd:cd07129 322 AAEG-GNQAAPTLFKVDAAAFLADpalQEEVFGPaslvVRY----DDAAELLAVAEALEGQLTATIHgeEDDLALARELL 396
|
.
gi 2734213326 448 R 448
Cdd:cd07129 397 P 397
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
78-458 |
1.11e-12 |
|
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: 70.20 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 78 WRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMA------RALDIPFAAEIYRY--------YAGWaTKLEG 143
Cdd:cd07127 100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfqaggpHAQDRGLEAVAYAWremsrippTAEW-EKPQG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 144 RSYNLALQgDPFHCYTLRQPLGVAAGIIP-WN-YPFAQASfkiapaLAAGCTVLLKPAeqtPLTALRLA-------ELVA 214
Cdd:cd07127 179 KHDPLAME-KTFTVVPRGVALVIGCSTFPtWNgYPGLFAS------LATGNPVIVKPH---PAAILPLAitvqvarEVLA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 215 EAGFPKgvvNVLTGFGETAGAAITAHRGVDK----VSFTGSTEIGKKIAQAATGnlKRVTLELGGKSPNVIFADADLDEA 290
Cdd:cd07127 249 EAGFDP---NLVTLAADTPEEPIAQTLATRPevriIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDLKAM 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 291 IPAAAMAIFGNSGQVCNAGSRLYV---------ERSAFDKVMA----GIEQVAANLKVGPGLdpnseIGPLMSEAQQRRV 357
Cdd:cd07127 324 LRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAAdlaaAIDGLLADPARAAAL-----LGAIQSPDTLARI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 358 TDFVEQGK--RDG---AHVAVGGARIgnsgyfMQPTVLTGTTPDMAVHTEEIFGPVLCAMPFDDPDKIPSVAND---TRF 429
Cdd:cd07127 399 AEARQLGEvlLASeavAHPEFPDARV------RTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvrEHG 472
|
410 420 430
....*....|....*....|....*....|....*....
gi 2734213326 430 GLAASIWTRD---LSRAHRLAR------SIN-AGAIWIN 458
Cdd:cd07127 473 AMTVGVYSTDpevVERVQEAALdagvalSINlTGGVFVN 511
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
150-375 |
8.82e-10 |
|
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: 60.70 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 150 LQGDPFHCYTLRQPLGVAAGIIPWNYPfAQASFKIAPALAAGCTVLLKPAEQTPLTAlRLAELVAEAGFPKGVVNVLTGF 229
Cdd:cd07077 87 LLPDNGETYVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHGPKILVLY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 230 GETAGA----AITAHRGVDKVSFTGSTEIGKKIAQAATGnlKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNsGQV 305
Cdd:cd07077 165 VPHPSDelaeELLSHPKIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 306 CNAGSRLYVERSAFDKVMAGIEQ--VAANLKVGPGLDPNS-------------EIGPLMSeaqQRRVTDFVEQGKRDGAH 370
Cdd:cd07077 242 CASEQNLYVVDDVLDPLYEEFKLklVVEGLKVPQETKPLSkettpsfddealeSMTPLEC---QFRVLDVISAVENAWMI 318
|
....*
gi 2734213326 371 VAVGG 375
Cdd:cd07077 319 IESGG 323
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
45-478 |
1.32e-09 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 60.83 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 45 DPATGRTIVEVAEAGAADVDAAVAAARSAFDGVWRDMAPAGRAALMARLADLVNANLEELAELEALDTGKPVSMARALDi 124
Cdd:COG0506 510 PAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAE- 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 125 pfAAEIYRYYAGWATKLEGRSYNLALQGDPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPL 204
Cdd:COG0506 589 --AAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALA 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 205 TALRLAELVAEAGFPKGVVNVLTGFGETAGAAITAHRGVDKVSFTGSTEIGKKIAQAATGNLKRVTLELGGKSPNVIFAD 284
Cdd:COG0506 667 AAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAA 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 285 ADLDEAIPAAAMAIFGNSGQVCNAGSRLYVERSAFDKVMAGIEQVAANLKVGPGLDPNSEIGPLMSEAQQRRVTDFVEQG 364
Cdd:COG0506 747 AAAAAAVAAVAASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAA 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 365 KRDGAHVAVGGARIGNSGYFMQPTVLTGTTPDMAVHTEEIFGPVLcampFDDPDKIPSVANDTRFGLAASIWTRDLSRAH 444
Cdd:COG0506 827 LELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVL----ALVLALALDLAALIGLGLTGGLLGGGGGIVG 902
|
410 420 430
....*....|....*....|....*....|....
gi 2734213326 445 RLARSINAGAIWINCFGVFDPNLPFGGMRESGWG 478
Cdd:COG0506 903 RRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGG 936
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
134-423 |
2.50e-08 |
|
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: 56.35 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 134 YAGWATKLEGRSYNLA--LQGDPFHCYtlRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAE 211
Cdd:cd07126 113 FAGDQVRFLARSFNVPgdHQGQQSSGY--RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 212 LVAEAGFPKGVVNVLTGFGETAGAAITAHRgVDKVSFTGSTEIGKKIAQAATGNLKrvtLELGGKSPNVIFAD-ADLDEA 290
Cdd:cd07126 191 LLHLCGMPATDVDLIHSDGPTMNKILLEAN-PRMTLFTGSSKVAERLALELHGKVK---LEDAGFDWKILGPDvSDVDYV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 291 IPAAAMAIFGNSGQVCNAGSRLYVERsafDKVMAGIEQVAANLKVGPGLDpNSEIGPLMSEAQQRRVTDFVEQGKRDGAH 370
Cdd:cd07126 267 AWQCDQDAYACSGQKCSAQSILFAHE---NWVQAGILDKLKALAEQRKLE-DLTIGPVLTWTTERILDHVDKLLAIPGAK 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2734213326 371 VAVGGARIGN----SGY-FMQPTVL------TGTTPDMAVHTEEIFGPVLCAMPFDDpDKIPSV 423
Cdd:cd07126 343 VLFGGKPLTNhsipSIYgAYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKD-EQLPLV 405
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
153-323 |
6.34e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 51.88 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 153 DPFHCYTLRQPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEA----GFPKGVVNVLTG 228
Cdd:cd07081 85 ENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDN 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 229 FGETAGAAITAHRGVDKVSFTGsteiGKKIAQAATGNLKRVTLELGGKSPNVIFADADLDEAIPAAAMAIFGNSGQVCNA 308
Cdd:cd07081 165 PSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
170
....*....|....*
gi 2734213326 309 GSRLYVERSAFDKVM 323
Cdd:cd07081 241 EQSVIVVDSVYDEVM 255
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
162-459 |
2.49e-04 |
|
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: 43.25 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 162 QPLGVAAGIIPWNYPFAQASFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEA----GFPKGVVNVLTGFGETAGAAI 237
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 238 TAHRGVDKVSFTGsteiGKKIAQAA--TGnlkrvTLELG---GKSPNVIFADADLDEAIPAAAMA-IFGNsGQVCNAGSR 311
Cdd:cd07122 174 MKHPDVDLILATG----GPGMVKAAysSG-----KPAIGvgpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 312 LYVERSAFDKVMAGIEQVAANlkvgpgldpnseigpLMSEAQQRRVTD--FVEQGKRDGAHVAVGGARIGNSGYFMQP-- 387
Cdd:cd07122 244 VIVDDEIYDEVRAELKRRGAY---------------FLNEEEKEKLEKalFDDGGTLNPDIVGKSAQKIAELAGIEVPed 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 388 -TVLTGTTPDmaVHTEEIF-----GPVLCAMPFDDPDKIPSVAND-TRFGLA---ASIWTRDLSRAHRLARSINAGAIWI 457
Cdd:cd07122 309 tKVLVAEETG--VGPEEPLsreklSPVLAFYRAEDFEEALEKARElLEYGGAghtAVIHSNDEEVIEEFALRMPVSRILV 386
|
..
gi 2734213326 458 NC 459
Cdd:cd07122 387 NT 388
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
154-345 |
4.55e-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: 42.65 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 154 PFHCYTLRQPLGVAAGIIPWNYPFAQAsFKIAPALAAGCTVLLKPAEQTPLTALRLAELVAEAGfPKGV------VNVLT 227
Cdd:cd07080 103 GRGGYIRAQPRGLVVHIIAGNVPLLPV-WSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVD-PNHPltdsisVVYWP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734213326 228 GFGETAGAAITAHRgvDKVSFTGSTEIGKKIAQAATGNLKrvTLELGGK-SPNVI----FADADLDEAIPAAAMAIFGNS 302
Cdd:cd07080 181 GGDAELEERILASA--DAVVAWGGEEAVKAIRSLLPPGCR--LIDFGPKySFAVIdreaLESEKLAEVADALAEDICRYD 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2734213326 303 GQVCNAGSRLYVERSAFDKVMAGIEQVAANL----KVGPGLDPNSEI 345
Cdd:cd07080 257 QQACSSPQVVFVEKDDDEELREFAEALAAALerlpRRYPALSLSAAE 303
|
|
| |
