|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
30-480 |
0e+00 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 689.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWsKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWL-RLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 DMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLT 189
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 190 ALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDA 269
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 270 NLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAEA-- 347
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVARAra 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 348 -DAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQ 426
Cdd:cd07109 320 rGARIVAGGRIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 517140063 427 KRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07109 400 LRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
13-483 |
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: 568.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESL 92
Cdd:COG1012 8 LFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 93 ARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPF-LNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPS 171
Cdd:COG1012 86 AALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 172 LAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFI 251
Cdd:COG1012 166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 GCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGP 330
Cdd:COG1012 246 RVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDpLDPGTDMGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 331 LISVRQKKRVESYIAEA---DAPLLARGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIA 407
Cdd:COG1012 326 LISEAQLERVLAYIEDAvaeGAELLTGGRRPDG--EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517140063 408 NCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIVDNH 483
Cdd:COG1012 404 NDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-479 |
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: 523.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 19 WLPASGGReIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESR 98
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 99 DNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNAT 178
Cdd:pfam00171 78 ENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 179 VLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELG 258
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 259 GKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSG-EDSILGPLISVRQK 337
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLdPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 338 KRVESYIAEA---DAPLLARGGIRPGvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGL 414
Cdd:pfam00171 318 ERVLKYVEDAkeeGAKLLTGGEAGLD---NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517140063 415 VASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
14-480 |
4.86e-169 |
|
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: 484.79 E-value: 4.86e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 14 LIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLA 93
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 94 RLESRDNGKPIKQAL-ADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:cd07091 87 ALESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR-NFI 251
Cdd:cd07091 167 AAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 GCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGP 330
Cdd:cd07091 247 KVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPfDPDTFQGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 331 LISVRQKKRVESYI---AEADAPLLArGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIA 407
Cdd:cd07091 327 QVSKAQFDKILSYIesgKKEGATLLT-GGERHG--SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 408 NCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNV-FDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
30-480 |
4.68e-167 |
|
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: 478.97 E-value: 4.68e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 DMIVTARYFEFYGSAADKVHGEVIPFLNG-YNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACL 188
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGdYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 189 TALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDD 268
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 269 ANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVESYIAEA 347
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDpLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 348 --DAPLLARGGIRPGVP--TDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADG 423
Cdd:cd07114 321 reEGARVLTGGERPSGAdlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 517140063 424 GRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRA-LSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-479 |
3.86e-166 |
|
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: 477.09 E-value: 3.86e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 25 GREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPI 104
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 105 KQALA-DMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPA 183
Cdd:cd07112 81 SDALAvDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 184 EDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR-NFIGCTLELGGKSP 262
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 263 QIVFDDA-NLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPLISVRQKKRV 340
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 341 ESYI--AEADAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASI 418
Cdd:cd07112 321 LGYIesGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517140063 419 WTADGGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDE-GDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
51-480 |
2.65e-165 |
|
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: 473.62 E-value: 2.65e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 51 ERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHG 130
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 131 EVIPFLN-GYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNI 209
Cdd:cd07078 79 EVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 210 VTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQT 289
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 290 CSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYIAEADAP---LLARGGIRPGVPtdG 365
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTdMGPLISAAQLDRVLAYIEDAKAEgakLLCGGKRLEGGK--G 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 366 YYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGA 445
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*
gi 517140063 446 GGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07078 397 GAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
15-482 |
2.44e-156 |
|
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: 452.92 E-value: 2.44e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPflNGYNVE--VHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD--VPPHVIsrTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIG 252
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 253 CTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDsGED--SILGP 330
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGN-GLDadTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 331 LISVRQKKRVESYIAEA--DAPLLARGGIRPGVP--TDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEI 406
Cdd:cd07119 319 LVSAEHREKVLSYIQLGkeEGARLVCGGKRPTGDelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517140063 407 ANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIVDN 482
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHP-YFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININ 473
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
30-479 |
6.94e-154 |
|
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: 445.34 E-value: 6.94e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQAL- 108
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 109 ADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACL 188
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 189 TALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDD 268
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 269 ANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYI--A 345
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTqMGPLVSQAQFDRVLDYVdvG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 346 EADAPLLARGGIRPGVPtdGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGR 425
Cdd:cd07115 319 REEGARLLTGGKRPGAR--GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 517140063 426 QKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNR-FDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
30-479 |
6.56e-149 |
|
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: 432.76 E-value: 6.56e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 -DMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACL 188
Cdd:cd07093 79 rDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 189 TALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDD 268
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 269 ANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSG-EDSILGPLISVRQKKRVESYI--A 345
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLdPDTEVGPLISKEHLEKVLGYVelA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 346 EADAPLLARGGIRPGVP--TDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADG 423
Cdd:cd07093 319 RAEGATILTGGGRPELPdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 517140063 424 GRQKRVAKKLKCGQVFINGYGAGggvEL--PFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVR---DLrtPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-480 |
5.80e-145 |
|
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: 423.07 E-value: 5.80e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQA-----------LADMIVTARYFEFygsaaDKVHGevipflngyNVEVHREPHGVTGHIIPWNYPA-Q 162
Cdd:cd07138 81 AITLEMGAPITLAraaqvglgighLRAAADALKDFEF-----EERRG---------NSLVVREPIGVCGLITPWNWPLnQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 163 MFGRsVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQI 242
Cdd:cd07138 147 IVLK-VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 243 QTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD- 321
Cdd:cd07138 226 AEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDp 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 322 SGEDSILGPLISVRQKKRVESYIA---EADAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFD 398
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQkgiEEGARLVAGGPGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 399 DEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINgyGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKT 478
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN--GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
..
gi 517140063 479 IV 480
Cdd:cd07138 464 IQ 465
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
30-480 |
3.93e-142 |
|
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: 415.60 E-value: 3.93e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 DMIVTARYFEFYGSAADKVH---GEVIPF-LNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAED 185
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQLDakaERAVPLpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 186 ACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIV 265
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 266 FDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPLISVRQKKRVESYI 344
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPlEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 345 --AEADAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTAD 422
Cdd:cd07110 319 arGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 517140063 423 GGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
30-480 |
8.25e-141 |
|
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: 412.41 E-value: 8.25e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSkATATERGRLLLELSRRILSESESLARLESRDNGKPIK--QA 107
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtaRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARyFEFYGSAADKVHGEVI-----PFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKP 182
Cdd:cd07089 80 MQVDGPIGH-LRYFADLADSFPWEFDlpvpaLRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 183 AEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSP 262
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 263 QIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVE 341
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDpADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 342 SYIA---EADAPLLARGGIRPGVPTdGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASI 418
Cdd:cd07089 319 GYIArgrDEGARLVTGGGRPAGLDK-GFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517140063 419 WTADGGRQKRVAKKLKCGQVFINGyGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGING-GGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-480 |
2.00e-139 |
|
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: 409.27 E-value: 2.00e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIK-QALADMIVTARYFEFYGSAADKV-HGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:cd07139 83 LWTAENGMPISwSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGrGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIG 252
Cdd:cd07139 163 AAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 253 CTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGPL 331
Cdd:cd07139 242 VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATqIGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 332 ISVRQKKRVESYIAEA--DAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANC 409
Cdd:cd07139 322 ASARQRERVEGYIAKGraEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAND 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517140063 410 TEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGveLPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07139 402 SDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG--APFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
15-479 |
2.81e-139 |
|
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: 409.49 E-value: 2.81e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQ-ALADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLA 173
Cdd:cd07144 91 IEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 174 MGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGC 253
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 254 TLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKArfEAIQASDSG----EDSILG 329
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVE--HVKQNYKVGspfdDDTVVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 330 PLISVRQKKRVESYI---AEADAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEI 406
Cdd:cd07144 329 PQVSKTQYDRVLSYIekgKKEGAKLVYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKK 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 407 ANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGaGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07144 409 ANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSN-DSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
30-479 |
9.04e-138 |
|
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: 404.12 E-value: 9.04e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 DMIVTARYFEFYGSAADKVHGEVIP-FLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACL 188
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 189 TALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDD 268
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 269 ANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVESYIAEA 347
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNgLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 348 ---DAPLLArGGIRPGVPtdGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGG 424
Cdd:cd07103 319 vakGAKVLT-GGKRLGLG--GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 517140063 425 RQKRVAKKLKCGQVFINGyGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07103 396 RAWRVAEALEAGMVGINT-GLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
13-479 |
5.81e-137 |
|
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: 403.26 E-value: 5.81e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESL 92
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 93 ARLESRDNGKPIKQAL-ADMIVTARYFEFYGSAADKVHGEVIPfLNGYNVEVH-REPHGVTGHIIPWNYPAQMFGRSVAP 170
Cdd:cd07559 81 AVAETLDNGKPIRETLaADIPLAIDHFRYFAGVIRAQEGSLSE-IDEDTLSYHfHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 171 SLAMGNATVLKPAEDACLTALRIGEMAVEVgFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNF 250
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 251 IGCTLELGGKSPQIVFDDAN------LDAALPVLVnAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-G 323
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQL-GFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPlD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 324 EDSILGPLISVRQKKRVESYIA---EADAPLLArGGIR--PGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFD 398
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDigkEEGAEVLT-GGERltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 399 DEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGY-----GAgggvelPFGGYRKSGHGREKGFAALHEF 473
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYhqypaHA------PFGGYKKSGIGRETHKMMLDHY 470
|
....*.
gi 517140063 474 STIKTI 479
Cdd:cd07559 471 QQTKNI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
14-480 |
4.09e-133 |
|
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: 393.40 E-value: 4.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 14 LIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLA 93
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 94 RLESRDNGKPIKQA-LADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:cd07142 87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR-NFI 251
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 GCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGP 330
Cdd:cd07142 247 PVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVeQGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 331 LISVRQKKRVESYI---AEADAPLLArGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIA 407
Cdd:cd07142 327 QVDKEQFEKILSYIehgKEEGATLIT-GGDRIG--SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 408 NCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGaGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYD-VFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
30-479 |
1.43e-132 |
|
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: 391.28 E-value: 1.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 DMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLT 189
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 190 ALRIGEMAVEVGFPAGAVNIVTGRGLVaGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDA 269
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 270 NLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPLISVRQKKRVESYIAEA- 347
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPlDEDTQMGALISEEHLEKVLGYIESAk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 348 -DAPLLARGGIRPGVP---TDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADG 423
Cdd:cd07090 318 qEGAKVLCGGERVVPEdglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 517140063 424 GRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNI-SPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
15-480 |
7.59e-132 |
|
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: 390.17 E-value: 7.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFD-GGEWSKATATERGRLLLELSRRILSESESLA 93
Cdd:cd07141 11 INNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlGSPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 94 RLESRDNGKPI-KQALADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:cd07141 91 SLETLDNGKPFsKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR-NFI 251
Cdd:cd07141 171 ACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNLK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 GCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSIL-GP 330
Cdd:cd07141 251 RVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEqGP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 331 LISVRQKKRVESYI--AEADAPLLARGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIAN 408
Cdd:cd07141 331 QIDEEQFKKILELIesGKKEGAKLECGGKRHG--DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517140063 409 CTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07141 409 NTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNV-VSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
12-484 |
2.09e-131 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 388.88 E-value: 2.09e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 12 MNLIGNKWlPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESES 91
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF--PEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 92 LARLESRDNGKPIKQALADMI-VTARYFEFYGSAADKVHGEVI-PFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVA 169
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIpAIVDVFRFFAGAARCLEGKAAgEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 170 PSLAMGNATVLKPAEDACLTALRIGEMAVEVgFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARN 249
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 250 FIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSIL 328
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDpDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 329 GPLISVRQKKRVESYIAEADAPLLAR---GGIRPGVPtdGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIE 405
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGHIRvvtGGEAPDGK--GYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517140063 406 IANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGREKGFAALHEFSTIKTIVDNHG 484
Cdd:PRK13473 398 WANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVS-EMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
56-480 |
4.12e-131 |
|
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: 384.27 E-value: 4.12e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 56 AARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPF 135
Cdd:cd06534 2 AARAAFK--AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 136 -LNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRG 214
Cdd:cd06534 80 pDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 215 LVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGA 294
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 295 RVLVQRGVYDqvavELKARFEAIqasdsgedsilgplisvrqkkrvesyiaeadapllarggirpgvptdgyyvapalFG 374
Cdd:cd06534 240 RLLVHESIYD----EFVEKLVTV-------------------------------------------------------LV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 375 PCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFG 454
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFG 340
|
410 420
....*....|....*....|....*.
gi 517140063 455 GYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-480 |
7.13e-131 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 388.71 E-value: 7.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 8 LPKAMNLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAF---DGGEWSKATATERGRLLLELSRR 84
Cdd:PLN02467 5 VPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 85 ILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEV-----IPfLNGYNVEVHREPHGVTGHIIPWNY 159
Cdd:PLN02467 85 ITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkapvsLP-METFKGYVLKEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 160 PAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVG 239
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 240 VQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQA 319
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 320 SDS-GEDSILGPLISVRQKKRVESYIAEAD---APLLArGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMI 395
Cdd:PLN02467 324 SDPlEEGCRLGPVVSEGQYEKVLKFISTAKsegATILC-GGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 396 PFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINgYGAGGGVELPFGGYRKSGHGREKGFAALHEFST 475
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN-CSQPCFCQAPWGGIKRSGFGRELGEWGLENYLS 481
|
....*
gi 517140063 476 IKTIV 480
Cdd:PLN02467 482 VKQVT 486
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
31-480 |
3.00e-130 |
|
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: 385.16 E-value: 3.00e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 31 VSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKAtATERGRLLLELSRRILSESESLARLESRDNGKPIKQALAD 110
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHD-PRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 111 M---IVTARYfefYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDAC 187
Cdd:cd07120 81 IsgaISELRY---YAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 188 LTALRIGEMAVEV-GFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVF 266
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 267 DDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQ---ASDSGEDsiLGPLISVRQKKRVESY 343
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKvgpGLDPASD--MGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 344 IAEA---DAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWT 420
Cdd:cd07120 316 VERAiaaGAEVVLRGGPVTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 421 ADGGRQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFA-EAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
30-480 |
1.10e-129 |
|
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: 384.02 E-value: 1.10e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIK-QAL 108
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 109 ADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACL 188
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 189 TALRIGEMAVEVgFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDD 268
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 269 ANLDAALPVLVNAI-IQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPLISVRQKKRVESYIAE 346
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 347 ADAP---LLARGGIRPGVPT--DGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTA 421
Cdd:cd07108 318 GLSTsgaTVLRGGPLPGEGPlaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 422 DGGRQKRVAKKLKCGQVFINgYGAGGGVELPFGGYRKSGHGREKGF-AALHEFSTIKTIV 480
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGREASLeGMLEHFTQKKTVN 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-479 |
2.07e-129 |
|
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: 384.19 E-value: 2.07e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQALA-DMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLA 173
Cdd:cd07143 91 IEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 174 MGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR-NFIG 252
Cdd:cd07143 171 AGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNLKK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 253 CTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPL 331
Cdd:cd07143 251 VTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPfAEDTFQGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 332 ISVRQKKRVESYI--AEADAPLLARGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANC 409
Cdd:cd07143 331 VSQIQYERIMSYIesGKAEGATVETGGKRHG--NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAND 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 410 TEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07143 409 STYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNL-LHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
8-479 |
4.61e-128 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 380.77 E-value: 4.61e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 8 LPKAMNLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLlelsRR--- 84
Cdd:PRK13252 4 QPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRIL----RRavd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 85 ILSE-SESLARLESRDNGKPIKQALADMIVT-ARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQ 162
Cdd:PRK13252 78 ILRErNDELAALETLDTGKPIQETSVVDIVTgADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 163 MFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVaGAALSSSRNIDFIAFTGSPEVGVQI 242
Cdd:PRK13252 158 IACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 243 QTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD- 321
Cdd:PRK13252 237 MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 322 SGEDSILGPLISVRQKKRVESYIAEAD---APLLARG-GIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPF 397
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEKGKaegARLLCGGeRLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 398 DDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIK 477
Cdd:PRK13252 397 DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGE-SPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
..
gi 517140063 478 TI 479
Cdd:PRK13252 476 SV 477
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
15-480 |
8.22e-128 |
|
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: 379.30 E-value: 8.22e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFLN-GYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLA 173
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRpNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 174 MGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGC 253
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 254 TLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLI 332
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDpFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 333 SVRQKKRVESYIAEA--DAPLLARGGIRPGVpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCT 410
Cdd:cd07088 320 NEAALDKVEEMVERAveAGATLLTGGKRPEG-EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDS 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517140063 411 EYGLVASIWTADGGRQKRVAKKLKCGQVFIN--------GYGAgggvelpfgGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07088 399 EYGLTSYIYTENLNTAMRATNELEFGETYINrenfeamqGFHA---------GWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
31-479 |
1.85e-127 |
|
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: 378.22 E-value: 1.85e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 31 VSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALAD 110
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 111 MIVTARYFEFYGSAADKVHGEvipflnGYNV-------EVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPA 183
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGD------SYNNlgddmlgLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 184 EDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQ 263
Cdd:cd07118 156 EFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 264 IVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPLISVRQKKRVES 342
Cdd:cd07118 236 IVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 343 YIAEA--DAPLLARGGIRPGVpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWT 420
Cdd:cd07118 316 YVDAGraEGATLLLGGERLAS-AAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWS 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 517140063 421 ADGGRQKRVAKKLKCGQVFINGYgAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07118 395 KDIDTALTVARRIRAGTVWVNTF-LDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
13-479 |
1.49e-125 |
|
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: 373.89 E-value: 1.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGREidVVSPID-GAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESES 91
Cdd:cd07097 3 NYIDGEWVAGGDGEE--NRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 92 LARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFLN-GYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAP 170
Cdd:cd07097 79 LARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRpGVEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 171 SLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNF 250
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 251 IGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LG 329
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVdIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 330 PLISVRQKKRVESYI--AEADAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIA 407
Cdd:cd07097 319 PVVSERQLEKDLRYIeiARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 408 NCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHG-REKGFAALHEFSTIKTI 479
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
30-477 |
1.06e-124 |
|
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: 370.89 E-value: 1.06e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 D-MIVTARYFEFYGSAADKVHGEVI-PFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDAC 187
Cdd:cd07092 79 DeLPGAVDNFRFFAGAARTLEGPAAgEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 188 LTALRIGEMAVEVgFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFD 267
Cdd:cd07092 159 LTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 268 DANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVESYIAE 346
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDpDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 347 A--DAPLLARGGIRPGvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGG 424
Cdd:cd07092 318 ApaHARVLTGGRRAEG---PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 517140063 425 RQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGREKGFAALHEFSTIK 477
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAA-EMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-480 |
5.70e-123 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 368.38 E-value: 5.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGK-PIKQALADMIVTARYFEFYGSAADKVHGEVIPF---LNGYNVevhREPHGVTGHIIPWNYPAQMFGRSVAP 170
Cdd:PLN02766 105 LDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMsrqLQGYTL---KEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 171 SLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR-N 249
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 250 FIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-L 328
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRArQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 329 GPLISVRQKKRVESYI--AEADAPLLARGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEI 406
Cdd:PLN02766 342 GPQVDKQQFEKILSYIehGKREGATLLTGGKPCG--DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKK 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517140063 407 ANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:PLN02766 420 ANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDP-DCPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
30-479 |
5.77e-123 |
|
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: 366.70 E-value: 5.77e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 DMIVTARYFEFYGSAADKVHGEVIPF-LNGYNVEVhREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACL 188
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVgGRNLHYTL-REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 189 TALRIGEMAVEVgFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDD 268
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 269 ANLDAALPVLVNAI-IQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVESYIAE 346
Cdd:cd07107 237 ADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDpTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 347 AD---APLLARGGIRPG-VPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTAD 422
Cdd:cd07107 317 AKregARLVTGGGRPEGpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 423 GGRQKRVAKKLKCGQVFINGYGA---GggveLPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRhflG----APFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
14-479 |
1.57e-122 |
|
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: 366.39 E-value: 1.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 14 LIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLA 93
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK--TWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 94 RLESRDNGKPIKQALA-DMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVgFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIG 252
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 253 CTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPL 331
Cdd:cd07117 241 ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPlDPDTQMGAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 332 ISVRQKKRVESYI---AEADAPLLARGGIRPGVPTD-GYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIA 407
Cdd:cd07117 321 VNKDQLDKILSYVdiaKEEGAKILTGGHRLTENGLDkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517140063 408 NCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYG---AGGgvelPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07117 401 NDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNqipAGA----PFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
14-480 |
1.69e-122 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 368.37 E-value: 1.69e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 14 LIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLA 93
Cdd:PLN02466 61 LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 94 RLESRDNGKPIKQAL-ADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:PLN02466 141 ALETWDNGKPYEQSAkAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPAL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR-NFI 251
Cdd:PLN02466 221 ACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNLK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 GCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGP 330
Cdd:PLN02466 301 PVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVeQGP 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 331 LISVRQKKRVESYI---AEADAPLLArGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIA 407
Cdd:PLN02466 381 QIDSEQFEKILRYIksgVESGATLEC-GGDRFG--SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRA 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 408 NCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVeLPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:PLN02466 458 NNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAA-IPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
13-484 |
4.65e-119 |
|
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: 357.43 E-value: 4.65e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGREIDVVSPIDGA-IFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESES 91
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFP--EWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 92 LARLESRDNGKPIKQALADM---IVTARYFefyGSAADKVHGEVIP--FLNGYNVEVhREPHGVTGHIIPWNYPAQMFGR 166
Cdd:cd07131 79 LARLVTREMGKPLAEGRGDVqeaIDMAQYA---AGEGRRLFGETVPseLPNKDAMTR-RQPIGVVALITPWNFPVAIPSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 167 SVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMA 246
Cdd:cd07131 155 KIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 247 ARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GED 325
Cdd:cd07131 235 ARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGlDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 326 SILGPLISVRQKKRVESYIA---EADAPLLARGG-IRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEA 401
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEigkEEGATLLLGGErLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 402 SAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHG-REKGFAALHEFSTIKTIV 480
Cdd:cd07131 395 EAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVY 474
|
....
gi 517140063 481 DNHG 484
Cdd:cd07131 475 VDYS 478
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-473 |
1.57e-118 |
|
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: 356.32 E-value: 1.57e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQAL-ADMIVTARYFEFYGSAADKVHGEvipfLNGYnvevhrEPHGVTGHIIPWNYPAQMFGRSVAPSLA 173
Cdd:cd07111 104 LESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLDTE----LAGW------KPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 174 MGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVaGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGC 253
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 254 TLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGPLI 332
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIdMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 333 SVRQKKRVESYIAEADAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEY 412
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517140063 413 GLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVeLPFGGYRKSGHGREKGFAALHEF 473
Cdd:cd07111 413 GLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAA-AGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
28-480 |
2.58e-118 |
|
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: 354.73 E-value: 2.58e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 28 IDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA 107
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVE-----VHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKP 182
Cdd:cd07145 79 RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNErriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 183 AEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSP 262
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 263 QIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPLISVRQKKRVE 341
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 342 SYIAEAdaplLARGG--IRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIW 419
Cdd:cd07145 319 NLVNDA----VEKGGkiLYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517140063 420 TADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
30-479 |
3.24e-117 |
|
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: 351.45 E-value: 3.24e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 30 VVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALA 109
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 110 DMIVTARYFEFYGSAADKVhgEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLT 189
Cdd:cd07106 79 EVGGAVAWLRYTASLDLPD--EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 190 ALRIGEMAVEVgFPAGAVNIVTGRGLVaGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDA 269
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 270 NLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVESYIAEA- 347
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDgLDPGTTLGPVQNKMQYDKVKELVEDAk 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 348 --DAPLLARGGIRPGvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGR 425
Cdd:cd07106 315 akGAKVLAGGEPLDG---PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 517140063 426 QKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGA-LDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
8-477 |
1.72e-113 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 343.98 E-value: 1.72e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 8 LPKAMNLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILS 87
Cdd:PLN02278 22 LLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 88 ESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIP--FLNGyNVEVHREPHGVTGHIIPWNYPAQMFG 165
Cdd:PLN02278 100 NKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPspFPDR-RLLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 166 RSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTM 245
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 246 AARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GE 324
Cdd:PLN02278 259 AAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGfEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 325 DSILGPLISVRQKKRVESYIAEA---DAPLLArGGIRpgVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEA 401
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAvskGAKVLL-GGKR--HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517140063 402 SAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINgYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIK 477
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVN-EGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
10-479 |
1.99e-110 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 335.71 E-value: 1.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 10 KAMNL-------IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELS 82
Cdd:PRK09847 12 KALSLaienrlfINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 83 RRILSESESLARLESRDNGKPIKQALADMIV-TARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPA 161
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPgAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 162 QMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQ 241
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 242 IQTMAAR-NFIGCTLELGGKSPQIVFDDA-NLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQA 319
Cdd:PRK09847 252 LLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 320 SDS-GEDSILGPLISVRQKKRVESYIAEADAP-LLARGGIRPGVPTdgyYVAPALFGPCDPYSRIAQEEVFGPVLCMIPF 397
Cdd:PRK09847 332 GHPlDPATTMGTLIDCAHADSVHSFIREGESKgQLLLDGRNAGLAA---AIGPTIFVDVDPNASLSREEIFGPVLVVTRF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 398 DDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGaGGGVELPFGGYRKSGHGREKGFAALHEFSTIK 477
Cdd:PRK09847 409 TSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYN-DGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
..
gi 517140063 478 TI 479
Cdd:PRK09847 488 TI 489
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
14-460 |
1.83e-108 |
|
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: 331.49 E-value: 1.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 14 LIGNKWLPasGGREIDVVSPID-GAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESL 92
Cdd:cd07124 36 VIGGKEVR--TEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFP--TWRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 93 ARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYP-AQMFGRSVAPs 171
Cdd:cd07124 112 AAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPlAILAGMTTAA- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 172 LAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFI 251
Cdd:cd07124 191 LVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 G------CTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGE- 324
Cdd:cd07124 271 GqkwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDp 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 325 DSILGPLISVRQKKRVESYIAEA--DAPLLArGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEAS 402
Cdd:cd07124 351 EVYMGPVIDKGARDRIRRYIEIGksEGRLLL-GGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 403 AIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFIN--GYGAGGGVElPFGGYRKSG 460
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQ-PFGGFKMSG 488
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
13-464 |
1.43e-105 |
|
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: 322.86 E-value: 1.43e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESL 92
Cdd:cd07116 3 NFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 93 ARLESRDNGKPIKQAL-ADMIVTARYFEFYGSAADKVHGEvIPFLNGYNVEVH-REPHGVTGHIIPWNYPAQMFGRSVAP 170
Cdd:cd07116 81 AVAETWDNGKPVRETLaADIPLAIDHFRYFAGCIRAQEGS-ISEIDENTVAYHfHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 171 SLAMGNATVLKPAEDACLTALRIGEMAVEVgFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNF 250
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 251 IGCTLELGGKSPQIVF------DDANLDAALPVLVnAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAI-QASDSG 323
Cdd:cd07116 239 IPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFV-MFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIkQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 324 EDSILGPLISVRQKKRVESYIA---EADAPLLARG--GIRPGVPTDGYYVAPALFGPCDpySRIAQEEVFGPVLCMIPFD 398
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDigkEEGAEVLTGGerNELGGLLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517140063 399 DEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGRE 464
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPA-HAAFGGYKQSGIGRE 460
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
49-479 |
5.77e-105 |
|
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: 319.48 E-value: 5.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 49 DVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKV 128
Cdd:cd07104 1 DVDRAYAAAAAAQ--KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 129 HGEVIPflngYNVE-----VHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLT-ALRIGEMAVEVGF 202
Cdd:cd07104 79 EGEILP----SDVPgkesmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 203 PAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAAlpvlVNAI 282
Cdd:cd07104 155 PKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLA----VSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 283 I------QngGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVESYIAEA---DAPLL 352
Cdd:cd07104 231 AfgaflhQ--GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDpRDPDTVIGPLINERQVDRVHAIVEDAvaaGARLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 353 ARGGIrpgvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKK 432
Cdd:cd07104 309 TGGTY------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAER 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 517140063 433 LKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07104 383 LETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
15-479 |
2.92e-104 |
|
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: 319.39 E-value: 2.92e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVS-AWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIkqALADMI---VTARYFEFYGSAADKVHGEV----IPFLNG--YNVEVHREPHGVTGHIIPWNYPAQMFG 165
Cdd:cd07113 83 LETLCSGKSI--HLSRAFevgQSANFLRYFAGWATKINGETlapsIPSMQGerYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 166 RSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVaGAALSSSRNIDFIAFTGSPEVGVQIQTM 245
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 246 AARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQ-ASDSGE 324
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQvGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 325 DSILGPLISVRQKKRVESYI--AEADAPLLARGGirPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEAS 402
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLddARAEGDEIVRGG--EALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517140063 403 AIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDP-AVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-479 |
3.39e-104 |
|
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: 318.50 E-value: 3.39e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 29 DVVSPIDGAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQAL 108
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 109 ADMIVTARYFEFYGSAADKVHGEVIPFL-NGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDAC 187
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSDsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 188 LTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFD 267
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 268 DANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGE-DSILGPLISVRQKKRVESYIAE 346
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDpDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 347 AdaplLARGG-IRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGR 425
Cdd:cd07150 320 A----VAKGAkLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 517140063 426 QKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07150 396 AFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
13-484 |
4.08e-103 |
|
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: 316.43 E-value: 4.08e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGReIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESL 92
Cdd:cd07086 1 GVIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK--EWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 93 ARLESRDNGKPIKQALAD---MIVTARYFefyGSAADKVHGEVIP------FLngynVEVhREPHGVTGHIIPWNYPAQM 163
Cdd:cd07086 78 GRLVSLEMGKILPEGLGEvqeMIDICDYA---VGLSRMLYGLTIPserpghRL----MEQ-WNPLGVVGVITAFNFPVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 164 FGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEV----GFPAGAVNIVTGRGLVaGAALSSSRNIDFIAFTGSPEVG 239
Cdd:cd07086 150 PGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 240 VQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQA 319
Cdd:cd07086 229 RRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 320 SDSGEDSIL-GPLISVRQKKRVESYIAEA---DAPLLArGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMI 395
Cdd:cd07086 309 GDPLDEGTLvGPLINQAAVEKYLNAIEIAksqGGTVLT-GGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 396 PFDDEASAIEIANCTEYGLVASIWTADGGRQKRV--AKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEF 473
Cdd:cd07086 388 KFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQY 467
|
490
....*....|.
gi 517140063 474 STIKTIVDNHG 484
Cdd:cd07086 468 MRRSTCTINYS 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
15-479 |
1.98e-102 |
|
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: 315.20 E-value: 1.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:cd07140 10 INGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEELAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGK----PIKQALADMIVTARYFEFYgsaADKVHGEVIPFLNG---YNVE-VHREPHGVTGHIIPWNYPAQMFGR 166
Cdd:cd07140 90 IESLDSGAvytlALKTHVGMSIQTFRYFAGW---CDKIQGKTIPINQArpnRNLTlTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 167 SVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQI-QTM 245
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHImKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 246 AARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGED 325
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 326 SIL-GPLISVRQKKRVESYI--AEADAPLLARGGIRpgVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDE-- 400
Cdd:cd07140 327 STDhGPQNHKAHLDKLVEYCerGVKEGATLVYGGKQ--VDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdv 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517140063 401 ASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNK-TDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
21-480 |
1.75e-100 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 311.04 E-value: 1.75e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 21 PASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAfdGGEWSKATATERGRLLLELSRRILSESESLARLESRDN 100
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 101 GKPIKQA---LADMIVTARYfefYGSAADKV-----HGEVIPFLNgyNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:PRK09407 105 GKARRHAfeeVLDVALTARY---YARRAPKLlaprrRAGALPVLT--KTTELRQPKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSssRNIDFIAFTGSPEVGVQIQTMAARNFIG 252
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 253 CTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAI---QASDSGEDsiLG 329
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMrlgAGYDYSAD--MG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 330 PLISVRQKKRVESYIAEA---DAPLLARGGIRPGV-PtdgYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIE 405
Cdd:PRK09407 336 SLISEAQLETVSAHVDDAvakGATVLAGGKARPDLgP---LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517140063 406 IANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFIN-GYGAG-GGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAwGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
50-480 |
2.88e-100 |
|
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: 307.46 E-value: 2.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 50 VERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYgsaADKVH 129
Cdd:cd07100 1 IEAALDRAHAAFL--AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 130 G----EVIPfLNGYNVEVHREPHGVTGHIIPWNYPA-QMFgRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPA 204
Cdd:cd07100 76 AfladEPIE-TDAGKAYVRYEPLGVVLGIMPWNFPFwQVF-RFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 205 GA-VNIVTGRGLVAgAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAII 283
Cdd:cd07100 154 GVfQNLLIDSDQVE-AIIADPR-VRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 284 QNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVESYIAEA---DAPLLARGGIRP 359
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDpMDEDTDLGPLARKDLRDELHEQVEEAvaaGATLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 360 GvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVF 439
Cdd:cd07100 312 G---PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 517140063 440 INGYGAgGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07100 389 INGMVK-SDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
31-481 |
5.67e-100 |
|
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: 307.61 E-value: 5.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 31 VSPIDGAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALAD 110
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQ--RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 111 MIVTARYFEFYGSAADKVHG-EVIP---FLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDA 186
Cdd:cd07099 79 VLLALEAIDWAARNAPRVLApRKVPtglLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 187 CLTALRIGEMAVEVGFPAGAVNIVTGRGLVaGAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVF 266
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 267 DDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAI-QASDSGEDSILGPLISVRQKKRVESYIA 345
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 346 EAdaplLARGG-IRPG---VPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTA 421
Cdd:cd07099 317 DA----VAKGAkALTGgarSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517140063 422 DGGRQKRVAKKLKCGQVFINGYGAGGGV-ELPFGGYRKSGHGREKGFAALHEFSTIKTIVD 481
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINDVLLTAGIpALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
28-480 |
1.28e-99 |
|
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: 306.83 E-value: 1.28e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 28 IDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA 107
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAK--EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVE-----VHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKP 182
Cdd:cd07149 79 RKEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEgrigfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 183 AEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIgcTLELGGKSP 262
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKV--TLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 263 QIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPLISVRQKKRVE 341
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDpLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 342 SYIAEA---DAPLLArGGIRpgvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASI 418
Cdd:cd07149 317 EWVEEAvegGARLLT-GGKR-----DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517140063 419 WTADGGRQKRVAKKLKCGQVFING---YGAGGgveLPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINDsstFRVDH---MPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
13-482 |
3.27e-96 |
|
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: 298.33 E-value: 3.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLpASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAfdgGEWSKATAT--ERGRLLLELSRRILSESE 90
Cdd:cd07082 4 YLINGEWK-ESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDA---GRGWWPTMPleERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 91 SLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVE-----VHREPHGVTGHIIPWNYPAQMFG 165
Cdd:cd07082 80 EVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaqVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 166 RSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTM 245
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 246 AARnfIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGED 325
Cdd:cd07082 240 HPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 326 S-ILGPLISVRQKKRVESYIAEAdaplLARGG--IRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEAS 402
Cdd:cd07082 318 GvDITPLIDPKSADFVEGLIDDA----VAKGAtvLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 403 AIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIVDN 482
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
17-479 |
8.46e-95 |
|
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: 294.60 E-value: 8.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 17 NKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAfdGGEWSKATATERGRLLLELSRRILSESESLARLE 96
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 97 SRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPflngYNVE-----VHREPHGVTGHIIPWNYPAQMFGRSVAPS 171
Cdd:cd07151 79 IRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILP----SDVPgkenrVYREPLGVVGVISPWNFPLHLSMRSVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 172 LAMGNATVLKPAEDACLTA-LRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNF 250
Cdd:cd07151 155 LALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 251 IGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILG 329
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDpSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 330 PLISVRQKKRVESYIAEA---DAPLLARGGIrpgvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEI 406
Cdd:cd07151 315 PLINESQVDGLLDKIEQAveeGATLLVGGEA------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALEL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 407 ANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07151 389 ANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
32-479 |
9.50e-95 |
|
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: 294.22 E-value: 9.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 32 SPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA---L 108
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQR--AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAfeeV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 109 ADMIVTARYfefYGSAADKV-----HGEVIPFLNgyNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPA 183
Cdd:cd07101 80 LDVAIVARY---YARRAERLlkprrRRGAIPVLT--RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 184 EDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSsrNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQ 263
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 264 IVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQ---ASDSGEDsiLGPLISVRQKKRV 340
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRlgaALDYGPD--MGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 341 ESYIAEA---DAPLLARGGIRPGV-PtdgYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVA 416
Cdd:cd07101 311 TAHVDDAvakGATVLAGGRARPDLgP---YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517140063 417 SIWTADGGRQKRVAKKLKCGQVFIN-GYGAG-GGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVNeGYAAAwASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-480 |
9.31e-92 |
|
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: 286.25 E-value: 9.31e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 28 IDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA 107
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARYFEFYGSAADKVHGEVIPFLNGYNVE-----VHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKP 182
Cdd:cd07094 79 RVEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDnrlawTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 183 AEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAArnFIGCTLELGGKSP 262
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 263 QIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDS-GEDSILGPLISVRQKKRVE 341
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 342 SYIAEA--DAPLLARGGIRpgvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIW 419
Cdd:cd07094 317 RWVEEAveAGARLLCGGER-----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517140063 420 TADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
33-482 |
8.40e-90 |
|
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: 281.88 E-value: 8.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 33 PIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKP-IKQALADM 111
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQR--EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 112 IVTA---RYFEFYGSAADKVHGEVIPFLNGYNV-EVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDAC 187
Cdd:cd07098 81 LVTCekiRWTLKHGEKALRPESRPGGLLMFYKRaRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 188 LTALRIGEMA----VEVGFPAGAVNIVTGRGlVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQ 263
Cdd:cd07098 161 WSSGFFLSIIreclAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 264 IVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAI-QASDSGEDSILGPLISVRQKKRVES 342
Cdd:cd07098 240 IVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 343 YIAEA---DAPLLARG--GIRPGVPTDGYYVaPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVAS 417
Cdd:cd07098 320 LVADAvekGARLLAGGkrYPHPEYPQGHYFP-PTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGAS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517140063 418 IWTADGGRQKRVAKKLKCGQVFINGYGAGGGV-ELPFGGYRKSGHGREKGFAALHEFSTIKTIVDN 482
Cdd:cd07098 399 VFGKDIKRARRIASQLETGMVAINDFGVNYYVqQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTED 464
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-477 |
3.15e-89 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 281.02 E-value: 3.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 1 MANTDLILPKAMNLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLE 80
Cdd:PRK11241 1 MQLNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 81 LSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPflnGYNVE----VHREPHGVTGHIIP 156
Cdd:PRK11241 79 WFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIP---GHQADkrliVIKQPIGVTAAITP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 157 WNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSP 236
Cdd:PRK11241 156 WNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 237 EVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEA 316
Cdd:PRK11241 236 EIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 317 IQASDSGEDSI-LGPLISVRQKKRVESYIAEAdaplLARGG--IRPGVPT--DGYYVAPALFGPCDPYSRIAQEEVFGPV 391
Cdd:PRK11241 316 LHIGDGLEKGVtIGPLIDEKAVAKVEEHIADA----LEKGArvVCGGKAHelGGNFFQPTILVDVPANAKVAKEETFGPL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 392 LCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGyGAGGGVELPFGGYRKSGHGREKGFAALH 471
Cdd:PRK11241 392 APLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT-GIISNEVAPFGGIKASGLGREGSKYGIE 470
|
....*.
gi 517140063 472 EFSTIK 477
Cdd:PRK11241 471 DYLEIK 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
78-473 |
1.06e-86 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 271.99 E-value: 1.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 78 LLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPF-LNGYNVEVHREPHGVTGHIIP 156
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSdRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 157 WNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSP 236
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 237 EVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEA 316
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 317 IQASD--SGEDSILGPLISVRQKKRVESYIAEA--DAPLLARGGIRpgVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVL 392
Cdd:PRK10090 241 VQFGNpaERNDIAMGPLINAAALERVEQKVARAveEGARVALGGKA--VEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 393 CMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFIN--GYGAGGGVElpfGGYRKSGHGREKGFAAL 470
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINreNFEAMQGFH---AGWRKSGIGGADGKHGL 395
|
...
gi 517140063 471 HEF 473
Cdd:PRK10090 396 HEY 398
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
49-479 |
1.34e-86 |
|
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: 272.53 E-value: 1.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 49 DVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKV 128
Cdd:cd07105 1 DADQAVEAAAAAF--PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 129 HGEVIPFLN-GYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAV 207
Cdd:cd07105 79 IGGSIPSDKpGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 208 NIVTGRGLVAGA---ALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAAlpvlVNAII- 283
Cdd:cd07105 159 NVVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAA----ANAALf 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 284 ---QNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSgedsILGPLISVRQKKRVESYIAEAdaplLARG----- 355
Cdd:cd07105 235 gafLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPV----VLGSLVSAAAADRVKELVDDA----LSKGaklvv 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 356 GIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKC 435
Cdd:cd07105 307 GGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIES 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 517140063 436 GQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07105 387 GAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
36-474 |
1.47e-84 |
|
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: 267.62 E-value: 1.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 36 GAIFTTIADSSAEDVERAIMAARAAfdGGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTA 115
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 116 RYFEFYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTA-LRIG 194
Cdd:cd07152 79 GELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 195 EMAVEVGFPAGAVNIVTGrGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAA 274
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 275 LPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYIAE---ADAP 350
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVaLGPLINARQLDRVHAIVDDsvaAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 351 LLArGGIRpgvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVA 430
Cdd:cd07152 318 LEA-GGTY-----DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 517140063 431 KKLKCGQVFINGYGAGGGVELPFGGYRKSGHG-REKGFAALHEFS 474
Cdd:cd07152 392 DRLRTGMLHINDQTVNDEPHNPFGGMGASGNGsRFGGPANWEEFT 436
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
28-480 |
4.39e-83 |
|
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: 263.72 E-value: 4.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 28 IDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA 107
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARYFEFYGSAADKVHGEVIPF-----LNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKP 182
Cdd:cd07147 79 RGEVARAIDTFRIAAEEATRIYGEVLPLdisarGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 183 AEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAgAALSSSRNIDFIAFTGSPEVGVQIQTMAARNfiGCTLELGGKSP 262
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 263 QIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGED-SILGPLISVRQKKRVE 341
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDaTDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 342 SYIAEA---DAPLLArGGIRpgvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASI 418
Cdd:cd07147 316 GWVNEAvdaGAKLLT-GGKR-----DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517140063 419 WTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLV 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
13-479 |
2.23e-82 |
|
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: 262.84 E-value: 2.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESL 92
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 93 ARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFL-NGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPS 171
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVaRGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 172 LAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGrGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFI 251
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 GCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQ---ASDSGEDsiL 328
Cdd:cd07085 240 RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKvgaGDDPGAD--M 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 329 GPLISVRQKKRVESYIAE-----ADAPLLARGGIRPGVPtDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASA 403
Cdd:cd07085 318 GPVISPAAKERIEGLIESgveegAKLVLDGRGVKVPGYE-NGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 404 IEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINgygagGGVELP-----FGGYRKS--GHGREKGFAALHEFSTI 476
Cdd:cd07085 397 IAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN-----VPIPVPlaffsFGGWKGSffGDLHFYGKDGVRFYTQT 471
|
...
gi 517140063 477 KTI 479
Cdd:cd07085 472 KTV 474
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
41-460 |
4.69e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 260.64 E-value: 4.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 41 TIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEF 120
Cdd:PRK03137 66 RVSKATKELAEKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 121 YGSAADKV-HGE-VIPFLNGYNvEVHREPHGVTGHIIPWNYP-AQMFGRSVAPsLAMGNATVLKPAEDACLTALRIGEMA 197
Cdd:PRK03137 144 YARQMLKLaDGKpVESRPGEHN-RYFYIPLGVGVVISPWNFPfAIMAGMTLAA-IVAGNTVLLKPASDTPVIAAKFVEVL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 198 VEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCT------LELGGKSPQIVFDDANL 271
Cdd:PRK03137 222 EEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIwlkrviAEMGGKDAIVVDEDADL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 272 DAAlpvlVNAIIQNG----GQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYI--A 345
Cdd:PRK03137 302 DLA----AESIVASAfgfsGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIeiG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 346 EADAPLLARGGirpGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGR 425
Cdd:PRK03137 378 KEEGRLVLGGE---GDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREH 454
|
410 420 430
....*....|....*....|....*....|....*..
gi 517140063 426 QKRVAKKLKCGQVFING--YGAGGGVElPFGGYRKSG 460
Cdd:PRK03137 455 LEKARREFHVGNLYFNRgcTGAIVGYH-PFGGFNMSG 490
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
31-462 |
4.69e-79 |
|
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: 253.32 E-value: 4.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 31 VSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA--- 107
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAgge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARYFefYGSAADKVHGEVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDAC 187
Cdd:cd07102 79 IRGMLERARYM--ISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 188 LTALRIGEMAVEVGFPAGAVNIVTGRGLVaGAALSSSRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFD 267
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 268 DANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYIAE 346
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTtLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 347 A---DAPLLARGGIRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADG 423
Cdd:cd07102 316 AiakGARALIDGALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDI 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 517140063 424 GRQKRVAKKLKCGQVFIN--GYGAGGgveLPFGGYRKSGHG 462
Cdd:cd07102 396 ARAEALGEQLETGTVFMNrcDYLDPA---LAWTGVKDSGRG 433
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-480 |
2.32e-77 |
|
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: 249.20 E-value: 2.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 28 IDVVSPIDGAIFTTIADSSAEDVERAIMAAraafdGGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA 107
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALA-----ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARYFEFYGSAADKVHGEVIPFLNGYN-----VEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKP 182
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFSCDLTANgkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 183 AEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAArnFIGCTLELGGKSP 262
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 263 QIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSG-EDSILGPLISVRQKKRVE 341
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMdPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 342 SYIAEA--DAPLLARGGIRpgvptDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIW 419
Cdd:cd07146 314 NRVEEAiaQGARVLLGNQR-----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVC 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 420 TADGGRQKRVAKKLKCGQVFINGyGAGGGVEL-PFGGYRKSGHG-REKGFAALHEFSTIKTIV 480
Cdd:cd07146 389 TNDLDTIKRLVERLDVGTVNVNE-VPGFRSELsPFGGVKDSGLGgKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
15-483 |
1.76e-73 |
|
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: 240.56 E-value: 1.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGGREIdvVSPID-GAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLA 93
Cdd:cd07083 23 IGGEWVDTKERMVS--VSPFApSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 94 RLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHG--EVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPS 171
Cdd:cd07083 99 ATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 172 LAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAARN-- 249
Cdd:cd07083 179 VAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 250 ----FIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGED 325
Cdd:cd07083 259 gqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 326 -SILGPLISVRQKKRVESYIAEADAPL-LARGGIRPGvpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMI--PFDDEA 401
Cdd:cd07083 339 gTDLGPVIDAEQEAKVLSYIEHGKNEGqLVLGGKRLE--GEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIryKDDDFA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 402 SAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFIN--GYGAGGGVElPFGGYRKSGHGREKGfaALH---EFSTI 476
Cdd:cd07083 417 EALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQ-PFGGFKLSGTNAKTG--GPHylrRFLEM 493
|
....*..
gi 517140063 477 KTIVDNH 483
Cdd:cd07083 494 KAVAERF 500
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
28-479 |
7.09e-72 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 235.02 E-value: 7.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 28 IDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA 107
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFR--DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 108 LADMIVTARYFEFYGSAADKVHGEV---IPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAE 184
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADEpadAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 185 DACLTALRIGEMAVEVGFPAGA-VNIVTGRGLVAgAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQ 263
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCfQTLLVGSGAVE-AILRDPR-VAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 264 IVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVES 342
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTdVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 343 YIAEA---DAPLLArGGIRPGVPtdGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIW 419
Cdd:PRK09406 319 QVDDAvaaGATILC-GGKRPDGP--GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 420 TADGGRQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMTVSYP-ELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
31-482 |
1.62e-70 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 231.67 E-value: 1.62e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 31 VSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALAD 110
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 111 MIVTARYFEFYGSaadkvHGEVI----PFL--NGYNVEVHRePHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAE 184
Cdd:PRK13968 90 VAKSANLCDWYAE-----HGPAMlkaePTLveNQQAVIEYR-PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 185 DACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQI 264
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 265 VFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASD-SGEDSILGPL--ISVRQK--KR 339
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDpRDEENALGPMarFDLRDElhHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 340 VESYIAEADAPLLarGGIRpgVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIW 419
Cdd:PRK13968 323 VEATLAEGARLLL--GGEK--IAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517140063 420 TADGGRQKRVAKKLKCGQVFINGYGAGGGvELPFGGYRKSGHGREKGFAALHEFSTIKTIVDN 482
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDA-RVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKD 460
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
16-466 |
5.11e-58 |
|
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: 198.97 E-value: 5.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 16 GNKWlpASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARL 95
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 96 ESRDNGKPIKQAL---------ADMIV-TARYFefygsaadkvHGEVIP-------FLNGYNvevhrePHGVTGHIIPWN 158
Cdd:cd07130 80 VSLEMGKILPEGLgevqemidiCDFAVgLSRQL----------YGLTIPserpghrMMEQWN------PLGVVGVITAFN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 159 YPAQMFGRSVAPSLAMGNATVLKPAEDACLTALR----IGEMAVEVGFPAGAVNIVTGrGLVAGAALSSSRNIDFIAFTG 234
Cdd:cd07130 144 FPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 235 SPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARF 314
Cdd:cd07130 223 STAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 315 EAIQASDSGEDSIL-GPLISVRQKKRVESYIAEADApllARGGIRPG---VPTDGYYVAPALFGPcDPYSRIAQEEVFGP 390
Cdd:cd07130 303 KQVRIGDPLDDGTLvGPLHTKAAVDNYLAAIEEAKS---QGGTVLFGgkvIDGPGNYVEPTIVEG-LSDAPIVKEETFAP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 391 VLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRV--AKKLKCGQVFIN----GYGAGGGvelpFGGYRKSGHGRE 464
Cdd:cd07130 379 ILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNigtsGAEIGGA----FGGEKETGGGRE 454
|
..
gi 517140063 465 KG 466
Cdd:cd07130 455 SG 456
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
143-481 |
6.65e-58 |
|
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: 197.36 E-value: 6.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 143 VHREPHGVTGHIIPWNYPAQMfgrSVAP---SLAMGNATVLKPAEDACLTALRIGEMaVEVGFPAGAVNIVTGRGLVAgA 219
Cdd:cd07087 96 VIPEPLGVVLIIGPWNYPLQL---ALAPligAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVEVA-T 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 220 ALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQ 299
Cdd:cd07087 171 ALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 300 RGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAEADaplLARGGirpGVPTDGYYVAPALFGPCDPY 379
Cdd:cd07087 250 ESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK---VVIGG---QVDKEERYIAPTILDDVSPD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 380 SRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGV-ELPFGGYRK 458
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIpNLPFGGVGN 403
|
330 340
....*....|....*....|...
gi 517140063 459 SGHGREKGFAALHEFSTIKTIVD 481
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
49-469 |
2.19e-56 |
|
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: 193.26 E-value: 2.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 49 DVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKV 128
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 129 HGEV-IPFLNGYNVEVHRePHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAV 207
Cdd:cd07095 79 TGERaTPMAQGRAVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 208 NIVTGrGLVAGAALSSSRNIDFIAFTGSPEVGVQI-QTMAARNFIGCTLELGGKSPQIVFDDANLDAAlpvlVNAIIQN- 285
Cdd:cd07095 158 NLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPGKILALEMGGNNPLVVWDVADIDAA----AYLIVQSa 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 286 ---GGQTCSAGARVLVQRGvydQVAVELKARF-EAIQASDSG----EDSILGPLISVRqkkRVESYIAEADApLLARGG- 356
Cdd:cd07095 233 fltAGQRCTCARRLIVPDG---AVGDAFLERLvEAAKRLRIGapdaEPPFMGPLIIAA---AAARYLLAQQD-LLALGGe 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 357 -IRPG--VPTDGYYVAPALFgPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKL 433
Cdd:cd07095 306 pLLAMerLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420 430
....*....|....*....|....*....|....*.
gi 517140063 434 KCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAA 469
Cdd:cd07095 385 RAGIVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-483 |
2.08e-55 |
|
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: 192.80 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 21 PASGGREI------DVVSPIDG-AIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLA 93
Cdd:cd07125 35 PIINGEETetgegaPVIDPADHeRTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGELI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 94 RLESRDNGKPIKQALADM---IVTARYfefYGSAADKVHGEVI-PFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVA 169
Cdd:cd07125 113 ALAAAEAGKTLADADAEVreaIDFCRY---YAAQARELFSDPElPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 170 PSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQI-QTMAAR 248
Cdd:cd07125 190 AALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLInRALAER 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 249 NfiGCTL----ELGGKSPQIVfdDAnldAALPVLVNA-IIQ----NGGQTCSAgARVL-VQRGVYDQVAVELKARFEAIQ 318
Cdd:cd07125 270 D--GPILpliaETGGKNAMIV--DS---TALPEQAVKdVVQsafgSAGQRCSA-LRLLyLQEEIAERFIEMLKGAMASLK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 319 ASDSGE-DSILGPLISVRQKKRVESYIA--EADAPLLARGGIRPGvptDGYYVAPALFGpcDPYSRIAQEEVFGPVLCMI 395
Cdd:cd07125 342 VGDPWDlSTDVGPLIDKPAGKLLRAHTElmRGEAWLIAPAPLDDG---NGYFVAPGIIE--IVGIFDLTTEVFGPILHVI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 396 PFDDE--ASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING--YGAGGGVElPFGGYRKSGHGReK--GFAA 469
Cdd:cd07125 417 RFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRniTGAIVGRQ-PFGGWGLSGTGP-KagGPNY 494
|
490
....*....|....
gi 517140063 470 LHEFSTIKTIVDNH 483
Cdd:cd07125 495 LLRFGNEKTVSLNT 508
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
138-474 |
7.33e-54 |
|
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: 186.66 E-value: 7.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 138 GYNVEVHREPHGVTGHIIPWNYPAQM-FGrSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVgFPAGAVNIVTGRGLV 216
Cdd:cd07134 91 GTKSKIRYEPKGVCLIISPWNYPFNLaFG-PLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 217 AGAALSSSrnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARV 296
Cdd:cd07134 169 AQALLELP--FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 297 LVQRGVYDQVAVELKA-------RFEAIQASDSgedsiLGPLISVRQKKRVESYIAEA---DAPLLARGGIRPgvptDGY 366
Cdd:cd07134 247 FVHESVKDAFVEHLKAeiekfygKDAARKASPD-----LARIVNDRHFDRLKGLLDDAvakGAKVEFGGQFDA----AQR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 367 YVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING---- 442
Cdd:cd07134 318 YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDvvlh 397
|
330 340 350
....*....|....*....|....*....|..
gi 517140063 443 YGAGGgveLPFGGYRKSGHGREKGFAALHEFS 474
Cdd:cd07134 398 FLNPN---LPFGGVNNSGIGSYHGVYGFKAFS 426
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-480 |
4.21e-51 |
|
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: 179.92 E-value: 4.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 28 IDVVSPIDGAIFTTIADSSAEDVERAIMAARAAF-DGGEWskATATERGRLLLELSRRILSESESLARLESRDNGKPikq 106
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 107 aLADMIVTAryfefyGSAADKVH----------GEVIPF-----LNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPS 171
Cdd:cd07148 76 -LVDAKVEV------TRAIDGVElaadelgqlgGREIPMgltpaSAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 172 LAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRnIDFIAFTGSPEVGVQIQTMAARNfI 251
Cdd:cd07148 149 IAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLRSKLAPG-T 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 252 GCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSG-EDSILGP 330
Cdd:cd07148 227 RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTdPDTEVGP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 331 LISVRQKKRVESYIAEADAP--LLARGGIRPGvptDGYYVAPALFGPCDPySRIAQEEVFGPVLCMIPFDDEASAIEIAN 408
Cdd:cd07148 307 LIRPREVDRVEEWVNEAVAAgaRLLCGGKRLS---DTTYAPTVLLDPPRD-AKVSTQEIFGPVVCVYSYDDLDEAIAQAN 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517140063 409 CTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:cd07148 383 SLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAV 454
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
127-481 |
2.64e-50 |
|
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: 177.41 E-value: 2.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 127 KVHGEVIPFLNGyNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMaVEVGFPAGA 206
Cdd:cd07135 89 KVKDGPLAFMFG-KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 207 VNIVTGRGLVAGAALSSSrnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNG 286
Cdd:cd07135 167 FQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 287 GQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAEadapllARGGIRPGVPTDG- 365
Cdd:cd07135 245 GQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT------TKGKVVIGGEMDEa 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 366 -YYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYG 444
Cdd:cd07135 319 tRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTL 398
|
330 340 350
....*....|....*....|....*....|....*...
gi 517140063 445 AGGGV-ELPFGGYRKSGHGREKGFAALHEFSTIKTIVD 481
Cdd:cd07135 399 IHVGVdNAPFGGVGDSGYGAYHGKYGFDTFTHERTVVK 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
20-482 |
3.24e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 184.25 E-value: 3.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 20 LPASGGREIDVVSPIDGA-IFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSESESLARLESR 98
Cdd:PRK11904 556 IINGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAELIALCVR 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 99 DNGKPIKQALADmIVTA----RYfefYGSAADKVHG--EVIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:PRK11904 634 EAGKTLQDAIAE-VREAvdfcRY---YAAQARRLFGapEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAAL 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQI-QTMAARN-- 249
Cdd:PRK11904 710 AAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTLAARDgp 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 250 ---FIGctlELGGKSPQIVfddanlDA-ALP--VLVNAII---QNGGQTCSAgARVL-VQRGVYDQVAVELKARFEAIQA 319
Cdd:PRK11904 790 ivpLIA---ETGGQNAMIV------DStALPeqVVDDVVTsafRSAGQRCSA-LRVLfVQEDIADRVIEMLKGAMAELKV 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 320 SDSGEDSI-LGPLISVRQKKRVESYIAE--ADAPLLARGGIrPGVPTDGYYVAPALFgpcdPYSRIAQ--EEVFGPVLCM 394
Cdd:PRK11904 860 GDPRLLSTdVGPVIDAEAKANLDAHIERmkREARLLAQLPL-PAGTENGHFVAPTAF----EIDSISQleREVFGPILHV 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 395 IPF--DDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFIN--GYGAGGGVElPFGGYRKSGHG-REKGFAA 469
Cdd:PRK11904 935 IRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNrnQIGAVVGVQ-PFGGQGLSGTGpKAGGPHY 1013
|
490
....*....|...
gi 517140063 470 LHEFSTIKTIVDN 482
Cdd:PRK11904 1014 LLRFATEKTVTVN 1026
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
143-482 |
7.35e-49 |
|
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: 173.84 E-value: 7.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 143 VHREPHGVTGHIIPWNYPAQMfgrSVAP---SLAMGNATVLKPAEDACLTALRIGEMAVEVgFPAGAVNIVTGRGLVAGA 219
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 220 ALSSSrnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQ 299
Cdd:cd07136 172 LLDQK--FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 300 RGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAEADaplLARGGirpGVPTDGYYVAPALFGPCDPY 379
Cdd:cd07136 250 ESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK---IVFGG---NTDRETLYIEPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 380 SRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADggrqKRVAKKlkcgqvFINGYGAGGGV---------- 449
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED----KKVEKK------VLENLSFGGGCindtimhlan 393
|
330 340 350
....*....|....*....|....*....|....
gi 517140063 450 -ELPFGGYRKSGHGREKGFAALHEFSTIKTIVDN 482
Cdd:cd07136 394 pYLPFGGVGNSGMGSYHGKYSFDTFSHKKSILKK 427
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
9-479 |
2.56e-48 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 175.71 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 9 PKAMNLIGNKWLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSE 88
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 89 SESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFL-NGYNVEVHREPHGVTGHIIPWNYPAQMFGRS 167
Cdd:PLN02419 190 MDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVsNGVDTYSIREPLGVCAGICPFNFPAMIPLWM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 168 VAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAaLSSSRNIDFIAFTGSPEVGVQIQTMAA 247
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 248 RNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVqrgVYDQVAVE--LKARFEAIQASDSGE- 324
Cdd:PLN02419 349 AKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVF---VGDAKSWEdkLVERAKALKVTCGSEp 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 325 DSILGPLISVRQKKRV----ESYIAEADAPLL-ARGGIRPGVpTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDD 399
Cdd:PLN02419 426 DADLGPVISKQAKERIcrliQSGVDDGAKLLLdGRDIVVPGY-EKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 400 EASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINgygAGGGVELP---FGGYRKSGHGREK--GFAALHEFS 474
Cdd:PLN02419 505 FDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN---VPIPVPLPffsFTGNKASFAGDLNfyGKAGVDFFT 581
|
....*
gi 517140063 475 TIKTI 479
Cdd:PLN02419 582 QIKLV 586
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
15-469 |
3.41e-48 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 172.84 E-value: 3.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWLPASGgREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:PRK09457 5 INGDWIAGQG-EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQAL---ADMI------VTArYFEFYGSAADkvhgeviPFLNGYNVEVHRePHGVTGHIIPWNYPAQMFG 165
Cdd:PRK09457 82 VIARETGKPLWEAAtevTAMInkiaisIQA-YHERTGEKRS-------EMADGAAVLRHR-PHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 166 RSVAPSLAMGNATVLKPAEdacLTAlRIGEMAVEV----GFPAGAVNIVTGrGLVAGAALSSSRNIDFIAFTGSPEVGVQ 241
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSE---LTP-WVAELTVKLwqqaGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 242 I-QTMAARNFIGCTLELGGKSPQIVFDDANLDAAlpvlVNAIIQNG----GQTCSAGARVLVQRGVY-DQVAVELKARFE 315
Cdd:PRK09457 228 LhRQFAGQPEKILALEMGGNNPLVIDEVADIDAA----VHLIIQSAfisaGQRCTCARRLLVPQGAQgDAFLARLVAVAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 316 AIQ--ASDSGEDSILGPLISVRQKKRvesyIAEADAPLLARGG---IRPGVPTDGY-YVAPALFGPCDpYSRIAQEEVFG 389
Cdd:PRK09457 304 RLTvgRWDAEPQPFMGAVISEQAAQG----LVAAQAQLLALGGkslLEMTQLQAGTgLLTPGIIDVTG-VAELPDEEYFG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 390 PVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAA 469
Cdd:PRK09457 379 PLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPSAYYA 458
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
141-479 |
9.95e-46 |
|
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: 164.97 E-value: 9.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 141 VEVHREPHGVTGHIIPWNYPAQMfgrSVAP---SLAMGNATVLKPAEDACLTALRIGEMAVEVgFPAGAVNIVTGRGLVA 217
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGGADVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 218 gAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAAlpvlVNAIIQ----NGGQTCSAG 293
Cdd:cd07133 171 -AAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKA----AERIAFgkllNAGQTCVAP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 294 ARVLVQRGVYDQVAVELKARFEAiQASDSGEDSILGPLISVRQKKRVESYIAEA-----------DAPLLARGGiRPGVP 362
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAK-MYPTLADNPDYTSIINERHYARLQGLLEDArakgarvielnPAGEDFAAT-RKLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 363 TdgyyvapALFGPcDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING 442
Cdd:cd07133 323 T-------LVLNV-TDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIND 394
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517140063 443 YGAGGGVE-LPFGGYRKSG----HGREkGFaalHEFSTIKTI 479
Cdd:cd07133 395 TLLHVAQDdLPFGGVGASGmgayHGKE-GF---LTFSHAKPV 432
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
142-483 |
3.03e-44 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 162.12 E-value: 3.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 142 EVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMaVEVGFPAGAVNIVTGRGLVAGAAL 221
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 222 SSSrnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRG 301
Cdd:PTZ00381 183 KEP--FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 302 VYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIaEADAPLLARGGirpGVPTDGYYVAPALFGPCDPYSR 381
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI-KDHGGKVVYGG---EVDIENKYVAPTIIVNPDLDSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 382 IAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING----YGAgggVELPFGGYR 457
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvfhLLN---PNLPFGGVG 413
|
330 340
....*....|....*....|....*.
gi 517140063 458 KSGHGREKGFAALHEFSTIKTIVDNH 483
Cdd:PTZ00381 414 NSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
10-466 |
1.97e-43 |
|
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: 160.08 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 10 KAMNLIGNKwlPASGGREIDVVSPID-GAIFTTIADSSAEDVERAIMAARAAFdgGEWSKATATERGRLLLELSRRILSE 88
Cdd:TIGR01238 37 QAAPIIGHS--YKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAF--PTWNATPAKERAAKLDRLADLLELH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 89 SESLARLESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEvipflngynvEVHRePHGVTGHIIPWNYPAQMFGRSV 168
Cdd:TIGR01238 113 MPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGE----------FSVE-SRGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 169 APSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQI-QTMAA 247
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInQTLAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 248 R--NFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGED 325
Cdd:TIGR01238 262 RedAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 326 SI-LGPLISVRQKKRVESYIAEADAPLLARGGIRPGVPTD---GYYVAPALFgPCDPYSRIaQEEVFGPVLCMIPF--DD 399
Cdd:TIGR01238 342 TTdVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRAcqhGTFVAPTLF-ELDDIAEL-SEEVFGPVLHVVRYkaRE 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517140063 400 EASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING--YGAGGGVElPFGGYRKSGHGREKG 466
Cdd:TIGR01238 420 LDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRnqVGAVVGVQ-PFGGQGLSGTGPKAG 487
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
10-462 |
3.61e-43 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 163.88 E-value: 3.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 10 KAMNLIGNkwlPASGGREIDVVSPID-GAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLlelsRRI--L 86
Cdd:PRK11905 554 HAAPLLAG---GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFP--EWSATPAAERAAIL----ERAadL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 87 SES--ESLARLESRDNGKpikqALADMIVTARyfefygsaadkvhgEVIPFLNGYNVEVHR-------EPHGVTGHIIPW 157
Cdd:PRK11905 625 MEAhmPELFALAVREAGK----TLANAIAEVR--------------EAVDFLRYYAAQARRllngpghKPLGPVVCISPW 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 158 NYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPE 237
Cdd:PRK11905 687 NFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTE 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 238 VGVQIQ-TMAARNFIGCTL--ELGGKSPQIVfdDAnldAALP------VLVNAiIQNGGQTCSAgARVL-VQRGVYDQVA 307
Cdd:PRK11905 767 VARLIQrTLAKRSGPPVPLiaETGGQNAMIV--DS---SALPeqvvadVIASA-FDSAGQRCSA-LRVLcLQEDVADRVL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 308 VELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYIA--EADAPLLARGGIRPGVPtDGYYVAPALFgpcdPYSRIAQ 384
Cdd:PRK11905 840 TMLKGAMDELRIGDPWRLSTdVGPVIDAEAQANIEAHIEamRAAGRLVHQLPLPAETE-KGTFVAPTLI----EIDSISD 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 385 --EEVFGPVLCMIPF--DDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING--YGAGGGVElPFGGYRK 458
Cdd:PRK11905 915 leREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRniIGAVVGVQ-PFGGEGL 993
|
....
gi 517140063 459 SGHG 462
Cdd:PRK11905 994 SGTG 997
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-482 |
1.77e-42 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 157.61 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 19 WLPASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSESESLARLESR 98
Cdd:PLN00412 24 WRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA--WAKTPLWKRAELLHKAAAILKEHKAPIAECLVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 99 DNGKPIKQALADMIVTARYFEFYGSAADKVHGEViPFL-------NGYN--VEVHREPHGVTGHIIPWNYPAQMFGRSVA 169
Cdd:PLN00412 102 EIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEG-KFLvsdsfpgNERNkyCLTSKIPLGVVLAIPPFNYPVNLAVSKIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 170 PSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSpEVGVQIQTMAArn 249
Cdd:PLN00412 181 PALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAG-- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 250 FIGCTLELGGKSPQIVFDDANLDAAlpvlVNAIIQNG----GQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGED 325
Cdd:PLN00412 258 MVPLQMELGGKDACIVLEDADLDLA----AANIIKGGfsysGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 326 SILGPLISVRQKKRVESYIAEAdaplLARGG-IRPGVPTDGYYVAPALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAI 404
Cdd:PLN00412 334 CDITPVVSESSANFIEGLVMDA----KEKGAtFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGI 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517140063 405 EIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKTIVDN 482
Cdd:PLN00412 410 HHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVIN 487
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
10-462 |
2.20e-42 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 161.26 E-value: 2.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 10 KAMNLIGNKwlpASGGREIDVVSPIDGA-IFTTIADSSAEDVERAIMAARAAFDGgeWSKATATERGRLLLELSRRILSE 88
Cdd:COG4230 557 QAAPLIAGE---AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAH 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 89 SESLARLESRDNGKPIKQALADMivtaRyfefygsaadkvhgEVIPFLNGYNVEV--------HREPHGVTGHIIPWNYP 160
Cdd:COG4230 632 RAELMALLVREAGKTLPDAIAEV----R--------------EAVDFCRYYAAQArrlfaaptVLRGRGVFVCISPWNFP 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 161 AQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGV 240
Cdd:COG4230 694 LAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETAR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 241 QIQ-TMAARN-----FIGctlELGGKSPQIVfddanlDA-ALP------VLVNAiIQNGGQTCSAgARVL-VQRGVYDQV 306
Cdd:COG4230 774 LINrTLAARDgpivpLIA---ETGGQNAMIV------DSsALPeqvvddVLASA-FDSAGQRCSA-LRVLcVQEDIADRV 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 307 AVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYIA--EADAPLLARGGIrPGVPTDGYYVAPALFgpcdpysRIA 383
Cdd:COG4230 843 LEMLKGAMAELRVGDPADLSTdVGPVIDAEARANLEAHIErmRAEGRLVHQLPL-PEECANGTFVAPTLI-------EID 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 384 -----QEEVFGPVLCMIPF--DDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING--YGAGGGVElPFG 454
Cdd:COG4230 915 sisdlEREVFGPVLHVVRYkaDELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRniIGAVVGVQ-PFG 993
|
....*...
gi 517140063 455 GYRKSGHG 462
Cdd:COG4230 994 GEGLSGTG 1001
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
15-484 |
8.83e-38 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 144.59 E-value: 8.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 15 IGNKWlpASGGREIDVVSPIDGAIFTTIADSSAEDVERAIMAARAAfdGGEWSKATATERGRLLLELSRRILSESESLAR 94
Cdd:PLN02315 25 VGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA--AKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 95 LESRDNGKPIKQALADMIVTARYFEFYGSAADKVHGEVIPFL--NGYNVEVHrEPHGVTGHIIPWNYPAQMFGRSVAPSL 172
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErpNHMMMEVW-NPLGIVGVITAFNFPCAVLGWNACIAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 173 AMGNATVLKPAEDACLTALRIGEMAVEV----GFPAGAVNIVTGrGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAAR 248
Cdd:PLN02315 180 VCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 249 NFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGE-DSI 327
Cdd:PLN02315 259 RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEkGTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 328 LGPLISVRQKKRVE---SYIAEADAPLLARGGIrpgVPTDGYYVAPALFgPCDPYSRIAQEEVFGPVLCMIPFDDEASAI 404
Cdd:PLN02315 339 LGPLHTPESKKNFEkgiEIIKSQGGKILTGGSA---IESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 405 EIANCTEYGLVASIWTadggRQKRVAKKL------KCGQVFINGYGAGGGVELPFGGYRKSGHGREKGFAALHEFSTIKT 478
Cdd:PLN02315 415 EINNSVPQGLSSSIFT----RNPETIFKWigplgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
|
....*.
gi 517140063 479 IVDNHG 484
Cdd:PLN02315 491 CTINYG 496
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
24-460 |
3.97e-35 |
|
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: 137.33 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 24 GGREI------DVVSPID-GAIFTTIADSSAEDVERAIMAARAAFDggEWSKATATERGRLLLE----LS---RRILSES 89
Cdd:cd07123 38 GGKEVrtgntgKQVMPHDhAHVLATYHYADAALVEKAIEAALEARK--EWARMPFEDRAAIFLKaadlLSgkyRYELNAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 90 ESLARlesrdnGKPIKQALADMIV-TARYFEFYGSAADKVHGE--VIPFLNGYNVEVHREPHGVTGHIIPWNYPAQMFGR 166
Cdd:cd07123 116 TMLGQ------GKNVWQAEIDAACeLIDFLRFNVKYAEELYAQqpLSSPAGVWNRLEYRPLEGFVYAVSPFNFTAIGGNL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 167 SVAPSLaMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMA 246
Cdd:cd07123 190 AGAPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 247 ARN---------FIGctlELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAI 317
Cdd:cd07123 269 GENldryrtyprIVG---ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 318 QASDSGEDSI-LGPLISVRQKKRVESYIAEA----DAPLLARGGirpgvpTD---GYYVAPALFGPCDPYSRIAQEEVFG 389
Cdd:cd07123 346 KMGDPDDFSNfMGAVIDEKAFDRIKGYIDHAksdpEAEIIAGGK------CDdsvGYFVEPTVIETTDPKHKLMTEEIFG 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517140063 390 PVLCMIPFDDE--ASAIE-IANCTEYGLVASIWTADGGRQKRVAKKLK--CGQVFINGYGAGGGV-ELPFGGYRKSG 460
Cdd:cd07123 420 PVLTVYVYPDSdfEETLElVDTTSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVgQQPFGGARASG 496
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
50-471 |
4.25e-35 |
|
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: 135.83 E-value: 4.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 50 VERAIMAARAafDGGEWSKATATERGRLLLELSRRILSESESLARLESRDNGKPIKQA--LADMIVTARYFEFYGSAADK 127
Cdd:cd07084 1 PERALLAADI--STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenICGDQVQLRARAFVIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 128 VHGEVIPFLNGYNVEVHRE--PHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVG-FPA 204
Cdd:cd07084 79 PHEPGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 205 GAVNIVTGRGLvAGAALSSSRNIDFIAFTGSPEVGVQIQTMAArnFIGCTLELGGKSPQIVFDDAN-LDAALPVLVNAII 283
Cdd:cd07084 159 EDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAK--QARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 284 QNGGQTCSAGARVLVQRgvydqvAVELKARFEAIQA---SDSGEDSILGPLISVRQKKRVESYIAEADAPLLARGGIRPG 360
Cdd:cd07084 236 ACSGQKCTAQSMLFVPE------NWSKTPLVEKLKAllaRRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSGKELKN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 361 VPTDGYY---VAPALFGPCDPYSR---IAQEEVFGPVLCMIPFDD--EASAIEIANCTEYGLVASIWTADGGRQKRVAKK 432
Cdd:cd07084 310 HSIPSIYgacVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDPIFLQELIGN 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 517140063 433 L-KCGQVFINGYGAGGGV--ELPFGGYRKSGHGREKGFA-ALH 471
Cdd:cd07084 390 LwVAGRTYAILRGRTGVApnQNHGGGPAADPRGAGIGGPeAIK 432
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
141-466 |
4.88e-34 |
|
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: 133.12 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 141 VEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMavevgFPA----GAVNIVTGrGLV 216
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKyldkECYPVVLG-GVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 217 AGAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARV 296
Cdd:cd07132 168 ETTELLKQR-FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 297 LVQRGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESyiaeadapLLARGGIRPGVPTDG--YYVAPALFG 374
Cdd:cd07132 247 LCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKK--------LLSGGKVAIGGQTDEkeRYIAPTVLT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 375 PCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING----YGAgggVE 450
Cdd:cd07132 319 DVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDtimhYTL---DS 395
|
330
....*....|....*.
gi 517140063 451 LPFGGYRKSGHGREKG 466
Cdd:cd07132 396 LPFGGVGNSGMGAYHG 411
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
13-457 |
4.84e-32 |
|
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: 128.54 E-value: 4.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLpASGGREIDVVSPIDGAIFTTIaDSSAEDVERAIMAARAafDGGEWSKA-TATERGRLLLELSRRILSESES 91
Cdd:cd07128 3 SYVAGQWH-AGTGDGRTLHDAVTGEVVARV-SSEGLDFAAAVAYARE--KGGPALRAlTFHERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 92 LARLeSRDNGKPIKQALADM---IVTARYfefYGSAADK--------VHGEVIP------FLnGYNVEVHRepHGVTGHI 154
Cdd:cd07128 79 LYAL-SAATGATRRDSWIDIdggIGTLFA---YASLGRRelpnahflVEGDVEPlskdgtFV-GQHILTPR--RGVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 155 IPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVG-FPAGAVNIVTGRglvAGAALSSSRNIDFIAFT 233
Cdd:cd07128 152 NAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS---VGDLLDHLGEQDVVAFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 234 GSPEVGVQIQTMAA--RNFIGCTLE--------LGgksPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVY 303
Cdd:cd07128 229 GSAATAAKLRAHPNivARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 304 DQVAVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYIAE--ADAPLLARGGIRPGV----PTDGYYVAPALFGPC 376
Cdd:cd07128 306 DAVIEALKARLAKVVVGDPRLEGVrMGPLVSREQREDVRAAVATllAEAEVVFGGPDRFEVvgadAEKGAFFPPTLLLCD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 377 DPYSRIA--QEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKC--GQVFIN---------GY 443
Cdd:cd07128 386 DPDAATAvhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLnrdsakestGH 465
|
490 500
....*....|....*....|....*..
gi 517140063 444 G-------------AGGGVELpfGGYR 457
Cdd:cd07128 466 GsplpqlvhggpgrAGGGEEL--GGLR 490
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
50-479 |
8.75e-32 |
|
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: 126.37 E-value: 8.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 50 VERAIMAARAAFDGG-----EWSKATATERGRLLLElsrrilSESESLARLESrDNGKPIKQALADMI--------VTAR 116
Cdd:cd07137 1 APRLVRELRETFRSGrtrsaEWRKSQLKGLLRLVDE------NEDDIFAALRQ-DLGKPSAESFRDEVsvlvssckLAIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 117 YFEFYgSAADKVHGEVIPFLNgyNVEVHREPHGVTGHIIPWNYPaqmFGRSVAP---SLAMGNATVLKPAEDACLTALRI 193
Cdd:cd07137 74 ELKKW-MAPEKVKTPLTTFPA--KAEIVSEPLGVVLVISAWNFP---FLLSLEPvigAIAAGNAVVLKPSELAPATSALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 194 GEMaVEVGFPAGAVNIVTGrGLVAGAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDA 273
Cdd:cd07137 148 AKL-IPEYLDTKAIKVIEG-GVPETTALLEQK-WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 274 ALP-VLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAEAD-APL 351
Cdd:cd07137 225 AVRrIAGGKWGCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSvADK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 352 LARGGirpGVPTDGYYVAPALFgpCDP--YSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRV 429
Cdd:cd07137 305 IVHGG---ERDEKNLYIEPTIL--LDPplDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 517140063 430 AKKLKCGQVFING----YGAGggvELPFGGYRKSGHGREKGFAALHEFSTIKTI 479
Cdd:cd07137 380 VAETSSGGVTFNDtvvqYAID---TLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
13-457 |
1.21e-31 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 127.51 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLpASGGREIDVVSPIDGAIFTTiADSSAEDVERAIMAARAafDGGEWSKA-TATERGRLLLELSRRILSESES 91
Cdd:PRK11903 7 NYVAGRWQ-AGSGAGTPLFDPVTGEELVR-VSATGLDLAAAFAFARE--QGGAALRAlTYAQRAALLAAIVKVLQANRDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 92 LARLESRDNGKPIKQALADM---IVTARYfefYGSAADKVhGEVIPFLNGYNVEVHREP-----------HGVTGHIIPW 157
Cdd:PRK11903 83 YYDIATANSGTTRNDSAVDIdggIFTLGY---YAKLGAAL-GDARLLRDGEAVQLGKDPafqgqhvlvptRGVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 158 NYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMAVEVG-FPAGAVNIVTGRglvAGAALSSSRNIDFIAFTGSP 236
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGS---SAGLLDHLQPFDVVSFTGSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 237 EVGVQIQTMAA--RNFIGCTLE--------LGgksPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQV 306
Cdd:PRK11903 236 ETAAVLRSHPAvvQRSVRVNVEadslnsalLG---PDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 307 AVELKARFEAIQASDSGEDSI-LGPLISVRQKKRVESYIA--EADAPLLARGGIRPGVPTD---GYYVAPALFGPCDP-- 378
Cdd:PRK11903 313 AEALAARLAKTTVGNPRNDGVrMGPLVSRAQLAAVRAGLAalRAQAEVLFDGGGFALVDADpavAACVGPTLLGASDPda 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 379 YSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKC--GQVFI---------NGYG--- 444
Cdd:PRK11903 393 ATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVispdvaalhTGHGnvm 472
|
490 500
....*....|....*....|...
gi 517140063 445 ----------AGGGVELpfGGYR 457
Cdd:PRK11903 473 pqslhggpgrAGGGEEL--GGLR 493
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
21-466 |
1.76e-29 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 122.77 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 21 PASGGREIDVVSPIDGA-IFTTIADSSAEDVERAIMAARAAfdGGEWSKATATERGRLLLELSRRILSESESLARLESRD 99
Cdd:PRK11809 654 PVAAGEMSPVINPADPRdIVGYVREATPAEVEQALESAVNA--APIWFATPPAERAAILERAADLMEAQMQTLMGLLVRE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 100 NGKPIKQALADMIVTARYFEFYgsaADKVHGEvipFLNgynvEVHRePHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATV 179
Cdd:PRK11809 732 AGKTFSNAIAEVREAVDFLRYY---AGQVRDD---FDN----DTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 180 LKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQ-TMAAR-----NFIGC 253
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQrNLAGRldpqgRPIPL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 254 TLELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAgARVL-VQRGVYDQVAVELKarfEAIQASDSGEDSIL---- 328
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSA-LRVLcLQDDVADRTLKMLR---GAMAECRMGNPDRLstdi 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 329 GPLISVRQKKRVESYIAEADAPllARGGIRPGVPTD-----GYYVAPALFgPCDPYSRIaQEEVFGPVLCMIPF--DDEA 401
Cdd:PRK11809 957 GPVIDAEAKANIERHIQAMRAK--GRPVFQAARENSedwqsGTFVPPTLI-ELDSFDEL-KREVFGPVLHVVRYnrNQLD 1032
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517140063 402 SAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFING--YGAGGGVElPFGGYRKSGHGREKG 466
Cdd:PRK11809 1033 ELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnmVGAVVGVQ-PFGGEGLSGTGPKAG 1098
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
124-480 |
1.06e-23 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 103.65 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 124 AADKVHGEVIPFLNgyNVEVHREPHGVTGHIIPWNYPaqmFGRSVAP---SLAMGNATVLKPAEDACLTALRIGEmAVEV 200
Cdd:PLN02203 87 APKKAKLPLVAFPA--TAEVVPEPLGVVLIFSSWNFP---IGLSLEPligAIAAGNAVVLKPSELAPATSAFLAA-NIPK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 201 GFPAGAVNIVTGrGLVAGAALSSSRnIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIvFDDANLDAALPVLVN 280
Cdd:PLN02203 161 YLDSKAVKVIEG-GPAVGEQLLQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCI-VDSLSSSRDTKVAVN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 281 AIIQN-----GGQTCSAGARVLVQRGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAE--ADAPLLA 353
Cdd:PLN02203 238 RIVGGkwgscAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDprVAASIVH 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 354 RGGIRPgvptDGYYVAPALF--GPCDpySRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAK 431
Cdd:PLN02203 318 GGSIDE----KKLFIEPTILlnPPLD--SDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILS 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 517140063 432 KLKCGQVFING----YGAGGgveLPFGGYRKSGHGREKGFAALHEFSTIKTIV 480
Cdd:PLN02203 392 ETSSGSVTFNDaiiqYACDS---LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
140-480 |
1.37e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 97.42 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 140 NVEVHREPHGVTGHIIPWNYPAQMFGRSVAPSLAMGNATVLKPAEDACLTALRIGEMaVEVGFPAGAVNIVTGRGLVAGA 219
Cdd:PLN02174 105 SAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 220 ALSssRNIDFIAFTGSPEVGVQIQTMAARNFIGCTLELGGKSPQIVFDDANLDAAL-PVLVNAIIQNGGQTCSAGARVLV 298
Cdd:PLN02174 184 LLE--QKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVrRIIAGKWGCNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 299 QRGVYDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAEAD-APLLARGGIRpgvPTDGYYVAPALFGPCD 377
Cdd:PLN02174 262 TKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEvSDKIVYGGEK---DRENLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 378 PYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGVE-LPFGGY 456
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGV 418
|
330 340
....*....|....*....|....
gi 517140063 457 RKSGHGREKGFAALHEFSTIKTIV 480
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
169-446 |
3.48e-16 |
|
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: 80.66 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 169 APSLAMGNATVLKpAEDACL-TALRIGEMAVEV----GFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQ 243
Cdd:cd07129 129 ASALAAGCPVVVK-AHPAHPgTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALF 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 244 TMAARN-----FIGctlELGGKSPQIVFDDA---NLDAALPVLVNAIIQNGGQTCSAGARVLVQRGVYDQVAVE-LKARF 314
Cdd:cd07129 208 DAAAARpepipFYA---ELGSVNPVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAGDAFIAaLAEAL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 315 EAIQASdsgedSILGPLISVRQKKRVESYIAEADAPLLARGgirpGVPTDGYYVAPALFGpCDPYSRIA----QEEVFGP 390
Cdd:cd07129 285 AAAPAQ-----TMLTPGIAEAYRQGVEALAAAPGVRVLAGG----AAAEGGNQAAPTLFK-VDAAAFLAdpalQEEVFGP 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 391 VLCMIPFDDEASAIEIANCTEYGLVASIWTADGGRQ--KRVAKKL--KCGQVFINGYGAG 446
Cdd:cd07129 355 ASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDLAlaRELLPVLerKAGRLLFNGWPTG 414
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
13-400 |
1.55e-12 |
|
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: 69.45 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 13 NLIGNKWLPASGGREIdvVSPIDGAIFTTIADSSAEDVERAIMAARAAFDGGEWSKATATERGRLLLELSRRILSE---- 88
Cdd:cd07126 1 NLVAGKWKGASNYTTL--LDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLLYGDVSHRVAHElrkp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 89 --SESLARLESRDNGKPIKQALADMIVTARYFEFYgsAADKVHgevipFL-NGYNV---------EVHREPHGVTGHIIP 156
Cdd:cd07126 79 evEDFFARLIQRVAPKSDAQALGEVVVTRKFLENF--AGDQVR-----FLaRSFNVpgdhqgqqsSGYRWPYGPVAIITP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 157 WNYPA-----QMFGrsvapSLAMGNATVLKPAEDACLTALRIGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSrNIDFIA 231
Cdd:cd07126 152 FNFPLeipalQLMG-----ALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEA-NPRMTL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 232 FTGSpevgvqiQTMAARnfigCTLELGGKspqIVFDDANLDAAlpvLVNAIIQN---------------GGQTCSAGARV 296
Cdd:cd07126 226 FTGS-------SKVAER----LALELHGK---VKLEDAGFDWK---ILGPDVSDvdyvawqcdqdayacSGQKCSAQSIL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 297 LVQRgvyDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKrvesyIAEADAPLLARGGIR---PGVPTDGYYVaPALF 373
Cdd:cd07126 289 FAHE---NWVQAGILDKLKALAEQRKLEDLTIGPVLTWTTER-----ILDHVDKLLAIPGAKvlfGGKPLTNHSI-PSIY 359
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 517140063 374 GPCDPYS--------------RIAQEEVFGPVLCMIPFDDE 400
Cdd:cd07126 360 GAYEPTAvfvpleeiaieenfELVTTEVFGPFQVVTEYKDE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
41-450 |
9.58e-07 |
|
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: 51.07 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 41 TIADSSAEDVERAIMAAR-AAFDGG-EWSKATATERGRLLLELSRRILSEsesLARLESrdngkpikqALADMIVTARYF 118
Cdd:cd07077 9 TLAVNHDEQRDLIINAIAnALYDTRqRLASEAVSERGAYIRSLIANWIAM---MGCSES---------KLYKNIDTERGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 119 EfygSAADKVHGEVIPflNGYNVEVHREPHGVTGHIIPWNYPAQMFgRSVAPSLAMGNATVLKPAEDACLTAlRIGEMAV 198
Cdd:cd07077 77 T---ASVGHIQDVLLP--DNGETYVRAFPIGVTMHILPSTNPLSGI-TSALRGIATRNQCIFRPHPSAPFTN-RALALLF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 199 EVGFPAGAVNI----VTGRGLVAGAALSSSRNIDFIAFTGSPEVGVQIQTMAarNFIGCTLELGGKSPQIVFDDANLDAA 274
Cdd:cd07077 150 QAADAAHGPKIlvlyVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 275 LPVLVNAIIQNgGQTCSAGARVLVQRGVYDQVAVELKARFEAIQasdsgedsilgplISVRQKKRVESYIAEADAPLLAR 354
Cdd:cd07077 228 SGSVHDSKFFD-QNACASEQNLYVVDDVLDPLYEEFKLKLVVEG-------------LKVPQETKPLSKETTPSFDDEAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 355 ggirpgvptdgyyvapalfgpcdpysriaqeEVFGPVLCMIPFDDEASAIEIA--NCTEYG--LVASIWTADGGRQKRVA 430
Cdd:cd07077 294 -------------------------------ESMTPLECQFRVLDVISAVENAwmIIESGGgpHTRCVYTHKINKVDDFV 342
|
410 420
....*....|....*....|....*..
gi 517140063 431 KKLKCGQVFIN-------GYGAGGGVE 450
Cdd:cd07077 343 QYIDTASFYPNesskkgrGAFAGKGVE 369
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
157-407 |
1.84e-06 |
|
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: 50.17 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 157 WN-YPAqMFGrsvapSLAMGNATVLKPAEDACLTALRIGEMAVEV----GFPAGAVNIVT-GRGLVAGAALSSSRNIDFI 230
Cdd:cd07127 208 WNgYPG-LFA-----SLATGNPVIVKPHPAAILPLAITVQVAREVlaeaGFDPNLVTLAAdTPEEPIAQTLATRPEVRII 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 231 AFTGSPEVGVQIQTMA--ARNFIgctlELGGKSPQIVFDDANLDAALPVLVNAIIQNGGQTCSAGARVLVQR-GV----- 302
Cdd:cd07127 282 DFTGSNAFGDWLEANArqAQVYT----EKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRdGIqtddg 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 303 ---YDQVAVELKARFEAIQASDSGEDSILGPLISVRQKKRVESYIAEADAPLLARGGIRPGVPtDGYYVAPALFGPCDPY 379
Cdd:cd07127 358 rksFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFP-DARVRTPLLLKLDASD 436
|
250 260
....*....|....*....|....*...
gi 517140063 380 SRIAQEEVFGPVLCMIPFDDEASAIEIA 407
Cdd:cd07127 437 EAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
171-449 |
2.76e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 49.41 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 171 SLAMGNATVLKP---AEDACLTALRI-GEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEV-------- 238
Cdd:cd07122 119 ALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGMvkaayssg 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 239 ----GVqiqtmaarnfigctlelG-GKSPQIVFDDANLDAALPVLV------NAIIqnggqtCSAGARVLVQRGVYDQVA 307
Cdd:cd07122 199 kpaiGV-----------------GpGNVPAYIDETADIKRAVKDIIlsktfdNGTI------CASEQSVIVDDEIYDEVR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 308 VELKARfeaiqasdsGedsilGPLISVRQKKRVESYIAEA-----------DAPLLA-RGGIRpgVPTD-GYYVAPA-LF 373
Cdd:cd07122 256 AELKRR---------G-----AYFLNEEEKEKLEKALFDDggtlnpdivgkSAQKIAeLAGIE--VPEDtKVLVAEEtGV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 374 GPCDPYSRiaqeEVFGPVLCMIPFDDEASAIEIAN-CTEY---GLVASIWTADGGRQKRVAKKLKCGQVFINGYGAGGGV 449
Cdd:cd07122 320 GPEEPLSR----EKLSPVLAFYRAEDFEEALEKAReLLEYggaGHTAVIHSNDEEVIEEFALRMPVSRILVNTPSSLGGI 395
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
48-414 |
6.63e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 38.73 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 48 EDVERAIMAARAAFDggEWSKATATERGRLLLELSRRILSESESLARLESRDNG------KPIKQALA--------DMIV 113
Cdd:PRK15398 36 ASVDDAVAAAKVAQQ--RYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNVAAaektpgveDLTT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 114 TARyfefygsAADkvHGEVIpflngynveVHREPHGVTGHIIPWNYP-AQMFGRSVApSLAMGNATVLKP---AEDACLT 189
Cdd:PRK15398 114 EAL-------TGD--NGLTL---------IEYAPFGVIGAVTPSTNPtETIINNAIS-MLAAGNSVVFSPhpgAKKVSLR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 190 ALR-IGEMAVEVGFPAGAVNIVTGRGLVAGAALSSSRNIDFIAFTGSPEVgVQiqtmAARNF----IGCtlelG-GKSPQ 263
Cdd:PRK15398 175 AIElLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAV-VK----AAMKSgkkaIGA----GaGNPPV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517140063 264 IVFDDANLDAAlpvlVNAIIqNGGQ-----TCSAGARVLVqrgvYDQVAVELKARFEAIQAS--DSGEDSILGPLIsVRQ 336
Cdd:PRK15398 246 VVDETADIEKA----ARDIV-KGASfdnnlPCIAEKEVIV----VDSVADELMRLMEKNGAVllTAEQAEKLQKVV-LKN 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517140063 337 KKRVESYIAEADAPLLARG-GIRPGVPTDgyyvapALFGPCDPYSRIAQEEVFGPVLCMIPFDDEASAIEIANCTEYGL 414
Cdd:PRK15398 316 GGTVNKKWVGKDAAKILEAaGINVPKDTR------LLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGN 388
|
|
| |
