|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
198-660 |
0e+00 |
|
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: 703.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 198 VPNLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKL 277
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 278 VTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVA 357
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 358 VTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQ 437
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 438 VQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVSVGS-SILWKKKLVECAKALKVNVGTDPNADLGPV 516
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDeADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 517 ITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIV 596
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047933800 597 NRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLP---------SSFND-----KAGLEFYTKLKRVAQQW 660
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAffsfggwkgSFFGDlhfygKDGVRFYTQTKTVTSRW 478
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
163-673 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 698.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 163 LSEKNFKSWRPN-ISLHANSSHTVIGDTVKHTHQLKVPNLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAV 241
Cdd:PLN02419 78 ISGNNLRPLRPQfLALRSSWLSTSPEQSTQPQMPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 242 NAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNA 321
Cdd:PLN02419 158 SAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 322 SDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHD 401
Cdd:PLN02419 238 SNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTND 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 402 IINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIV 481
Cdd:PLN02419 318 TVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 482 VSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTI 561
Cdd:PLN02419 398 VFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTI 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 562 LSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLPS-- 639
Cdd:PLN02419 478 LSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFfs 557
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2047933800 640 ------------SFNDKAGLEFYTKLKRVAQQWKN-SASIGVSMTAS 673
Cdd:PLN02419 558 ftgnkasfagdlNFYGKAGVDFFTQIKLVTQKQKDiHSPFSLAIPIL 604
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
198-660 |
0e+00 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 548.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 198 VPNLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKL 277
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 278 VTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVA 357
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 358 VTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQ 437
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 438 VQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVI 517
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 518 TKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVN 597
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALIN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047933800 598 RNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLP---------SSFND-----KAGLEFYTKLKRVAQQW 660
Cdd:TIGR01722 401 ASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPyfsftgwkdSFFGDhhiygKQGTHFYTRGKTVTTRW 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
197-660 |
3.31e-155 |
|
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: 467.68 E-value: 3.31e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 197 KVPNLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDK 276
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 277 LVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPV 356
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 357 AVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATG 435
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 436 KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADL 513
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLL-VHESIYdeFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 514 GPVITKEVKDRFCRLVQSGIEDGARLLLDGRdivVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAI 593
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGR---RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047933800 594 SIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLP---------SSFNDKAG---LEFYTKLKRVAQQW 660
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqapfggvkqSGIGREGGregLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
215-656 |
1.74e-144 |
|
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: 439.27 E-value: 1.74e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 215 VDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQN 294
Cdd:pfam00171 9 IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 295 DIICGLEVVKHVCGLATMQMGEFVPNaSDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPG 374
Cdd:pfam00171 89 EVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 375 ASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPD 453
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 454 ANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQS 531
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAGQVCTATSRLL-VHESIYdeFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVED 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 532 GIEDGARLLLDGRdivvPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTS 611
Cdd:pfam00171 327 AKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2047933800 612 GIYARKFQSEVEVGMVGINVAVTVPLP---------SSFND---KAGLEFYTKLKRV 656
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDADglpfggfkqSGFGReggPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
239-656 |
1.39e-106 |
|
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: 338.80 E-value: 1.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 239 AAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFV 318
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 319 PNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHG 398
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 399 THDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMA 477
Cdd:cd07078 162 DGDEVgAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 478 INiVVSVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRdivVPGYENGN 555
Cdd:cd07078 242 AS-RLLVHESIYdeFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGK---RLEGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 556 FVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN---VA 632
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINdysVG 397
|
410 420 430
....*....|....*....|....*....|...
gi 2047933800 633 VTVPLP---------SSFNDKAGLEFYTKLKRV 656
Cdd:cd07078 398 AEPSAPfggvkqsgiGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
199-656 |
3.18e-98 |
|
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: 318.04 E-value: 3.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 199 PNLIGGEFLDSHNcpVVDVINPA-TQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKL 277
Cdd:cd07097 2 RNYIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 278 VTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVA 357
Cdd:cd07097 80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 358 VTCGNTFVLKPCETYPG-ASMLLAALAvEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATG 435
Cdd:cd07097 160 LAYGNTVVFKPAELTPAsAWALVEILE-EAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 436 KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLG 514
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSrLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 515 PVITKEVKDRFCRLVQSGIEDGARLLLDGRDIvvPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAIS 594
Cdd:cd07097 319 PVVSERQLEKDLRYIEIARSEGAKLVYGGERL--KRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 595 IVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVT-----VPL----PSSFNDK----AGLEFYTKLKRV 656
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgvdyhVPFggrkGSSYGPReqgeAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
200-656 |
3.66e-97 |
|
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: 315.44 E-value: 3.66e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 200 NLIGGEFLDSHNCPVVDVINPA-TQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLV 278
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 279 TNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAV 358
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 359 TCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQ 437
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 438 VQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPV 516
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSrLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 517 ITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIV 596
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047933800 597 NRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN---VAVTVPLPSSFNDKAG----------LEFYTKLKRV 656
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaptIGAEVHLPFGGVKKSGnghreagttaLDAFTEWKAV 473
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
217-658 |
1.03e-95 |
|
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: 310.52 E-value: 1.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDI 296
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 297 ICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICsfnhPatvslWMFPVA-VT--------CGNTFVLK 367
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAIT----P-----WNFPAAmITrkiapalaAGCTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 368 PCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGks 446
Cdd:cd07103 152 PAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 447 HA--IIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTDPNADLGPVITKEVK 522
Cdd:cd07103 230 NApfIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIY-VHESIYDEfvEKLVERVKKLKVGNGLDEGTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 523 DRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNR 602
Cdd:cd07103 309 EKVEALVEDAVAKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYG 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047933800 603 NGASIFTTSGIYARKFQSEVEVGMVGINVAV--TVPLP------SSF---NDKAGLEFYTKLKRVAQ 658
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALEAGMVGINTGLisDAEAPfggvkeSGLgreGGKEGLEEYLETKYVSL 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
202-630 |
4.36e-93 |
|
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: 304.19 E-value: 4.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNI 281
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 282 VIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHP-ATVSLWMFPvAVTC 360
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 361 GNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQ 439
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 440 SHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINiVVSVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVI 517
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAE-RVYVHEDIYdeFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 518 TKEVKDRFCRLVQSGIEDGARLLLDGRdivVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVN 597
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGK---RPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430
....*....|....*....|....*....|...
gi 2047933800 598 RNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
217-657 |
7.97e-88 |
|
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: 289.47 E-value: 7.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQN-D 295
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGA 375
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGAL-NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 376 SMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDA 454
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 455 NMEATLNALVDAGFGTSGQTCMAinivvsvGSSIL--------WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFC 526
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLA-------GSRILvqrsiydeFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 527 RLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGAS 606
Cdd:cd07093 313 GYVELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047933800 607 IFTTSGIYARKFQSEVEVGMVGINVAVTVPLPSSFND-----------KAGLEFYTKLKRVA 657
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGvkasgigreggDYSLEFYTELKNVC 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
200-631 |
3.62e-84 |
|
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: 280.22 E-value: 3.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 200 NLIGGEFLDShNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:cd07086 1 GVIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVT 359
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 360 CGNTFVLKPCETYPGASMLLAALAVEA----GLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATG 435
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 436 KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN--IV-VSVGSSILwkKKLVECAKALKVNVGTDPNAD 512
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRrlIVhESVYDEFL--ERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 513 LGPVITKEVKDRFCRLVQSGIEDGARLLLDGRdiVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEA 592
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2047933800 593 ISIVNRNKNRNGASIFTTSGIYARKFQS--EVEVGMVGINV 631
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLGpkGSDCGIVNVNI 436
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
217-636 |
3.79e-82 |
|
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: 273.64 E-value: 3.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDI 296
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 297 ICGLEVVKHVcglATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGAS 376
Cdd:cd07106 81 GGAVAWLRYT---ASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 377 MLLAALAVEAgLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANM 456
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 457 EATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIE 534
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKRLY-VHESIYdeFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 535 DGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIY 614
Cdd:cd07106 316 KGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420
....*....|....*....|....*.
gi 2047933800 615 ARKFQSEVEVGMVGIN----VAVTVP 636
Cdd:cd07106 392 AEAVARRLEAGTVWINthgaLDPDAP 417
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
202-630 |
4.22e-81 |
|
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: 272.26 E-value: 4.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS--WKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVT 359
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVI-SRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 360 CGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQV 438
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 439 QSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCmainivvSVGSSIL----WKKK----LVECAKALKVNVGTDPN 510
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVC-------SAGSRLLveesIHDKfvaaLAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 511 ADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLE 590
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2047933800 591 EAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07119 394 EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
216-630 |
9.47e-81 |
|
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: 269.97 E-value: 9.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 216 DVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQND 295
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGA 375
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 376 SMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDA 454
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 455 NMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGI 533
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASrIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 534 EDGARLLldgrdivVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGI 613
Cdd:cd07150 322 AKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
410
....*....|....*..
gi 2047933800 614 YARKFQSEVEVGMVGIN 630
Cdd:cd07150 395 RAFKLAERLESGMVHIN 411
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
217-630 |
1.65e-80 |
|
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: 269.81 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAF--PSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQN 294
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 295 DIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPG 374
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 375 ASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPD 453
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 454 ANMEATLNALVDAGFGTSGQTCMAinivvsvGSSIL--------WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRF 525
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVA-------GSRLLvqrsiydeFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 526 CRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGA 605
Cdd:cd07114 314 ERYVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420
....*....|....*....|....*
gi 2047933800 606 SIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVN 418
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
202-630 |
3.53e-79 |
|
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: 266.29 E-value: 3.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNI 281
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 282 VIEQGKTLKDAQND-IICGLEVVKH-VCGLATMQMGEFVPNasdgidSYCIRDPIGVCAGICSFNHPA-TVSLWMFPvAV 358
Cdd:cd07138 83 TLEMGAPITLARAAqVGLGIGHLRAaADALKDFEFEERRGN------SLVVREPIGVCGLITPWNWPLnQIVLKVAP-AL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 359 TCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQ 437
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDgPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 438 VQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILwkKKLVECAKAL--KVNVG--TDPNADL 513
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRML-VPRSRY--AEAEEIAAAAaeAYVVGdpRDPATTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 514 GPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVpGYENGNFVGPTILSDVTTDMECYKEEFLGPVlLCMQA-DNLEEA 592
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPE-GLERGYFVKPTVFADVTPDMTIAREEIFGPV-LSIIPyDDEDEA 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 2047933800 593 ISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN 428
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
190-630 |
1.41e-78 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 265.79 E-value: 1.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 190 VKHTHQLKVPNLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQEL 269
Cdd:PLN02278 17 LRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 270 ILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATV 349
Cdd:PLN02278 97 IIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 350 SLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHG-THDIINYICDDEDIKAISFASSCSAGKNIY 428
Cdd:PLN02278 177 ITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGdAPEIGDALLASPKVRKITFTGSTAVGKKLM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 429 ARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGT 507
Cdd:PLN02278 257 AGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANrILVQEGIYDKFAEAFSKAVQKLVVGDGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 508 DPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRdivvPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQAD 587
Cdd:PLN02278 337 EEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGK----RHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK 412
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2047933800 588 NLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PLN02278 413 TEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVN 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
217-656 |
1.63e-77 |
|
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: 261.47 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDI 296
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 297 ICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGAS 376
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSF-AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 377 MLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANM 456
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 457 EATLNALVDAGFGTSGQTCMaiNIV-VSVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGI 533
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCS--NGTrVFVQRSIKdeFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 534 EDGARLLLDGRDIVV-PGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSG 612
Cdd:cd07090 318 QEGAKVLCGGERVVPeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 613 IYARKFQSEVEVGMVGIN----VAVTVPL----PSSF---NDKAGLEFYTKLKRV 656
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINtyniSPVEVPFggykQSGFgreNGTAALEHYTQLKTV 452
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
238-630 |
7.49e-77 |
|
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: 258.61 E-value: 7.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 238 KAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEF 317
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 318 VPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCE-TYPGASMLLAALAVEAGLPDGVLNIV 396
Cdd:cd07104 83 LPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrTPVTGGLLIAEIFEEAGLPKGVLNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 397 HGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTC 475
Cdd:cd07104 163 PGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 476 MAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRdivvpgyEN 553
Cdd:cd07104 243 MAAGRIL-VHESVYdeFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT-------YE 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047933800 554 GNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07104 315 GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
215-630 |
1.28e-76 |
|
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: 258.82 E-value: 1.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 215 VDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQN 294
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 295 DIICGLEVVKHVCGLATMQMGEFVPnaSDGID------SYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKP 368
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIP--VDAYEynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 369 CETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSH 447
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 448 AIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTDPNADLGPVITKEVKDRF 525
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRIL-VEEEVYDKflKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 526 CRLVQSGIEDGARLLLDGRDIvvpgyeNGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGA 605
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRD------EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420
....*....|....*....|....*
gi 2047933800 606 SIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN 416
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
201-656 |
2.66e-74 |
|
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: 253.29 E-value: 2.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 201 LIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFP--SWKNTPISTRQCVMFKFQELILRDMDKLV 278
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 279 TNIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVA 357
Cdd:cd07091 87 ALESLDNGKPLEESAKgDVALSIKCLRYYAGWADKIQGKTIPIDGNFL-AYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 358 VTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATG- 435
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAgAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 436 KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTDPNADL 513
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIF-VQESIYDEfvEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 514 GPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAI 593
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047933800 594 SIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN----VAVTVPL----PSSF---NDKAGLEFYTKLKRV 656
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtynvFDAAVPFggfkQSGFgreLGEEGLEEYTQVKAV 474
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
243-656 |
2.17e-73 |
|
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: 247.14 E-value: 2.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 243 AAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNAS 322
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 323 DGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDI 402
Cdd:cd06534 82 PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 403 I-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAI-NI 480
Cdd:cd06534 162 VgAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAsRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 481 VVSVGssilwkkklvecakalkvnvgtdpnadlgpvITKEVKDRFCrlvqsgiedgarllldgrdivvpgyengnfvgpT 560
Cdd:cd06534 242 LVHES-------------------------------IYDEFVEKLV---------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 561 ILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN---VAVTVPL 637
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINdssIGVGPEA 337
|
410 420
....*....|....*....|....*...
gi 2047933800 638 P------SSFND---KAGLEFYTKLKRV 656
Cdd:cd06534 338 PfggvknSGIGReggPYGLEEYTRTKTV 365
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
217-657 |
9.44e-73 |
|
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: 248.30 E-value: 9.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS-WKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQND 295
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLATMQMGEFVPnASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGA 375
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 376 SMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIyARAAAtgKQVQS---HFGGKSHAIIM 451
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAV-MRAAA--ENVVPvtlELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 452 PDANMEATLNALVDAGFGTSGQTCmainivvSVGSSILWKK--------KLVECAKALKVNVGTDpNADLGPVITKEVKD 523
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTC-------SAGSRLLVHRsiydevleRLVERFRALRVGPGLE-DPDLGPLISAKQLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 524 RFCRLVQSGIEDGARLLLDGRdIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRN 603
Cdd:cd07109 309 RVEGFVARARARGARIVAGGR-IAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047933800 604 GASIFTTSGIYARKFQSEVEVGMVGIN---VAVTVPLP------SSFNDKAGLEF---YTKLKRVA 657
Cdd:cd07109 388 VAGVWTRDGDRALRVARRLRAGQVFVNnygAGGGIELPfggvkkSGHGREKGLEAlynYTQTKTVA 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
217-656 |
9.74e-73 |
|
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: 248.12 E-value: 9.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQN-D 295
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLATMQMGEFVPNASDGIDsYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGA 375
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLN-YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 376 SMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDA 454
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 455 NMEATLNALVDAGFGTSGQTCMAinivvsvGSSILWKKK--------LVECAKALKVNVGTDPNADLGPVITKEVKDRFC 526
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTA-------GSRLLVHESiydeflerFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 527 RLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGAS 606
Cdd:cd07115 313 DYVDVGREEGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047933800 607 IFTTSGIYARKFQSEVEVGMVGINV--AVTVPLP------SSF---NDKAGLEFYTKLKRV 656
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWINTynRFDPGSPfggykqSGFgreMGREALDEYTEVKSV 449
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
216-630 |
6.99e-72 |
|
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: 245.97 E-value: 6.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 216 DVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQND 295
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLATMQMGEFVP-NASDGIDS---YCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCET 371
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIPfDASPGGEGrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 372 YPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIyARAAATgKQVQSHFGGKSHAII 450
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAI-ARKAGL-KKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 451 MPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRL 528
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIF-VHEDIYdeFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 529 VQSGIEDGARLLLdgrdivvPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIF 608
Cdd:cd07149 319 VEEAVEGGARLLT-------GGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420
....*....|....*....|..
gi 2047933800 609 TTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMIN 413
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
202-656 |
2.67e-71 |
|
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: 245.39 E-value: 2.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWK-NTPISTRQCVMFKFQELILRDMDKLVTN 280
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWsKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 281 IVIEQGKTLK-DAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVT 359
Cdd:cd07144 92 EALDSGKPYHsNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 360 CGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQV 438
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 439 QSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAiNIVVSVGSSILWK--KKLVE-CAKALKVNVGTDPNADLGP 515
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTA-TSRIYVQESIYDKfvEKFVEhVKQNYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 516 VITKEVKDRFCRLVQSGIEDGARLLLDGrDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISI 595
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYGG-EKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKK 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047933800 596 VNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVA----VTVPlpssFN-----------DKAGLEFYTKLKRV 656
Cdd:cd07144 409 ANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP----FGgfkmsgigrelGEYGLETYTQTKAV 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
195-656 |
2.90e-71 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 245.18 E-value: 2.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 195 QLKVPNLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQElILRDM 274
Cdd:PRK13252 4 QPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVD-ILRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 275 -DKLVTNIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPnASDGIDSYCIRDPIGVCAGICSFNHPATVSLW 352
Cdd:PRK13252 83 nDELAALETLDTGKPIQETSVvDIVTGADVLEYYAGLAPALEGEQIP-LRGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 353 MFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAA 432
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 433 ATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMaiN-IVVSVGSSIL--WKKKLVECAKALKVNVGTDP 509
Cdd:PRK13252 242 ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCT--NgTRVFVQKSIKaaFEARLLERVERIRIGDPMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 510 NADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNL 589
Cdd:PRK13252 320 ATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047933800 590 EEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINV--AVTVPLP------SSF---NDKAGLEFYTKLKRV 656
Cdd:PRK13252 400 DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMPvggykqSGIgreNGIATLEHYTQIKSV 477
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
202-630 |
6.83e-71 |
|
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: 243.64 E-value: 6.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS--WKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQNdiicglevvkHVCGLATMQMG-----------EFVPNASDGIDSYCIRDPIGVCAGICSFNHPAT 348
Cdd:cd07139 83 LWTAENGMPISWSRR----------AQGPGPAALLRyyaalardfpfEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 349 VSLWMFPVAVTCGNTFVLKPC-ETyPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNI 427
Cdd:cd07139 153 LAALKIAPALAAGCTVVLKPSpET-PLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 428 YARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVG 506
Cdd:cd07139 232 AAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTrILVPRSRYDEVVEALAAAVAALKVGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 507 TDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDivVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQA 586
Cdd:cd07139 312 LDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPY 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2047933800 587 DNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07139 390 DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN 433
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
198-630 |
1.38e-70 |
|
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: 244.05 E-value: 1.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 198 VPNLIGGEFLDSHncPVVDVINPA-TQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDK 276
Cdd:cd07124 33 YPLVIGGKEVRTE--EKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 277 LVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLAtMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPV 356
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREM-LRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 357 AVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATG 435
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 436 ------KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGT 507
Cdd:cd07124 270 pgqkwlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVI-VHESVYDEflERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 508 DPNADLGPVITKEVKDRFCRLVQSGIEDGaRLLLDGRdiVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQAD 587
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2047933800 588 NLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN 468
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
217-656 |
3.18e-70 |
|
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: 241.08 E-value: 3.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDI 296
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 297 ICG-LEVVKHVCGLA-TMQ---MGEFVPnasdGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCET 371
Cdd:cd07092 81 LPGaVDNFRFFAGAArTLEgpaAGEYLP----GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 372 YPGASMLLAALAVEaGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAII 450
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 451 MPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRL 528
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVY-VHESVYDEfvAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 529 VqSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIF 608
Cdd:cd07092 315 V-ERAPAHARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVW 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2047933800 609 TTSGIYARKFQSEVEVGMVGIN--VAVTVPLP------SSF---NDKAGLEFYTKLKRV 656
Cdd:cd07092 390 TRDVGRAMRLSARLDFGTVWVNthIPLAAEMPhggfkqSGYgkdLSIYALEDYTRIKHV 448
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
199-630 |
3.39e-70 |
|
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: 241.71 E-value: 3.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 199 PNLIGGEFLDShNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNT-PISTRQCVMFKFQELILRDMDKL 277
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 278 VTNIVIEQGKTLKDAQ----------NDIIcglEVVKHVcglatmqMGEFVP----NASDGIDSYCIRDPIGVCAGICSF 343
Cdd:cd07082 82 ANLLMWEIGKTLKDALkevdrtidyiRDTI---EELKRL-------DGDSLPgdwfPGTKGKIAQVRREPLGVVLAIGPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 344 NHPA--TVSLwMFPVAVTcGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASS 420
Cdd:cd07082 152 NYPLnlTVSK-LIPALIM-GNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 421 CSAGKNIyaRAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECA 498
Cdd:cd07082 230 TEVGNRL--KKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVL-VHESVAdeLVELLKEEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 499 KALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGrdivvpGYENGNFVGPTILSDVTTDMECYKEEFLG 578
Cdd:cd07082 307 AKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFG 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2047933800 579 PVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07082 381 PVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
218-630 |
3.54e-69 |
|
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: 238.30 E-value: 3.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 218 INPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDII 297
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 298 CGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASM 377
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 378 LLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANME 457
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 458 ATLNALVDAGFGTSGQTCMAINiVVSVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIED 535
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIE-RIYVHESIYdaFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 536 GARLLLDGRDIVVPGyENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYA 615
Cdd:cd07102 320 GARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410
....*....|....*
gi 2047933800 616 RKFQSEVEVGMVGIN 630
Cdd:cd07102 399 EALGEQLETGTVFMN 413
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
217-630 |
3.62e-69 |
|
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: 238.40 E-value: 3.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQ--- 293
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 294 NDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYP 373
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 374 GASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMP 452
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTgDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 453 DANMEATLNALVDAGFGTSGQTCMAINIVV---SVGSSILwkKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLV 529
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLvheSIADAFL--ERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 530 QSGIEDGARLLLDGRdivVP-GYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIF 608
Cdd:cd07110 319 ARGKEEGARLLCGGR---RPaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420
....*....|....*....|..
gi 2047933800 609 TTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWIN 417
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
217-630 |
1.23e-67 |
|
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: 234.06 E-value: 1.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWK-NTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTL---KDA 292
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmtaRAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 293 QNDIicGLEVVKHVCGLATMQMGEF-VPNASDGID---SYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKP 368
Cdd:cd07089 81 QVDG--PIGHLRYFADLADSFPWEFdLPVPALRGGpgrRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 369 CETYPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSH 447
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSdNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 448 AIIMPDANMEATLNALVDAGFGTSGQTC-MAINIVV--SVgssilwKKKLVECAKAL--KVNVG--TDPNADLGPVITKE 520
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCaLTTRLLVprSR------YDEVVEALAAAfeALPVGdpADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 521 VKDRFCRLVQSGIEDGARLLLDGRdiVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNK 600
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSD 390
|
410 420 430
....*....|....*....|....*....|
gi 2047933800 601 NRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07089 391 YGLSGGVWSADVDRAYRVARRIRTGSVGIN 420
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
239-656 |
1.60e-67 |
|
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: 232.85 E-value: 1.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 239 AAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFV 318
Cdd:cd07105 4 QAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 319 PNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVH- 397
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTh 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 398 ---GTHDIINYICDDEDIKAISFASSCSAGKnIYARAAATG-KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQ 473
Cdd:cd07105 164 speDAPEVVEALIAHPAVRKVNFTGSTRVGR-IIAETAAKHlKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 474 TCMAINIVVsVGSSIL--WKKKLVECAKALkvnvgTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGy 551
Cdd:cd07105 243 ICMSTERII-VHESIAdeFVEKLKAAAEKL-----FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPS- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 552 enGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN- 630
Cdd:cd07105 316 --GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINg 393
|
410 420 430
....*....|....*....|....*....|....*..
gi 2047933800 631 --VAVTVPLP-----SS----FNDKAGLEFYTKLKRV 656
Cdd:cd07105 394 mtVHDEPTLPhggvkSSgygrFNGKWGIDEFTETKWI 430
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
215-630 |
7.45e-67 |
|
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: 231.94 E-value: 7.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 215 VDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQN 294
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 295 DIICGLEVVKHVCGLATMQMGEFVP----NASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCE 370
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPldatQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 371 TYPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIyaRAAATGKQVQSHFGGKSHAI 449
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 450 IMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCR 527
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIY-VHEELYdeFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 528 LVQSGIEDGARLLLDgrdivvpGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASI 607
Cdd:cd07094 318 WVEEAVEAGARLLCG-------GERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420
....*....|....*....|...
gi 2047933800 608 FTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVN 413
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
218-656 |
1.26e-66 |
|
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: 231.07 E-value: 1.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 218 INPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS--WKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQND 295
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGA 375
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 376 SMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDA 454
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 455 NMEATLNALVDAGFGTSGQTCMAinivvsvGSSIL--------WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFC 526
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNS-------GSRLLvhesiadaFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 527 RLVQSGIEDGARLLLDGRDIvvpGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGAS 606
Cdd:cd07118 315 DYVDAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047933800 607 IFTTSGIYARKFQSEVEVGMVGINVAV--TVPLP------SSF---NDKAGLEFYTKLKRV 656
Cdd:cd07118 392 VWSKDIDTALTVARRIRAGTVWVNTFLdgSPELPfggfkqSGIgreLGRYGVEEYTELKTV 452
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
217-630 |
4.25e-66 |
|
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: 229.95 E-value: 4.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDI 296
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 297 ICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGAS 376
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 377 MLLAALAVEAgLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDAN 455
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 456 MEATLNALVDA-GFGTSGQTCMAINIVV---SVGSSILwkKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQS 531
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFvheSIYDEVL--ARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 532 GIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTS 611
Cdd:cd07107 317 AKREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410
....*....|....*....
gi 2047933800 612 GIYARKFQSEVEVGMVGIN 630
Cdd:cd07107 397 ISQAHRTARRVEAGYVWIN 415
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
218-638 |
1.63e-65 |
|
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: 227.87 E-value: 1.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 218 INPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDII 297
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 298 CGLEVVKHVCGLA-------TMQMGEFVPNASDGIDsyciRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCE 370
Cdd:cd07099 81 LALEAIDWAARNAprvlaprKVPTGLLMPNKKATVE----YRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 371 TYPGASMLLAALAVEAGLPDGVLNIVHGTHD----IINYICDdedikAISFASSCSAGKNIYARAAATGKQVQSHFGGKS 446
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAtgaaLIDAGVD-----KVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 447 HAIIMPDANMEATLNALVDAGFGTSGQTCMAIN---IVVSVGSSILwkKKLVECAKALKVNVGTDPNADLGPVITKEVKD 523
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVErvyVHESVYDEFV--ARLVAKARALRPGADDIGDADIGPMTTARQLD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 524 RFCRLVQSGIEDGARLLLDGRDIVVPGyengNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRN 603
Cdd:cd07099 310 IVRRHVDDAVAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGL 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 2047933800 604 GASIFTTSGIYARKFQSEVEVGMVGIN-VAVTVPLP 638
Cdd:cd07099 386 SASVFSRDLARAEAIARRLEAGAVSINdVLLTAGIP 421
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
204-630 |
5.71e-65 |
|
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: 226.80 E-value: 5.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 204 GEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVI 283
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 284 EQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNT 363
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 364 FVLKPCETYP-GASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSH 441
Cdd:cd07151 161 VVLKPASDTPiTGGLLLAKIFEEAGLPKGVLNVVVGAgSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 442 FGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITK 519
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRII-VHEDVYdeFVEKFVERVKALPYGDPSDPDTVVGPLINE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 520 EVKDRFCRLVQSGIEDGARLLLDGRdivvpgyENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRN 599
Cdd:cd07151 320 SQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDT 392
|
410 420 430
....*....|....*....|....*....|.
gi 2047933800 600 KNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQFARRIDAGMTHIN 423
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
217-630 |
5.85e-65 |
|
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: 226.47 E-value: 5.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLK-DAQND 295
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLATMQMGEFVPnASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGA 375
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 376 SMLLAALAVEAgLPDGVLNIVHGTHDIINY-ICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDA 454
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 455 NMEATLNALVDA-GFGTSGQTCMA---INIVVSVGSSILwkKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQ 530
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAgsrLFVHEDIYDAFL--EKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 531 SGIE-DGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFT 609
Cdd:cd07108 317 LGLStSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420
....*....|....*....|.
gi 2047933800 610 TSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVN 417
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
200-630 |
6.33e-65 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 227.10 E-value: 6.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 200 NLIGGEFLDSHNcPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:PRK13473 5 LLINGELVAGEG-EKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQNDIICGLE--------VVKHVCGLATmqmGEFVPnasdGIDSYCIRDPIGVCAGICSFNHPATVSL 351
Cdd:PRK13473 84 LESLNCGKPLHLALNDEIPAIVdvfrffagAARCLEGKAA---GEYLE----GHTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 352 WMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAgLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYAR 430
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRgATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 431 AAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTD 508
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY-AQRGIYDDlvAKLAAAVATLKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 509 PNADLGPVITKEVKDRFCRLVQSGIEDG-ARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQAD 587
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPVVSVTPFD 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2047933800 588 NLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PRK13473 391 DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVN 433
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
202-656 |
2.49e-64 |
|
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: 225.40 E-value: 2.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS-WKNTPISTRQCVMFKFQELILRDMDKLVTN 280
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 281 IVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGE-----FVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMF 354
Cdd:cd07113 84 ETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGEtlapsIPSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 355 PVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAAT 434
Cdd:cd07113 164 GAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 435 GKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMA----------INIVVSvgssilwkkKLVECAKALKVN 504
Cdd:cd07113 244 LTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAperfyvhrskFDELVT---------KLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 505 VGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCM 584
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 585 QADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN----VAVTVPLPSSFNDKAGLEF-------YTKL 653
Cdd:cd07113 391 PYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtfLDPAVPFGGMKQSGIGREFgsafiddYTEL 470
|
...
gi 2047933800 654 KRV 656
Cdd:cd07113 471 KSV 473
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
202-656 |
1.13e-63 |
|
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: 223.76 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAF---PSWKNTPISTRQCVMFKFQELILRDMDKLV 278
Cdd:cd07141 11 INNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 279 TNIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPnaSDG-IDSYCIRDPIGVCAGICSFNHPATVSLWMFPV 356
Cdd:cd07141 91 SLETLDNGKPFSKSYLvDLPGAIKVLRYYAGWADKIHGKTIP--MDGdFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 357 AVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIIN-YICDDEDIKAISFASSCSAGKNIYARAAATG 435
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGaAISSHPDIDKVAFTGSTEVGKLIQQAAGKSN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 436 -KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTDPNAD 512
Cdd:cd07141 249 lKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTF-VQESIYDEfvKRSVERAKKRVVGNPFDPKTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 513 LGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEA 592
Cdd:cd07141 328 QGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 593 ISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLPSSF-----------NDKAGLEFYTKLKRV 656
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFggykmsgngreLGEYGLQEYTEVKTV 478
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
202-656 |
3.89e-63 |
|
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: 222.40 E-value: 3.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFP-SW-KNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAV 358
Cdd:cd07143 91 IEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIETDIKKL-TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 359 TCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAAATG-K 436
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNlK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 437 QVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMA-INIVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGP 515
Cdd:cd07143 250 KVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAgSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 516 VITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISI 595
Cdd:cd07143 330 QVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047933800 596 VNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLPSSFN-----------DKAGLEFYTKLKRV 656
Cdd:cd07143 406 ANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGgykqsgigrelGEYALENYTQIKAV 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
190-630 |
2.24e-61 |
|
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: 216.98 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 190 VKHThQLkvpnLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFP--SWKNTPISTRQCVMFKFQ 267
Cdd:cd07142 1 VKHT-KL----FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 268 ELILRDMDKLVTNIVIEQGKTLKDA-QNDIICGLEVVKHVCGLATMQMGEFVPnaSDGI-DSYCIRDPIGVCAGICSFNH 345
Cdd:cd07142 76 DLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLP--ADGPhHVYTLHEPIGVVGQIIPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 346 PATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIIN-YICDDEDIKAISFASSCSAG 424
Cdd:cd07142 154 PLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGaAIASHMDVDKVAFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 425 KNIYARAAATG-KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILwkKKLVECAK--AL 501
Cdd:cd07142 234 KIIMQLAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF-VHESIY--DEFVEKAKarAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 502 KVNVGT--DPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGP 579
Cdd:cd07142 311 KRVVGDpfRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGP 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2047933800 580 VLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07142 387 VQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN 437
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
239-630 |
3.18e-61 |
|
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: 215.02 E-value: 3.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 239 AAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIicglEVVKHVC-----GLATMQ 313
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEV----EKCAWICryyaeNAEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 314 MGEFVPnaSDGIDSYCIRDPIGVCAGICSFNHPatvsLW-MFPVAV---TCGNTFVLKPCETYPGASMLLAALAVEAGLP 389
Cdd:cd07100 79 ADEPIE--TDAGKAYVRYEPLGVVLGIMPWNFP----FWqVFRFAApnlMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 390 DGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFG 469
Cdd:cd07100 153 EGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 470 TSGQTCMAIN--IVVSvgsSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRd 545
Cdd:cd07100 233 NAGQSCIAAKrfIVHE---DVYdeFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 546 iVVPGyeNGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVG 625
Cdd:cd07100 309 -RPDG--PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
....*
gi 2047933800 626 MVGIN 630
Cdd:cd07100 386 MVFIN 390
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
218-630 |
4.34e-61 |
|
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: 215.67 E-value: 4.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 218 INPATQEVVSHVPLTTYEEFKAAVNAAKQAF--PSWKNTPiSTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQND 295
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 296 IICGLEVVKHVCGLA---TMQMGEFVPnasdGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPcety 372
Cdd:cd07120 81 ISGAISELRYYAGLArteAGRMIEPEP----GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKP---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 373 PGASMLLAA-----LAVEAGLPDGVLNIVHG-THDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKS 446
Cdd:cd07120 153 AGQTAQINAaiiriLAEIPSLPAGVVNLFTEsGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 447 HAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDR 524
Cdd:cd07120 233 PCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVL-VQRSIAdeVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 525 FCRLVQSGIEDGARLLLDGRDiVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNG 604
Cdd:cd07120 312 VDRMVERAIAAGAEVVLRGGP-VTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
410 420
....*....|....*....|....*.
gi 2047933800 605 ASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07120 391 ASVWTRDLARAMRVARAIRAGTVWIN 416
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
216-654 |
5.31e-60 |
|
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: 212.85 E-value: 5.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 216 DVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS--WKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQ 293
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 294 NDIICG-LEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETY 372
Cdd:cd07112 85 AVDVPSaANTFRWYAEAIDKVYGEVAPTGPDAL-ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 373 PGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAAT-GKQVQSHFGGKSHAII 450
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFgHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 451 MPDA-NMEATLNALVDAGFGTSGQTCMAinivvsvGSSILWKK--------KLVECAKALKVNVGTDPNADLGPVITKEV 521
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSA-------GSRLLVHEsikdefleKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 522 KDRFCRLVQSGIEDGARLLLDG-RDIVVPGyenGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNK 600
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGkRVLTETG---GFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 601 NRNGASIFTTSGIYARKFQSEVEVGMVGIN----VAVTVPL----PSSF-NDKA--GLEFYTKLK 654
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTPFggfkQSGNgRDKSlhALDKYTELK 458
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
224-630 |
9.90e-60 |
|
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: 211.38 E-value: 9.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 224 EVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVV 303
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 304 KHVCGLATMQMGEFVPNAsDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGAS-MLLAAL 382
Cdd:cd07152 82 HEAAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 383 AVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNA 462
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 463 LVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLL 541
Cdd:cd07152 241 GAWGAFLHQGQICMAAGrHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 542 DGRdivvpgYEnGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSE 621
Cdd:cd07152 321 GGT------YD-GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADR 393
|
....*....
gi 2047933800 622 VEVGMVGIN 630
Cdd:cd07152 394 LRTGMLHIN 402
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
215-630 |
1.59e-58 |
|
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: 208.25 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 215 VDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQN 294
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 295 DIICGLEVVKHVCGLATMQMGEFVP----NASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCE 370
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 371 TYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAAtgKQVQSHFGGKSHAII 450
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 451 MPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRL 528
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVL-VHRSVYdeFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 529 VQSGIEDGARLLldgrdivVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIF 608
Cdd:cd07147 318 VNEAVDAGAKLL-------TGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420
....*....|....*....|..
gi 2047933800 609 TTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVIN 412
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
201-656 |
3.44e-57 |
|
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: 205.00 E-value: 3.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 201 LIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTN 280
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 281 IVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVT 359
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTL-SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 360 CGNTFVLKPCETYPgASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQV 438
Cdd:cd07117 163 AGNTVVIKPSSTTS-LSLLELAKIIQDVLPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 439 QSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMA-INIVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVI 517
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAgSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 518 TKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVN 597
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 598 RNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLPSSF-----------NDKAGLEFYTKLKRV 656
Cdd:cd07117 402 DSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFggykksgigreTHKSMLDAYTQMKNI 471
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
196-630 |
1.88e-56 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 203.90 E-value: 1.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 196 LKVPNL------IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFP--SWKNTPISTRQCVMFKFQ 267
Cdd:PLN02766 13 VKVPEIkftklfINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 268 ELILRDMDKLVTNIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEfVPNASDGIDSYCIRDPIGVCAGICSFNHP 346
Cdd:PLN02766 93 DLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGE-TLKMSRQLQGYTLKEPIGVVGHIIPWNFP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 347 ATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIIN-YICDDEDIKAISFASSCSAGK 425
Cdd:PLN02766 172 STMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGaAIASHMDVDKVSFTGSTEVGR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 426 NIYARAAATG-KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIV-VSVGSSILWKKKLVECAKALKV 503
Cdd:PLN02766 252 KIMQAAATSNlKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVyVQEGIYDEFVKKLVEKAKDWVV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 504 NVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRdivvPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLC 583
Cdd:PLN02766 332 GDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSL 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2047933800 584 MQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PLN02766 408 MKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
200-654 |
2.30e-56 |
|
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: 202.96 E-value: 2.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 200 NLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAV 358
Cdd:cd07559 83 AETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEIDEDTL-SYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 359 TCGNTFVLKPCETYPgASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQ 437
Cdd:cd07559 162 AAGNTVVLKPASQTP-LSILVLMELIGDLLPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 438 VQSHFGGKSHAIIMPDANMEAtlNALVDAGFGtsGQTCMAINI--VVSVGSSIL--------WKKKLVECAKALKVNVGT 507
Cdd:cd07559 241 VTLELGGKSPNIFFDDAMDAD--DDFDDKAEE--GQLGFAFNQgeVCTCPSRALvqesiydeFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 508 DPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQAD 587
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047933800 588 NLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLPSSF-----------NDKAGLEFYTKLK 654
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFggykksgigreTHKMMLDHYQQTK 474
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
189-631 |
1.05e-54 |
|
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: 198.49 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 189 TVKHTHQLkvpnLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS--WKNTPISTRQCVMFKF 266
Cdd:cd07140 1 TLKMPHQL----FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 267 QELILRDMDKLVTNIVIEQGKTLKDA-QNDIICGLEVVKHVCGLATMQMGEFVP--NASDGID-SYCIRDPIGVCAGICS 342
Cdd:cd07140 77 ADLMEEHQEELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNlTLTKREPIGVCGIVIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 343 FNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSC 421
Cdd:cd07140 157 WNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGST 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 422 SAGKNIYARAAATG-KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECA 498
Cdd:cd07140 237 PIGKHIMKSCAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLF-VEESIHdeFVRRVVEEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 499 KALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLG 578
Cdd:cd07140 316 KKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFG 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 579 PVLLC--MQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINV 631
Cdd:cd07140 392 PIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT 446
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
195-633 |
1.11e-54 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 198.21 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 195 QLKVPNL------IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQE 268
Cdd:PRK11241 2 QLNDSTLfrqqalINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 269 LILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPAT 348
Cdd:PRK11241 82 LMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 349 VSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTH-DIINYICDDEDIKAISFASSCSAGKNI 427
Cdd:PRK11241 162 MITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 428 YARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVG 506
Cdd:PRK11241 242 MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANrLYVQDGVYDRFAEKLQQAVSKLHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 507 TDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRdivvPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQA 586
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGK----AHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2047933800 587 DNLEEAISIVNrNKNRNGASIFttsgiYAR------KFQSEVEVGMVGINVAV 633
Cdd:PRK11241 398 KDEADVIAQAN-DTEFGLAAYF-----YARdlsrvfRVGEALEYGIVGINTGI 444
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
217-630 |
3.09e-54 |
|
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: 196.04 E-value: 3.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 217 VINPATQEVVSHVPLTTYEEFKAAvnAAKQAFPSWKNTPiSTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDI 296
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREA--LALAASYRSTLTR-YQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 297 ICGLEVVKHVCGLATMQMGEFVP----NASDGIDSYCIRDPIGVCAGICSFNHPAT-VSLWMFPvAVTCGNTFVLKPCET 371
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFScdltANGKARKIFTLREPLGVVLAITPFNHPLNqVAHKIAP-AIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 372 YPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAatGKQVQSHFGGKSHAII 450
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 451 MPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLV 529
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKrILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 530 QSGIEDGARLLLDGRdivvpgyENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFT 609
Cdd:cd07146 317 EEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420
....*....|....*....|.
gi 2047933800 610 TSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVN 410
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
193-630 |
5.36e-54 |
|
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: 196.08 E-value: 5.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 193 THQLKVPNLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILR 272
Cdd:cd07111 17 AHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 273 DMDKLVTNIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFvPNasdgidsyciRDPIGVCAGICSFNHPATVSL 351
Cdd:cd07111 97 HQRLFAVLESLDNGKPIRESRDcDIPLVARHFYHHAGWAQLLDTEL-AG----------WKPVGVVGQIVPWNFPLLMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 352 WMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARA 431
Cdd:cd07111 166 WKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 432 AATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAinivvsvGSSILWK--------KKLVECAKALKV 503
Cdd:cd07111 246 AGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCA-------GSRLLVQesvaeeliRKLKERMSHLRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 504 NVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLC 583
Cdd:cd07111 319 GDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2047933800 584 MQADNLEEAISIVNrNKNRNG-ASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07111 395 LTFRTAKEAVALAN-NTPYGLaASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
199-597 |
2.79e-53 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 194.77 E-value: 2.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 199 PNLIGGEFLDSHNcpVVDVINPA-TQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKL 277
Cdd:PRK03137 38 PLIIGGERITTED--KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 278 VTNIVIEQGKTLKDAQNDI---ICGLEVVkhvcGLATMQMGEFVPNAS-DGIDSYCIRDPIGVCAGICSFNHPATVSLWM 353
Cdd:PRK03137 116 SAWLVKEAGKPWAEADADTaeaIDFLEYY----ARQMLKLADGKPVESrPGEHNRYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 354 FPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIYARAA 432
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 433 ATG------KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN--IVV-SVGSSILwkKKLVECAKALKV 503
Cdd:PRK03137 272 KVQpgqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSraIVHeDVYDEVL--EKVVELTKELTV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 504 NVGTDpNADLGPVITKEVKDRFCRLVQSGIEDGaRLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLC 583
Cdd:PRK03137 350 GNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410
....*....|....
gi 2047933800 584 MQADNLEEAISIVN 597
Cdd:PRK03137 424 IKAKDFDHALEIAN 437
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
219-630 |
3.13e-52 |
|
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: 190.59 E-value: 3.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 219 NPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQ-NDII 297
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 298 CGLEVVKHvcglaTMQMGEFV--PNASDG------IDSYCIRDPIGVCAGICSFNHPATvSLWMfPV--AVTCGNTFVLK 367
Cdd:cd07098 82 VTCEKIRW-----TLKHGEKAlrPESRPGgllmfyKRARVEYEPLGVVGAIVSWNYPFH-NLLG-PIiaALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 368 PCE-----TYPGASMLLAALAvEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHF 442
Cdd:cd07098 155 VSEqvawsSGFFLSIIRECLA-ACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 443 GGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTDPNADLGPVITKE 520
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVI-VHEKIYDKllEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 521 VKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNK 600
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430
....*....|....*....|....*....|
gi 2047933800 601 NRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07098 393 YGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
190-630 |
2.60e-51 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 189.63 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 190 VKHThQLkvpnLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS--WKNTPISTRQCVMFKFQ 267
Cdd:PLN02466 55 VSYT-QL----LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 268 ELILRDMDKLVTNIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPnaSDGIDS-YCIRDPIGVCAGICSFNH 345
Cdd:PLN02466 130 DLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVP--ADGPHHvQTLHEPIGVAGQIIPWNF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 346 PATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIIN-YICDDEDIKAISFASSCSAG 424
Cdd:PLN02466 208 PLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGaALASHMDVDKLAFTGSTDTG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 425 KNIYARAAATG-KQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAinivvsvGSSILWKKKL----VECAK 499
Cdd:PLN02466 288 KIVLELAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-------GSRTFVHERVydefVEKAK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 500 --ALKVNVGtDP---NADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKE 574
Cdd:PLN02466 361 arALKRVVG-DPfkkGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQD 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2047933800 575 EFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PLN02466 436 EIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN 491
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
210-631 |
6.14e-50 |
|
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: 184.33 E-value: 6.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 210 HNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTL 289
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 290 KDAQNDI-----ICGLEVvkhvcGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTF 364
Cdd:cd07130 89 PEGLGEVqemidICDFAV-----GLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 365 VLKPCETYPgasmlLAALAVEA---------GLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIyaraaatG 435
Cdd:cd07130 164 VWKPSPTTP-----LTAIAVTKivarvleknGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQV-------G 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 436 KQVQSHF-------GGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAI-NIVV--SVGSSILwkKKLVECAKALKVNV 505
Cdd:cd07130 232 QAVAARFgrsllelGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTrRLIVheSIYDEVL--ERLKKAYKQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 506 GTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPgyenGNFVGPTILSdVTTDMECYKEEFLGPVLLCMQ 585
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP----GNYVEPTIVE-GLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2047933800 586 ADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEV--EVGMVGINV 631
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNI 432
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
218-630 |
3.28e-49 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 181.60 E-value: 3.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 218 INPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNdii 297
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 298 cglEVVKH--VC------GLATMQMGEFVPNASDGIDSYcirDPIGVCAGICSFNHPatvsLWMF-----PVaVTCGNTF 364
Cdd:PRK13968 89 ---EVAKSanLCdwyaehGPAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 365 VLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGG 444
Cdd:PRK13968 158 LLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 445 KSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITKEVKD 523
Cdd:PRK13968 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKrFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 524 RFCRLVQSGIEDGARLLLDGRDIVvpgyENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRN 603
Cdd:PRK13968 318 ELHHQVEATLAEGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGL 393
|
410 420
....*....|....*....|....*..
gi 2047933800 604 GASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PRK13968 394 SATIFTTDETQARQMAARLECGGVFIN 420
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
202-630 |
3.66e-49 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 182.62 E-value: 3.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFP-----SWKNTPISTRQCVMFKFQELILRDMDK 276
Cdd:PLN02467 12 IGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnkgkDWARTTGAVRAKYLRAIAAKITERKSE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 277 LVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLA-----------TMQMGEFvpnasdgiDSYCIRDPIGVCAGICSFNH 345
Cdd:PLN02467 92 LAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAealdakqkapvSLPMETF--------KGYVLKEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 346 PATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAG 424
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 425 KNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSIL--WKKKLVECAKALK 502
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLL-VHERIAseFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 503 VNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGrdiVVPGY-ENGNFVGPTILSDVTTDMECYKEEFLGPVL 581
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG---KRPEHlKKGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2047933800 582 LCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
263-630 |
1.07e-48 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 178.78 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 263 MFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICS 342
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 343 FNHPA-TVSLWMFPVAVTcGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASS 420
Cdd:PRK10090 81 WNFPFfLIARKMAPALLT-GNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 421 CSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCmaiNIV--VSVGSSIL--WKKKLVE 496
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVC---NCAerVYVQKGIYdqFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 497 CAKALKV-NVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEE 575
Cdd:PRK10090 237 AMQAVQFgNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 576 FLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
202-656 |
3.95e-48 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 179.32 E-value: 3.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPS--WKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:PRK09847 24 INGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQNDIICG-LEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAV 358
Cdd:PRK09847 104 LETLDTGKPIRHSLRDDIPGaARAIRWYAEAIDKVYGEVATTSSHEL-AMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 359 TCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHG-THDIINYICDDEDIKAISFASSCSAGKNIYARAAATG-K 436
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNmK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 437 QVQSHFGGKSHAIIMPDA-NMEATLNALVDAGFGTSGQTCMA---INIVVSVGSSILwkKKLVECAKALKVNVGTDPNAD 512
Cdd:PRK09847 263 RVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAgtrLLLEESIADEFL--ALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 513 LGPVITKEVKDRFCRLVQSGIEDGaRLLLDGRDIVVPGYengnfVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEA 592
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 593 ISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINV----AVTVPL---PSSFN--DKA--GLEFYTKLKRV 656
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVPFggyKQSGNgrDKSlhALEKFTELKTI 489
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
238-630 |
2.51e-44 |
|
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: 166.68 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 238 KAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDIicglEVVKHVCGLATMQMGEF 317
Cdd:cd07095 3 DAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEV----AAMAGKIDISIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 318 VPN-ASDGID-SYCIR-DPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLN 394
Cdd:cd07095 79 TGErATPMAQgRAVLRhRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 395 IVHGTHDIINYICDDEDIKAISFASSCSAGKNIY-ARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQ 473
Cdd:cd07095 159 LVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHrQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 474 TCMAIN--IVV--SVGSSILwkKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVvp 549
Cdd:cd07095 239 RCTCARrlIVPdgAVGDAFL--ERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 550 gyENGNFVGPTILsDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGI 629
Cdd:cd07095 315 --AGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNW 391
|
.
gi 2047933800 630 N 630
Cdd:cd07095 392 N 392
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
208-630 |
3.05e-43 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 165.82 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 208 DSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGK 287
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 288 TLKDAQNDI----ICGLEVVKHVCG-LATMQMGEFVPNASDGIDsycIRDPIGVCAGICSFNHPATVSLW-MFPvAVTCG 361
Cdd:PRK09407 107 ARRHAFEEVldvaLTARYYARRAPKlLAPRRRAGALPVLTKTTE---LRQPKGVVGVISPWNYPLTLAVSdAIP-ALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 362 NTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIkaISFASSCSAGKNIYARAAATGKQVQS 440
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFSL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 441 HFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITK 519
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIErIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 520 EVKDRFCRLVQSGIEDGARLLLDGR---DIvvpG---YEngnfvgPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAI 593
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVLAGGKarpDL---GplfYE------PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAV 411
|
410 420 430
....*....|....*....|....*....|....*..
gi 2047933800 594 SIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:PRK09407 412 ERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
218-630 |
6.94e-43 |
|
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: 162.86 E-value: 6.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 218 INPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNDII 297
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 298 CGLEVVKH---VCG--LATMQMGEFVPNASDGIDSYcirDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETY 372
Cdd:cd07101 81 DVAIVARYyarRAErlLKPRRRRGAIPVLTRTTVNR---RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 373 PGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIkaISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIM 451
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 452 PDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQ 530
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIErIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 531 SGIEDGARLLLDGR---DIVVPGYEngnfvgPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASI 607
Cdd:cd07101 316 DAVAKGATVLAGGRarpDLGPYFYE------PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420
....*....|....*....|...
gi 2047933800 608 FTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVN 412
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
218-638 |
7.59e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 154.13 E-value: 7.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 218 INPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKDAQNdii 297
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 298 cglEVVKHVCGL---ATMQMGEFVPNASDGIDS-----YCIRDPIGVCAGICSFNHPatvsLWM---FPV-AVTCGNTFV 365
Cdd:PRK09406 83 ---EALKCAKGFryyAEHAEALLADEPADAAAVgasraYVRYQPLGVVLAVMPWNFP----LWQvvrFAApALMAGNVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 366 LKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGK 445
Cdd:PRK09406 156 LKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 446 SHAIIMPDANMEATLNALVDAGFGTSGQTCMAIN-IVVSVGSSILWKKKLVECAKALKVNVGTDPNADLGPVITKEVKDR 524
Cdd:PRK09406 236 DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKrFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 525 FCRLVQSGIEDGARLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNG 604
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLG 391
|
410 420 430
....*....|....*....|....*....|....
gi 2047933800 605 ASIFTTSGIYARKFQSEVEVGMVGINvAVTVPLP 638
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYP 424
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
200-641 |
2.63e-39 |
|
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: 152.99 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 200 NLIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:cd07116 3 NFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQN-DIICGLEVVKHVCGLATMQMGEFVPNASDGIdSYCIRDPIGVCAGICSFNHPATVSLWMFPVAV 358
Cdd:cd07116 83 AETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISEIDENTV-AYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 359 TCGNTFVLKPCETYPGASMLLAALAVEAgLPDGVLNIVHGTH-DIINYICDDEDIKAISFASSCSAGKNIYARAAATGKQ 437
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGlEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 438 VQSHFGGKSHAIIMPDANMEAtlNALVDA---GFG----TSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTD 508
Cdd:cd07116 241 VTLELGGKSPNIFFADVMDAD--DAFFDKaleGFVmfalNQGEVCTCPSRAL-IQESIYDRfmERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 509 PNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVPGYENGNFVGPTILSDvTTDMECYKEEFLGPVLLCMQADN 588
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2047933800 589 LEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAVTVPLPSSF 641
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAF 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
201-632 |
4.05e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 152.99 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 201 LIGGEFLDSHNCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTN 280
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 281 IVIEQGKTLKDAQNDIICGLEVVKHVC--GLATMQMGEFVPNAS---DGIDSYCI--RDPIGVCAGICSFNHPATVSLWM 353
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSDSfpgNERNKYCLtsKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 354 FPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASScSAGKNIYARAA 432
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 433 ATgkQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVV---SVGSSILWKKKlvecAKALKVNVGT-D 508
Cdd:PLN00412 258 MV--PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLvmeSVADALVEKVN----AKVAKLTVGPpE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 509 PNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRdivvpgyENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADN 588
Cdd:PLN00412 332 DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK-------REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2047933800 589 LEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVA 632
Cdd:PLN00412 405 VEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA 448
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
215-609 |
1.00e-38 |
|
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: 150.65 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 215 VDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAF---PSWknTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKD 291
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 292 AQNDI---ICGLEVVKHVCGLAT---MQMGefVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFV 365
Cdd:cd07148 79 AKVEVtraIDGVELAADELGQLGgreIPMG--LTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 366 LKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYARAAAtGKQVQSHFGGK 445
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP-GTRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 446 SHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILWK--KKLVECAKALKVNVGTDPNADLGPVITKEVKD 523
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVF-VPAEIADDfaQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 524 RFCRLVQSGIEDGARLLLDGRDIVVPGYEngnfvgPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRN 603
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
....*.
gi 2047933800 604 GASIFT 609
Cdd:cd07148 389 QAAVFT 394
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
188-646 |
5.77e-38 |
|
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: 149.27 E-value: 5.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 188 DTVKHTHQLKVPNLIGGEFLDSHNcpVVDVINP-ATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKF 266
Cdd:cd07083 9 RRVKEEFGRAYPLVIGGEWVDTKE--RMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 267 QELILRDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMG--EFVPNASDGIDSYCIRdPIGVCAGICSFN 344
Cdd:cd07083 87 ADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYV-GLGAGVVISPWN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 345 HPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSA 423
Cdd:cd07083 166 FPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLET 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 424 GKNIYaRAAATGKQVQSHF-------GGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVSVGSsiLW---KKK 493
Cdd:cd07083 246 GKKIY-EAAARLAPGQTWFkrlyvetGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQG--AYepvLER 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 494 LVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGaRLLLDGRDIVVPGYengnFVGPTILSDVTTDMECYK 573
Cdd:cd07083 323 LLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGY----FVAPTVVEEVPPKARIAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 574 EEFLGPVL--LCMQADNLEEAISIVnrnknrNGASIFTTSGIYARK------FQSEVEVGMVGINVAVTVPL----P--- 638
Cdd:cd07083 398 EEIFGPVLsvIRYKDDDFAEALEVA------NSTPYGLTGGVYSRKrehleeARREFHVGNLYINRKITGALvgvqPfgg 471
|
490
....*....|.
gi 2047933800 639 ---SSFNDKAG 646
Cdd:cd07083 472 fklSGTNAKTG 482
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
211-609 |
8.88e-34 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 136.89 E-value: 8.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 211 NCPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLK 290
Cdd:PLN02315 32 NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 291 DAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCE 370
Cdd:PLN02315 112 EGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 371 TYP----GASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNIYaraaatgKQVQSHFG--- 443
Cdd:PLN02315 192 TTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQ-------QTVNARFGkcl 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 444 ----GKSHAIIMPDANMEATLNALVDAGFGTSGQ---TCMAINIVVSVGSSILwkKKLVECAKALKVNVGTDPNADLGPV 516
Cdd:PLN02315 265 lelsGNNAIIVMDDADIQLAVRSVLFAAVGTAGQrctTCRRLLLHESIYDDVL--EQLLTVYKQVKIGDPLEKGTLLGPL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 517 ITKEVKDRFCRLVQSGIEDGARLLLDGRDIvvpgYENGNFVGPTILsDVTTDMECYKEEFLGPVLLCMQADNLEEAISIV 596
Cdd:PLN02315 343 HTPESKKNFEKGIEIIKSQGGKILTGGSAI----ESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEIN 417
|
410
....*....|...
gi 2047933800 597 NRNKNRNGASIFT 609
Cdd:PLN02315 418 NSVPQGLSSSIFT 430
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
327-638 |
1.20e-32 |
|
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: 131.88 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 327 SYCIRDPIGVCAGICSFNHPatVSLWMFPV--AVTCGNTFVLKPCETYPGASMLLAALaVEAGLPDGVLNIVHGTHDIIN 404
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYP--LQLALAPLigAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 405 YICDdEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsV 484
Cdd:cd07087 171 ALLA-EPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL-V 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 485 GSSIlwKKKLVE-CAKALKVNVGTDP--NADLGPVITkevKDRFCRLVQsgiedgarlLLDGRDIVVPGY--ENGNFVGP 559
Cdd:cd07087 249 HESI--KDELIEeLKKAIKEFYGEDPkeSPDYGRIIN---ERHFDRLAS---------LLDDGKVVIGGQvdKEERYIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 560 TILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN---VAVTVP 636
Cdd:cd07087 315 TILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvlLHAAIP 394
|
...
gi 2047933800 637 -LP 638
Cdd:cd07087 395 nLP 397
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
201-630 |
3.47e-32 |
|
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: 132.32 E-value: 3.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 201 LIGGEFLDSHNcpVVDVINPA-TQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:cd07125 36 IINGEETETGE--GAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVPNASDGIDSYCIRDPIGVcaGICsfnhpatVSLWMFPVAVT 359
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGV--FVC-------ISPWNFPLAIF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 360 CG---------NTFVLKPCETYPgasmLLAALAV----EAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGK 425
Cdd:cd07125 185 TGqiaaalaagNTVIAKPAEQTP----LIAARAVellhEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 426 NIyARAAATGKQVQSHF----GGKSHAIIMPDANME-ATLNALVDAgFGTSGQTCMAINIVVSVGSsiLWK---KKLVEC 497
Cdd:cd07125 261 LI-NRALAERDGPILPLiaetGGKNAMIVDSTALPEqAVKDVVQSA-FGSAGQRCSALRLLYLQEE--IAErfiEMLKGA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 498 AKALKVNVGTDPNADLGPVITKEVKDRFCRLVQsGIEDGARLL----LDGrdivvpgyENGNFVGPTILSDVTTDmeCYK 573
Cdd:cd07125 337 MASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE-LMRGEAWLIapapLDD--------GNGYFVAPGIIEIVGIF--DLT 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047933800 574 EEFLGPVLLCMQAD--NLEEAISIVNrnknrngASIF-TTSGIYAR------KFQSEVEVGMVGIN 630
Cdd:cd07125 406 TEVFGPILHVIRFKaeDLDEAIEDIN-------ATGYgLTLGIHSRdereieYWRERVEAGNLYIN 464
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
202-606 |
1.48e-31 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 130.08 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 202 IGGEFLDSHNcPVVDVINPATQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNI 281
Cdd:PRK09457 5 INGDWIAGQG-EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 282 VIEQGKTLKDAQNdiicglEVvkhvcglATM-------------QMGEFVPNASDGidSYCIR-DPIGVCAGICSFNHPA 347
Cdd:PRK09457 84 ARETGKPLWEAAT------EV-------TAMinkiaisiqayheRTGEKRSEMADG--AAVLRhRPHGVVAVFGPYNFPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 348 TVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHGTHDIINYICDDEDIKAISFASSCSAGKNI 427
Cdd:PRK09457 149 HLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 428 YAR-AAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCM-AINIVVSVGS---SILwkKKLVECAKALK 502
Cdd:PRK09457 229 HRQfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAqgdAFL--ARLVAVAKRLT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 503 VNVgtdPNAD----LGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVvpgyENGNFVGPTILsDVTTDMECYKEEFLG 578
Cdd:PRK09457 307 VGR---WDAEpqpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQ----AGTGLLTPGII-DVTGVAELPDEEYFG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2047933800 579 PVLLCMQADNLEEAIS-------------------------------IVNRNKNRNGAS 606
Cdd:PRK09457 379 PLLQVVRYDDFDEAIRlanntrfglsagllsddredydqflleiragIVNWNKPLTGAS 437
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
232-633 |
2.76e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 120.13 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 232 TTYEEFKAAVNAAKQAFPSWKNTPISTRQCV------MFK-----FQELILRDMDK-LVTNIVIEQGKTLKDAQNDIicg 299
Cdd:PTZ00381 4 DNPEIIPPIVKKLKESFLTGKTRPLEFRKQQlrnllrMLEenkqeFSEAVHKDLGRhPFETKMTEVLLTVAEIEHLL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 300 levvKHVCGLATMQMGEfVPNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLL 379
Cdd:PTZ00381 81 ----KHLDEYLKPEKVD-TVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 380 AALaVEAGLPDGVLNIVHGTHDIINYICdDEDIKAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEAT 459
Cdd:PTZ00381 156 AKL-LTKYLDPSYVRVIEGGVEVTTELL-KEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 460 LNALVDAGFGTSGQTCMAINIVVsVGSSIlwKKKLV-ECAKALKVNVGTDP--NADLGPVITKEVKDRfcrlVQSGIEDg 536
Cdd:PTZ00381 234 ARRIAWGKFLNAGQTCVAPDYVL-VHRSI--KDKFIeALKEAIKEFFGEDPkkSEDYSRIVNEFHTKR----LAELIKD- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 537 arlllDGRDIVVPGY--ENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIY 614
Cdd:PTZ00381 306 -----HGGKVVYGGEvdIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRH 380
|
410
....*....|....*....
gi 2047933800 615 ARKFQSEVEVGMVGINVAV 633
Cdd:PTZ00381 381 KELVLENTSSGAVVINDCV 399
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
327-630 |
6.08e-25 |
|
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: 109.13 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 327 SYCIRDPIGVCAGICSFNHPatVSLWMFPV--AVTCGNTFVLKPCETYPGASMLLAALaVEAGLPDGVLNIVHGTHDIIN 404
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYP--FQLALAPLigAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 405 YICDdEDIKAISFASSCSAGKNIYARAAatgKQ---VQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIV 481
Cdd:cd07136 171 ELLD-QKFDYIFFTGSVRVGKIVMEAAA---KHltpVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 482 VsVGSSIlwKKKLVECAKA-LKVNVGTDP--NADLGpvitKEVKDR-FCRLVQsgiedgarlLLDGRDIVVPGY--ENGN 555
Cdd:cd07136 247 L-VHESV--KEKFIKELKEeIKKFYGEDPleSPDYG----RIINEKhFDRLAG---------LLDNGKIVFGGNtdRETL 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 556 FVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07136 311 YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN 385
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
194-630 |
8.50e-25 |
|
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: 109.61 E-value: 8.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 194 HQLKVPNLIGGEFLDSHNC-PVVdviNPAT-QEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELIL 271
Cdd:TIGR01238 34 KTWQAAPIIGHSYKADGEAqPVT---NPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 272 RDMDKLVTNIVIEQGKTLKDAQNDIICGLEVVKHVCGLATMQMGEFVpnasdgidsyciRDPIGVCAGICSFNHPATVSL 351
Cdd:TIGR01238 111 LHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFS------------VESRGVFVCISPWNFPLAIFT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 352 WMFPVAVTCGNTFVLKPCETYPgasmLLAALAV----EAGLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAG-- 424
Cdd:TIGR01238 179 GQISAALAAGNTVIAKPAEQTS----LIAYRAVelmqEAGFPAGTIQLLPGRgADVGAALTSDPRIAGVAFTGSTEVAql 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 425 --KNIYARAAATGKQVqSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIV-----VSVGSSILWKKKLVEC 497
Cdd:TIGR01238 255 inQTLAQREDAPVPLI-AETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLcvqedVADRVLTMIQGAMQEL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 498 akalKVNVGTDPNADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVpGYENGNFVGPTILSdvTTDMECYKEEFL 577
Cdd:TIGR01238 334 ----KVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSR-ACQHGTFVAPTLFE--LDDIAELSEEVF 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047933800 578 GPVLLCMQ--ADNLEEAISIVnrnkNRNGASIftTSGIYAR------KFQSEVEVGMVGIN 630
Cdd:TIGR01238 407 GPVLHVVRykARELDQIVDQI----NQTGYGL--TMGVHSRiettyrWIEKHARVGNCYVN 461
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
324-597 |
9.89e-25 |
|
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: 108.47 E-value: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 324 GIDSYCIRDPIGVCAGICSFNHPatVSLWMFPV--AVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDGVlNIVHGTHD 401
Cdd:cd07134 91 GTKSKIRYEPKGVCLIISPWNYP--FNLAFGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGDAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 402 IINYICD---DEdikaISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAI 478
Cdd:cd07134 168 VAQALLElpfDH----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 479 NIVVsVGSSIlwKKKLVE-CAKALKVNVGTDP----NADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIvvpgyEN 553
Cdd:cd07134 244 DYVF-VHESV--KDAFVEhLKAEIEKFYGKDAarkaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AA 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2047933800 554 GNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVN 597
Cdd:cd07134 316 QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYIN 359
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
331-598 |
1.14e-24 |
|
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: 108.46 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 331 RDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALaVEAGLPDGVLNIVHGTHDIINYICDDE 410
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGGVPETTALLEQK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 411 DIKaISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVVsVGSSILw 490
Cdd:cd07135 185 FDK-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL-VDPSVY- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 491 kKKLVE-CAKALKVNVGTDPNA--DLGPVITKEVKDRFCRLVQSgiedgarlllDGRDIVVPGYENG--NFVGPTILSDV 565
Cdd:cd07135 262 -DEFVEeLKKVLDEFYPGGANAspDYTRIVNPRHFNRLKSLLDT----------TKGKVVIGGEMDEatRFIPPTIVSDV 330
|
250 260 270
....*....|....*....|....*....|...
gi 2047933800 566 TTDMECYKEEFLGPVLLCMQADNLEEAISIVNR 598
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDLDEAIKVINS 363
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
194-581 |
7.40e-24 |
|
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: 106.90 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 194 HQLKVPNLIGGEFLDSHNcpVVDVINPAT-QEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELI-- 270
Cdd:cd07123 29 LTVEIPLVIGGKEVRTGN--TGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 271 -LRDmdKLVTNIVIEQGKTLKDAQNDIICglEV-------VKHVCGLATMQmgefvPNASD-GIDSYCIRDPI-GVCAGI 340
Cdd:cd07123 107 kYRY--ELNAATMLGQGKNVWQAEIDAAC--ELidflrfnVKYAEELYAQQ-----PLSSPaGVWNRLEYRPLeGFVYAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 341 CSFNH-------PATVSLwMfpvavtcGNTFVLKPCETYPGASMLLAALAVEAGLPDGVLNIVHG-THDIINYICDDEDI 412
Cdd:cd07123 178 SPFNFtaiggnlAGAPAL-M-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGdGPVVGDTVLASPHL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 413 KAISFASSCSAGKNIYARAAA------TGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAinivVS--- 483
Cdd:cd07123 250 AGLHFTGSTPTFKSLWKQIGEnldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA----ASray 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 484 VGSSIlW---KKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFcrlvQSGIE-----DGARLLLDGR--DIVvpGYen 553
Cdd:cd07123 326 VPESL-WpevKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRI----KGYIDhaksdPEAEIIAGGKcdDSV--GY-- 396
|
410 420 430
....*....|....*....|....*....|
gi 2047933800 554 gnFVGPTILsdVTTD--MECYKEEFLGPVL 581
Cdd:cd07123 397 --FVEPTVI--ETTDpkHKLMTEEIFGPVL 422
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
238-630 |
1.25e-22 |
|
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: 102.30 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 238 KAAVNAAKQAFPSWKNTPIStrqcvmFKFQEL--ILRDMDKLVTNIVIEQGKTL-KDAQNDIICGLEVVKHVCGLATMQM 314
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLE------FRIQQLeaLLRMLEENEDEIVEALAKDLrKPKFEAVLSEILLVKNEIKYAISNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 315 GEFV---------PNASDGIdsYCIRDPIGVCAGICSFNHPatVSLWMFPV--AVTCGNTFVLKPCETYPGASMLLAAL- 382
Cdd:cd07132 75 PEWMkpepvkknlATLLDDV--YIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELi 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 383 ----------AVEAGLPDgvlnivhgTHDIINYICDdedikAISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMP 452
Cdd:cd07132 151 pkyldkecypVVLGGVEE--------TTELLKQRFD-----YIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 453 DANMEATLNALVDAGFGTSGQTCMAINIVVSVGSSilwKKKLVECAK-ALKVNVGTDP--NADLGPVITKEvkdRFCRLV 529
Cdd:cd07132 218 SCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEV---QEKFVEALKkTLKEFYGEDPkeSPDYGRIINDR---HFQRLK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 530 QsgiedgarlLLDGRDIVVPGY--ENGNFVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASI 607
Cdd:cd07132 292 K---------LLSGGKVAIGGQtdEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYV 362
|
410 420
....*....|....*....|...
gi 2047933800 608 FTTSGIYARKFQSEVEVGMVGIN 630
Cdd:cd07132 363 FSNNKKVINKILSNTSSGGVCVN 385
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
194-598 |
2.22e-22 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 104.13 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 194 HQLKVPNLIGGefldshNCPVVDVINPA-TQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILR 272
Cdd:PRK11904 549 KQWQAGPIING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 273 DMDKLVTNIVIEQGKTLKDAQNDIicgLEVV---KHVCGLATMQMG--EFVPnASDGIDSYCIRDPIGVcagicsFnhpA 347
Cdd:PRK11904 623 NRAELIALCVREAGKTLQDAIAEV---REAVdfcRYYAAQARRLFGapEKLP-GPTGESNELRLHGRGV------F---V 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 348 TVSLWMFPVAVTC---------GNTFVLKPCETYPgasmLLAALAV----EAGLPDGVLNIVHGTHDII-NYICDDEDIK 413
Cdd:PRK11904 690 CISPWNFPLAIFLgqvaaalaaGNTVIAKPAEQTP----LIAAEAVkllhEAGIPKDVLQLLPGDGATVgAALTADPRIA 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 414 AISFASSCSAGKNI----YARAAA-------TGKQvqshfggksHAIIMpD--ANMEATLNALVDAGFGTSGQTCMAINI 480
Cdd:PRK11904 766 GVAFTGSTETARIInrtlAARDGPivpliaeTGGQ---------NAMIV-DstALPEQVVDDVVTSAFRSAGQRCSALRV 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 481 VV---SVGSSILwkKKLVECAKALKVNVGTDPNADLGPVITKEVKDRFCRLVQSgIEDGARLLLDGRdiVVPGYENGNFV 557
Cdd:PRK11904 836 LFvqeDIADRVI--EMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLLAQLP--LPAGTENGHFV 910
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2047933800 558 GPTI-----LSDVttdmecyKEEFLGPVL--LCMQADNLEEAISIVNR 598
Cdd:PRK11904 911 APTAfeidsISQL-------EREVFGPILhvIRYKASDLDKVIDAINA 951
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
330-633 |
1.35e-21 |
|
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: 99.02 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 330 IRDPIGVCAGICSFNHPatVSLWMFPV--AVTCGNTFVLKPCETYPGASMLLAALaVEAGLPDGVLNIVHGTHDIINYIC 407
Cdd:cd07137 98 VSEPLGVVLVISAWNFP--FLLSLEPVigAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 408 DDEDIKaISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGT-SGQTCMAINIVVSVGS 486
Cdd:cd07137 175 EQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 487 silWKKKLVECAK-ALKVNVGTDP--NADLGPVITKEVKDRFCRL-----VQSGIEDGARllldgRDivvpgyENGNFVG 558
Cdd:cd07137 254 ---FAPTLIDALKnTLEKFFGENPkeSKDLSRIVNSHHFQRLSRLlddpsVADKIVHGGE-----RD------EKNLYIE 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047933800 559 PTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAV 633
Cdd:cd07137 320 PTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV 394
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
194-581 |
1.28e-19 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 95.00 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 194 HQLKVPNLIGGEFLDShncPVVDVINPA-TQEVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILR 272
Cdd:COG4230 554 KQWQAAPLIAGEAASG---EARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 273 DMDKLVTNIVIEQGKTLKDAQNdiicglEV-------------VKHVCGLATmqmgefvpnasdgidsycIRDPIGVCAG 339
Cdd:COG4230 631 HRAELMALLVREAGKTLPDAIA------EVreavdfcryyaaqARRLFAAPT------------------VLRGRGVFVC 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 340 IcsfnhpatvSLWMFPVA----------VTcGNTFVLKPCETYPgasmLLAALAV----EAGLPDGVLNIVHGTHDII-N 404
Cdd:COG4230 687 I---------SPWNFPLAiftgqvaaalAA-GNTVLAKPAEQTP----LIAARAVrllhEAGVPADVLQLLPGDGETVgA 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 405 YICDDEDIKAISFASSCSAGKNIyAR--AAATGKQVQshF----GGkshaiimpdanmeatLNAL-VDA----------- 466
Cdd:COG4230 753 ALVADPRIAGVAFTGSTETARLI-NRtlAARDGPIVP--LiaetGG---------------QNAMiVDSsalpeqvvddv 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 467 ---GFGTSGQTCMAINIVvsvgssilwkkkLV--ECA-----------KALKVNVGTDPNADLGPVITKEVKDRFCRLVQ 530
Cdd:COG4230 815 lasAFDSAGQRCSALRVL------------CVqeDIAdrvlemlkgamAELRVGDPADLSTDVGPVIDAEARANLEAHIE 882
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2047933800 531 SgIEDGARLLLDGRdiVVPGYENGNFVGPTI-----LSDVTtdmecyKEEFlGPVL 581
Cdd:COG4230 883 R-MRAEGRLVHQLP--LPEECANGTFVAPTLieidsISDLE------REVF-GPVL 928
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
213-597 |
2.29e-19 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 94.16 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 213 PVVDVINPATQ-EVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVTNIVIEQGKTLKD 291
Cdd:PRK11905 567 GTRPVLNPADHdDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLAN 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 292 AqndIicgLEVVKHV--CGLATMQMGEFVPNASdgidsyciRDPIGVCAGIcsfnhpatvSLWMFPVA----------VT 359
Cdd:PRK11905 647 A---I---AEVREAVdfLRYYAAQARRLLNGPG--------HKPLGPVVCI---------SPWNFPLAiftgqiaaalVA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 360 cGNTFVLKPCETYPgasmLLAALAV----EAGLPDGVLNIVHGTHDII-NYICDDEDIKAISFASSCSAGKNIY-ARAAA 433
Cdd:PRK11905 704 -GNTVLAKPAEQTP----LIAARAVrllhEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQrTLAKR 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 434 TGKQVQ--SHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINiVVSVGSSIlwKKKLVECAK-ALK-VNVGtDP 509
Cdd:PRK11905 779 SGPPVPliAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALR-VLCLQEDV--ADRVLTMLKgAMDeLRIG-DP 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 510 ---NADLGPVITKEVKDrfcrlvqsGIEDG-ARLLLDGRDI----VVPGYENGNFVGPTI-----LSDVttdmecyKEEF 576
Cdd:PRK11905 855 wrlSTDVGPVIDAEAQA--------NIEAHiEAMRAAGRLVhqlpLPAETEKGTFVAPTLieidsISDL-------EREV 919
|
410 420
....*....|....*....|...
gi 2047933800 577 LGPVL--LCMQADNLEEAISIVN 597
Cdd:PRK11905 920 FGPVLhvVRFKADELDRVIDDIN 942
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
330-637 |
1.18e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 90.49 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 330 IRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALaVEAGLPDGVLNIVHGTHDIINYICDD 409
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 410 EDIKaISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAIIMPDANMEATLNALVDAGFG-TSGQTCMAINIVVSVGSsi 488
Cdd:PLN02174 188 KWDK-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKE-- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 489 lWKKKLVECAK-ALKVNVGTDPnadlgpvitKEVKDrFCRLVQSGIEDGARLLLDGRDI---VVPGYENGN---FVGPTI 561
Cdd:PLN02174 265 -YAPKVIDAMKkELETFYGKNP---------MESKD-MSRIVNSTHFDRLSKLLDEKEVsdkIVYGGEKDRenlKIAPTI 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047933800 562 LSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGIN-VAVTVPL 637
Cdd:PLN02174 334 LLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLAL 410
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
201-633 |
2.86e-17 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 87.34 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 201 LIGGEFLDShncPVVDVINPATQ-EVVSHVPLTTYEEFKAAVNAAKQAFPSWKNTPISTRQCVMFKFQELILRDMDKLVT 279
Cdd:PRK11809 650 MLEDPVAAG---EMSPVINPADPrDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMG 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 280 NIVIEQGKTLKDAqndiicglevvkhvcglatmqMGEfVPNASDGIDSYC--IRD--------PIG--VCagicsfnhpa 347
Cdd:PRK11809 727 LLVREAGKTFSNA---------------------IAE-VREAVDFLRYYAgqVRDdfdndthrPLGpvVC---------- 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 348 tVSLWMFPVAVTC---------GNTFVLKPCETYPgasmLLAALAV----EAGLPDGVLNIVHGTHDII-NYICDDEDIK 413
Cdd:PRK11809 775 -ISPWNFPLAIFTgqvaaalaaGNSVLAKPAEQTP----LIAAQAVrillEAGVPAGVVQLLPGRGETVgAALVADARVR 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 414 AISFASSCSAG----KNIYARAAATGKQVQ--SHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMAINIVV---SV 484
Cdd:PRK11809 850 GVMFTGSTEVArllqRNLAGRLDPQGRPIPliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLClqdDV 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 485 GSSIL--WKKKLVECakalkvNVGtDP---NADLGPVITKEVKDRFCRLVQSGIEDGARLLLDGRDIVVpGYENGNFVGP 559
Cdd:PRK11809 930 ADRTLkmLRGAMAEC------RMG-NPdrlSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSE-DWQSGTFVPP 1001
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 560 TILS-DVTTDMecyKEEFLGPVLLCM-----QADNLEEAIsivnrnknrNGASIFTTSGIYAR------KFQSEVEVG-- 625
Cdd:PRK11809 1002 TLIElDSFDEL---KREVFGPVLHVVrynrnQLDELIEQI---------NASGYGLTLGVHTRidetiaQVTGSAHVGnl 1069
|
490
....*....|...
gi 2047933800 626 -----MVGINVAV 633
Cdd:PRK11809 1070 yvnrnMVGAVVGV 1082
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
333-630 |
6.68e-16 |
|
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: 81.38 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 333 PIGVCAGICSFNHPatVSLWMFPV--AVTCGNTFVLKPCETYPGASMLLAALAVEAGLPDgVLNIVHGTHDIinyicdde 410
Cdd:cd07133 101 PLGVVGIIVPWNYP--LYLALGPLiaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADV-------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 411 dikAISFAS----------SCSAGKNIyARAAA---TgkQVQSHFGGKSHAIIMPDANMEATLNALVDAGFGTSGQTCMA 477
Cdd:cd07133 170 ---AAAFSSlpfdhllftgSTAVGRHV-MRAAAenlT--PVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 478 INIVvsvgssILWKKKLVECAKALKVNV----GTDP-NADLGPVITKEVKDRFCRLVQSGIEDGARllldgrdIVVPGYE 552
Cdd:cd07133 244 PDYV------LVPEDKLEEFVAAAKAAVakmyPTLAdNPDYTSIINERHYARLQGLLEDARAKGAR-------VIELNPA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 553 NGNFVG-----PTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMV 627
Cdd:cd07133 311 GEDFAAtrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV 390
|
...
gi 2047933800 628 GIN 630
Cdd:cd07133 391 TIN 393
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
332-633 |
1.46e-14 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 77.46 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 332 DPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAAlAVEAGLPDGVLNIVHGTHDIINYICDDED 411
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-NIPKYLDSKAVKVIEGGPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 412 IKaISFASSCSAGKNIYARAAATGKQVQSHFGGKSHAI---IMPDANMEATLNALVDAGFGT-SGQTCMAINIVvsvgss 487
Cdd:PLN02203 186 DK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYV------ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 488 iLWKKK----LVECAKA-LKVNVGTDPN--ADLGPVITKEvkdRFCRLvqsgiedgARLLLDGR---DIVVPGY--ENGN 555
Cdd:PLN02203 259 -LVEERfapiLIELLKStIKKFFGENPResKSMARILNKK---HFQRL--------SNLLKDPRvaaSIVHGGSidEKKL 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047933800 556 FVGPTILSDVTTDMECYKEEFLGPVLLCMQADNLEEAISIVNRNKNRNGASIFTTSGIYARKFQSEVEVGMVGINVAV 633
Cdd:PLN02203 327 FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
319-610 |
2.59e-12 |
|
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: 70.34 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 319 PNASDGIDSYCIRDPIGVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCETYPGASMLLAALAVEAG-LPDGVLNIVH 397
Cdd:cd07084 86 LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLIN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 398 GTHDIINYICDDEDIKAISFASSCSAGKNIYARAAATgkQVQSHFGGKSHAIIMPDAN-MEATLNALVDAGFGTSGQTCM 476
Cdd:cd07084 166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 477 AINIVVSVGSsilW-KKKLVECAKALkVNVGTDPNADLGPVITKEVKdrfCRLVQSGIEDGARLLLDGRDivVPGYENGN 555
Cdd:cd07084 244 AQSMLFVPEN---WsKTPLVEKLKAL-LARRKLEDLLLGPVQTFTTL---AMIAHMENLLGSVLLFSGKE--LKNHSIPS 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047933800 556 FVGPTILSD--VTTD-----MECYKEEFLGPVLLCMQADNLEEA--ISIVNRNKNRNGASIFTT 610
Cdd:cd07084 315 IYGACVASAlfVPIDeilktYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSN 378
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
335-618 |
2.61e-11 |
|
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: 67.29 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 335 GVCAGICSFNHPATVSLWMFPVAVTCGNTFVLKPCEtypgASMLLA----ALAVEAG-LPDGVLNIVHG-THDIINYIcD 408
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPAT----ATAYLTeavvKDIVESGlLPEGALQLICGsVGDLLDHL-G 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 409 DEDIkaISFASScsagkniyaraAATGKQVQSHFGGKSHAIIMpdaNMEA-TLNALV---DAGFGT-------------- 470
Cdd:cd07128 221 EQDV--VAFTGS-----------AATAAKLRAHPNIVARSIRF---NAEAdSLNAAIlgpDATPGTpefdlfvkevarem 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 471 ---SGQTCMAINivvsvgsSILWKKKLVEC-AKAL-----KVNVGtDPNAD---LGPVITKEVKDRfcrlVQSGIED--- 535
Cdd:cd07128 285 tvkAGQKCTAIR-------RAFVPEARVDAvIEALkarlaKVVVG-DPRLEgvrMGPLVSREQRED----VRAAVATlla 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 536 GARLLLDGRD---IVVPGYENGNFVGPTIL-------SDVTTDMECYkeeflGPVLLCMQADNLEEAISIVNRNKNRNGA 605
Cdd:cd07128 353 EAEVVFGGPDrfeVVGADAEKGAFFPPTLLlcddpdaATAVHDVEAF-----GPVATLMPYDSLAEAIELAARGRGSLVA 427
|
330
....*....|...
gi 2047933800 606 SIFTTSGIYARKF 618
Cdd:cd07128 428 SVVTNDPAFAREL 440
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
361-598 |
5.31e-06 |
|
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: 50.23 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 361 GNTFVLKPCETYPGASMLLAALAVEA----GLPDGVLNIVHGT-HDIINYICDDEDIKAISFASSCSAGKNIYARAAA-- 433
Cdd:cd07129 135 GCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGGgREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArp 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 434 TGKQVQSHFGGKSHAIIMPDAnMEATLNALVDaGFGTS-----GQTCMAINIVVSVGSSILwkKKLVEcakALKVNVGTD 508
Cdd:cd07129 215 EPIPFYAELGSVNPVFILPGA-LAERGEAIAQ-GFVGSltlgaGQFCTNPGLVLVPAGPAG--DAFIA---ALAEALAAA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047933800 509 PNadlGPVITKEVKDRFCRLVQSGIE-DGARLLLDGrdivvPGYENGNFVGPTIL----SDVTTDMECYKEEFlGPVLLC 583
Cdd:cd07129 288 PA---QTMLTPGIAEAYRQGVEALAAaPGVRVLAGG-----AAAEGGNQAAPTLFkvdaAAFLADPALQEEVF-GPASLV 358
|
250
....*....|....*
gi 2047933800 584 MQADNLEEAISIVNR 598
Cdd:cd07129 359 VRYDDAAELLAVAEA 373
|
|
| |
