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Conserved domains on  [gi|1734334313|ref|NP_001360568|]
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Aldehyde dehydrogenase [Caenorhabditis elegans]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 10162890)

aldehyde dehydrogenase family protein similar to NAD(P)-dependent benzaldehyde dehydrogenase that catalyzes the conversion of benzaldehyde into benzoate in the (R)-mandelate degradation pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
5-430 0e+00

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: 719.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07087     2 ELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07087    82 RVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07087   162 VEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDktQGAVLIGGERDRADLYIPPTVL-D 323
Cdd:cd07087   242 APDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD--DGKVVIGGQVDKEERYIAPTILdD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07087   320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFG 399
                         410       420
                  ....*....|....*....|....*..
gi 1734334313 404 GVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07087   400 GVGNSGMGAYHGKAGFDTFSHLKSVLK 426
 
Name Accession Description Interval E-value
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
5-430 0e+00

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: 719.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07087     2 ELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07087    82 RVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07087   162 VEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDktQGAVLIGGERDRADLYIPPTVL-D 323
Cdd:cd07087   242 APDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD--DGKVVIGGQVDKEERYIAPTILdD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07087   320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFG 399
                         410       420
                  ....*....|....*....|....*..
gi 1734334313 404 GVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07087   400 GVGNSGMGAYHGKAGFDTFSHLKSVLK 426
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
7-459 0e+00

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 596.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHV 86
Cdd:PTZ00381   13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  87 EKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVN 166
Cdd:PTZ00381   93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 167 GGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAP 246
Cdd:PTZ00381  173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 247 DYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGAVLIGGERDRADLYIPPTVL-DVE 325
Cdd:PTZ00381  253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENKYVAPTIIvNPD 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 326 KSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFGGV 405
Cdd:PTZ00381  333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1734334313 406 GVSGMGRYRGKYGFDTFTHEKSVLHRGFFGESLLAARYPPLSQQKLDQMRRLTG 459
Cdd:PTZ00381  413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLK 466
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
7-428 8.43e-107

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: 326.31  E-value: 8.43e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAvwkdlrrrhestEILEIGMTIQE--------IDYF----- 73
Cdd:COG1012    49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL------------LTLETGKPLAEargevdraADFLryyag 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  74 -LKNIDDWVKPTHVEKTFTtaldkpVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL 152
Cdd:COG1012   117 eARRLYGETIPSDAPGTRA------YVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAEL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 153 I-----PKyfesKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADID 225
Cdd:COG1012   191 LeeaglPA----GVLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLD 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 226 ISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQG 302
Cdd:COG1012   267 AAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEdaVAEG 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 303 A-VLIGGERDRAD--LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLL 378
Cdd:COG1012   347 AeLLTGGRRPDGEggYFVEPTVLaDVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVA 426
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734334313 379 NETSSGGVTVNDVLMHiTVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:COG1012   427 RRLEAGMVWINDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
7-428 8.08e-97

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: 299.83  E-value: 8.08e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRR-RHESTEilEIGMTIQEIDYF---LKNIDDWVK 82
Cdd:pfam00171  35 IAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKpLAEARG--EVDRAIDVLRYYaglARRLDGETL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  83 P-THVEKTFTTaldkpvieKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PKy 156
Cdd:pfam00171 113 PsDPGRLAYTR--------REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFeeaglPA- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 157 fesKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:pfam00171 184 ---GVLNVVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFG 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 235 KWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER 310
Cdd:pfam00171 261 AFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVEdaKEEGAkLLTGGEA 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 311 DRAD-LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTV 388
Cdd:pfam00171 341 GLDNgYFVEPTVLaNVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWI 420
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1734334313 389 NDVLMhITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:pfam00171 421 NDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
25-426 1.42e-48

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 173.84  E-value: 1.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQEIDYflKNIDDWVKPTHVEKTFTTALDKPVIE---- 100
Cdd:TIGR01804  59 RGRILRRAADLIRERNEELAK------------LETLDTGKTLQETIV--ADMDSGADVFEFFAGLAPALNGEIIPlggp 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 ------KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVA-ATFEKLIPKYFESKYVTVVNGGIPETT 173
Cdd:TIGR01804 125 sfaytiREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTAlKVAEIMEEAGLPKGVFNVVQGDGAEVG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 174 DLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILV 251
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 252 NSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD-----LYIPPTVL 322
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEkgKAEGAtLATGGGRPENVglqngFFVEPTVF 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 323 -DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLP 401
Cdd:TIGR01804 365 aDCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEAP 442
                         410       420
                  ....*....|....*....|....*
gi 1734334313 402 FGGVGVSGMGRYRGKYGFDTFTHEK 426
Cdd:TIGR01804 443 FGGYKQSGIGRENGKAALAHYTEVK 467
 
Name Accession Description Interval E-value
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
5-430 0e+00

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: 719.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07087     2 ELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07087    82 RVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07087   162 VEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDktQGAVLIGGERDRADLYIPPTVL-D 323
Cdd:cd07087   242 APDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD--DGKVVIGGQVDKEERYIAPTILdD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07087   320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFG 399
                         410       420
                  ....*....|....*....|....*..
gi 1734334313 404 GVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07087   400 GVGNSGMGAYHGKAGFDTFSHLKSVLK 426
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
5-447 0e+00

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: 659.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07132     2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07132    82 PVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07132   162 VLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKtqGAVLIGGERDRADLYIPPTVL-D 323
Cdd:cd07132   242 APDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSG--GKVAIGGQTDEKERYIAPTVLtD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07132   320 VKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFG 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1734334313 404 GVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGESLLAARYPPLS 447
Cdd:cd07132   400 GVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
5-456 0e+00

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: 622.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07136     2 SLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07136    82 RVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07136   162 VEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDktQGAVLIGGERDRADLYIPPTVLD- 323
Cdd:cd07136   242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLD--NGKIVFGGNTDRETLYIEPTILDn 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07136   320 VTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFG 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1734334313 404 GVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGEslLAARYPPlSQQKLDQMRR 456
Cdd:cd07136   400 GVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPP-YKGKKKKLKK 449
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
7-459 0e+00

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 596.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHV 86
Cdd:PTZ00381   13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  87 EKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVN 166
Cdd:PTZ00381   93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 167 GGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAP 246
Cdd:PTZ00381  173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 247 DYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGAVLIGGERDRADLYIPPTVL-DVE 325
Cdd:PTZ00381  253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENKYVAPTIIvNPD 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 326 KSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFGGV 405
Cdd:PTZ00381  333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1734334313 406 GVSGMGRYRGKYGFDTFTHEKSVLHRGFFGESLLAARYPPLSQQKLDQMRRLTG 459
Cdd:PTZ00381  413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLK 466
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
2-430 0e+00

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: 594.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   2 AFTELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWV 81
Cdd:cd07135     6 EIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  82 KPTHVEKT-FTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK 160
Cdd:cd07135    86 KDEKVKDGpLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 161 YVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07135   166 AFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 241 QTCLAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGAVLIGGERDRADLYIPPT 320
Cdd:cd07135   246 QICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGKVVIGGEMDEATRFIPPT 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 321 -VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDT 399
Cdd:cd07135   326 iVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDN 405
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1734334313 400 LPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07135   406 APFGGVGDSGYGAYHGKYGFDTFTHERTVVK 436
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
5-429 0e+00

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: 518.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07134     2 RVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07134    82 RVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07134   162 FEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGED--VKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRADLYIPP 319
Cdd:cd07134   242 APDYVFVHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDDAvaKGAkVEFGGQFDAAQRYIAP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 320 TVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVD 398
Cdd:cd07134   322 TVLtNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNP 401
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1734334313 399 TLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07134   402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
4-430 6.99e-176

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: 501.24  E-value: 6.99e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   4 TELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDL-RRRHESTEILEIGMTIQEIDYFLKNIDDWVK 82
Cdd:cd07133     1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  83 PT--HVEKTFTTAldKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK 160
Cdd:cd07133    81 PSrrHVGLLFLPA--KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 161 YVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07133   159 EVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 241 QTCLAPDYILVNSTVKPKLVAAIRKYVNEFYGeDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI----GGERDRAD 314
Cdd:cd07133   239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdaRAKGARVIelnpAGEDFAAT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 315 LYIPPT-VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLM 393
Cdd:cd07133   318 RKLPPTlVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1734334313 394 HITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07133   398 HVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
5-429 2.81e-171

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: 489.23  E-value: 2.81e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07137     3 RLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07137    83 KVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNC-GQTC 243
Cdd:cd07137   163 IEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQAC 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 244 LAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLYIPPT- 320
Cdd:cd07137   243 IAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpSVADKIVHGGERDEKNLYIEPTi 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 321 VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTL 400
Cdd:cd07137   323 LLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTL 402
                         410       420
                  ....*....|....*....|....*....
gi 1734334313 401 PFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07137   403 PFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
PLN02203 PLN02203
aldehyde dehydrogenase
5-457 1.88e-152

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 443.40  E-value: 1.88e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:PLN02203   10 GSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:PLN02203   90 KAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVE---DDADIDISAKRIAWGKWLNC-G 240
Cdd:PLN02203  170 IEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCaG 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 241 QTCLAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLYIP 318
Cdd:PLN02203  250 QACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKdpRVAASIVHGGSIDEKKLFIE 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 319 PTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITV 397
Cdd:PLN02203  330 PTILlNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAC 409
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 398 DTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGEslLAARYPPLSQQKLDQMRRL 457
Cdd:PLN02203  410 DSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKLGFLRLV 467
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
5-429 2.94e-136

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: 400.05  E-value: 2.94e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07078     2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEKTFTTALdkpVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK-YVT 163
Cdd:cd07078    81 IPSPDPGELA---IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPgVLN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 164 VVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQ 241
Cdd:cd07078   158 VVTGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 242 TCLAPDYILVNSTVKPKLVAAIRKYVNEFYGED-VKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD--L 315
Cdd:cd07078   238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdaKAEGAkLLCGGKRLEGGkgY 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 316 YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMH 394
Cdd:cd07078   318 FVPPTVLtDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1734334313 395 iTVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07078   398 -AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
6-462 5.77e-127

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 378.23  E-value: 5.77e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   6 LVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTH 85
Cdd:PLN02174   15 LVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  86 VEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVV 165
Cdd:PLN02174   95 AKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 166 NGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKW-LNCGQTCL 244
Cdd:PLN02174  175 EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACI 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGA--VLIGGERDRADLYIPPTV- 321
Cdd:PLN02174  255 SPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSdkIVYGGEKDRENLKIAPTIl 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 322 LDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLP 401
Cdd:PLN02174  335 LDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLP 414
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734334313 402 FGGVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGESllAARYPPLSQQKLDQMRRLTGKRI 462
Cdd:PLN02174  415 FGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDS--AVRYPPYSRGKLRLLKALVDSNI 473
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
8-429 9.69e-112

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: 334.97  E-value: 9.69e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   8 ETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYFLKNIDDWVKPTHVE 87
Cdd:cd06534     1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPELPS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  88 KTFTTALdkpVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK-YVTVVN 166
Cdd:cd06534    80 PDPGGEA---YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPgVVNVVP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 167 GGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd06534   157 GGGDEVGAALlsHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRkyvnefygedvkaskdyarminqrhfdrisglldktqgavliggerdradlyippTVL-D 323
Cdd:cd06534   237 AASRLLVHESIYDEFVEKLV-------------------------------------------------------TVLvD 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHiTVDTLPFG 403
Cdd:cd06534   262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG-VGPEAPFG 340
                         410       420
                  ....*....|....*....|....*.
gi 1734334313 404 GVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd06534   341 GVKNSGIGREGGPYGLEEYTRTKTVV 366
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
7-428 8.43e-107

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: 326.31  E-value: 8.43e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAvwkdlrrrhestEILEIGMTIQE--------IDYF----- 73
Cdd:COG1012    49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL------------LTLETGKPLAEargevdraADFLryyag 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  74 -LKNIDDWVKPTHVEKTFTtaldkpVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL 152
Cdd:COG1012   117 eARRLYGETIPSDAPGTRA------YVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAEL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 153 I-----PKyfesKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADID 225
Cdd:COG1012   191 LeeaglPA----GVLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLD 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 226 ISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQG 302
Cdd:COG1012   267 AAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEdaVAEG 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 303 A-VLIGGERDRAD--LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLL 378
Cdd:COG1012   347 AeLLTGGRRPDGEggYFVEPTVLaDVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVA 426
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734334313 379 NETSSGGVTVNDVLMHiTVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:COG1012   427 RRLEAGMVWINDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
7-428 8.08e-97

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: 299.83  E-value: 8.08e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRR-RHESTEilEIGMTIQEIDYF---LKNIDDWVK 82
Cdd:pfam00171  35 IAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKpLAEARG--EVDRAIDVLRYYaglARRLDGETL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  83 P-THVEKTFTTaldkpvieKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PKy 156
Cdd:pfam00171 113 PsDPGRLAYTR--------REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFeeaglPA- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 157 fesKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:pfam00171 184 ---GVLNVVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFG 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 235 KWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER 310
Cdd:pfam00171 261 AFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVEdaKEEGAkLLTGGEA 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 311 DRAD-LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTV 388
Cdd:pfam00171 341 GLDNgYFVEPTVLaNVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWI 420
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1734334313 389 NDVLMhITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:pfam00171 421 NDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
18-430 3.12e-90

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: 282.96  E-value: 3.12e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  18 ETKPVKFRKQQLLKLKKFIEENREALSEAVWKDL-RRRHESTeiLEIGMTIQEIDYFLKNIDDWVKPTHVEKTFTTALDK 96
Cdd:cd07099    35 AALGVEGRAQRLLRWKRALADHADELAELLHAETgKPRADAG--LEVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKK 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  97 PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSEL----SENVAATFEKLIPkyfESKYVTVVNGGIPET 172
Cdd:cd07099   113 ATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVtplvGELLAEAWAAAGP---PQGVLQVVTGDGATG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 173 TDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVN 252
Cdd:cd07099   190 AALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVH 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 253 STVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD-LYIPPTVL-DVEK 326
Cdd:cd07099   270 ESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdaVAKGAkALTGGARSNGGgPFYEPTVLtDVPH 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 327 SDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFGGVG 406
Cdd:cd07099   350 DMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVK 429
                         410       420
                  ....*....|....*....|....
gi 1734334313 407 VSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07099   430 DSGGGRRHGAEGLREFCRPKAIAR 453
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
25-429 4.09e-76

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: 246.44  E-value: 4.09e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHVEKTFTTALDKPVIEKDPK 104
Cdd:cd07098    42 RRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFES-----KYVTVVNGgIPETTDLLKE- 178
Cdd:cd07098   122 GVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAAcghdpDLVQLVTC-LPETAEALTSh 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 179 -RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKP 257
Cdd:cd07098   201 pVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYD 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 258 KLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLL--DKTQGAVLI-GGER-----DRADLYIPPTVL-DVEKS 327
Cdd:cd07098   281 KLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadAVEKGARLLaGGKRyphpeYPQGHYFPPTLLvDVTPD 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 328 DPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFGGVGV 407
Cdd:cd07098   361 MKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKG 440
                         410       420
                  ....*....|....*....|..
gi 1734334313 408 SGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07098   441 SGFGRFAGEEGLRGLCNPKSVT 462
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
98-428 2.36e-74

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: 241.57  E-value: 2.36e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  98 VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfesKYVTVVNGGIPET 172
Cdd:cd07103   112 LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELaeeagLPA----GVLNVVTGSPAEI 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 173 TDLLKERFD--HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYIL 250
Cdd:cd07103   188 GEALCASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIY 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 251 VNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADLYIPPTVL-DV 324
Cdd:cd07103   268 VHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEdaVAKGAkVLTGGKRlGLGGYFYEPTVLtDV 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 325 EKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLmhITVDTLPFGG 404
Cdd:cd07103   348 TDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL--ISDAEAPFGG 425
                         330       340
                  ....*....|....*....|....
gi 1734334313 405 VGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07103   426 VKESGLGREGGKEGLEEYLETKYV 449
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
25-426 6.24e-71

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: 232.04  E-value: 6.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALseAVWkdLRRRHESTEI---LEIGMTIQEIDY---FLKNIDDWVKPTHVEKTFTTAldkpv 98
Cdd:cd07104    24 RAAILRKAAEILEERRDEI--ADW--LIRESGSTRPkaaFEVGAAIAILREaagLPRRPEGEILPSDVPGKESMV----- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  99 iEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATfekLIPKYFE-----SKYVTVVNGGIPETT 173
Cdd:cd07104    95 -RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGL---LIAEIFEeaglpKGVLNVVPGGGSEIG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 174 DLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILV 251
Cdd:cd07104   171 DALVEhpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 252 NSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDraDLYIPPTVL-DVEK 326
Cdd:cd07104   251 HESVYDEFVEKLVAKAKALpVGDPRDPDTVIGPLINERQVDRVHAIVEDAvaAGArLLTGGTYE--GLFYQPTVLsDVTP 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 327 SDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlmhiTVD---TLPFG 403
Cdd:cd07104   329 DMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ----TVNdepHVPFG 404
                         410       420
                  ....*....|....*....|...
gi 1734334313 404 GVGVSGMGRYRGKYGFDTFTHEK 426
Cdd:cd07104   405 GVKASGGGRFGGPASLEEFTEWQ 427
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
25-430 1.72e-69

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: 228.75  E-value: 1.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHVE--KTFTTaldkpVIEKD 102
Cdd:cd07092    43 RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAGAARTLEGPAAGEylPGHTS-----MIRRE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPETTDLL--KERF 180
Cdd:cd07092   118 PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALvaHPRV 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 181 DHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLV 260
Cdd:cd07092   198 RMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFV 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 261 AAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKT-QGA-VLIGGER-DRADLYIPPTVL-DVEKSDPFMHDEI 335
Cdd:cd07092   278 AALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVERApAHArVLTGGRRaEGPGYFYEPTVVaGVAQDDEIVQEEI 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 336 FGPVLpiiTVQSFS---ESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmHITVDT-LPFGGVGVSGMG 411
Cdd:cd07092   358 FGPVV---TVQPFDdedEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHGGFKQSGYG 431
                         410
                  ....*....|....*....
gi 1734334313 412 RYRGKYGFDTFTHEKSVLH 430
Cdd:cd07092   432 KDLSIYALEDYTRIKHVMV 450
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
7-428 4.93e-69

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: 227.83  E-value: 4.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLknidDWVKpTHV 86
Cdd:cd07093    25 VAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRFFA----DYIL-QLD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  87 EKTFTTALD-KPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVTV 164
Cdd:cd07093   100 GESYPQDGGaLNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQT 242
Cdd:cd07093   180 VHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEV 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 243 CLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD---- 314
Cdd:cd07093   260 CLAGSRILVQRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVElaRAEGAtILTGGGRPELPdleg 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 315 -LYIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:cd07093   340 gYFVEPTVItGLDNDSRVAQEEIFGPVV---TVIPFDDEEEAIElanDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN 416
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1734334313 390 DVLMHitvD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07093   417 CWLVR---DlRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
98-428 1.05e-68

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: 226.30  E-value: 1.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  98 VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELS----ENVAATFEKL-IPKyfesKYVTVVNGG---I 169
Cdd:cd07105    93 MVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSprthWLIGRVFHEAgLPK----GVLNVVTHSpedA 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 170 PETTDLLkerFDH-----ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07105   169 PEVVEAL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICM 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKdyarMINQRHFDRISGLLDKTQ--GAVLIGGERDR---ADLYIPP 319
Cdd:cd07105   246 STERIIVHESIADEFVEKLKAAAEKLFAGPVVLGS----LVSAAAADRVKELVDDALskGAKLVVGGLADespSGTSMPP 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 320 TVLD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHitvD 398
Cdd:cd07105   322 TILDnVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH---D 398
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1734334313 399 --TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07105   399 epTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
7-428 1.69e-66

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: 221.27  E-value: 1.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETK--PVKFRKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQEI-----------DYF 73
Cdd:cd07114    25 VAAARAAFEGGAWRklTPTERGKLLRRLADLIEANAEELAE------------LETRDNGKLIRETraqvrylaewyRYY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  74 ---LKNIDDWVKPTHVEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFE 150
Cdd:cd07114    93 aglADKIEGAVIPVDKGDYLNFTRREPL------GVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 151 KLIPKY-FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDIS 227
Cdd:cd07114   167 KLAEEAgFPPGVVNVVTGFGPETGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 228 AKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA- 303
Cdd:cd07114   247 VNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIrVGDPLDPETQMGPLATERQLEKVERYVAraREEGAr 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 304 VLIGGER-DRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKV 374
Cdd:cd07114   327 VLTGGERpSGADLgagyFFEPTILaDVTNDMRIAQEEVFGPVL---SVIPFDDEEEAIAlanDSEYGLAAGIWTRDLARA 403
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1734334313 375 KRLLNETSSGGVTVNDvlMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07114   404 HRVARAIEAGTVWVNT--YRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
101-428 3.40e-66

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: 220.18  E-value: 3.40e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVTVVNGGIPETTDLLKE- 178
Cdd:cd07109   115 REPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAALVAh 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 179 -RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKP 257
Cdd:cd07109   195 pGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYD 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 258 KLVAAIRKYVNEF---YGEDvkaSKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRADL----YIPPTVLD-VEK 326
Cdd:cd07109   275 EVLERLVERFRALrvgPGLE---DPDLGPLISAKQLDRVEGFVAraRARGArIVAGGRIAEGAPaggyFVAPTLLDdVPP 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 327 SDPFMHDEIFGPVLPIITVQSFSESLEyIADG-EKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDtLPFGGV 405
Cdd:cd07109   352 DSRLAQEEIFGPVLAVMPFDDEAEAIA-LANGtDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIE-LPFGGV 429
                         330       340
                  ....*....|....*....|...
gi 1734334313 406 GVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07109   430 KKSGHGREKGLEALYNYTQTKTV 452
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
7-428 7.38e-66

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: 219.83  E-value: 7.38e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKdlrrrhESTEIL-----EIGMTIQEIDYFLKN---ID 78
Cdd:cd07088    41 VDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVE------EQGKTLslarvEVEFTADYIDYMAEWarrIE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  79 DWVKPTHVEKtfttalDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----I 153
Cdd:cd07088   115 GEIIPSDRPN------ENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 154 PKyfesKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRI 231
Cdd:cd07088   189 PA----GVLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAI 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 232 AWGKWLNCGQTCLAPDYILVNSTVKP----KLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-V 304
Cdd:cd07088   265 VDSRIINCGQVCTCAERVYVHEDIYDefmeKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVEEMVERAveAGAtL 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 305 LIGGERDRAD--LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:cd07088   342 LTGGKRPEGEkgYFYEPTVLtNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNEL 421
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1734334313 382 SSGGVTVN----DVL--MHitvdtlpfGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07088   422 EFGETYINrenfEAMqgFH--------AGWKKSGLGGADGKHGLEEYLQTKVV 466
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
7-428 5.91e-64

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: 214.77  E-value: 5.91e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGE--TKPVKFRKQQLLKLKKFIEENREALS--EAV--WKDLRrrhESTEIlEIGMTIQEIDYF---LKNI 77
Cdd:cd07091    47 VKAARAAFETGWwrKMDPRERGRLLNKLADLIERDRDELAalESLdnGKPLE---ESAKG-DVALSIKCLRYYagwADKI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  78 DDWVKPTHVEKTFTTaldkpviEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY- 156
Cdd:cd07091   123 QGKTIPIDGNFLAYT-------RREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAg 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 157 FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:cd07091   196 FPPGVVNIVPGFGPTAGAAISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAF 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 234 GKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGE 309
Cdd:cd07091   276 GIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIEsgKKEGAtLLTGGE 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 310 R-DRADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVT 387
Cdd:cd07091   356 RhGSKGYFIQPTVFtDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVW 435
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1734334313 388 VN--DVLMHitvdTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07091   436 VNtyNVFDA----AVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
7-428 6.69e-64

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: 214.96  E-value: 6.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETK-PVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFlkniDDWVKPTH 85
Cdd:cd07144    51 VKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYY----AGWADKIQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  86 vEKTFTTALDK-PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVT 163
Cdd:cd07144   127 -GKTIPTSPNKlAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVN 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 164 VVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQ 241
Cdd:cd07144   206 IIPGYGAVAGSALAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQ 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 242 TCLAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKD--YARMINQRHFDRISGLLD--KTQGAVLI-GGERDRADL- 315
Cdd:cd07144   286 NCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDtvVGPQVSKTQYDRVLSYIEkgKKEGAKLVyGGEKAPEGLg 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 316 ---YIPPTV-LDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDV 391
Cdd:cd07144   366 kgyFIPPTIfTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS 445
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1734334313 392 LM-HITVdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07144   446 NDsDVGV---PFGGFKMSGIGRELGEYGLETYTQTKAV 480
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
7-428 2.90e-63

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: 212.58  E-value: 2.90e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTG--ETKPVKFRKQQLLKLKKFIEENREALseAVWkdlrrrhestEILEIGMTIQ----EIDYflkNIDDW 80
Cdd:cd07118    25 VAAARKAFDKGpwPRMSGAERAAVLLKVADLIRARRERL--ALI----------ETLESGKPISqargEIEG---AADLW 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  81 ------VKPTHVEkTFTTALDK--PVIEKDPKGVVLIISPWNYPVsMILLPMVP-AIAAGNTVVIKPSELSEnvAATF-- 149
Cdd:cd07118    90 ryaaslARTLHGD-SYNNLGDDmlGLVLREPIGVVGIITPWNFPF-LILSQKLPfALAAGCTVVVKPSEFTS--GTTLml 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 150 -EKLIPKYFESKYVTVVNG-----GIPETTDllkERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDAD 223
Cdd:cd07118   166 aELLIEAGLPAGVVNIVTGygatvGQAMTEH---PDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 224 IDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAI----RKYVnefYGEDVKASKDYARMINQRHFDRISGLLD- 298
Cdd:cd07118   243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVvarsRKVR---VGDPLDPETKVGAIINEAQLAKITDYVDa 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 299 -KTQGA-VLIGGERD--RADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAK 373
Cdd:cd07118   320 gRAEGAtLLLGGERLasAAGLFYQPTIFtDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734334313 374 VKRLLNETSSGGVTVNDVLmhitvDT---LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07118   400 ALTVARRIRAGTVWVNTFL-----DGspeLPFGGFKQSGIGRELGRYGVEEYTELKTV 452
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
17-428 1.03e-62

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: 211.03  E-value: 1.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  17 GETKPVKfRKQQLLKLKKFIEENREALSEAVwkdlrrrhesteILEIGMTIQEIDY-------FLKNIDDWVK------- 82
Cdd:cd07150    38 AATTPSE-RERILLKAAEIMERRADDLIDLL------------IDEGGSTYGKAWFettftpeLLRAAAGECRrvrgetl 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  83 PTHVEKTFTTALdkpvieKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyf 157
Cdd:cd07150   105 PSDSPGTVSMSV------RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEImeeagLPK-- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 158 esKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGK 235
Cdd:cd07150   177 --GVFNVVTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 236 WLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLIGGERdR 312
Cdd:cd07150   255 FMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVEDavAKGAKLLTGGK-Y 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 313 ADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDV 391
Cdd:cd07150   334 DGNFYQPTVLtDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDP 413
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1734334313 392 LMH--ITVdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07150   414 TILdeAHV---PFGGVKASGFGREGGEWSMEEFTELKWI 449
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
5-428 2.05e-62

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: 210.18  E-value: 2.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAV-WKDLRRRHESTEilEIGMTIQEIDYFLKNIDDWVKP 83
Cdd:cd07102    22 AALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELtWQMGRPIAQAGG--EIRGMLERARYMISIAEEALAD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  84 THVEKTfttALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELS----ENVAATF-EKLIPKyfe 158
Cdd:cd07102   100 IRVPEK---DGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAAAFaEAGLPE--- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 159 sKYVTVVNGGIPETTDLLKE-RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWL 237
Cdd:cd07102   174 -GVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFF 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 238 NCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRA 313
Cdd:cd07102   253 NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGArALIDGALFPE 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 314 DL----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTV 388
Cdd:cd07102   333 DKaggaYLAPTVLtNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFM 412
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1734334313 389 N--DVlmhitVD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07102   413 NrcDY-----LDpALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
7-428 2.18e-62

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: 210.37  E-value: 2.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYF---LKNIDDWVKP 83
Cdd:cd07115    25 VAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPRAADTFRYYagwADKIEGEVIP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  84 thVEKTFTTALdkpviEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYV 162
Cdd:cd07115   105 --VRGPFLNYT-----VREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 163 TVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07115   178 NVVTGFGEVAGAALVEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQG 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 241 QTCLAPDYILVNSTVKPK----LVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRA 313
Cdd:cd07115   258 QMCTAGSRLLVHESIYDEflerFTSLARSLR---PGDPLDPKTQMGPLVSQAQFDRVLDYVDvgREEGArLLTGGKRPGA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 314 D-LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIADG-EKPLAAYIFTRNEAKVKRLLNETSSGGVTVNd 390
Cdd:cd07115   335 RgFFVEPTIFaAVPPEMRIAQEEIFGPVVSVMRFRDEEEALR-IANGtEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN- 412
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1734334313 391 vlMHITVDT-LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07115   413 --TYNRFDPgSPFGGYKQSGFGREMGREALDEYTEVKSV 449
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
7-428 1.05e-61

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: 208.61  E-value: 1.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTG---ETKPVKfRKQQLLKLKKFIEENREALseAVWKDLRRRHESTEIL--EIGMTIQEIDYFLKNID--- 78
Cdd:cd07112    30 VAAARRAFESGvwsRLSPAE-RKAVLLRLADLIEAHRDEL--ALLETLDMGKPISDALavDVPSAANTFRWYAEAIDkvy 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  79 DWVKPTHVEktfTTALdkpvIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----I 153
Cdd:cd07112   107 GEVAPTGPD---ALAL----ITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 154 PKyfesKYVTVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDA-DIDISAK 229
Cdd:cd07112   180 PA----GVLNVVPGFGHTAGEALGLHmdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 230 RIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VL 305
Cdd:cd07112   256 AAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIEsgKAEGArLV 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 306 IGGERDRAD---LYIPPTVLD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:cd07112   336 AGGKRVLTEtggFFVEPTVFDgVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRL 415
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1734334313 382 SSGGVTVNdvlmhiTVD----TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07112   416 RAGTVWVN------CFDegdiTTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
25-428 1.16e-61

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: 208.15  E-value: 1.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYFLKNIddwVKPTHVEKTFTTaldKPVIEKDPK 104
Cdd:cd07106    43 RRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGGAVAWLRYTASLD---LPDEVIEDDDTR---RVELRRKPL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGiPETTDLLKE--RFDH 182
Cdd:cd07106   116 GVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGG-DELGPALTShpDIRK 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 183 ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAA 262
Cdd:cd07106   195 ISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEA 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 263 IRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADLYIPPTVL-DVEKSDPFMHDEIF 336
Cdd:cd07106   275 LVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdaKAKGAkVLAGGEPlDGPGYFIPPTIVdDPPEGSRIVDEEQF 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 337 GPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN---DVLMHItvdtlPFGGVGVSGMGRY 413
Cdd:cd07106   355 GPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINthgALDPDA-----PFGGHKQSGIGVE 429
                         410
                  ....*....|....*
gi 1734334313 414 RGKYGFDTFTHEKSV 428
Cdd:cd07106   430 FGIEGLKEYTQTQVI 444
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
70-428 1.32e-61

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 209.16  E-value: 1.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  70 IDYFL---KNIDDWVKPTHVEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVA 146
Cdd:PLN02278  130 LEYFAeeaKRVYGDIIPSPFPDRRLLVLKQPV------GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTA 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 147 ATFEKL-----IPkyfeSKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVE 219
Cdd:PLN02278  204 LAAAELalqagIP----PGVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVF 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 220 DDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD 298
Cdd:PLN02278  280 DDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVQ 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 299 K--TQGA-VLIGGERDRADL-YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAK 373
Cdd:PLN02278  360 DavSKGAkVLLGGKRHSLGGtFYEPTVLgDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQR 439
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1734334313 374 VKRLLNETSSGGVTVNDVLmhITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PLN02278  440 AWRVSEALEYGIVGVNEGL--ISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
99-431 1.38e-61

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 208.61  E-value: 1.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPETTDLL-- 176
Cdd:PRK13473  134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALvg 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK 256
Cdd:PRK13473  214 HPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 257 PKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKTQGA----VLIGGER-DRADLYIPPTVL-DVEKSDP 329
Cdd:PRK13473  294 DDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVERAKALghirVVTGGEApDGKGYYYEPTLLaGARQDDE 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 330 FMHDEIFGPVLpiiTVQSFS---ESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmHIT-VDTLPFGGV 405
Cdd:PRK13473  374 IVQREVFGPVV---SVTPFDdedQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMlVSEMPHGGQ 447
                         330       340
                  ....*....|....*....|....*.
gi 1734334313 406 GVSGMGRYRGKYGFDTFTHEKSVLHR 431
Cdd:PRK13473  448 KQSGYGKDMSLYGLEDYTVVRHVMVK 473
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
14-428 1.25e-59

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: 202.30  E-value: 1.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  14 FRTGETKPVKFRKQQLLKLKKFIEENREALSEAVwkdlrrrhesteILEIGMTI----QEI-------DYFLKNIDDWVK 82
Cdd:cd07100    12 FLAWRKTSFAERAALLRKLADLLRERKDELARLI------------TLEMGKPIaearAEVekcawicRYYAENAEAFLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  83 PTHVEktftTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPK--YFESK 160
Cdd:cd07100    80 DEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREagFPEGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 161 YVTVVNGGiPETTDLLK-ERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNC 239
Cdd:cd07100   156 FQNLLIDS-DQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 240 GQTCLAPDYILVNSTV----KPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGER-D 311
Cdd:cd07100   235 GQSCIAAKRFIVHEDVydefLEKFVEAMAALK---VGDPMDEDTDLGPLARKDLRDELHEQVEEAvaAGAtLLLGGKRpD 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 312 RADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:cd07100   312 GPGAFYPPTVLtDVTPGMPAYDEELFGPVAAVIKVKDEEEAIA-LAnDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1734334313 390 DvlmHITVDT-LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07100   391 G---MVKSDPrLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
7-428 4.28e-59

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: 202.19  E-value: 4.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRrhestEILEIGMTIQEIdyflknID--DWVKPT 84
Cdd:cd07131    43 VEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGK-----PLAEGRGDVQEA------IDmaQYAAGE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 hVEKTFTTALDKPVIEKD------PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATF-EKLIPKYF 157
Cdd:cd07131   112 -GRRLFGETVPSELPNKDamtrrqPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLvELFAEAGL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 158 ESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGK 235
Cdd:cd07131   191 PPGVVNVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSA 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 236 WLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER- 310
Cdd:cd07131   271 FGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNEigKEEGAtLLLGGERl 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 311 DRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGG 385
Cdd:cd07131   351 TGGGYekgyFVEPTVFtDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGI 430
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1734334313 386 VTVNDVLMHITVDtLPFGGVGVSGMG-RYRGKYGFDTFTHEKSV 428
Cdd:cd07131   431 TYVNAPTIGAEVH-LPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
21-428 9.53e-59

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: 200.55  E-value: 9.53e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  21 PVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHV-EKTFTTALDKPVI 99
Cdd:cd07089    40 DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEFDLpVPALRGGPGRRVV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 100 EKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPS--------ELSENVAATFeklIPKyfesKYVTVVNGGIPE 171
Cdd:cd07089   120 RREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPApdtplsalLLGEIIAETD---LPA----GVVNVVTGSDNA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 172 TTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYI 249
Cdd:cd07089   193 VGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRL 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 250 LVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRAD--LYIPPTVL 322
Cdd:cd07089   273 LVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIArgRDEGArLVTGGGRpAGLDkgFYVEPTLF 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 323 -DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTl 400
Cdd:cd07089   353 aDVDNDMRIAQEEIFGPVLVVIPYDDDDEAVR-IAnDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGG-GGYGPDA- 429
                         410       420
                  ....*....|....*....|....*...
gi 1734334313 401 PFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07089   430 PFGGYKQSGLGRENGIEGLEEFLETKSI 457
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
25-430 1.46e-58

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: 200.22  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEAvwkdLRRRHESTEI---LEIGMT---IQEIDYFLKNIDDWVKPTHVEktfttalDKP- 97
Cdd:cd07151    56 RAEILEKAAQILEERRDEIVEW----LIRESGSTRIkanIEWGAAmaiTREAATFPLRMEGRILPSDVP-------GKEn 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  98 VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSElseNVAATFEKLIPKYFESK-----YVTVVNGGIPET 172
Cdd:cd07151   125 RVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPAS---DTPITGGLLLAKIFEEAglpkgVLNVVVGAGSEI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 173 TDLLKE----RFdhILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDY 248
Cdd:cd07151   202 GDAFVEhpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 249 ILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDraDLYIPPTVL-D 323
Cdd:cd07151   280 IIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEQAveEGAtLLVGGEAE--GNVLEPTVLsD 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmhITVD---TL 400
Cdd:cd07151   358 VTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIND----QPVNdepHV 433
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1734334313 401 PFGGVGVSGMGRYRGKYGFDTFTHEK--SVLH 430
Cdd:cd07151   434 PFGGEKNSGLGRFNGEWALEEFTTDKwiSVQH 465
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
11-430 1.16e-57

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: 198.30  E-value: 1.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  11 RKYFRTGE--TKPVKFRKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQEIDYflkNIDDWVkptHVEK 88
Cdd:cd07119    45 RRAFDSGEwpHLPAQERAALLFRIADKIREDAEELAR------------LETLNTGKTLRESEI---DIDDVA---NCFR 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  89 TFTTALDKP-------------VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPK 155
Cdd:cd07119   107 YYAGLATKEtgevydvpphvisRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 156 Y-FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIA 232
Cdd:cd07119   187 AgLPAGVVNLVTGSGATVGAELAEspDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQAL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 233 WGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI-GG 308
Cdd:cd07119   267 NGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIQlgKEEGARLVcGG 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 309 ER-DRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETS 382
Cdd:cd07119   347 KRpTGDELakgyFVEPTIFdDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLR 426
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1734334313 383 SGGVTVNDvlMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07119   427 AGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
2-430 1.36e-57

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: 197.53  E-value: 1.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   2 AFTELVETQRKYFRTgetkPVKFRKQQLLKLKKFIEENREALSeavwkDL-------RRRHESTEILEIGMTIQeidYFL 74
Cdd:cd07101    23 AFARARAAQRAWAAR----PFAERAAVFLRFHDLVLERRDELL-----DLiqletgkARRHAFEEVLDVAIVAR---YYA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  75 KNIDDWVKPTHVEKTFTTaLDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVA-ATFEKLI 153
Cdd:cd07101    91 RRAERLLKPRRRRGAIPV-LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAlWAVELLI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 154 PKYFESKYVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:cd07101   170 EAGLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVR 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 234 GKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGER 310
Cdd:cd07101   250 ACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdaVAKGATVLAGGR 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 311 DRADL---YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGV 386
Cdd:cd07101   330 ARPDLgpyFYEPTVLtGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTV 409
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1734334313 387 TVND--VLMHITVDTlPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07101   410 NVNEgyAAAWASIDA-PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
103-424 2.24e-57

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: 196.75  E-value: 2.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSenvAATFEKLIPKYFE-----SKYVTVVNGGiPETTDLLK 177
Cdd:cd07152   110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT---PVSGGVVIARLFEeaglpAGVLHVLPGG-ADAGEALV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 178 E--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV 255
Cdd:cd07152   186 EdpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 256 KPKLVAA-IRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGA---VLIGGERDraDLYIPPTVL-DVEKSDPF 330
Cdd:cd07152   266 ADAYTAKlAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAgarLEAGGTYD--GLFYRPTVLsGVKPGMPA 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 331 MHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlmhiTVD---TLPFGGVGV 407
Cdd:cd07152   344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNdepHNPFGGMGA 419
                         330
                  ....*....|....*...
gi 1734334313 408 SGMG-RYRGKYGFDTFTH 424
Cdd:cd07152   420 SGNGsRFGGPANWEEFTQ 437
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
38-430 5.48e-57

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: 196.18  E-value: 5.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  38 ENREALSEAVWKDLRRRHE---STEILEIG------------MTIQEIDYFLKNIDDWvkpthvekTFTTALDKPVIEKD 102
Cdd:cd07138    58 EERAALLERIAEAYEARADelaQAITLEMGapitlaraaqvgLGIGHLRAAADALKDF--------EFEERRGNSLVVRE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PK-YFeskyvTVVNGGIPETTDLL 176
Cdd:cd07138   130 PIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILdeaglPAgVF-----NLVNGDGPVVGEAL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 KE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNST 254
Cdd:cd07138   205 SAhpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRS 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 255 VKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLIGGERDRAD-----LYIPPTVL-DVe 325
Cdd:cd07138   285 RYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKgiEEGARLVAGGPGRPEglergYFVKPTVFaDV- 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 326 ksDPFM---HDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHItvdTLP 401
Cdd:cd07138   364 --TPDMtiaREEIFGPVLSIIPYDDEDEAIA-IAnDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAP 437
                         410       420
                  ....*....|....*....|....*....
gi 1734334313 402 FGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07138   438 FGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
7-428 1.08e-56

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: 195.83  E-value: 1.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTgeTKPVKF----RKQQLLKLKKFIEENREALSeavwkdlrrrheSTEILEIGMTIQEIDYF--------L 74
Cdd:cd07143    50 VEVAHAAFET--DWGLKVsgskRGRCLSKLADLMERNLDYLA------------SIEALDNGKTFGTAKRVdvqasadtF 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  75 KNIDDWVKPTH------VEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAAT 148
Cdd:cd07143   116 RYYGGWADKIHgqvietDIKKLTYTRHEPI------GVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALY 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 149 FEKLIPKY-FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADI 224
Cdd:cd07143   190 MTKLIPEAgFPPGVINVVSGYGRTCGNAISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADL 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 225 DISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQ 301
Cdd:cd07143   270 ESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLkVGDPFAEDTFQGPQVSQIQYERIMSYIEsgKAE 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 302 GA-VLIGGERDRADLY-IPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLL 378
Cdd:cd07143   350 GAtVETGGKRHGNEGYfIEPTIFtDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVA 429
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1734334313 379 NETSSGGVTVNDV-LMHITVdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07143   430 NALKAGTVWVNCYnLLHHQV---PFGGYKQSGIGRELGEYALENYTQIKAV 477
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
5-426 1.13e-54

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: 189.87  E-value: 1.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYF---LKNIDDWV 81
Cdd:cd07145    25 EAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV-EVERTIRLFKLAaeeAKVLRGET 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  82 KPthVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESK 160
Cdd:cd07145   104 IP--VDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 161 YVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLN 238
Cdd:cd07145   182 VINVVTGYGSEVGDEIvtNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFEN 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 239 CGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGA-VLIGGERDRAD 314
Cdd:cd07145   262 AGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVNDavEKGGkILYGGKRDEGS 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 315 lYIPPTVLDVEKSD-PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlM 393
Cdd:cd07145   342 -FFPPTVLENDTPDmIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-T 419
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1734334313 394 HITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEK 426
Cdd:cd07145   420 RFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
101-428 5.40e-54

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: 187.80  E-value: 5.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATF-EKLIPKYFESKYVTVVNGGIPETTDLLKE- 178
Cdd:cd07149   121 REPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLaELLLEAGLPKGALNVVTGSGETVGDALVTd 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 179 -RFDHILYTGCPPVAKIIMTAAAkhLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK- 256
Cdd:cd07149   201 pRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYd 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 257 ---PKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAdlYIPPTVL-DVEKSDP 329
Cdd:cd07149   279 eflERFVAATKKLV---VGDPLDEDTDVGPMISEAEAERIEEWVEeaVEGGArLLTGGKRDGA--ILEPTVLtDVPPDMK 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 330 FMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTLPFGGVGVSG 409
Cdd:cd07149   354 VVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS-STFRVDHMPYGGVKESG 432
                         330
                  ....*....|....*....
gi 1734334313 410 MGRYRGKYGFDTFTHEKSV 428
Cdd:cd07149   433 TGREGPRYAIEEMTEIKLV 451
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
5-428 9.98e-54

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: 187.26  E-value: 9.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAV-------WKDLRRrhestEILEIGMTIQEIDYFLKNI 77
Cdd:cd07094    25 EALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIaceggkpIKDARV-----EVDRAIDTLRLAAEEAERI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  78 DDWVKPTHVEKTFTTALdkPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-PKY 156
Cdd:cd07094   100 RGEEIPLDATQGSDNRL--AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 157 FESKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKhlTPVTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:cd07094   178 VPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKG 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 235 KWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGER 310
Cdd:cd07094   256 GFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVEEavEAGARLLcGGER 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 311 DRADLYipPTVLDVEKSDPFM-HDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:cd07094   336 DGALFK--PTVLEDVPRDTKLsTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVN 413
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1734334313 390 DVlMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07094   414 DS-SAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
29-389 1.05e-53

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 186.10  E-value: 1.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  29 LLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYflknIDDWVKPTHVEktfTTALDKP----VIEKDPK 104
Cdd:PRK10090    1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDY----MAEWARRYEGE---IIQSDRPgeniLLFKRAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYV-TVVNGGIPETTDLL--KERFD 181
Cdd:PRK10090   73 GVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVfNLVLGRGETVGQELagNPKVA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 182 HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVA 261
Cdd:PRK10090  153 MVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 262 AIRKYVNEF-YGEDVKASK-DYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRAD-LYIPPTVL-DVEKSDPFMHDE 334
Cdd:PRK10090  233 RLGEAMQAVqFGNPAERNDiAMGPLINAAALERVEQKVARAveEGArVALGGKAVEGKgYYYPPTLLlDVRQEMSIMHEE 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1734334313 335 IFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:PRK10090  313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
40-429 1.63e-53

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: 187.01  E-value: 1.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  40 REALSEAVWKDL-----------------RRRHESTEI--LEIGMTI------------QEIDYFLKNIDDWVKPTHVEk 88
Cdd:cd07139    46 RRAFDNGPWPRLspaeraavlrrladaleARADELARLwtAENGMPIswsrraqgpgpaALLRYYAALARDFPFEERRP- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  89 tfTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE--------LSENVAatfEKLIPKyfesK 160
Cdd:cd07139   125 --GSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPetpldaylLAEAAE---EAGLPP----G 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 161 YVTVVNGGIpETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLN 238
Cdd:cd07139   196 VVNVVPADR-EVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMN 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 239 CGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGERdRAD 314
Cdd:cd07139   275 NGQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIAKgrAEGARLVtGGGR-PAG 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 315 L----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTV 388
Cdd:cd07139   354 LdrgwFVEPTLFaDVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR-IAnDSDYGLSGSVWTADVERGLAVARRIRTGTVGV 432
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1734334313 389 NdvlmHITVD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07139   433 N----GFRLDfGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
99-428 1.67e-53

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: 186.68  E-value: 1.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATF-EKLIPKYFESKYVTVVNGGIPETTDLLK 177
Cdd:cd07147   119 VRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILgEVLAETGLPKGAFSVLPCSRDDADLLVT 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 178 -ERFDHILYTGCPPVAKIIMTAAAKHltPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV- 255
Cdd:cd07147   199 dERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVy 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 256 ---KPKLVAAIRKYVNefyGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRADLYipPTVL-DVEKSD 328
Cdd:cd07147   277 defKSRLVARVKALKT---GDPKDDATDVGPMISESEAERVEGWVNEAvdAGAkLLTGGKRDGALLE--PTILeDVPPDM 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 329 PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTLPFGGVGVS 408
Cdd:cd07147   352 EVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV-PTFRVDHMPYGGVKDS 430
                         330       340
                  ....*....|....*....|
gi 1734334313 409 GMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07147   431 GIGREGVRYAIEEMTEPRLL 450
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
101-428 1.83e-53

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: 187.07  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKyfeskyvtvvnGGIPE--------- 171
Cdd:cd07097   133 REPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEE-----------AGLPAgvfnlvmgs 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 172 --------TTDllkERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTC 243
Cdd:cd07097   202 gsevgqalVEH---PDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRC 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 244 LAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI-GGER-DRAD--LY 316
Cdd:cd07097   279 TASSRLIVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIEiaRSEGAKLVyGGERlKRPDegYY 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 317 IPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN----DV 391
Cdd:cd07097   359 LAPALFaGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptaGV 438
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1734334313 392 LMHitvdtLPFGGVGVSGMG-RYRGKYGFDTFTHEKSV 428
Cdd:cd07097   439 DYH-----VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
7-431 1.45e-52

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: 184.57  E-value: 1.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRT--GETKPVKfRKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQ-----EIDY---FLKN 76
Cdd:cd07113    43 VASAWRAFVSawAKTTPAE-RGRILLRLADLIEQHGEELAQ------------LETLCSGKSIHlsrafEVGQsanFLRY 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  77 IDDWVkpTHVE-KTFTTALDKPVIE-------KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----N 144
Cdd:cd07113   110 FAGWA--TKINgETLAPSIPSMQGErytaftrREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPltllR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 145 VA--ATfEKLIPkyfeSKYVTVVNGgipeTTDLLKERFDH-----ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVV 217
Cdd:cd07113   188 VAelAK-EAGIP----DGVLNVVNG----KGAVGAQLISHpdvakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 218 VEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGL 296
Cdd:cd07113   259 FLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSY 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 297 LDKTQGA---VLIGGER-DRADLYIPPT-VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNE 371
Cdd:cd07113   339 LDDARAEgdeIVRGGEAlAGEGYFVQPTlVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNL 418
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734334313 372 AKVKRLLNETSSGGVTVNdvlMHITVD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLHR 431
Cdd:cd07113   419 SKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
7-429 2.34e-52

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: 184.08  E-value: 2.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRT-GETKPVKfRKQQLLKLKKFIEENREALSEA-VW---KDLRrrhESTEIlEIGMTIQEIDYF-------- 73
Cdd:cd07559    44 VDAAHEAFKTwGKTSVAE-RANILNKIADRIEENLELLAVAeTLdngKPIR---ETLAA-DIPLAIDHFRYFagviraqe 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  74 --LKNIDdwvkpthvEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----NVAA 147
Cdd:cd07559   119 gsLSEID--------EDTLSYHFHEPL------GVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPlsilVLME 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 148 TFEKLIPKyfesKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDA--- 222
Cdd:cd07559   185 LIGDLLPK----GVVNVVTGFGSEAGKPLAShpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAmda 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 223 --DIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVA-AIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD- 298
Cdd:cd07559   261 ddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIErAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDi 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 299 -KTQGA-VLIGGER------DRADLYIPPTVLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRN 370
Cdd:cd07559   341 gKEEGAeVLTGGERltlgglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRD 420
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734334313 371 EAKVKRLLNETSSGGVTVNdvLMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07559   421 INRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
9-428 2.69e-52

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: 183.31  E-value: 2.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   9 TQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVwkdlrrRHESTEIL-----EIGMTIQEIDYFLKNIddwvkp 83
Cdd:cd07120    28 ARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLL------ALENGKILgearfEISGAISELRYYAGLA------ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  84 thvEKTFTTALD-KP----VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIP--KY 156
Cdd:cd07120    96 ---RTEAGRMIEpEPgsfsLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAeiPS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 157 FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:cd07120   173 LPAGVVNLFTESGSEGAAHLVAspDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERA 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 235 KWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVnefygEDVK------ASKDYARMINQRHFDRISGLLDK--TQGA--V 304
Cdd:cd07120   253 LTIFAGQFCMAGSRVLVQRSIADEVRDRLAARL-----AAVKvgpgldPASDMGPLIDRANVDRVDRMVERaiAAGAevV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 305 LIGG---ERDRADLYIPPTVLDVEKSD-PFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKVKRL 377
Cdd:cd07120   328 LRGGpvtEGLAKGAFLRPTLLEVDDPDaDIVQEEIFGPVL---TLETFDDEAEAVAlanDTDYGLAASVWTRDLARAMRV 404
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1734334313 378 LNETSSGGVTVNDvlmHITV-DTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07120   405 ARAIRAGTVWIND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
7-429 4.55e-52

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: 182.94  E-value: 4.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDL-RRRHESTeiLEIGMTIQEIDYFLKNIDDWvkPTH 85
Cdd:cd07110    25 VRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNgKPLDEAA--WDVDDVAGCFEYYADLAEQL--DAK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  86 VEKTFTTALD--KPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LSENVAATF--EKLIPKyfe 158
Cdd:cd07110   101 AERAVPLPSEdfKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEltsLTELELAEIaaEAGLPP--- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 159 sKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKW 236
Cdd:cd07110   178 -GVLNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCF 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 237 LNCGQTCLAPDYILVNSTVK----PKLVAAIRKY-VNEFYGEDVkaskDYARMINQRHFDRISGLLD--KTQGAVLIGGE 309
Cdd:cd07110   257 WNNGQICSATSRLLVHESIAdaflERLATAAEAIrVGDPLEEGV----RLGPLVSQAQYEKVLSFIArgKEEGARLLCGG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 310 RDRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:cd07110   333 RRPAHLekgyFIAPTVFaDVPTDSRIWREEIFGPVL---CVRSFATEDEAIAlanDSEYGLAAAVISRDAERCDRVAEAL 409
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1734334313 382 SSGGVTVNDVlmHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07110   410 EAGIVWINCS--QPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
101-429 5.33e-52

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: 182.56  E-value: 5.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----NVAATFEKLIPkyfeSKYVTVVNGGIPETTDLL 176
Cdd:cd07108   115 REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPlavlLLAEILAQVLP----AGVLNVITGYGEECGAAL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 KER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKR-IAWGKWLNCGQTCLAPDYILVNS 253
Cdd:cd07108   191 VDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAGMRFTRQGQSCTAGSRLFVHE 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 254 TVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD---KTQGA-VLIGGE-----RDRADLYIPPTVL- 322
Cdd:cd07108   271 DIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglSTSGAtVLRGGPlpgegPLADGFFVQPTIFs 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 323 DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLPF 402
Cdd:cd07108   351 GVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ--GGGQQPGQSY 428
                         330       340
                  ....*....|....*....|....*...
gi 1734334313 403 GGVGVSGMGRYRGKYG-FDTFTHEKSVL 429
Cdd:cd07108   429 GGFKQSGLGREASLEGmLEHFTQKKTVN 456
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
2-428 6.60e-52

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 183.93  E-value: 6.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   2 AFTELVETQRKYFRTgetkPVKFRKQQLLKLKKFIEENREALSeavwkDL-------RRRHESTEILEIGMTIqeiDYFL 74
Cdd:PRK09407   59 AFARARAAQRAWAAT----PVRERAAVLLRFHDLVLENREELL-----DLvqletgkARRHAFEEVLDVALTA---RYYA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  75 KNIDDWVKPTHVEKTFTTaLDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKP-SELSENVAATFEKLI 153
Cdd:PRK09407  127 RRAPKLLAPRRRAGALPV-LTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPdSQTPLTALAAVELLY 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 154 PKYFESKYVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:PRK09407  206 EAGLPRDLWQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVR 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 234 GKWLNCGQTCLAPDYILVNSTVKPKLVaaiRKYVNEFYGEDVKASKDY-ARM---INQRHFDRISGLLD--KTQGA-VLI 306
Cdd:PRK09407  286 ACFSNAGQLCISIERIYVHESIYDEFV---RAFVAAVRAMRLGAGYDYsADMgslISEAQLETVSAHVDdaVAKGAtVLA 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 307 GGeRDRADL---YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETS 382
Cdd:PRK09407  363 GG-KARPDLgplFYEPTVLtGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIR 441
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1734334313 383 SGGVTVND--VLMHITVDTlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PRK09407  442 AGTVNVNEgyAAAWGSVDA-PMGGMKDSGLGRRHGAEGLLKYTESQTI 488
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
96-428 2.48e-51

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: 180.63  E-value: 2.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  96 KPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyFES----KYVTVVNGGIPE 171
Cdd:cd07146   113 KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLL---YEAglppDMLSVVTGEPGE 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 172 TTDLL--KERFDHILYTGCPPVAKIIM-TAAAKHLTpvtLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDY 248
Cdd:cd07146   190 IGDELitHPDVDLVTFTGGVAVGKAIAaTAGYKRQL---LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 249 ILVNSTV----KPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRADLYipPTV 321
Cdd:cd07146   267 ILVHESVadefVDLLVEKSAALV---VGDPMDPATDMGTVIDEEAAIQIENRVEEAiaQGArVLLGNQRQGALYA--PTV 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 322 LD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTL 400
Cdd:cd07146   342 LDhVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELS 420
                         330       340
                  ....*....|....*....|....*....
gi 1734334313 401 PFGGVGVSGMGRYRG-KYGFDTFTHEKSV 428
Cdd:cd07146   421 PFGGVKDSGLGGKEGvREAMKEMTNVKTY 449
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
101-428 1.03e-50

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: 179.85  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVTVVNGGIPETTDLLKER 179
Cdd:cd07141   143 HEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSH 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 180 --FDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK 256
Cdd:cd07141   223 pdIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIY 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 257 PKLV------AAIRKYVNEFygedvKASKDYARMINQRHFDRISGLLD--KTQGAVL-IGGER--DRAdLYIPPTVL-DV 324
Cdd:cd07141   303 DEFVkrsverAKKRVVGNPF-----DPKTEQGPQIDEEQFKKILELIEsgKKEGAKLeCGGKRhgDKG-YFIQPTVFsDV 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 325 EKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdVLMHITVDTlPFGG 404
Cdd:cd07141   377 TDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN-CYNVVSPQA-PFGG 454
                         330       340
                  ....*....|....*....|....
gi 1734334313 405 VGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07141   455 YKMSGNGRELGEYGLQEYTEVKTV 478
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
7-429 4.07e-50

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: 178.03  E-value: 4.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIddwvkptHV 86
Cdd:cd07117    44 VKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVI-------RA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  87 EKTFTTALDK---PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----NVAATFEKLIPKyfes 159
Cdd:cd07117   117 EEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSlsllELAKIIQDVLPK---- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 160 KYVTVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWL 237
Cdd:cd07117   193 GVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILF 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 238 NCGQTCLAPDYILVNSTVKPKLVAA-IRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER--- 310
Cdd:cd07117   273 NQGQVCCAGSRIFVQEGIYDEFVAKlKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDiaKEEGAkILTGGHRlte 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 311 DRAD--LYIPPTVLDVEKSD-PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVT 387
Cdd:cd07117   353 NGLDkgFFIEPTLIVNVTNDmRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVW 432
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1734334313 388 VNdvLMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07117   433 VN--TYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIY 472
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
7-429 4.38e-50

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: 178.07  E-value: 4.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGE--TKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLknidDWVKPT 84
Cdd:cd07142    47 VKAARKAFDEGPwpRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYYA----GWADKI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 HVEktfTTALDKPVIE---KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESK 160
Cdd:cd07142   123 HGM---TLPADGPHHVytlHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDG 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 161 YVTVVNGGIPETTDLLKERF--DHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWL 237
Cdd:cd07142   200 VLNIVTGFGPTAGAAIASHMdvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFF 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 238 NCGQTCLAPDYILVNSTVKPKLV-AAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI-GGER-DR 312
Cdd:cd07142   280 NQGQCCCAGSRTFVHESIYDEFVeKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEhgKEEGATLItGGDRiGS 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 313 ADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN-- 389
Cdd:cd07142   360 KGYYIQPTIFsDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcy 439
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1734334313 390 DVLmhitVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07142   440 DVF----DASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
25-426 1.42e-48

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 173.84  E-value: 1.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQEIDYflKNIDDWVKPTHVEKTFTTALDKPVIE---- 100
Cdd:TIGR01804  59 RGRILRRAADLIRERNEELAK------------LETLDTGKTLQETIV--ADMDSGADVFEFFAGLAPALNGEIIPlggp 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 ------KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVA-ATFEKLIPKYFESKYVTVVNGGIPETT 173
Cdd:TIGR01804 125 sfaytiREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTAlKVAEIMEEAGLPKGVFNVVQGDGAEVG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 174 DLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILV 251
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 252 NSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD-----LYIPPTVL 322
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEkgKAEGAtLATGGGRPENVglqngFFVEPTVF 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 323 -DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLP 401
Cdd:TIGR01804 365 aDCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEAP 442
                         410       420
                  ....*....|....*....|....*
gi 1734334313 402 FGGVGVSGMGRYRGKYGFDTFTHEK 426
Cdd:TIGR01804 443 FGGYKQSGIGRENGKAALAHYTEVK 467
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
18-431 2.14e-48

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: 173.14  E-value: 2.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  18 ETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYF---LKNID-DWVKPTHVEKTFTTa 93
Cdd:cd07082    56 PTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALK-EVDRTIDYIRDTieeLKRLDgDSLPGDWFPGTKGK- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  94 ldKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPselsenvaATFEKLIP----KYFES-----KYVTV 164
Cdd:cd07082   134 --IAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP--------ATQGVLLGiplaEAFHDagfpkGVVNV 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 165 VNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKhlTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQT 242
Cdd:cd07082   204 VTGRGREIGDPLVThgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQR 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 243 CLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLYIPP 319
Cdd:cd07082   282 CTAIKRVLVHESVADELVELLKEEVAKLkVGMPWDNGVDITPLIDPKSADFVEGLIDdaVAKGATVLNGGGREGGNLIYP 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 320 TVLDVEKSDpfM---HDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHiT 396
Cdd:cd07082   362 TLLDPVTPD--MrlaWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQR-G 438
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1734334313 397 VDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLHR 431
Cdd:cd07082   439 PDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
PLN02467 PLN02467
betaine aldehyde dehydrogenase
99-428 6.15e-47

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 169.91  E-value: 6.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELS-----ENVAATFEKLIPkyfeSKYVTVVNGGIPETT 173
Cdd:PLN02467  147 VLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELAsvtclELADICREVGLP----PGVLNVVTGLGTEAG 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 174 DLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILV 251
Cdd:PLN02467  223 APLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLV 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 252 NSTVKPKLVAAIRKYVnefygEDVKASKDYAR------MINQRHFDRISGLLD--KTQGA-VLIGGERD---RADLYIPP 319
Cdd:PLN02467  303 HERIASEFLEKLVKWA-----KNIKISDPLEEgcrlgpVVSEGQYEKVLKFIStaKSEGAtILCGGKRPehlKKGFFIEP 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 320 TVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdvLMHITVD 398
Cdd:PLN02467  378 TIItDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFC 455
                         330       340       350
                  ....*....|....*....|....*....|
gi 1734334313 399 TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PLN02467  456 QAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
100-428 7.52e-47

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: 168.64  E-value: 7.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 100 EKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSenvAATFEKLIPKYFE----SKYVTVVNGGiPETTDL 175
Cdd:cd07090   113 RREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT---PLTALLLAEILTEaglpDGVFNVVQGG-GETGQL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 176 LKERFD--HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDiSAKRIA-WGKWLNCGQTCLAPDYILVN 252
Cdd:cd07090   189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLE-NAVNGAmMANFLSQGQVCSNGTRVFVQ 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 253 STVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRADL------YIPPTVL 322
Cdd:cd07090   268 RSIKDEFTERLVERTKKIrIGDPLDEDTQMGALISEEHLEKVLGYIEsaKQEGAkVLCGGERVVPEDglengfYVSPCVL 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 323 -DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLP 401
Cdd:cd07090   348 tDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVP 425
                         330       340
                  ....*....|....*....|....*..
gi 1734334313 402 FGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07090   426 FGGYKQSGFGRENGTAALEHYTQLKTV 452
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
25-429 2.87e-46

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 168.08  E-value: 2.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDwvkpTHVEKTFTTALDKPVIEKDPK 104
Cdd:PLN02766   84 RGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADK----IHGETLKMSRQLQGYTLKEPI 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LSENVAATFEKL--IPkyfeSKYVTVVNGGIPETTDLLKER 179
Cdd:PLN02766  160 GVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEqtpLSALFYAHLAKLagVP----DGVINVVTGFGPTAGAAIASH 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 180 FD--HILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVN---- 252
Cdd:PLN02766  236 MDvdKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQegiy 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 253 STVKPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRAD--LYIPPTVL-DVEKS 327
Cdd:PLN02766  316 DEFVKKLVEKAKDWV---VGDPFDPRARQGPQVDKQQFEKILSYIEhgKREGATLLTGGKPCGDkgYYIEPTIFtDVTED 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 328 DPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdvlMHITVDT-LPFGGVG 406
Cdd:PLN02766  393 MKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFDPdCPFGGYK 469
                         410       420
                  ....*....|....*....|...
gi 1734334313 407 VSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:PLN02766  470 MSGFGRDQGMDALDKYLQVKSVV 492
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
103-428 1.08e-45

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: 166.20  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK-----YVTVVNGGiPETTDLLK 177
Cdd:cd07086   133 PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNglppgVVNLVTGG-GDGGELLV 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 178 --ERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV 255
Cdd:cd07086   212 hdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESV 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 256 KPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRAD--LYIPPTVLDVEK-S 327
Cdd:cd07086   292 YDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEiaKSQGGtVLTGGKRiDGGEpgNYVEPTIVTGVTdD 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 328 DPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSS--GGVTVNdvlmhitVDT------ 399
Cdd:cd07086   372 ARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVN-------IPTsgaeig 444
                         330       340
                  ....*....|....*....|....*....
gi 1734334313 400 LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07086   445 GAFGGEKETGGGRESGSDAWKQYMRRSTC 473
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
100-428 1.25e-44

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: 162.93  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 100 EKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPETTDLLKER 179
Cdd:cd07107   113 LREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRH 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 180 FD--HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWG---KWlnCGQTCLAPDYILVNST 254
Cdd:cd07107   193 PDvkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGmnfTW--CGQSCGSTSRLFVHES 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 255 VKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI--GGERDRADL----YIPPTVL-DV 324
Cdd:cd07107   271 IYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIDsaKREGARLVtgGGRPEGPALeggfYVEPTVFaDV 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 325 EKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITvdTLPFGG 404
Cdd:cd07107   351 TPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGG 428
                         330       340
                  ....*....|....*....|....
gi 1734334313 405 VGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07107   429 VKNSGIGREECLEELLSYTQEKNV 452
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
25-429 2.61e-41

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 155.35  E-value: 2.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLknidDWVKPTHvekTFTTALDKP---VIEK 101
Cdd:PLN02466  121 RSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYA----GWADKIH---GLTVPADGPhhvQTLH 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 102 DPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LSENVAATF--EKLIPkyfeSKYVTVVNGGIPETTDLL 176
Cdd:PLN02466  194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEqtpLSALYAAKLlhEAGLP----PGVLNVVSGFGPTAGAAL 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 KERF--DHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNS 253
Cdd:PLN02466  270 ASHMdvDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHE 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 254 TVKPKLVA-----AIRKYVnefyGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGER-DRADLYIPPTVL-D 323
Cdd:PLN02466  350 RVYDEFVEkakarALKRVV----GDPFKKGVEQGPQIDSEQFEKILRYIKSgvESGATLEcGGDRfGSKGYYIQPTVFsN 425
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN--DVLmhitvD-TL 400
Cdd:PLN02466  426 VQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVF-----DaAI 500
                         410       420
                  ....*....|....*....|....*....
gi 1734334313 401 PFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:PLN02466  501 PFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
25-428 5.07e-41

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: 153.42  E-value: 5.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  25 RKQQLLKLKKFIEENREAL-------SEAVWKDLRRRHesteileIGMTIQEIDYFLKNID---------DWVKPTHVeK 88
Cdd:cd07140    69 RGRLMYRLADLMEEHQEELatiesldSGAVYTLALKTH-------VGMSIQTFRYFAGWCDkiqgktipiNQARPNRN-L 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  89 TFTtaldkpviEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfeskyvT 163
Cdd:cd07140   141 TLT--------KREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtvkagFPK-------G 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 164 VVNgGIPETTDLLKERF-DH-----ILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKW 236
Cdd:cd07140   206 VIN-ILPGSGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVF 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 237 LNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGER-D 311
Cdd:cd07140   285 FNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVEYCERgvKEGATLVyGGKQvD 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 312 RADLYIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSES-----LEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGG 385
Cdd:cd07140   365 RPGFFFEPTVFtDVEDHMFIAKEESFGPIM---IISKFDDGdvdgvLQRANDTEYGLASGVFTKDINKALYVSDKLEAGT 441
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1734334313 386 VTVN-----DVlmhitvdTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07140   442 VFVNtynktDV-------AAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
7-428 1.16e-40

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: 152.29  E-value: 1.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWK-----------DLRRRHESTEiLEIGMTIQEIDYFLK 75
Cdd:cd07085    44 VAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLehgktladargDVLRGLEVVE-FACSIPHLLKGEYLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  76 NIddwvkpthvektfTTALDKpVIEKDPKGVVLIISPWNYPVsMILLPMVP-AIAAGNTVVIKPSELSENVAATFEKLIP 154
Cdd:cd07085   123 NV-------------ARGIDT-YSYRQPLGVVAGITPFNFPA-MIPLWMFPmAIACGNTFVLKPSERVPGAAMRLAELLQ 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 155 kyfESKY----VTVVNGGIPETTDLLkerfDH-----ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADID 225
Cdd:cd07085   188 ---EAGLpdgvLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 226 ISAKRIAWGKWLNCGQTCLA-PDYILVNSTVK---PKLVAAIRKY-VNEFYGEDVkaskDYARMINQRHFDRISGLLDK- 299
Cdd:cd07085   261 QTANALVGAAFGAAGQRCMAlSVAVAVGDEADewiPKLVERAKKLkVGAGDDPGA----DMGPVISPAAKERIEGLIESg 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 300 -TQGA-VLIGGERDRADLY-----IPPTVLD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNE 371
Cdd:cd07085   337 vEEGAkLVLDGRGVKVPGYengnfVGPTILDnVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSG 416
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1734334313 372 AKVKRLLNETSSGGVTVN-----DVLMHitvdtlPFGGVGVS--GMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07085   417 AAARKFQREVDAGMVGINvpipvPLAFF------SFGGWKGSffGDLHFYGKDGVRFYTQTKTV 474
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
103-409 1.62e-40

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 152.40  E-value: 1.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSmILLPM-VPAIAAGNTVVIKPSELSENVAATF-----EKLIPKyfeskyvTVVN---GGIPETT 173
Cdd:PRK03137  171 PLGVGVVISPWNFPFA-IMAGMtLAAIVAGNTVLLKPASDTPVIAAKFvevleEAGLPA-------GVVNfvpGSGSEVG 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 174 DLL----KERFdhILYTGCPPVAKIIMTAAAK------HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTC 243
Cdd:PRK03137  243 DYLvdhpKTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 244 LAPDYILVNSTVKPKLVAAIRKYVNEFygeDVKASKDYARM---INQRHFDRISGLLD--KTQGAVLIGGERDRAD-LYI 317
Cdd:PRK03137  321 SACSRAIVHEDVYDEVLEKVVELTKEL---TVGNPEDNAYMgpvINQASFDKIMSYIEigKEEGRLVLGGEGDDSKgYFI 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 318 PPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHIT 396
Cdd:PRK03137  398 QPTIFaDVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAI 477
                         330
                  ....*....|...
gi 1734334313 397 VDTLPFGGVGVSG 409
Cdd:PRK03137  478 VGYHPFGGFNMSG 490
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
103-428 2.15e-40

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: 152.38  E-value: 2.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSmILLPM-VPAIAAGNTVVIKPSELSENVAATFEKLIpkyFESKY----VTVVNGGIPETTDLLK 177
Cdd:cd07124   166 PLGVGAVISPWNFPLA-ILAGMtTAALVTGNTVVLKPAEDTPVIAAKLVEIL---EEAGLppgvVNFLPGPGEEVGDYLV 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 178 E--RFDHILYTGCPPVAKIIMTAAAK------HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYI 249
Cdd:cd07124   242 EhpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRV 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 250 LVNSTVK----PKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADL---YIPPT 320
Cdd:cd07124   322 IVHESVYdeflERLVERTKALK---VGDPEDPEVYMGPVIDKGARDRIRRYIEigKSEGRLLLGGEVLELAAegyFVQPT 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 321 VL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdvlMHIT--- 396
Cdd:cd07124   399 IFaDVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN---RKITgal 475
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1734334313 397 VDTLPFGGVGVSGMGRYRGkyGFDT---FTHEKSV 428
Cdd:cd07124   476 VGRQPFGGFKMSGTGSKAG--GPDYllqFMQPKTV 508
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
7-428 4.76e-40

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 150.82  E-value: 4.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGE---TKPVKfRKQQLLKLKKFIEENREALSeavwkdlrrrhesteILEIGMTIQEIDYFLKniDDWVKP 83
Cdd:PRK09847   63 VSAARGVFERGDwslSSPAK-RKAVLNKLADLMEAHAEELA---------------LLETLDTGKPIRHSLR--DDIPGA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  84 THVEKTFTTALDK-------------PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFE 150
Cdd:PRK09847  125 ARAIRWYAEAIDKvygevattsshelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 151 KLIPKY-FESKYVTVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMT-AAAKHLTPVTLELGGKCP-VVVEDDADID 225
Cdd:PRK09847  205 GLAKEAgLPDGVLNVVTGFGHEAGQALSRHndIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSAnIVFADCPDLQ 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 226 ISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQG 302
Cdd:PRK09847  285 QAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegESKG 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 303 AVLIGGERDRADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:PRK09847  365 QLLLDGRNAGLAAAIGPTIFvDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRL 444
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734334313 382 SSGGVTV---NDVLMhitvdTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PRK09847  445 KAGSVFVnnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
17-429 3.19e-38

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: 145.67  E-value: 3.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  17 GETKPVKfRKQQLLKLKKFIEENREALSEA-VWKDLRRRHESTEIlEIGMTIQEIDYFLKNIddwvkptHVEKTFTTALD 95
Cdd:cd07116    55 GKTSVAE-RANILNKIADRMEANLEMLAVAeTWDNGKPVRETLAA-DIPLAIDHFRYFAGCI-------RAQEGSISEID 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  96 KPVIE---KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPET 172
Cdd:cd07116   126 ENTVAyhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEA 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 173 TDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCP------VVVEDDADIDISAKRIAWGKwLNCGQTCL 244
Cdd:cd07116   206 GKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadVMDADDAFFDKALEGFVMFA-LNQGEVCT 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 245 APDYILVNSTVKPKLVA-AIRKyvnefygedVKASK-----DYARMI----NQRHFDRISGLLD--KTQGA-VLIGGERD 311
Cdd:cd07116   285 CPSRALIQESIYDRFMErALER---------VKAIKqgnplDTETMIgaqaSLEQLEKILSYIDigKEEGAeVLTGGERN 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 312 RAD------LYIPPTVLDVEKSDPFmHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGG 385
Cdd:cd07116   356 ELGgllgggYYVPTTFKGGNKMRIF-QEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGR 434
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1734334313 386 VTVNdvLMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07116   435 VWTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
95-422 7.21e-38

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 144.66  E-value: 7.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  95 DKPVIE-KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfesKYVTVVNGG 168
Cdd:PRK11241  137 DKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELairagIPA----GVFNVVTGS 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 169 IPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAP 246
Cdd:PRK11241  213 AGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCA 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 247 DYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHF----DRISGLLDKtqGA-VLIGGE-RDRADLYIPP 319
Cdd:PRK11241  293 NRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVakveEHIADALEK--GArVVCGGKaHELGGNFFQP 370
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 320 TVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLmhITVD 398
Cdd:PRK11241  371 TILvDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNE 448
                         330       340
                  ....*....|....*....|....
gi 1734334313 399 TLPFGGVGVSGMGRYRGKYGFDTF 422
Cdd:PRK11241  449 VAPFGGIKASGLGREGSKYGIEDY 472
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
7-431 1.60e-36

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: 141.18  E-value: 1.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALseavwkdlrrrhESTEILEIGMTIQE--------IDYFLKNID 78
Cdd:cd07083    61 LEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRREL------------IATLTYEVGKNWVEaiddvaeaIDFIRYYAR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  79 DWVK---PTHVEKTFTTALDKPVIEkdPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENV-AATFEKLIP 154
Cdd:cd07083   129 AALRlryPAVEVVPYPGEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVgYKVFEIFHE 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 155 KYFESKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLT------PVTLELGGKCPVVVEDDADIDI 226
Cdd:cd07083   207 AGFPPGVVQFLPGVGEEVGAYLteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFEL 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 227 SAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA 303
Cdd:cd07083   287 VVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEhgKNEGQ 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 304 VLIGGERDRADLY-IPPTVLD-VEKSDPFMHDEIFGPVLPIITVQS--FSESLEYIADGEKPLAAYIFTRNEAKVKRLLN 379
Cdd:cd07083   367 LVLGGKRLEGEGYfVAPTVVEeVPPKARIAQEEIFGPVLSVIRYKDddFAEALEVANSTPYGLTGGVYSRKREHLEEARR 446
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1734334313 380 ETSSGGVTVNDVLMHITVDTLPFGGVGVSGMGRYRGKYGFDT-FTHEKSVLHR 431
Cdd:cd07083   447 EFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRrFLEMKAVAER 499
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
102-418 2.09e-36

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: 140.61  E-value: 2.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 102 DPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PKyfesKYVTVVNGGiPETTDLL 176
Cdd:cd07111   146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICaeaglPP----GVLNIVTGN-GSFGSAL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 KE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNST 254
Cdd:cd07111   221 ANhpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQES 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 255 VKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI--GGERDRADLYIPPT-VLDVEKSD 328
Cdd:cd07111   301 VAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEegRAEGADVFqpGADLPSKGPFYPPTlFTNVPPAS 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 329 PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmHITVD-TLPFGGVGV 407
Cdd:cd07111   381 RIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING---HNLFDaAAGFGGYRE 457
                         330
                  ....*....|.
gi 1734334313 408 SGMGRYRGKYG 418
Cdd:cd07111   458 SGFGREGGKEG 468
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
7-420 4.35e-33

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: 130.47  E-value: 4.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAV--------WkdlrrrhESTEilEIGMTIQEIDYFLKNID 78
Cdd:cd07095     6 VAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLIsretgkplW-------EAQT--EVAAMAGKIDISIKAYH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  79 DWVKPTHVEKTFTTAldkpVIEKDPKGVVLIISPWNYPVSmilLP---MVPAIAAGNTVVIKPSELSENVAA-TFEKLIP 154
Cdd:cd07095    77 ERTGERATPMAQGRA----VLRHRPHGVMAVFGPFNFPGH---LPnghIVPALLAGNTVVFKPSELTPAVAElMVELWEE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 155 KYFESKYVTVVNGGiPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHltP---VTLELGGKCPVVVEDDADIDISAK 229
Cdd:cd07095   150 AGLPPGVLNLVQGG-RETGEALaaHEGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAY 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 230 RIAWGKWLNCGQTCLAPDYILVNSTVK-----PKLVAAIRKY-VNEFYGEDvkaskdyARMINQRHFDRISGLLDKTQGA 303
Cdd:cd07095   227 LIVQSAFLTAGQRCTCARRLIVPDGAVgdaflERLVEAAKRLrIGAPDAEP-------PFMGPLIIAAAAARYLLAQQDL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 304 VLIGGE-------RDRADLYIPPTVLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKR 376
Cdd:cd07095   300 LALGGEpllamerLVAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFER 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1734334313 377 LLNETSSGGVTVNDVLMHITvDTLPFGGVGVSGMGRYRGKYGFD 420
Cdd:cd07095   380 FLARIRAGIVNWNRPTTGAS-STAPFGGVGLSGNHRPSAYYAAD 422
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
101-429 6.72e-33

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 130.77  E-value: 6.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSElseNVAATFEKLIPKYFES---KYVTVVNGGIPETTDLLK 177
Cdd:PRK13252  140 REPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE---VTPLTALKLAEIYTEAglpDGVFNVVQGDGRVGAWLT 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 178 E--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDiSAKRIAW-GKWLNCGQTCLAPDYILVNST 254
Cdd:PRK13252  217 EhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLD-RAADIAMlANFYSSGQVCTNGTRVFVQKS 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 255 VKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADL----YIPPTVL-DV 324
Cdd:PRK13252  296 IKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIEkgKAEGArLLCGGERlTEGGFangaFVAPTVFtDC 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 325 EKSDPFMHDEIFGPVLPIITvqsFSESLEYIA---DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN-----DVLMhit 396
Cdd:PRK13252  376 TDDMTIVREEIFGPVMSVLT---FDDEDEVIAranDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwgesPAEM--- 449
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1734334313 397 vdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:PRK13252  450 ----PVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
103-430 3.85e-32

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 127.93  E-value: 3.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPK--YFESKYVTVVNGGIPETTDLLKERF 180
Cdd:PRK09406  123 PLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRagFPDGCFQTLLVGSGAVEAILRDPRV 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 181 DHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV----K 256
Cdd:PRK09406  203 AAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVydafA 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 257 PKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGER-DRADLYIPPTVL-DVEKSDPFM 331
Cdd:PRK09406  283 EKFVARMAALR---VGDPTDPDTDVGPLATEQGRDEVEKQVDDAvaAGAtILCGGKRpDGPGWFYPPTVItDITPDMRLY 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 332 HDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLPFGGVGVSGMG 411
Cdd:PRK09406  360 TEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSGYG 437
                         330
                  ....*....|....*....
gi 1734334313 412 RYRGKYGFDTFTHEKSVLH 430
Cdd:PRK09406  438 RELSAHGIREFCNIKTVWI 456
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
82-428 4.51e-31

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 124.97  E-value: 4.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  82 KPTHVEKtfttalDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPselSENVAATFEkLIPKYFESK- 160
Cdd:PRK13968  111 EPTLVEN------QQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH---APNVMGCAQ-LIAQVFKDAg 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 161 -------YVTVVNGGIPETTDllKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:PRK13968  181 ipqgvygWLNADNDGVSQMIN--DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVA 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 234 GKWLNCGQTCLAPDYILVNSTVKP----KLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLI 306
Cdd:PRK13968  259 GRYQNTGQVCAAAKRFIIEEGIASafteRFVAAAAALK---MGDPRDEENALGPMARFDLRDELHHQVEATlaEGArLLL 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 307 GGER-DRADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSG 384
Cdd:PRK13968  336 GGEKiAGAGNYYAPTVLaNVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECG 415
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1734334313 385 GVTVNDvlmHITVDT-LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PRK13968  416 GVFING---YCASDArVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
101-411 1.44e-27

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 115.24  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSElSENVAA--TFEKLIPKYFESKYVTVVNGGIPETTDLLKE 178
Cdd:PLN00412  156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPT-QGAVAAlhMVHCFHLAGFPKGLISCVTGKGSEIGDFLTM 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 179 R--FDHILYTGCPPVAKIIMTAAakhLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK 256
Cdd:PLN00412  235 HpgVNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVA 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 257 PKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLyIPPTVLDVEKSDpfMH-- 332
Cdd:PLN00412  312 DALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMdaKEKGATFCQEWKREGNL-IWPLLLDNVRPD--MRia 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 333 -DEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHiTVDTLPFGGVGVSGMG 411
Cdd:PLN00412  389 wEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPAR-GPDHFPFQGLKDSGIG 467
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
101-411 2.92e-27

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: 114.05  E-value: 2.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LS--ENVAATFEKLIPKYFESKYVTVVNGGIPETTDl 175
Cdd:cd07148   122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALatpLSclAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTD- 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 176 lkERFDHILYTGCPPVAKIIMTAAAKHlTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVN--- 252
Cdd:cd07148   201 --PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPaei 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 253 -STVKPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDK--TQGA-VLIGGERDRADLYIPPTVLDVEKSD 328
Cdd:cd07148   278 aDDFAQRLAAAAEKLV---VGDPTDPDTEVGPLIRPREVDRVEEWVNEavAAGArLLCGGKRLSDTTYAPTVLLDPPRDA 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 329 PFMHDEIFGPVlpiITVQSFSESLEYIADGEK-PLA--AYIFTRNEAKVKRLLNETSSGGVTVNDvlmHIT--VDTLPFG 403
Cdd:cd07148   355 KVSTQEIFGPV---VCVYSYDDLDEAIAQANSlPVAfqAAVFTKDLDVALKAVRRLDATAVMVND---HTAfrVDWMPFA 428

                  ....*...
gi 1734334313 404 GVGVSGMG 411
Cdd:cd07148   429 GRRQSGYG 436
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
99-411 1.02e-26

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: 113.06  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfesKYVTVVNG-GIPET 172
Cdd:cd07125   163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELlheagVPR----DVLQLVPGdGEEIG 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 173 TDLLK-ERFDHILYTGCPPVAKIIMTAAAKH---LTPVTLELGGKCPVVVEDDADIDISAKRI---AWGkwlNCGQTCLA 245
Cdd:cd07125   239 EALVAhPRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVvqsAFG---SAGQRCSA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 246 PDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKTQGAVLIGGERDRADL---YIPPTV 321
Cdd:cd07125   316 LRLLYLQEEIAERFIEMLKGAMASLkVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGngyFVAPGI 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 322 LDVEKSDpFMHDEIFGPVLPIITVQSF--SESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlmhIT--- 396
Cdd:cd07125   396 IEIVGIF-DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRN---ITgai 471
                         330
                  ....*....|....*
gi 1734334313 397 VDTLPFGGVGVSGMG 411
Cdd:cd07125   472 VGRQPFGGWGLSGTG 486
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
103-389 3.70e-26

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: 111.14  E-value: 3.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPV------SMIllpmvpAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYV-----TVVNGGIPE 171
Cdd:cd07130   132 PLGVVGVITAFNFPVavwgwnAAI------ALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLpgaiaSLVCGGADV 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 172 TTDLLK-ERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYIL 250
Cdd:cd07130   206 GEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 251 VNSTVKPKLVAAIRK-YVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADLYIPPTVLDVE 325
Cdd:cd07130   286 VHESIYDEVLERLKKaYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEeaKSQGGtVLFGGKViDGPGNYVEPTIVEGL 365
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734334313 326 KSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSS--GGVTVN 389
Cdd:cd07130   366 SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVN 431
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
103-411 1.37e-21

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: 97.67  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAA-TFEKLIPKYFESKYVTVVNG-----GIPETTDll 176
Cdd:TIGR01238 160 SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYrAVELMQEAGFPAGTIQLLPGrgadvGAALTSD-- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 kERFDHILYTGCPPVAKIIMTAAAKHL---TPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNS 253
Cdd:TIGR01238 238 -PRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQE 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 254 TVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQ-------RHFDRISGLLDKTQGAVLIGGERDRADLYIPPTVLDVE 325
Cdd:TIGR01238 317 DVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAeakqnllAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFELD 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 326 KSDPfMHDEIFGPVLPIITVQS--FSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:TIGR01238 397 DIAE-LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFG 475

                  ....*...
gi 1734334313 404 GVGVSGMG 411
Cdd:TIGR01238 476 GQGLSGTG 483
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
3-431 8.76e-21

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 95.58  E-value: 8.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   3 FTELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVW----KDLRRRH----ESTEILE--IGMTIQEIDY 72
Cdd:PLN02419  153 FKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITteqgKTLKDSHgdifRGLEVVEhaCGMATLQMGE 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  73 FLKNIDDWVKPTHVektfttaldkpvieKDPKGVVLIISPWNYPvSMILLPMVP-AIAAGNTVVIKPSELSENVAATFEK 151
Cdd:PLN02419  233 YLPNVSNGVDTYSI--------------REPLGVCAGICPFNFP-AMIPLWMFPvAVTCGNTFILKPSEKDPGASVILAE 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 152 LIPKYFESKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAK 229
Cdd:PLN02419  298 LAMEAGLPDGVLNIVHGTNDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLN 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 230 RIAWGKWLNCGQTCLAPDYILVNSTVKP---KLVAAIrKYVNEFYGEDVKAskDYARMINQRHFDRISGLLDK--TQGAV 304
Cdd:PLN02419  378 ALLAAGFGAAGQRCMALSTVVFVGDAKSwedKLVERA-KALKVTCGSEPDA--DLGPVISKQAKERICRLIQSgvDDGAK 454
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 305 LIGGERD------RADLYIPPTVLDVEKSD-PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRL 377
Cdd:PLN02419  455 LLLDGRDivvpgyEKGNFIGPTILSGVTPDmECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKF 534
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734334313 378 LNETSSGGVTVNdVLMHITVDTLPFGGVGVSGMG--RYRGKYGFDTFTHEKSVLHR 431
Cdd:PLN02419  535 QMDIEAGQIGIN-VPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLVTQK 589
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
103-412 2.31e-18

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: 87.29  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKP----SELSENVAATFEK--LIPkyfeSKYVTVVNGGIPETTDLL 176
Cdd:cd07084   100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhtavSIVMQIMVRLLHYagLLP----PEDVTLINGDGKTMQALL 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 KE-RFDHILYTGCPPVAKIImtAAAKHLTPVTLELGGKCPVVVEDDAD-IDISAKRIAWGKWLNCGQTCLAPDYILVNST 254
Cdd:cd07084   176 LHpNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPEN 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 255 -----VKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFD-----RISGLLDKTQGAVLIGGERDRADLYIPPTVLDv 324
Cdd:cd07084   254 wsktpLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENLlgsvlLFSGKELKNHSIPSIYGACVASALFVPIDEIL- 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 325 eKSDPFMHDEIFGPVLPIITVQSFSES--LEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPF 402
Cdd:cd07084   333 -KTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQN 411
                         330
                  ....*....|
gi 1734334313 403 GGVGVSGMGR 412
Cdd:cd07084   412 HGGGPAADPR 421
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
87-409 2.49e-18

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 87.32  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  87 EKTFTTALDKPVIEKDPKGVVLIISPWNYPVSmilLP---MVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfe 158
Cdd:PRK09457  118 EKRSEMADGAAVLRHRPHGVVAVFGPYNFPGH---LPnghIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLPA--- 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 159 sKYVTVVNGGIPETTDLLKER-FDHILYTGCPPVAKIIMTAAAKHltP---VTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:PRK09457  192 -GVLNLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQS 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 235 KWLNCGQTCLAPDYILVNSTVK-----PKLVAAIRKY-VNEFYGE---------DVKASKdyaRMIN-QRHfdrisgLLD 298
Cdd:PRK09457  269 AFISAGQRCTCARRLLVPQGAQgdaflARLVAVAKRLtVGRWDAEpqpfmgaviSEQAAQ---GLVAaQAQ------LLA 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 299 KTqGAVLIGGERDRADL-YIPPTVLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRL 377
Cdd:PRK09457  340 LG-GKSLLEMTQLQAGTgLLTPGIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQF 418
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1734334313 378 LNETSSGGVTVNDVLMHITvDTLPFGGVGVSG 409
Cdd:PRK09457  419 LLEIRAGIVNWNKPLTGAS-SAAPFGGVGASG 449
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
105-409 2.40e-14

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: 75.32  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 105 GVVLIISPWNYPVSMILLPMVPAIAaGNTVVIKPSelSENVAATFekLIPKYFESKYVT--VVN---GGIPETTD--LLK 177
Cdd:cd07123   172 GFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPS--DTAVLSNY--LVYKILEEAGLPpgVINfvpGDGPVVGDtvLAS 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 178 ERFDHILYTGCPPVAKIIMTAAAKHLT-----P-VTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLA------ 245
Cdd:cd07123   247 PHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAasrayv 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 246 PDYILvnSTVKPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKTQGA----VLIGGERDRADLY-IPPT 320
Cdd:cd07123   327 PESLW--PEVKERLLEELKEIK---MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpeaeIIAGGKCDDSVGYfVEPT 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 321 VldVEKSDP---FMHDEIFGPVLpiiTVQ-----SFSESLEYIAD-GEKPLAAYIFTRNEAKVKRLLNE--TSSGGVTVN 389
Cdd:cd07123   402 V--IETTDPkhkLMTEEIFGPVL---TVYvypdsDFEETLELVDTtSPYALTGAIFAQDRKAIREATDAlrNAAGNFYIN 476
                         330       340
                  ....*....|....*....|
gi 1734334313 390 DVLMHITVDTLPFGGVGVSG 409
Cdd:cd07123   477 DKPTGAVVGQQPFGGARASG 496
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
102-424 2.69e-14

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 75.26  E-value: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 102 DPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYV-----TVVNGGIPETTDLL 176
Cdd:PLN02315  153 NPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgaifTSFCGGAEIGEAIA 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 177 KE-RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV 255
Cdd:PLN02315  233 KDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 256 KPKLVAA-IRKYVNEFYGEDVKASKDYARM---INQRHFDRISGLLDKTQGAVLIGGER-DRADLYIPPTVLDVEKSDPF 330
Cdd:PLN02315  313 YDDVLEQlLTVYKQVKIGDPLEKGTLLGPLhtpESKKNFEKGIEIIKSQGGKILTGGSAiESEGNFVQPTIVEISPDADV 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 331 MHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSS--GGVTVNdvlmhitvdtLP------- 401
Cdd:PLN02315  393 VKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVN----------IPtngaeig 462
                         330       340
                  ....*....|....*....|....*
gi 1734334313 402 --FGGVGVSGMGRYRGKYGFDTFTH 424
Cdd:PLN02315  463 gaFGGEKATGGGREAGSDSWKQYMR 487
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
103-411 3.99e-13

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 72.15  E-value: 3.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLipkYFESkyvtvvngGIPE----------- 171
Cdd:PRK11904   684 GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKL---LHEA--------GIPKdvlqllpgdga 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  172 ------TTDllkERFDHILYTGCPPVAKII-MTAAAKHLTPVTL--ELGGKCPVVVEDDA-------DIDISAKRIAwgk 235
Cdd:PRK11904   753 tvgaalTAD---PRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTAlpeqvvdDVVTSAFRSA--- 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  236 wlncGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-------YGEDV-----KASKDyarMINqRHFDRIsglldkTQGA 303
Cdd:PRK11904   827 ----GQRCSALRVLFVQEDIADRVIEMLKGAMAELkvgdprlLSTDVgpvidAEAKA---NLD-AHIERM------KREA 892
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  304 VLI-----GGERDRADlYIPPTVLDVEKSDpFMHDEIFGPVLPIITVQSF--SESLEYIADGEKPLAAYIFTRNEAKVKR 376
Cdd:PRK11904   893 RLLaqlplPAGTENGH-FVAPTAFEIDSIS-QLEREVFGPILHVIRYKASdlDKVIDAINATGYGLTLGIHSRIEETADR 970
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1734334313  377 LLNETSSGGVTVNDVLMHITVDTLPFGGVGVSGMG 411
Cdd:PRK11904   971 IADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
103-411 1.18e-12

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 70.77  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyfeskyvtvVNGGIPE-TTDLL----- 176
Cdd:PRK11809   768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL-----------LEAGVPAgVVQLLpgrge 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  177 --------KERFDHILYTGCPPVAKIIMTAAAKHL------TPVTLELGGKCPVVVEDDA-------DIDISAKRIAwgk 235
Cdd:PRK11809   837 tvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSAlteqvvaDVLASAFDSA--- 913
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  236 wlncGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMIN-------QRHfdrISGLLDK----TQgA 303
Cdd:PRK11809   914 ----GQRCSALRVLCLQDDVADRTLKMLRGAMAECrMGNPDRLSTDIGPVIDaeakaniERH---IQAMRAKgrpvFQ-A 985
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  304 VLIGGERDRADLYIPPTVLDVEKSDPfMHDEIFGPVLPIITVQS--FSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:PRK11809   986 ARENSEDWQSGTFVPPTLIELDSFDE-LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSA 1064
                          330       340       350
                   ....*....|....*....|....*....|
gi 1734334313  382 SSGGVTVNDVLMHITVDTLPFGGVGVSGMG 411
Cdd:PRK11809  1065 HVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
103-411 4.76e-11

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 65.66  E-value: 4.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyFESkyvtvvngGIPETT-DLL----- 176
Cdd:PRK11905   676 PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLL---HEA--------GVPKDAlQLLpgdgr 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  177 --------KERFDHILYTGCPPVAKIIMTAAAKHLT-PVTL--ELGGKCPVVVEDDA-------DIDISAKRIAwgkwln 238
Cdd:PRK11905   745 tvgaalvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSAlpeqvvaDVIASAFDSA------ 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  239 cGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGAVL----IGGERD 311
Cdd:PRK11905   819 -GQRCSALRVLCLQEDVADRVLTMLKGAMDELRiGDPWRLSTDVGPVIDAEAQANIEAHIEamRAAGRLVhqlpLPAETE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  312 RAdLYIPPTVLDVEK-SDpfMHDEIFGPVLPIITVQSfSESLEYIAD------GekpLAAYIFTRNEAKVKRLLNETSSG 384
Cdd:PRK11905   898 KG-TFVAPTLIEIDSiSD--LEREVFGPVLHVVRFKA-DELDRVIDDinatgyG---LTFGLHSRIDETIAHVTSRIRAG 970
                          330       340
                   ....*....|....*....|....*..
gi 1734334313  385 GVTVNDVLMHITVDTLPFGGVGVSGMG 411
Cdd:PRK11905   971 NIYVNRNIIGAVVGVQPFGGEGLSGTG 997
ALDH_EutE cd07121
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ...
7-370 7.05e-11

Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.


Pssm-ID: 143439 [Multi-domain]  Cd Length: 429  Bit Score: 64.18  E-value: 7.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYFRtgetKPVKFRKQQLLKLKKFIEENREALSEAvwkdlrrrhestEILEIGMTIQEiDYFLKNIDDWVKPTHV 86
Cdd:cd07121    14 KAAQKQYRK----CTLADREKIIEAIREALLSNAEELAEM------------AVEETGMGRVE-DKIAKNHLAAEKTPGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  87 EKTFTTAL--DK--PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFES--- 159
Cdd:cd07121    77 EDLTTTAWsgDNglTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEagg 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 160 --KYVTVVNGGIPETTDLLkerFDH-----ILYTGCPPVAKIIMTAAAKhltpvtlELG---GKCPVVVEDDADIDISAK 229
Cdd:cd07121   157 pdNLVVTVEEPTIETTNEL---MAHpdinlLVVTGGPAVVKAALSSGKK-------AIGagaGNPPVVVDETADIEKAAR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 230 RIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYvNEFYGEDVKASKDYARMINQRHFDRIS-GLLDKTQGAVLigg 308
Cdd:cd07121   227 DIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRN-GAYVLNDEQAEQLLEVVLLTNKGATPNkKWVGKDASKIL--- 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734334313 309 erDRADLYIPPT----VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPL--AAYIFTRN 370
Cdd:cd07121   303 --KAAGIEVPADirliIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKN 368
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
50-377 1.51e-09

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143400 [Multi-domain]  Cd Length: 439  Bit Score: 59.97  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  50 DLRRRHESTEILEIGMTIQEiDYFLKNIDDWVKPTHVEKTFTT----ALDKP---VIEKDPKGVVLIISPWNYPVSMILL 122
Cdd:cd07081    36 DARIDLAKLAVSETGMGRVE-DKVIKNHFAAEYIYNVYKDEKTcgvlTGDENggtLIIAEPIGVVASITPSTNPTSTVIF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 123 PMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYF------ESKYVTVVNGGIPETTDLLKE-RFDHILYTGCPPVAKii 195
Cdd:cd07081   115 KSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaagapENLIGWIDNPSIELAQRLMKFpGIGLLLATGGPAVVK-- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 196 mtAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVaairkyvnefygedv 275
Cdd:cd07081   193 --AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVM--------------- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 276 kaskdyaRMINQRHFDRISG-LLDKTQGAVLIGGERDR-------------ADLYIPPT-------VLDVEKSDPFMHdE 334
Cdd:cd07081   256 -------RLFEGQGAYKLTAeELQQVQPVILKNGDVNRdivgqdaykiaaaAGLKVPQEtriligeVTSLAEHEPFAH-E 327
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1734334313 335 IFGPVLPIITVQSFSESLE----YIADGEKPLAAYIFTRNEAKVKRL 377
Cdd:cd07081   328 KLSPVLAMYRAANFADADAkalaLKLEGGCGHTSAMYSDNIKAIENM 374
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
103-390 4.94e-09

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: 58.44  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 103 PK-GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyfeskyvtVVNGGIPE---------T 172
Cdd:cd07128   143 PRrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDI----------VESGLLPEgalqlicgsV 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 173 TDLLK--ERFDHILYTGCPPVAKIIMT--AAAKHLTPVTLE--------LGgkcPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07128   213 GDLLDhlGEQDVVAFTGSAATAAKLRAhpNIVARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAG 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 241 QTCLAPDYILVNS----TVKPKLVAAIRKYVnefYG----EDVK----ASKDyarminQRHfDRISGLLDKTQGAVLIGG 308
Cdd:cd07128   290 QKCTAIRRAFVPEarvdAVIEALKARLAKVV---VGdprlEGVRmgplVSRE------QRE-DVRAAVATLLAEAEVVFG 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 309 ERDRADL---------YIPPTVLDVEKSD--PFMHD-EIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKR 376
Cdd:cd07128   360 GPDRFEVvgadaekgaFFPPTLLLCDDPDaaTAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
                         330
                  ....*....|....*.
gi 1734334313 377 LLNETSS--GGVTVND 390
Cdd:cd07128   440 LVLGAAPyhGRLLVLN 455
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
127-394 7.41e-09

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: 57.94  E-value: 7.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 127 AIAAGNTVVIK--PS--ELSENVAATFEKLIPKY-FESKYVTVVNGGIPET-TDLLKerfdH-----ILYTGCPPVAKII 195
Cdd:cd07129   131 ALAAGCPVVVKahPAhpGTSELVARAIRAALRATgLPAGVFSLLQGGGREVgVALVK----HpaikaVGFTGSRRGGRAL 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 196 MTAAAKHLT--PVTLELGGKCPVVV------EDDADIdisAKRIAWGKWLNCGQTCLAPDYILV-NSTVKPKLVAAIRKY 266
Cdd:cd07129   207 FDAAAARPEpiPFYAELGSVNPVFIlpgalaERGEAI---AQGFVGSLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEA 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 267 VNEFYGedvkaskdyARMIN---QRHFDR-ISGLLDKTQGAVLIGGERDRADLYIPPTVLDVEKS----DPFMHDEIFGP 338
Cdd:cd07129   284 LAAAPA---------QTMLTpgiAEAYRQgVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAaflaDPALQEEVFGP 354
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1734334313 339 VLPIITVQSFSE------SLE-------YIADGEKPLAAYIFTRNEAKVKRLLNetsSG---GVTVNDVLMH 394
Cdd:cd07129   355 ASLVVRYDDAAEllavaeALEgqltatiHGEEDDLALARELLPVLERKAGRLLF---NGwptGVEVCPAMVH 423
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
8-383 1.96e-08

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 56.46  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   8 ETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT--- 84
Cdd:cd07077     1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITasv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  85 -HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVpAIAAGNTVVIKPSELSE--NVAAT--FEKLIPKYFES 159
Cdd:cd07077    81 gHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALR-GIATRNQCIFRPHPSAPftNRALAllFQAADAAHGPK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 160 KYV-TVVNGGIPETTDLLK-ERFDHILYTGCPPVAKiimtAAAKH--LTPVTLELGGKCPVVVEDDADIDISAKRIAWGK 235
Cdd:cd07077   160 ILVlYVPHPSDELAEELLShPKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 236 WLNcGQTCLAPDYILVNSTVKPKLvaairkyvnefygedvkaskdyarminqrhFDRIsglldKTQGAVliggerDRADL 315
Cdd:cd07077   236 FFD-QNACASEQNLYVVDDVLDPL------------------------------YEEF-----KLKLVV------EGLKV 273
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734334313 316 YIPPTVLDVE---KSDPFMHDEiFGPVLPIITVQSFSESLE----YIADGEKPLAAYIFTRNEAKVKRLLN--ETSS 383
Cdd:cd07077   274 PQETKPLSKEttpSFDDEALES-MTPLECQFRVLDVISAVEnawmIIESGGGPHTRCVYTHKINKVDDFVQyiDTAS 349
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
103-411 2.66e-08

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 56.48  E-value: 2.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyFESkyvtvvngGIPE----------- 171
Cdd:COG4230    680 GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLL---HEA--------GVPAdvlqllpgdge 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  172 ------TTDllkERFDHILYTGCPPVAKII-MTAAAKHLTPVTL--ELGGKCPVVVedD---------ADIDISAkriaw 233
Cdd:COG4230    749 tvgaalVAD---PRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIV--DssalpeqvvDDVLASA----- 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  234 gkWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNE-------FYGEDV-----KASKDyarMInQRHFDRIsglldKTQ 301
Cdd:COG4230    819 --FDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAElrvgdpaDLSTDVgpvidAEARA---NL-EAHIERM-----RAE 887
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  302 GAVLIGGERDRAD---LYIPPTVLDVEKSDpFMHDEIFGPVLPIITVQsfSESLEYIAD-----GekplaaY-----IFT 368
Cdd:COG4230    888 GRLVHQLPLPEECangTFVAPTLIEIDSIS-DLEREVFGPVLHVVRYK--ADELDKVIDainatG------YgltlgVHS 958
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1734334313  369 RNEAKVKRLLNETSSGGVTVNdvlMHIT---VDTLPFGGVGVSGMG 411
Cdd:COG4230    959 RIDETIDRVAARARVGNVYVN---RNIIgavVGVQPFGGEGLSGTG 1001
PRK15398 PRK15398
aldehyde dehydrogenase;
7-377 7.99e-08

aldehyde dehydrogenase;


Pssm-ID: 237956  Cd Length: 465  Bit Score: 54.52  E-value: 7.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313   7 VETQRKYfrtgETKPVKFRKQQLLKLKKFIEENREALSEAVWKdlrrrhesteilEIGMTIQEiDYFLKNIDDWVKPTHV 86
Cdd:PRK15398   46 KVAQQRY----QQKSLAMRQRIIDAIREALLPHAEELAELAVE------------ETGMGRVE-DKIAKNVAAAEKTPGV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  87 EKTFTTAL--DK--PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFES--- 159
Cdd:PRK15398  109 EDLTTEALtgDNglTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAagg 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 160 --KYVTVVNGGIPETTDLLkerFDH-----ILYTGCPPVAKIIMT-------AAAkhltpvtlelgGKCPVVVEDDADID 225
Cdd:PRK15398  189 peNLVVTVAEPTIETAQRL---MKHpgialLVVTGGPAVVKAAMKsgkkaigAGA-----------GNPPVVVDETADIE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 226 ISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYvnefyGedvkaskdyARMINQRHFDRISGLLDKTQGAV- 304
Cdd:PRK15398  255 KAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKN-----G---------AVLLTAEQAEKLQKVVLKNGGTVn 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 305 --LIGGER----DRADLYIPPT----VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPL--AAYIFTRNea 372
Cdd:PRK15398  321 kkWVGKDAakilEAAGINVPKDtrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRN-- 398

                  ....*
gi 1734334313 373 kVKRL 377
Cdd:PRK15398  399 -VDNL 402
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
83-389 1.01e-07

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.


Pssm-ID: 143445  Cd Length: 549  Bit Score: 54.41  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313  83 PTHVEKTFTtaldkPViekdPKGVVLIIS-----PWN-YPvsmillPMVPAIAAGNTVVIKPSE-----LSENVAATFEK 151
Cdd:cd07127   182 PLAMEKTFT-----VV----PRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHPaailpLAITVQVAREV 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 152 LIPKYFESKYVTVVNGGIPEttDLLKERFDH-----ILYTGCPPVAKIIMTAAAKHLtpVTLELGGKCPVVVEDDADIDI 226
Cdd:cd07127   247 LAEAGFDPNLVTLAADTPEE--PIAQTLATRpevriIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKA 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 227 SAKRIAWGKWLNCGQTCLAPDYILV--------NSTVKPKLVAA-IRKYVNEFYGEDVKASKDYARMINQRHFDRISgll 297
Cdd:cd07127   323 MLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtdDGRKSFDEVAAdLAAAIDGLLADPARAAALLGAIQSPDTLARIA--- 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734334313 298 DKTQGAVLIGGERDRADLYIP------PTVLDVEKSDPFMHD-EIFGPVLPIITVQSFSESLE---YIADGEKPLAAYIF 367
Cdd:cd07127   400 EARQLGEVLLASEAVAHPEFPdarvrtPLLLKLDASDEAAYAeERFGPIAFVVATDSTDHSIElarESVREHGAMTVGVY 479
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1734334313 368 TRNEAKVKRL----------LNETSSGGVTVN 389
Cdd:cd07127   480 STDPEVVERVqeaaldagvaLSINLTGGVFVN 511
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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