NCBI Conserved Domain Search

Conserved domains on [gi|1054401713|ref|NP_001317079|]

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aldehyde dehydrogenase, dimeric NADP-preferring isoform 2 [Homo sapiens]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 34081)

aldehyde dehydrogenase family protein is an NAD(P)(+)-dependent enzyme that may oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and may play an important role in detoxification

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

ALDH-SF super family

cl11961

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...

1-374

0e+00

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.

The actual alignment was detected with superfamily member cd07132:

Pssm-ID: 448367 [Multi-domain] Cd Length: 443 Bit Score: 761.38 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI 80
Cdd:cd07132    70 AISNLPEWMKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 IPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 160
Cdd:cd07132   150 IPKYLDKECYPVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 161 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAAT 240
Cdd:cd07132   230 WGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKE 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 241 RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIV 320
Cdd:cd07132   310 RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIM 389

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054401713 321 HITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPPSP 374
Cdd:cd07132   390 HYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443

Name

Accession

Description

Interval

E-value

ALDH_F3AB

cd07132

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...

1-374

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: 761.38 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI 80
Cdd:cd07132    70 AISNLPEWMKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 IPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 160
Cdd:cd07132   150 IPKYLDKECYPVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 161 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAAT 240
Cdd:cd07132   230 WGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKE 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 241 RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIV 320
Cdd:cd07132   310 RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIM 389

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054401713 321 HITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPPSP 374
Cdd:cd07132   390 HYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443

PTZ00381

aldehyde dehydrogenase family protein; Provisional

1-372

0e+00

aldehyde dehydrogenase family protein; Provisional

Pssm-ID: 240392 Cd Length: 493 Bit Score: 577.37 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI 80
Cdd:PTZ00381   79 LLKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 IPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 160
Cdd:PTZ00381  159 LTKYLDPSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIA 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 161 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE--GQKVAYGGTGDA 238
Cdd:PTZ00381  239 WGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDI 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 239 ATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDV 318
Cdd:PTZ00381  319 ENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDC 398

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054401713 319 IVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPP 372
Cdd:PTZ00381  399 VFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPP 452

AdhE

COG1012

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...

7-354

2.02e-109

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: 328.62 E-value: 2.02e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPV----EKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII 81
Cdd:COG1012   112 RYYAGEARrlygETIPSDAPGTRaYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  82 PQY-LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRR 158
Cdd:COG1012   192 EEAgLPAGVLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEA 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 159 IAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAY 232
Cdd:COG1012   272 AVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLT 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 233 GGT--GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 310
Cdd:COG1012   352 GGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEA 431

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1054401713 311 GGVAANDVIVHITLHsLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:COG1012   432 GMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETKT 474

Aldedh

pfam00171

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...

7-354

3.08e-100

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: 304.45 E-value: 3.08e-100

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPV----EKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIP 82
Cdd:pfam00171  98 RYYAGLARrldgETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  83 QY-LDKDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRI 159
Cdd:pfam00171 178 EAgLPAGVLNVVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAA 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 160 AWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYG 233
Cdd:pfam00171 258 VFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTG 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 234 GTGDAAT-RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGG 312
Cdd:pfam00171 338 GEAGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGM 417

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1054401713 313 VAANDVIVhITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:pfam00171 418 VWINDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458

BADH

TIGR01804

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...

15-350

3.91e-52

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: 180.01 E-value: 3.91e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  15 EKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVI 93
Cdd:TIGR01804 117 EIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVV 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  94 NGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTC 171
Cdd:TIGR01804 197 QGDGAEVGPLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVC 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 172 VAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-------TGDA 238
Cdd:TIGR01804 277 SNGTRVFVHKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIekgkaEGATLATGGgrpenvgLQNG 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 239 AtrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDv 318
Cdd:TIGR01804 357 F--FVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT- 433

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1054401713 319 iVHITLHSLPFGGVGNSGMGSYHGKKSFETFS 350
Cdd:TIGR01804 434 -YNLYPAEAPFGGYKQSGIGRENGKAALAHYT 464

Name

Accession

Description

Interval

E-value

ALDH_F3AB

cd07132

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...

1-374

0e+00

Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 761.38 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI 80
Cdd:cd07132    70 AISNLPEWMKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 IPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 160
Cdd:cd07132   150 IPKYLDKECYPVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 161 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAAT 240
Cdd:cd07132   230 WGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKE 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 241 RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIV 320
Cdd:cd07132   310 RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIM 389

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054401713 321 HITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPPSP 374
Cdd:cd07132   390 HYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443

ALDH_F3-13-14_CALDH-like

cd07087

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...

1-357

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: 656.14 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI 80
Cdd:cd07087    70 ALKHLKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 IPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 160
Cdd:cd07087   150 IPKYFDPEAVAVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIA 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 161 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAAT 240
Cdd:cd07087   230 WGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEE 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 241 RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIV 320
Cdd:cd07087   310 RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLL 389

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1054401713 321 HITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07087   390 HAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426

ALDH_YwdH-P39616

cd07136

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...

1-377

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: 593.71 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVeKTPQTQQ-DELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLAT 79
Cdd:cd07136    70 AIKHLKKWMKPKRV-KTPLLNFpSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  80 IIPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRI 159
Cdd:cd07136   149 IIEETFDEEYVAVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRI 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 160 AWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAA 239
Cdd:cd07136   229 VWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRE 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 240 TRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVI 319
Cdd:cd07136   309 TLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTI 388

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054401713 320 VHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDegLKVRYPPSPAKM 377
Cdd:cd07136   389 MHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKK 444

PTZ00381

aldehyde dehydrogenase family protein; Provisional

1-372

0e+00

aldehyde dehydrogenase family protein; Provisional

Pssm-ID: 240392 Cd Length: 493 Bit Score: 577.37 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI 80
Cdd:PTZ00381   79 LLKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 IPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 160
Cdd:PTZ00381  159 LTKYLDPSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIA 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 161 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE--GQKVAYGGTGDA 238
Cdd:PTZ00381  239 WGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDI 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 239 ATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDV 318
Cdd:PTZ00381  319 ENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDC 398

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054401713 319 IVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPP 372
Cdd:PTZ00381  399 VFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPP 452

ALDH_F14-YMR110C

cd07135

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...

1-354

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: 556.83 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTQQ-DELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLAT 79
Cdd:cd07135    77 MLKNLKKWAKDEKVKDGPLAFMfGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  80 IIPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRI 159
Cdd:cd07135   157 LVPKYLDPDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRI 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 160 AWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE--GQKVAYGGTGD 237
Cdd:cd07135   237 LWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMD 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 238 AATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAND 317
Cdd:cd07135   317 EATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIND 396

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1054401713 318 VIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07135   397 TLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433

ALDH_AlkH-like

cd07134

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...

2-357

4.01e-178

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: 502.14 E-value: 4.01e-178

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   2 IQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII 81
Cdd:cd07134    71 IKHLKKWMKPKRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKII 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  82 PQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 161
Cdd:cd07134   151 REAFDEDEVAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAW 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 162 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDA--KKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG 234
Cdd:cd07134   231 GKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGG 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 235 TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVA 314
Cdd:cd07134   311 QFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVV 390

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1054401713 315 ANDVIVHItLHS-LPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07134   391 VNDVVLHF-LNPnLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433

ALDH_F3FHI

cd07137

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...

2-357

3.39e-164

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: 466.50 E-value: 3.39e-164

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   2 IQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII 81
Cdd:cd07137    72 IKELKKWMAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  82 PQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 161
Cdd:cd07137   152 PEYLDTKAIKVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 162 GKF-MNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVA----YGGTG 236
Cdd:cd07137   232 GKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVAdkivHGGER 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 237 DAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN 316
Cdd:cd07137   312 DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN 391

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1054401713 317 DVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07137   392 DTVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432

ALDH_CALDH_CalB

cd07133

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...

2-354

8.80e-162

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: 460.41 E-value: 8.80e-162

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   2 IQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII 81
Cdd:cd07133    72 RKHLKKWMKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  82 PQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 161
Cdd:cd07133   152 AEYFDEDEVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAF 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 162 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGeDAKKSRDYGRIISARHFQRVMGLIE-----GQKV---AYG 233
Cdd:cd07133   232 GKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakGARVielNPA 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 234 GTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 313
Cdd:cd07133   311 GEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV 390

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1054401713 314 AANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07133   391 TINDTLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431

PLN02203

aldehyde dehydrogenase

2-372

2.48e-142

aldehyde dehydrogenase

Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 412.97 E-value: 2.48e-142

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   2 IQKLPEWAADE----PVEKTPQTQQdelyIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLL 77
Cdd:PLN02203   79 LSNLKKWMAPKkaklPLVAFPATAE----VVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  78 ATIIPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVD---KNCDLDV 154
Cdd:PLN02203  155 AANIPKYLDSKAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKV 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 155 ACRRIAWGKFMN-SGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVA-- 231
Cdd:PLN02203  235 AVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAas 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 232 --YGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETS 309
Cdd:PLN02203  315 ivHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETS 394

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054401713 310 SGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDegLKVRYPP 372
Cdd:PLN02203  395 SGSVTFNDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPP 455

ALDH

cd07078

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...

5-357

2.55e-135

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: 393.11 E-value: 2.55e-135

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   5 LPEWAADEPVEKTPQTQqdeLYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY 84
Cdd:cd07078    73 ARRLHGEVIPSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  85 -LDKDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 161
Cdd:cd07078   150 gLPPGVLNVVTGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVF 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 162 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGED-AKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT 235
Cdd:cd07078   230 GAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 236 --GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 313
Cdd:cd07078   310 rlEGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTV 389

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1054401713 314 AANDVIVHITLHsLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07078   390 WINDYSVGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432

PLN02174

aldehyde dehydrogenase family 3 member H1

2-372

2.13e-127

aldehyde dehydrogenase family 3 member H1

Pssm-ID: 177831 Cd Length: 484 Bit Score: 375.15 E-value: 2.13e-127

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   2 IQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII 81
Cdd:PLN02174   83 LKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  82 PQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 161
Cdd:PLN02174  163 EQYLDSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIA 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 162 GKF-MNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE----GQKVAYGGTG 236
Cdd:PLN02174  243 GKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEK 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 237 DAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN 316
Cdd:PLN02174  323 DRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN 402

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054401713 317 DVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGlkVRYPP 372
Cdd:PLN02174  403 DIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPP 456

AdhE

COG1012

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...

7-354

2.02e-109

Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 328.62 E-value: 2.02e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPV----EKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII 81
Cdd:COG1012   112 RYYAGEARrlygETIPSDAPGTRaYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  82 PQY-LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRR 158
Cdd:COG1012   192 EEAgLPAGVLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEA 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 159 IAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAY 232
Cdd:COG1012   272 AVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLT 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 233 GGT--GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 310
Cdd:COG1012   352 GGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEA 431

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1054401713 311 GGVAANDVIVHITLHsLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:COG1012   432 GMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETKT 474

ALDH-SF

cd06534

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...

7-357

6.25e-108

Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 321.10 E-value: 6.25e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPVEKTPQT-QQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY- 84
Cdd:cd06534    67 GLADKLGGPELPSPdPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAg 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  85 LDKDLYPVINGGVPET-TELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWG 162
Cdd:cd06534   147 LPPGVVNVVPGGGDEVgAALLShPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFG 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 163 KFMNSGQTCVAPDYILCDPSIQNQIVEKLKkslkefygedakksrdygriisarhfqrvmgliegqkvayggtgdaatry 242
Cdd:cd06534   227 AFFNAGQICTAASRLLVHESIYDEFVEKLV-------------------------------------------------- 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 243 iapTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHI 322
Cdd:cd06534   257 ---TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV 333

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1054401713 323 TLHsLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd06534   334 GPE-APFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367

Aldedh

pfam00171

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...

7-354

3.08e-100

Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 304.45 E-value: 3.08e-100

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPV----EKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIP 82
Cdd:pfam00171  98 RYYAGLARrldgETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  83 QY-LDKDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRI 159
Cdd:pfam00171 178 EAgLPAGVLNVVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAA 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 160 AWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYG 233
Cdd:pfam00171 258 VFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTG 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 234 GTGDAAT-RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGG 312
Cdd:pfam00171 338 GEAGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGM 417

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1054401713 313 VAANDVIVhITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:pfam00171 418 VWINDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458

ALDH_DDALDH

cd07099

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...

6-357

4.29e-91

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: 281.03 E-value: 4.29e-91

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   6 PEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSEL----SENMASLLATII 81
Cdd:cd07099    94 PRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVtplvGELLAEAWAAAG 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  82 PqylDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 161
Cdd:cd07099   174 P---PQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVW 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 162 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG- 234
Cdd:cd07099   251 GAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdavakGAKALTGGa 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 235 --TGDAatRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGG 312
Cdd:cd07099   331 rsNGGG--PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGA 408

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1054401713 313 VAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07099   409 VSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453

ALDH_F15-22

cd07098

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...

26-363

9.46e-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: 241.82 E-value: 9.46e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYL-----DKDLYPVINGgVPET 100
Cdd:cd07098   115 RVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacghDPDLVQLVTC-LPET 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 101 TELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYIL 178
Cdd:cd07098   194 AEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVI 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 179 CDPSIQNQIVEKLKK---SLKEFYGEDakKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-----TGDAATRYIAP 245
Cdd:cd07098   274 VHEKIYDKLLEILTDrvqALRQGPPLD--GDVDVGAMISPARFDRLEELVadaveKGARLLAGGkryphPEYPQGHYFPP 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 246 TILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLH 325
Cdd:cd07098   352 TLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQ 431

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1054401713 326 SLPFGGVGNSGMGSYHGKKSFetfshRRSCLVRPLMND 363
Cdd:cd07098   432 QLPFGGVKGSGFGRFAGEEGL-----RGLCNPKSVTED 464

ALDH_BenzADH-like

cd07104

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...

30-353

5.35e-75

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: 238.97 E-value: 5.35e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLL-ATIIPQY-LDKDLYPVINGGVPETTELLKE- 106
Cdd:cd07104    97 VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEAgLPKGVLNVVPGGGSEIGDALVEh 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 -RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQN 185
Cdd:cd07104   177 pRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYD 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 186 QIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAatRYIAPTILTDVDPQSPV 257
Cdd:cd07104   257 EFVEKLVakaKALP--VGDPRDPDTVIGPLINERQVDRVHAIVEdavaaGARLLTGGTYEG--LFYQPTVLSDVTPDMPI 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 258 MQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIKkmIAETS-SGGVAANDVIVHITLHSlPFGGVGNS 335
Cdd:cd07104   333 FREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlERAMA--FAERLeTGMVHINDQTVNDEPHV-PFGGVKAS 409

                         330
                  ....*....|....*...
gi 1054401713 336 GMGSYHGKKSFETFSHRR 353
Cdd:cd07104   410 GGGRFGGPASLEEFTEWQ 427

ALDH_F8_HMSADH

cd07093

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...

26-350

7.35e-73

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: 234.00 E-value: 7.35e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyLDKDLYP----VINGGVPETT 101
Cdd:cd07093   112 YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA---NEAGLPPgvvnVVHGFGPEAG 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 102 ELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILC 179
Cdd:cd07093   189 AALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILV 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 180 DPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATR-----YIAPTIL 248
Cdd:cd07093   269 QRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVelaraEGATILTGGGRPELPDleggyFVEPTVI 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 249 TDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIV-HITlhsL 327
Cdd:cd07093   349 TGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVrDLR---T 425

                         330       340
                  ....*....|....*....|...
gi 1054401713 328 PFGGVGNSGMGSYHGKKSFETFS 350
Cdd:cd07093   426 PFGGVKASGIGREGGDYSLEFYT 448

ALDH_F5_SSADH_GabD

cd07103

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...

30-339

2.28e-70

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: 227.32 E-value: 2.28e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELLKERF 108
Cdd:cd07103   116 QPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASP 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 109 D--HILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQ 186
Cdd:cd07103   196 RvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDE 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 187 IVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAAT-RYIAPTILTDVDPQSPVMQ 259
Cdd:cd07103   276 FVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEdavakGAKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMN 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 260 EEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIvhITLHSLPFGGVGNSGMGS 339
Cdd:cd07103   356 EETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL--ISDAEAPFGGVKESGLGR 433

ALDH_SaliADH

cd07105

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...

30-350

1.44e-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: 222.07 E-value: 1.44e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIipqYLDKDLYP-VIN------GGVPETTE 102
Cdd:cd07105    97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRV---FHEAGLPKgVLNvvthspEDAPEVVE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 103 LLkerFDH-----ILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYI 177
Cdd:cd07105   174 AL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 178 LCDPSIQNQIVEKLKKSLKEFYGEDAKKsrdyGRIISARHFQRVMGLIE-----GQKVAYGGTGD--AATRYIAPTILTD 250
Cdd:cd07105   251 IVHESIADEFVEKLKAAAEKLFAGPVVL----GSLVSAAAADRVKELVDdalskGAKLVVGGLADesPSGTSMPPTILDN 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 251 VDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITlHSLPFG 330
Cdd:cd07105   327 VTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDE-PTLPHG 405

                         330       340
                  ....*....|....*....|
gi 1054401713 331 GVGNSGMGSYHGKKSFETFS 350
Cdd:cd07105   406 GVKSSGYGRFNGKWGIDEFT 425

ALDH_CddD-AldA-like

cd07089

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...

27-354

1.69e-68

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: 222.89 E-value: 1.69e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  27 IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyLDKDLYP-VIN---GGVPETTE 102
Cdd:cd07089   119 VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEII---AETDLPAgVVNvvtGSDNAVGE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 103 LLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCD 180
Cdd:cd07089   196 ALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVP 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 181 PSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDAATRYIAPTILTDV 251
Cdd:cd07089   276 RSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIargrdEGARLVTGGgrpAGLDKGFYVEPTLFADV 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 252 DPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDviVHITLHSLPFGG 331
Cdd:cd07089   356 DNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGING--GGGYGPDAPFGG 433

                         330       340
                  ....*....|....*....|...
gi 1054401713 332 VGNSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07089   434 YKQSGLGRENGIEGLEEFLETKS 456

ALDH_VaniDH_like

cd07150

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...

30-353

5.99e-68

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: 221.05 E-value: 5.99e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL--KE 106
Cdd:cd07150   118 RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELvdDP 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQ 186
Cdd:cd07150   198 RVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 187 IVEKL---KKSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAatRYIAPTILTDVDPQSPVM 258
Cdd:cd07150   278 FVKKFvarASKLK--VGDPRDPDTVIGPLISPRQVERIKRQVEdavakGAKLLTGGKYDG--NFYQPTVLTDVTPDMRIF 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 259 QEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHsLPFGGVGNSGMG 338
Cdd:cd07150   354 REETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAH-VPFGGVKASGFG 432

                         330
                  ....*....|....*
gi 1054401713 339 SYHGKKSFETFSHRR 353
Cdd:cd07150   433 REGGEWSMEEFTELK 447

ALDH_LactADH-AldA

cd07088

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...

25-316

8.49e-68

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: 221.37 E-value: 8.49e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  25 LYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTEL 103
Cdd:cd07088   127 IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDA 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 104 L--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDP 181
Cdd:cd07088   207 LvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHE 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 182 SIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAATR--YIAPTILTDVDP 253
Cdd:cd07088   287 DIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgyFYEPTVLTNVRQ 366

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN 316
Cdd:cd07088   367 DMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429

ALDH_EDX86601

cd07102

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...

1-354

1.40e-67

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: 220.20 E-value: 1.40e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   1 MIQKLPEWAADEPVEKTPQTqqdELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELS----ENMASL 76
Cdd:cd07102    89 MISIAEEALADIRVPEKDGF---ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAAA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  77 LATI-IPqyldKDLYPVINGGVPETTELLKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDV 154
Cdd:cd07102   166 FAEAgLP----EGVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDA 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 155 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQ 228
Cdd:cd07102   242 AAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaiakGA 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 229 KVAYGG----TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKM 304
Cdd:cd07102   322 RALIDGalfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEAL 401

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054401713 305 IAETSSGGVAAN--DVIVhitlHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07102   402 GEQLETGTVFMNrcDYLD----PALAWTGVKDSGRGVTLSRLGYDQLTRPKS 449

ALDH_AAS00426

cd07109

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...

26-347

1.41e-67

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: 1.41e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL 104
Cdd:cd07109   112 YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAAL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 KE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07109   192 VAhpGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRS 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKLKKSLKEF---YGEDakkSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT--GDAATR--YIAPTILTD 250
Cdd:cd07109   272 IYDEVLERLVERFRALrvgPGLE---DPDLGPLISAKQLDRVEGFVArararGARIVAGGRiaEGAPAGgyFVAPTLLDD 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 251 VDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAND------Vivhitl 324
Cdd:cd07109   349 VPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNygagggI------ 422

                         330       340
                  ....*....|....*....|....
gi 1054401713 325 hSLPFGGVGNSGmgsyHGK-KSFE 347
Cdd:cd07109   423 -ELPFGGVKKSG----HGReKGLE 441

ALDH_ALD2-YMR170C

cd07144

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...

9-349

1.21e-66

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: 218.82 E-value: 1.21e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   9 AADEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LD 86
Cdd:cd07144   121 WADKIQGKTIPTSPNKLaYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFP 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  87 KDLYPVINGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF 164
Cdd:cd07144   201 PGVVNIIPGYGAVAGSALAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIM 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 165 MNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY--GEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT-- 235
Cdd:cd07144   281 YNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEkgkkeGAKLVYGGEka 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 236 --GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 313
Cdd:cd07144   361 peGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMV 440

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1054401713 314 ---AANDVIVHItlhslPFGGVGNSGMGSYHGKKSFETF 349
Cdd:cd07144   441 winSSNDSDVGV-----PFGGFKMSGIGRELGEYGLETY 474

ALDH_CddD_SSP0762

cd07138

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...

27-349

6.44e-64

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: 210.82 E-value: 6.44e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  27 IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELLK 105
Cdd:cd07138   126 VVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALS 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 106 E--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSI 183
Cdd:cd07138   206 AhpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSR 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 184 QNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTG--DAATR--YIAPTILTDVDP 253
Cdd:cd07138   286 YAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIqkgieEGARLVAGGPGrpEGLERgyFVKPTVFADVTP 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHItlhSLPFGGVG 333
Cdd:cd07138   366 DMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYK 442

                         330
                  ....*....|....*.
gi 1054401713 334 NSGMGSYHGKKSFETF 349
Cdd:cd07138   443 QSGNGREWGRYGLEEF 458

ALDH_SNDH

cd07118

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...

30-357

8.82e-64

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: 210.27 E-value: 8.82e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELLKE-- 106
Cdd:cd07118   118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEhp 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQ 186
Cdd:cd07118   198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 187 IVEKLK-KSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG--TGDAATRYIAPTILTDVDPQSPVM 258
Cdd:cd07118   278 FVAAVVaRSRKVRVGDPLDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGerLASAAGLFYQPTIFTDVTPDMAIA 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 259 QEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIkKMIAETSSGGVAANDVIVhiTLHSLPFGGVGNSGM 337
Cdd:cd07118   358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDiDTAL-TVARRIRAGTVWVNTFLD--GSPELPFGGFKQSGI 434

                         330       340
                  ....*....|....*....|
gi 1054401713 338 GSYHGKKSFETFSHRRSCLV 357
Cdd:cd07118   435 GRELGRYGVEEYTELKTVHL 454

ALDH_DhaS

cd07114

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...

30-354

1.01e-62

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: 207.79 E-value: 1.01e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELLKE-- 106
Cdd:cd07114   118 EPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEhp 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQ 186
Cdd:cd07114   198 LVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDE 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 187 IVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-----TGDAATRYIAPTILTDVDP 253
Cdd:cd07114   278 FVERLVaraRAIR--VGDPLDPETQMGPLATERQLEKVERYVarareEGARVLTGGerpsgADLGAGYFFEPTILADVTN 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDviVHITLHSLPFGGVG 333
Cdd:cd07114   356 DMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALSPSSPFGGFK 433

                         330       340
                  ....*....|....*....|.
gi 1054401713 334 NSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07114   434 DSGIGRENGIEAIREYTQTKS 454

ALDH_BenzADH

cd07152

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...

31-353

3.50e-62

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: 205.99 E-value: 3.50e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKP---SELSENMasLLATIIPQY-LDKDLYPVINGGvPETTELLKE 106
Cdd:cd07152   110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV--VIARLFEEAgLPAGVLHVLPGG-ADAGEALVE 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 --RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQ 184
Cdd:cd07152   187 dpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVA 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 185 NQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAatRYIAPTILTDVDPQSPVM 258
Cdd:cd07152   267 DAYTAKLAAKAKHLpVGDPATGQVALGPLINARQLDRVHAIVDdsvaaGARLEAGGTYDG--LFYRPTVLSGVKPGMPAF 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 259 QEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSlPFGGVGNSGMG 338
Cdd:cd07152   345 DEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHN-PFGGMGASGNG 423

                         330
                  ....*....|....*.
gi 1054401713 339 SYHG-KKSFETFSHRR 353
Cdd:cd07152   424 SRFGgPANWEEFTQWQ 439

ALDH_ABALDH-YdcW

cd07092

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...

26-338

4.85e-62

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: 205.64 E-value: 4.85e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELL- 104
Cdd:cd07092   113 MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALv 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 -KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSI 183
Cdd:cd07092   193 aHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESV 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 184 QNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE----GQKVAYGG-TGDAATRYIAPTILTDVDPQSPV 257
Cdd:cd07092   273 YDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGrRAEGPGYFYEPTVVAGVAQDDEI 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 258 MQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDvivHITLHS-LPFGGVGNSG 336
Cdd:cd07092   353 VQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHGGFKQSG 429


                  ..
gi 1054401713 337 MG 338
Cdd:cd07092   430 YG 431

ALDH_F9_TMBADH

cd07090

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...

26-358

5.51e-62

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: 205.62 E-value: 5.51e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGvPETTELL 104
Cdd:cd07090   111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQLL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 KERFD--HILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07090   190 CEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRS 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKL-KKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGT------GDAATRYIAPTILTD 250
Cdd:cd07090   270 IKDEFTERLvERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIesakqEGAKVLCGGErvvpedGLENGFYVSPCVLTD 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 251 VDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDviVHITLHSLPFG 330
Cdd:cd07090   350 CTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPFG 427

                         330       340
                  ....*....|....*....|....*...
gi 1054401713 331 GVGNSGMGSYHGKKSFETFSHRRSCLVR 358
Cdd:cd07090   428 GYKQSGFGRENGTAALEHYTQLKTVYVE 455

ALDH_KGSADH-YcbD

cd07097

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...

24-339

5.81e-61

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: 203.63 E-value: 5.81e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  24 ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldkdlypvinGGVPETT-- 101
Cdd:cd07097   128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEE-----------AGLPAGVfn 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 102 -----------ELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 169
Cdd:cd07097   197 lvmgsgsevgqALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQ 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 170 TCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDA 238
Cdd:cd07097   277 RCTASSRLIVTEGIHDRFVEALVertKALK--VGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGerlKRPD 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 239 ATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDV 318
Cdd:cd07097   355 EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLP 434

                         330       340
                  ....*....|....*....|.
gi 1054401713 319 IVHITLHsLPFGGVGNSGMGS 339
Cdd:cd07097   435 TAGVDYH-VPFGGRKGSSYGP 454

ALDH_HMSADH_HapE

cd07115

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...

26-354

9.44e-61

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: 202.28 E-value: 9.44e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL 104
Cdd:cd07115   112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAAL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 KER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07115   192 VEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKL---KKSLKefYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATR-YIAPTILTDVDP 253
Cdd:cd07115   272 IYDEFLERFtslARSLR--PGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfFVEPTIFAAVPP 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvIVHITLHSLPFGGVG 333
Cdd:cd07115   350 EMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYK 427

                         330       340
                  ....*....|....*....|.
gi 1054401713 334 NSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07115   428 QSGFGREMGREALDEYTEVKS 448

ALDH_GABALDH-PuuC

cd07112

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...

9-338

3.82e-60

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.

Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 200.91 E-value: 3.82e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   9 AADEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI-----IP 82
Cdd:cd07112   101 AIDKVYGEVAPTGPDALaLITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  83 qyldKDLYPVINGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNC-DLDVACRR 158
Cdd:cd07112   181 ----AGVLNVVPGFGHTAGEALGLHmdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 159 IAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDA-KKSRDYGRIISARHFQRVMGLI-----EGQKVAY 232
Cdd:cd07112   257 AAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMGALVSEAHFDKVLGYIesgkaEGARLVA 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 233 GGTGDAATR---YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETS 309
Cdd:cd07112   337 GGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLR 416

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1054401713 310 SGGVAAN-----DVIVhitlhslPFGGVGNSGMG 338
Cdd:cd07112   417 AGTVWVNcfdegDITT-------PFGGFKQSGNG 443

ALDH_HBenzADH

cd07151

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...

24-350

3.90e-60

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: 200.99 E-value: 3.90e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  24 ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLL-ATIIPQY-LDKDLYPVINGGVPETT 101
Cdd:cd07151   123 ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLlAKIFEEAgLPKGVLNVVVGAGSEIG 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 102 ELLKE----RFdhILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYI 177
Cdd:cd07151   203 DAFVEhpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRI 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 178 LCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIEgQKVAYGGT----GDAATRYIAPTILTDVD 252
Cdd:cd07151   281 IVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIE-QAVEEGATllvgGEAEGNVLEPTVLSDVT 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 253 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHsLPFGGV 332
Cdd:cd07151   360 NDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPH-VPFGGE 438

                         330
                  ....*....|....*...
gi 1054401713 333 GNSGMGSYHGKKSFETFS 350
Cdd:cd07151   439 KNSGLGRFNGEWALEEFT 456

ALDH_MGR_2402

cd07108

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...

26-357

6.97e-60

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: 200.28 E-value: 6.97e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLK 105
Cdd:cd07108   112 YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAALV 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 106 ER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRR-IAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07108   192 DHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAGMRFTRQGQSCTAGSRLFVHED 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE------GQKVAYGGTGDAATR-----YIAPTILTD 250
Cdd:cd07108   272 IYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGGPLPGEGPladgfFVQPTIFSG 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 251 VDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDviVHITLHSLPFG 330
Cdd:cd07108   352 VDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ--GGGQQPGQSYG 429

                         330       340       350
                  ....*....|....*....|....*....|
gi 1054401713 331 GVGNSGMG---SYHGkkSFETFSHRRSCLV 357
Cdd:cd07108   430 GFKQSGLGreaSLEG--MLEHFTQKKTVNI 457

ALDH_AldA-AAD23400

cd07106

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...

11-343

9.28e-60

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: 199.68 E-value: 9.28e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  11 DEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLY 90
Cdd:cd07106    94 DLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  91 PVINGGvPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSG 168
Cdd:cd07106   174 NVVSGG-DELGPALTShpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSG 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 169 QTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAATRY 242
Cdd:cd07106   253 QVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdakakGAKVLAGGEPLDGPGY 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 243 -IAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN---DV 318
Cdd:cd07106   333 fIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINthgAL 412

                         330       340
                  ....*....|....*....|....*
gi 1054401713 319 IVHItlhslPFGGVGNSGMGSYHGK 343
Cdd:cd07106   413 DPDA-----PFGGHKQSGIGVEFGI 432

ALDH_F1-2_Ald2-like

cd07091

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...

16-338

1.10e-59

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: 200.13 E-value: 1.10e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  16 KTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPqyldKDLYP--- 91
Cdd:cd07091   125 KTIPIDGNFLaYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK----EAGFPpgv 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  92 --VINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMN 166
Cdd:cd07091   201 vnIVPGFGPTAGAAISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFN 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 167 SGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGT--GDA 238
Cdd:cd07091   281 QGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIesgkkEGATLLTGGErhGSK 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 239 ATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAND- 317
Cdd:cd07091   361 GY-FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTy 439

                         330       340
                  ....*....|....*....|.
gi 1054401713 318 VIVHitlHSLPFGGVGNSGMG 338
Cdd:cd07091   440 NVFD---AAVPFGGFKQSGFG 457

ALDH_y4uC

cd07149

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...

30-338

4.34e-59

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: 198.20 E-value: 4.34e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQ-YLDKDLYPVINGGVPET-TELLK-E 106
Cdd:cd07149   122 EPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVgDALVTdP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 RFDHILYTGSTGVGKIIMTAAAkhLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQ 186
Cdd:cd07149   202 RVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDE 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 187 IVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAAtrYIAPTILTDVDPQSPVMQE 260
Cdd:cd07149   280 FLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEeavegGARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCE 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 261 EIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDV----IVHitlhsLPFGGVGNSG 336
Cdd:cd07149   358 EVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSstfrVDH-----MPYGGVKESG 432


                  ..
gi 1054401713 337 MG 338
Cdd:cd07149   433 TG 434

PLN02278

succinic semialdehyde dehydrogenase

7-349

3.52e-58

succinic semialdehyde dehydrogenase

Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 196.84 E-value: 3.52e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPV----EKTPQTQQD-ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI- 80
Cdd:PLN02278  131 EYFAEEAKrvygDIIPSPFPDrRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELa 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 ----IPQyldkDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDV 154
Cdd:PLN02278  211 lqagIPP----GVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDV 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 155 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQ 228
Cdd:PLN02278  287 AVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVqdavsKGA 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 229 KVAYGGT--GDAATRYiAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIA 306
Cdd:PLN02278  367 KVLLGGKrhSLGGTFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSE 445

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1054401713 307 ETSSGGVAANDVIvhITLHSLPFGGVGNSGMGSYHGKKSFETF 349
Cdd:PLN02278  446 ALEYGIVGVNEGL--ISTEVAPFGGVKQSGLGREGSKYGIDEY 486

ALDH_AldA-Rv0768

cd07139

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...

9-349

1.60e-57

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: 194.33 E-value: 1.60e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   9 AADEPVEKTPQTQQ-DELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldK 87
Cdd:cd07139   114 ARDFPFEERRPGSGgGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEE---A 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  88 DLYP----VINGGVpETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 161
Cdd:cd07139   191 GLPPgvvnVVPADR-EVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVP 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 162 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYG 233
Cdd:cd07139   270 ASLMNNGQVCVALTRILVPRSRYDEVVEALAaavAALK--VGDPLDPATQIGPLASARQRERVEGYIakgraEGARLVTG 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 234 GTGDAA-TR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSND----KVIKKMia 306
Cdd:cd07139   348 GGRPAGlDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVerglAVARRI-- 425

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1054401713 307 etSSGGVAANDVIVHItlhSLPFGGVGNSGMGSYHGKKSFETF 349
Cdd:cd07139   426 --RTGTVGVNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463

ALDH_PhpJ

cd07146

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...

26-342

2.09e-57

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: 193.73 E-value: 2.09e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL 104
Cdd:cd07146   115 FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDEL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 --KERFDHILYTGSTGVGKIIM-TAAAKHLTpvtLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDP 181
Cdd:cd07146   195 itHPDVDLVTFTGGVAVGKAIAaTAGYKRQL---LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 182 SIQNQIVEKL-KKSLKEFYGEDAKKSRDYGRIIS---ARHFQ-RVMGLIE-GQKVAYGGTGDAAtrYIAPTILTDVDPQS 255
Cdd:cd07146   272 SVADEFVDLLvEKSAALVVGDPMDPATDMGTVIDeeaAIQIEnRVEEAIAqGARVLLGNQRQGA--LYAPTVLDHVPPDA 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 256 PVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDViVHITLHSLPFGGVGNS 335
Cdd:cd07146   350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDS 428


                  ....*..
gi 1054401713 336 GMGSYHG 342
Cdd:cd07146   429 GLGGKEG 435

ALDH_BADH-GbsA

cd07119

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...

26-350

2.07e-56

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: 191.76 E-value: 2.07e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL 104
Cdd:cd07119   129 RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAEL 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 KE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07119   209 AEspDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEES 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKLKKSLKEF---YGEDAkkSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDAATR--YIAPTILT 249
Cdd:cd07119   289 IHDKFVAALAERAKKIklgNGLDA--DTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGkrpTGDELAKgyFVEPTIFD 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 250 DVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDviVHITLHSLPF 329
Cdd:cd07119   367 DVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPW 444

                         330       340
                  ....*....|....*....|.
gi 1054401713 330 GGVGNSGMGSYHGKKSFETFS 350
Cdd:cd07119   445 GGYKQSGIGRELGPTGLEEYQ 465

ALDH_LactADH_F420-Bios

cd07145

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...

13-338

6.52e-56

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: 6.52e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  13 PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYP 91
Cdd:cd07145   105 PVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVIN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  92 VINGGVPET-TELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 169
Cdd:cd07145   185 VVTGYGSEVgDEIVTnPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQ 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 170 TCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATrYI 243
Cdd:cd07145   265 VCNAVKRILVEEEVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYGGKRDEGS-FF 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 244 APTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDViVHIT 323
Cdd:cd07145   344 PPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-TRFR 422

                         330
                  ....*....|....*
gi 1054401713 324 LHSLPFGGVGNSGMG 338
Cdd:cd07145   423 WDNLPFGGFKKSGIG 437

ALDH_PutA-P5CDH-RocA

cd07124

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...

7-339

1.05e-55

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: 190.51 E-value: 1.05e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPVEKTPQTQQDELYIHS----EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIp 82
Cdd:cd07124   138 EYYAREMLRLRGFPVEMVPGEDNryvyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIL- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  83 qyLDKDLYP-VIN--GGVPET-----TELLKERFdhILYTGSTGVGKIIMTAAAK------HLTPVTLELGGKSPCYVDK 148
Cdd:cd07124   217 --EEAGLPPgVVNflPGPGEEvgdylVEHPDVRF--IAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDE 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 149 NCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLI 225
Cdd:cd07124   293 DADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVertKALK--VGDPEDPEVYMGPVIDKGARDRIRRYI 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 226 E----GQKVAYGGTGDA-ATR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSND 298
Cdd:cd07124   371 EigksEGRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSP 450

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1054401713 299 KVIKKMIAETSSGGVAAND------VIVHitlhslPFGGVGNSGMGS 339
Cdd:cd07124   451 EHLERARREFEVGNLYANRkitgalVGRQ------PFGGFKMSGTGS 491

PRK10090

aldehyde dehydrogenase A; Provisional

7-311

1.83e-55

aldehyde dehydrogenase A; Provisional

Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 187.25 E-value: 1.83e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPVEKTPQTQQDE-LYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY- 84
Cdd:PRK10090   46 EWARRYEGEIIQSDRPGEnILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIg 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  85 LDKDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWG 162
Cdd:PRK10090  126 LPKGVFNLVLGRGETVGQELagNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDS 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 163 KFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSR-DYGRIISARHFQRVMGLI-----EGQKVAYGGT 235
Cdd:PRK10090  206 RVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVqFGNPAERNDiAMGPLINAAALERVEQKVaraveEGARVALGGK 285

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054401713 236 GDAATRYI-APTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSG 311
Cdd:PRK10090  286 AVEGKGYYyPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362

ALDH_AldH-CAJ73105

cd07131

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...

31-354

7.76e-55

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: 187.55 E-value: 7.76e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSElsenMASLLATIIPQYLDKDLYP--VIN---GGVPETTELLK 105
Cdd:cd07131   135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAE----DTPACALKLVELFAEAGLPpgVVNvvhGRGEEVGEALV 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 106 E--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSI 183
Cdd:cd07131   211 EhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESV 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 184 QNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDAATR--YIAPTILTDVD 252
Cdd:cd07131   291 YDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNeigkeEGATLLLGGerlTGGGYEKgyFVEPTVFTDVT 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 253 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHsLPFGGV 332
Cdd:cd07131   371 PDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVH-LPFGGV 449

                         330       340
                  ....*....|....*....|...
gi 1054401713 333 GNSGMGSYH-GKKSFETFSHRRS 354
Cdd:cd07131   450 KKSGNGHREaGTTALDAFTEWKA 472

ALDH_SSADH1_GabD1

cd07100

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...

6-346

7.80e-55

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: 186.13 E-value: 7.80e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   6 PEWAADEPVEktpqTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY- 84
Cdd:cd07100    75 EAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAg 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  85 LDKDLYPVINGGVPETTELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGK 163
Cdd:cd07100   151 FPEGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 164 FMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT-- 235
Cdd:cd07100   231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLGPLARKDLRDELHEQVEeavaaGATLLLGGKrp 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 236 -GDAAtrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVA 314
Cdd:cd07100   311 dGPGA--FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1054401713 315 ANDVIVhiTLHSLPFGGVGNSGMG---SYHGKKSF 346
Cdd:cd07100   389 INGMVK--SDPRLPFGGVKRSGYGrelGRFGIREF 421

ALDH_SSADH2_GabD2

cd07101

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...

20-343

1.82e-54

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: 185.98 E-value: 1.82e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  20 TQQDELYihsEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASLLATI---IPQYLDKDLYPVINGG 96
Cdd:cd07101   110 TRTTVNR---RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTALTALWAVellIEAGLPRDLWQVVTGP 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  97 VPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDY 176
Cdd:cd07101   185 GSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIER 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 177 ILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTG--DAATRYIAPTIL 248
Cdd:cd07101   265 IYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdavakGATVLAGGRArpDLGPYFYEPTVL 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 249 TDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVhITLHSL- 327
Cdd:cd07101   345 TGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYA-AAWASId 423

                         330
                  ....*....|....*..
gi 1054401713 328 -PFGGVGNSGMGSYHGK 343
Cdd:cd07101   424 aPMGGMKDSGLGRRHGA 440

ALDH_ACDHII_AcoD-like

cd07559

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...

19-357

2.88e-54

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: 186.01 E-value: 2.88e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  19 QTQQDELYIH-SEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGV 97
Cdd:cd07559   123 EIDEDTLSYHfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFG 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  98 PETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYV-----DKNCDLDVACRRIAWGKFMNSGQT 170
Cdd:cd07559   203 SEAGKPLAShpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEV 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 171 CVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-----TGDAA 239
Cdd:cd07559   283 CTCPSRALVQESIYDEFIERAVERFEAIkVGNPLDPETMMGAQVSKDQLEKILSYVdigkeEGAEVLTGGerltlGGLDK 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 240 TRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvi 319
Cdd:cd07559   363 GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--- 439

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1054401713 320 vhiTLHSLP----FGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07559   440 ---CYHQYPahapFGGYKKSGIGRETHKMMLDHYQQTKNILV 478

ALDH_F10_BADH

cd07110

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...

26-338

5.85e-54

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: 184.48 E-value: 5.85e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL 104
Cdd:cd07110   115 RVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 KE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07110   195 AAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHES 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATR---YIAPTILTDVDP 253
Cdd:cd07110   275 IADAFLERLATAAEAIrVGDPLEEGVRLGPLVSQAQYEKVLSFIargkeEGARLLCGGRRPAHLEkgyFIAPTVFADVPT 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLpivCVRSL---EEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvIVHITLHSLPFG 330
Cdd:cd07110   355 DSRIWREEIFGPVL---CVRSFateDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWG 429


                  ....*...
gi 1054401713 331 GVGNSGMG 338
Cdd:cd07110   430 GYKRSGIG 437

PRK03137

1-pyrroline-5-carboxylate dehydrogenase; Provisional

7-339

2.53e-53

1-pyrroline-5-carboxylate dehydrogenase; Provisional

Pssm-ID: 179543 Cd Length: 514 Bit Score: 184.37 E-value: 2.53e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPVEKTPQTQQDELYIhsePLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-L 85
Cdd:PRK03137  150 KLADGKPVESRPGEHNRYFYI---PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgL 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  86 DKDLYPVINGGVPETTELL----KERFdhILYTGSTGVGKIIMTAAAK------HLTPVTLELGGKSPCYVDKNCDLDVA 155
Cdd:PRK03137  227 PAGVVNFVPGSGSEVGDYLvdhpKTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLA 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 156 CRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKV 230
Cdd:PRK03137  305 AESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEigkeeGRLV 384

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 231 AYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 310
Cdd:PRK03137  385 LGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHV 464

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1054401713 311 GGVAAND------VIVHitlhslPFGGVGNSGMGS 339
Cdd:PRK03137  465 GNLYFNRgctgaiVGYH------PFGGFNMSGTDS 493

PLN02467

betaine aldehyde dehydrogenase

26-351

3.71e-53

betaine aldehyde dehydrogenase

Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 183.78 E-value: 3.71e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELsenmASL----LATIIPQY-LDKDLYPVINGGVPET 100
Cdd:PLN02467  146 YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSEL----ASVtcleLADICREVgLPPGVLNVVTGLGTEA 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 101 TELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYIL 178
Cdd:PLN02467  222 GAPLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLL 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 179 CDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGT---GDAATRYIAPTILT 249
Cdd:PLN02467  302 VHERIASEFLEKLVKWAKNIkISDPLEEGCRLGPVVSEGQYEKVLKFIstaksEGATILCGGKrpeHLKKGFFIEPTIIT 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 250 DVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvIVHITLHSLPF 329
Cdd:PLN02467  382 DVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPW 459

                         330       340
                  ....*....|....*....|..
gi 1054401713 330 GGVGNSGMGSYHGKKSFETFSH 351
Cdd:PLN02467  460 GGIKRSGFGRELGEWGLENYLS 481

ALDH_AldA_AN0554

cd07143

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...

8-358

5.00e-53

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: 182.73 E-value: 5.00e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   8 WAaDEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-L 85
Cdd:cd07143   121 WA-DKIHGQVIETDIKKLtYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgF 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  86 DKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWG 162
Cdd:cd07143   200 PPGVINVVSGYGRTCGNAISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYG 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 163 KFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT- 235
Cdd:cd07143   280 IFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLkVGDPFAEDTFQGPQVSQIQYERIMSYIEsgkaeGATVETGGKr 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 236 -GDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVA 314
Cdd:cd07143   360 hGNEGY-FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVW 438

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1054401713 315 ANDV-IVHitlHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVR 358
Cdd:cd07143   439 VNCYnLLH---HQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480

PRK13473

aminobutyraldehyde dehydrogenase;

26-339

1.27e-52

aminobutyraldehyde dehydrogenase;

Pssm-ID: 237391 Cd Length: 475 Bit Score: 181.65 E-value: 1.27e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyldKDLYP--VIN---GGVPET 100
Cdd:PRK13473  133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELA-----ADILPpgVLNvvtGRGATV 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 101 TELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYIL 178
Cdd:PRK13473  208 GDALvgHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 179 CDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE---GQK----VAYGGTGDAATRYIAPTIL 248
Cdd:PRK13473  288 AQRGIYDDLVAKLAaavATLK--VGDPDDEDTELGPLISAAHRDRVAGFVErakALGhirvVTGGEAPDGKGYYYEPTLL 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 249 TDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDvivHITLHS-L 327
Cdd:PRK13473  366 AGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMLVSeM 442

                         330
                  ....*....|..
gi 1054401713 328 PFGGVGNSGMGS 339
Cdd:PRK13473  443 PHGGQKQSGYGK 454

BADH

TIGR01804

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...

15-350

3.91e-52

Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 180.01 E-value: 3.91e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  15 EKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVI 93
Cdd:TIGR01804 117 EIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVV 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  94 NGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTC 171
Cdd:TIGR01804 197 QGDGAEVGPLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVC 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 172 VAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-------TGDA 238
Cdd:TIGR01804 277 SNGTRVFVHKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIekgkaEGATLATGGgrpenvgLQNG 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 239 AtrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDv 318
Cdd:TIGR01804 357 F--FVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT- 433

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1054401713 319 iVHITLHSLPFGGVGNSGMGSYHGKKSFETFS 350
Cdd:TIGR01804 434 -YNLYPAEAPFGGYKQSGIGRENGKAALAHYT 464

ALDH_PhdK-like

cd07107

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...

30-358

1.04e-50

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: 176.03 E-value: 1.04e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKERFD 109
Cdd:cd07107   115 EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPD 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 110 --HILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGkfMN---SGQTCVAPDYILCDPSIQ 184
Cdd:cd07107   195 vkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNftwCGQSCGSTSRLFVHESIY 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 185 NQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDAATR--YIAPTILTDVDP 253
Cdd:cd07107   273 DEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrpEGPALEGgfYVEPTVFADVTP 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITlhSLPFGGVG 333
Cdd:cd07107   353 GMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVK 430

                         330       340
                  ....*....|....*....|....*
gi 1054401713 334 NSGMGSYHGKKSFETFSHRRSCLVR 358
Cdd:cd07107   431 NSGIGREECLEELLSYTQEKNVNVR 455

ALDH_F2BC

cd07142

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...

8-354

1.34e-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: 176.15 E-value: 1.34e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   8 WAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LD 86
Cdd:cd07142   118 WADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLP 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  87 KDLYPVINGGVPETTELLKERF--DHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGK 163
Cdd:cd07142   198 DGVLNIVTGFGPTAGAAIASHMdvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFAL 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 164 FMNSGQTCVAPDYILCDPSIQNQIVEKLK-KSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG--T 235
Cdd:cd07142   278 FFNQGQCCCAGSRTFVHESIYDEFVEKAKaRALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIehgkeEGATLITGGdrI 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 236 GDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAA 315
Cdd:cd07142   358 GSKGY-YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWV 436

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1054401713 316 NdvIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07142   437 N--CYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKA 473

gabD2

PRK09407

succinic semialdehyde dehydrogenase; Reviewed

20-342

1.91e-50

succinic semialdehyde dehydrogenase; Reviewed

Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 176.61 E-value: 1.91e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  20 TQQDELYIhsePLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASLLATIIPQY---LDKDLYPVINGG 96
Cdd:PRK09407  146 TKTTELRQ---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTPLTALAAVELLYeagLPRDLWQVVTGP 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  97 VPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDY 176
Cdd:PRK09407  221 GPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 177 ILCDPSIQNQIVEKL---KKSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTG--DAATRYIAPT 246
Cdd:PRK09407  301 IYVHESIYDEFVRAFvaaVRAMR--LGAGYDYSADMGSLISEAQLETVSAHVDdavakGATVLAGGKArpDLGPLFYEPT 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 247 ILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVhITLHS 326
Cdd:PRK09407  379 VLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYA-AAWGS 457

                         330
                  ....*....|....*...
gi 1054401713 327 L--PFGGVGNSGMGSYHG 342
Cdd:PRK09407  458 VdaPMGGMKDSGLGRRHG 475

ALDH_StaphAldA1

cd07117

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...

27-357

2.38e-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: 175.72 E-value: 2.38e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  27 IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKE 106
Cdd:cd07117   132 VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLN 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 R--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQ 184
Cdd:cd07117   212 HpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIY 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 185 NQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-----TGDAATRYIAPTILTDVDP 253
Cdd:cd07117   292 DEFVAKLKEKFENVkVGNPLDPDTQMGAQVNKDQLDKILSYVdiakeEGAKILTGGhrlteNGLDKGFFIEPTLIVNVTN 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvIVHITLHSLPFGGVG 333
Cdd:cd07117   372 DMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYK 449

                         330       340
                  ....*....|....*....|....
gi 1054401713 334 NSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07117   450 KSGIGRETHKSMLDAYTQMKNIYI 473

ALDH_F7_AASADH-like

cd07086

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...

31-357

3.68e-50

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: 175.06 E-value: 3.68e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPF-----NLTIqpmvgAIAAGNSVVLKPSELsenmASLLATIIPQYL-----DKDLYP----VINGG 96
Cdd:cd07086   133 PLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSET----TPLTAIAVTKILaevleKNGLPPgvvnLVTGG 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  97 VpETTELLK--ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAP 174
Cdd:cd07086   204 G-DGGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTT 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 175 DYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG---TGDAATRYIAP 245
Cdd:cd07086   283 RRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEiaksqGGTVLTGGkriDGGEPGNYVEP 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 246 TILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIKKMIAETSSGGvaandvIVHITL 324
Cdd:cd07086   363 TIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDlREAFRWLGPKGSDCG------IVNVNI 436

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1054401713 325 HS------LPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07086   437 PTsgaeigGAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475

ALDH_F11_NP-GAPDH

cd07082

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...

13-354

1.00e-49

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: 173.91 E-value: 1.00e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  13 PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYP 91
Cdd:cd07082   123 PGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVN 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  92 VINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKhlTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 169
Cdd:cd07082   203 VVTGRGREIGDPLVThgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQ 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 170 TCVAPDYILCDPSIQNQIVEKLKK---SLKEFYGEDA---------KKSRDYgriisarhfqrVMGLIE-----GQKVAY 232
Cdd:cd07082   281 RCTAIKRVLVHESVADELVELLKEevaKLKVGMPWDNgvditplidPKSADF-----------VEGLIDdavakGATVLN 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 233 GGTGDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGG 312
Cdd:cd07082   350 GGGREGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGT 428

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1054401713 313 VAANDVIVHITLHsLPFGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:cd07082   429 VNINSKCQRGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKG 469

ALDH_F21_LactADH-like

cd07094

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...

30-338

1.34e-49

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: 173.00 E-value: 1.34e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII-PQYLDKDLYPVINGGVPETTELL--KE 106
Cdd:cd07094   122 EPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTGEREVLGDAFaaDE 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 RFDHILYTGSTGVGKIIMTAAAKhlTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILcdpsiqnq 186
Cdd:cd07094   202 RVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIY-------- 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 187 IVEKLKKSLKEFYGEDAKKSR---------DYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAATRYiaPTILTDVD 252
Cdd:cd07094   272 VHEELYDEFIEAFVAAVKKLKvgdpldedtDVGPLISEEAAERVERWVEeaveaGARLLCGGERDGALFK--PTVLEDVP 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 253 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDViVHITLHSLPFGGV 332
Cdd:cd07094   350 RDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGV 428


                  ....*.
gi 1054401713 333 GNSGMG 338
Cdd:cd07094   429 KESGVG 434

ALDH_PsfA-ACA09737

cd07120

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...

27-350

3.20e-49

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: 172.14 E-value: 3.20e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  27 IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQ--YLDKDLYPVINGGVPETTELL 104
Cdd:cd07120   113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 KE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07120   193 VAspDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRS 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE------GQKVAYGGTGD---AATRYIAPTILTDVD 252
Cdd:cd07120   273 IADEVRDRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVDRMVEraiaagAEVVLRGGPVTeglAKGAFLRPTLLEVDD 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 253 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDvivHITLHS-LPFGG 331
Cdd:cd07120   353 PDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLFAeAEEGG 429

                         330
                  ....*....|....*....
gi 1054401713 332 VGNSGMGSYHGKKSFETFS 350
Cdd:cd07120   430 YRQSGLGRLHGVAALEDFI 448

ALDH_PADH_NahF

cd07113

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...

30-358

6.89e-47

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: 166.46 E-value: 6.89e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSE----NMASLL--ATIIPQYLDkdlypVINGGVPETTEL 103
Cdd:cd07113   141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPltllRVAELAkeAGIPDGVLN-----VVNGKGAVGAQL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 104 LKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:cd07113   216 ISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATRY-IAPTILTDVDPQS 255
Cdd:cd07113   296 KFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEALAGEGYfVQPTLVLARSADS 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 256 PVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdviVHITLH-SLPFGGVGN 334
Cdd:cd07113   376 RLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQ 452

                         330       340
                  ....*....|....*....|....
gi 1054401713 335 SGMGSYHGKKSFETFSHRRSCLVR 358
Cdd:cd07113   453 SGIGREFGSAFIDDYTELKSVMIR 476

ALDH_F1AB_F2_RALDH1

cd07141

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...

26-350

3.26e-46

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: 164.44 E-value: 3.26e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldkDLYP--VIN---GGVPET 100
Cdd:cd07141   140 YTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKE----AGFPpgVVNvvpGYGPTA 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 101 TELLKER--FDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYI 177
Cdd:cd07141   216 GAAISSHpdIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRT 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 178 LCDPSIQNQIVEK-LKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGT--GDAATrYIAPTILT 249
Cdd:cd07141   296 FVQESIYDEFVKRsVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIesgkkEGAKLECGGKrhGDKGY-FIQPTVFS 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 250 DVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIkkmiaeTSSGGVAANDVIV----HITL 324
Cdd:cd07141   375 DVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDiDKAI------TFSNALRAGTVWVncynVVSP 448

                         330       340
                  ....*....|....*....|....*.
gi 1054401713 325 HSlPFGGVGNSGMGSYHGKKSFETFS 350
Cdd:cd07141   449 QA-PFGGYKMSGNGRELGEYGLQEYT 473

ALDH_F21_RNP123

cd07147

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...

7-338

6.48e-46

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: 163.19 E-value: 6.48e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADE---------PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLL 77
Cdd:cd07147    90 RIAAEEatriygevlPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALIL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  78 ATII-PQYLDKDLYPVINGGVPETTELLK-ERFDHILYTGSTGVGKIIMTAAAKHltPVTLELGGKSPCYVDKNCDLDVA 155
Cdd:cd07147   170 GEVLaETGLPKGAFSVLPCSRDDADLLVTdERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFA 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 156 CRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKL---KKSLKEfyGEDAKKSRDYGRIISARHFQRVMGLIE-----G 227
Cdd:cd07147   248 AQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLvarVKALKT--GDPKDDATDVGPMISESEAERVEGWVNeavdaG 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 228 QKVAYGGTGDAATryIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAE 307
Cdd:cd07147   326 AKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDE 403

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1054401713 308 TSSGGVAANDVIVhITLHSLPFGGVGNSGMG 338
Cdd:cd07147   404 LEVGGVVINDVPT-FRVDHMPYGGVKDSGIG 433

ALDH_F16

cd07111

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...

19-343

2.54e-45

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: 162.18 E-value: 2.54e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  19 QTQQDELYIHsEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldKDLYP-VIN--G 95
Cdd:cd07111   136 QLLDTELAGW-KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAE---AGLPPgVLNivT 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  96 GVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVA 173
Cdd:cd07111   212 GNGSFGSALANhpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCA 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 174 PDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIEGQKvAYGG----TGDAATR---YIAP 245
Cdd:cd07111   292 GSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGAdvfqPGADLPSkgpFYPP 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 246 TILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDvivhitlH 325
Cdd:cd07111   371 TLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING-------H 443

                         330       340
                  ....*....|....*....|...
gi 1054401713 326 SL-----PFGGVGNSGMGSYHGK 343
Cdd:cd07111   444 NLfdaaaGFGGYRESGFGREGGK 466

ALDH_F6_MMSDH

cd07085

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...

30-353

7.50e-44

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: 158.06 E-value: 7.50e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPF--NLTIQPMvgAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELLke 106
Cdd:cd07085   135 QPLGVVAGITPFNFPAmiPLWMFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAVNALL-- 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 rfDH-----ILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDP 181
Cdd:cd07085   211 --DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVG 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 182 SIQNQIVEKLK---KSLKEFYGEDAKKsrDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATRY-----IAPTIL 248
Cdd:cd07085   289 DEADEWIPKLVeraKKLKVGAGDDPGA--DMGPVISPAAKERIEGLIesgveEGAKLVLDGRGVKVPGYengnfVGPTIL 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 249 TDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdVIVHITLHSLP 328
Cdd:cd07085   367 DNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN-VPIPVPLAFFS 445

                         330       340
                  ....*....|....*....|....*..
gi 1054401713 329 FGGVGNSGMGSYH--GKKSFETFSHRR 353
Cdd:cd07085   446 FGGWKGSFFGDLHfyGKDGVRFYTQTK 472

PRK09847

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional

9-350

1.65e-43

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional

Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 157.75 E-value: 1.65e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   9 AADEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LD 86
Cdd:PRK09847  134 AIDKVYGEVATTSSHELaMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLP 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  87 KDLYPVINGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNC-DLDVACRRIAWG 162
Cdd:PRK09847  214 DGVLNVVTGFGHEAGQALSRHndIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAG 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 163 KFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLIEG----QKVAYGGTGD 237
Cdd:PRK09847  294 IFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIREgeskGQLLLDGRNA 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 238 AATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN- 316
Cdd:PRK09847  374 GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNn 453

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1054401713 317 ----DVIVhitlhslPFGGVGNSGMGSYHGKKSFETFS 350
Cdd:PRK09847  454 yndgDMTV-------PFGGYKQSGNGRDKSLHALEKFT 484

PLN02466

aldehyde dehydrogenase family 2 member

30-362

2.52e-43

aldehyde dehydrogenase family 2 member

Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 158.05 E-value: 2.52e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSE---LSENMASLL---ATIIPQYLDkdlypVINGGVPETTEL 103
Cdd:PLN02466  194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEqtpLSALYAAKLlheAGLPPGVLN-----VVSGFGPTAGAA 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 104 LKERF--DHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCD 180
Cdd:PLN02466  269 LASHMdvDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 181 PSIQNQIVEKLK-KSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGtGDAATR--YIAPTILTDVD 252
Cdd:PLN02466  349 ERVYDEFVEKAKaRALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKsgvesGATLECGG-DRFGSKgyYIQPTVFSNVQ 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 253 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN--DVIVhitlHSLPFG 330
Cdd:PLN02466  428 DDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD----AAIPFG 503

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1054401713 331 GVGNSGMGSYHGKKSFETFSHRRScLVRPLMN 362
Cdd:PLN02466  504 GYKMSGIGREKGIYSLNNYLQVKA-VVTPLKN 534

PLN02766

coniferyl-aldehyde dehydrogenase

26-362

5.99e-43

coniferyl-aldehyde dehydrogenase

Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 156.13 E-value: 5.99e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKD-LYPVINGGVPETTELL 104
Cdd:PLN02766  153 YTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDgVINVVTGFGPTAGAAI 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 KERFD--HILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDP 181
Cdd:PLN02766  233 ASHMDvdKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQE 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 182 SIQNQIVEKLKKSLKEFYGEDAKKSR-DYGRIISARHFQRVMGLI-----EGQKVAYGG--TGDAATrYIAPTILTDVDP 253
Cdd:PLN02766  313 GIYDEFVKKLVEKAKDWVVGDPFDPRaRQGPQVDKQQFEKILSYIehgkrEGATLLTGGkpCGDKGY-YIEPTIFTDVTE 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVikkmiAETSSGGVAANDVIVHITL---HSLPFG 330
Cdd:PLN02766  392 DMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDV-----ANTVSRSIRAGTIWVNCYFafdPDCPFG 466

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1054401713 331 GVGNSGMGSYHGKKSFETFSHRRScLVRPLMN 362
Cdd:PLN02766  467 GYKMSGFGRDQGMDALDKYLQVKS-VVTPLYN 497

PRK13252

betaine aldehyde dehydrogenase; Provisional

26-357

8.57e-43

betaine aldehyde dehydrogenase; Provisional

Pssm-ID: 183918 Cd Length: 488 Bit Score: 155.42 E-value: 8.57e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPfnltIQ-------PmvgAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVING-G 96
Cdd:PRK13252  137 YTRREPLGVCAGIGAWNYP----IQiacwksaP---ALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGdG 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  97 vpETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAP 174
Cdd:PRK13252  210 --RVGAWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNG 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 175 DYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDAATR--YI 243
Cdd:PRK13252  288 TRVFVQKSIKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIekgkaEGARLLCGGerlTEGGFANgaFV 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 244 APTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN----DKVIKKMIAET----SSGGVAA 315
Cdd:PRK13252  368 APTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQLEAGIcwinTWGESPA 447

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1054401713 316 ndvivhitlhSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:PRK13252  448 ----------EMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479

ALDH_P5CDH

cd07083

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...

31-342

3.42e-40

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: 148.88 E-value: 3.42e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSElsenMASLLATIIPQYLDKDLYP--VINGgVPETTELL---- 104
Cdd:cd07083   154 GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAE----DAVVVGYKVFEIFHEAGFPpgVVQF-LPGVGEEVgayl 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 --KERFDHILYTGSTGVGKIIMTAAAKHLT------PVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDY 176
Cdd:cd07083   229 teHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASR 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 177 ILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAATRYIAPTILTD 250
Cdd:cd07083   309 LILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEhgkneGQLVLGGKRLEGEGYFVAPTVVEE 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 251 VDPQSPVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLP 328
Cdd:cd07083   389 VPPKARIAQEEIFGPVLSVIRYKDddFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQP 468

                         330
                  ....*....|....
gi 1054401713 329 FGGVGNSGMGSYHG 342
Cdd:cd07083   469 FGGFKLSGTNAKTG 482

ALDH_F1L_FTFDH

cd07140

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...

26-338

4.32e-38

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: 142.63 E-value: 4.32e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSenmaSLLATIIPQYLDKDLYP--VINGgVPETTEL 103
Cdd:cd07140   142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVT----PLTALKFAELTVKAGFPkgVINI-LPGSGSL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 104 LKERF-DH-----ILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDY 176
Cdd:cd07140   217 VGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGR 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 177 ILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVM-----GLIEGQKVAYGGTG-DAATRYIAPTILT 249
Cdd:cd07140   297 LFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVeycerGVKEGATLVYGGKQvDRPGFFFEPTVFT 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 250 DVDPQSPVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSsndKVIKKmiAETSSGGVAANDVIVHI---TL 324
Cdd:cd07140   377 DVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFT---KDINK--ALYVSDKLEAGTVFVNTynkTD 451

                         330
                  ....*....|....
gi 1054401713 325 HSLPFGGVGNSGMG 338
Cdd:cd07140   452 VAAPFGGFKQSGFG 465

gabD

PRK11241

NADP-dependent succinate-semialdehyde dehydrogenase I;

7-349

6.50e-37

NADP-dependent succinate-semialdehyde dehydrogenase I;

Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 139.27 E-value: 6.50e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADEPV----EKTPQTQQDE-LYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI- 80
Cdd:PRK11241  117 EWFAEEGKriygDTIPGHQADKrLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELa 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 ----IPqyldKDLYPVINGGVPET-TELLKERFDHIL-YTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDV 154
Cdd:PRK11241  197 iragIP----AGVFNVVTGSAGAVgGELTSNPLVRKLsFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDK 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 155 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLIE-----GQ 228
Cdd:PRK11241  273 AVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEEHIAdalekGA 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 229 KVAYGGTGDA-ATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAE 307
Cdd:PRK11241  353 RVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEA 432

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1054401713 308 TSSGGVAANDVIvhITLHSLPFGGVGNSGMGSYHGKKSFETF 349
Cdd:PRK11241  433 LEYGIVGINTGI--ISNEVAPFGGIKASGLGREGSKYGIEDY 472

ALDH_ACDHII-AcoD

cd07116

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...

26-357

9.07e-35

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: 133.35 E-value: 9.07e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  26 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELL- 104
Cdd:cd07116   131 YHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLa 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 -KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSP--CYVDKNCDLDVACRRIAWGKFM---NSGQTCVAPDYIL 178
Cdd:cd07116   211 sSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniFFADVMDADDAFFDKALEGFVMfalNQGEVCTCPSRAL 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 179 CDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-----TGDAATRYIAPTI 247
Cdd:cd07116   291 IQESIYDRFMERALERVKAIkQGNPLDTETMIGAQASLEQLEKILSYIdigkeEGAEVLTGGernelGGLLGGGYYVPTT 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 248 LTDVDpQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvIVHITLHSL 327
Cdd:cd07116   371 FKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHA 447

                         330       340       350
                  ....*....|....*....|....*....|
gi 1054401713 328 PFGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:cd07116   448 AFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477

PRK13968

putative succinate semialdehyde dehydrogenase; Provisional

27-338

2.19e-34

putative succinate semialdehyde dehydrogenase; Provisional

Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 132.29 E-value: 2.19e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  27 IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELLK 105
Cdd:PRK13968  122 IEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQMIN 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 106 E-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQ 184
Cdd:PRK13968  202 DsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIA 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 185 NQIVEKL---KKSLKefYGEDAKKSRDYGRIisAR-------HFQRVMGLIEGQKVAYGGTGDA-ATRYIAPTILTDVDP 253
Cdd:PRK13968  282 SAFTERFvaaAAALK--MGDPRDEENALGPM--ARfdlrdelHHQVEATLAEGARLLLGGEKIAgAGNYYAPTVLANVTP 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 254 QSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV-----AANDVIVhitlhslP 328
Cdd:PRK13968  358 EMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVfingyCASDARV-------A 430

                         330
                  ....*....|
gi 1054401713 329 FGGVGNSGMG 338
Cdd:PRK13968  431 FGGVKKSGFG 440

ALDH_SGSD_AstD

cd07095

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...

31-336

2.93e-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: 128.54 E-value: 2.93e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII-PQYLDKDLYPVINGGVPETTELLK-ERF 108
Cdd:cd07095    97 PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLVQGGRETGEALAAhEGI 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 109 DHILYTGSTGVGKIIMTAAAKHltP---VTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCV-APDYILCDPSIQ 184
Cdd:cd07095   177 DGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTcARRLIVPDGAVG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 185 NQIVEKLKKSLKEFY--GEDAKKSRDYGRIISA------RHFQRVMGLiEGQKVAYGGTGDAATRYIAPTILtDVDPQSP 256
Cdd:cd07095   255 DAFLERLVEAAKRLRigAPDAEPPFMGPLIIAAaaarylLAQQDLLAL-GGEPLLAMERLVAGTAFLSPGII-DVTDAAD 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 257 VMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdviVHITLHS--LPFGGVGN 334
Cdd:cd07095   333 VPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN---RPTTGASstAPFGGVGL 409


                  ..
gi 1054401713 335 SG 336
Cdd:cd07095   410 SG 411

PLN00412

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional

31-339

5.42e-30

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional

Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 120.25 E-value: 5.42e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASLLATI-------IPqyldKDLYPVINGGVPETTEL 103
Cdd:PLN00412  158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP--TQGAVAALHMVhcfhlagFP----KGLISCVTGKGSEIGDF 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 104 LKER--FDHILYTG-STGvgkiIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCD 180
Cdd:PLN00412  232 LTMHpgVNCISFTGgDTG----IAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVM 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 181 PSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKvAYGGTgdAATRY------IAPTILTDVDPQ 254
Cdd:PLN00412  308 ESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAK-EKGAT--FCQEWkregnlIWPLLLDNVRPD 384

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 255 SPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIkkMIAET-SSGGVAANDVIVHITLHsLPFGGV 332
Cdd:PLN00412  385 MRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAI--LISDAmETGTVQINSAPARGPDH-FPFQGL 461


                  ....*..
gi 1054401713 333 GNSGMGS 339
Cdd:PLN00412  462 KDSGIGS 468

ALDH_PutA-P5CDH

cd07125

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...

30-338

6.16e-30

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: 120.38 E-value: 6.16e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI-----IPQYLdkdLYPVINGGVPETTELL 104
Cdd:cd07125   166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELlheagVPRDV---LQLVPGDGEEIGEALV 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 K-ERFDHILYTGSTGVGKIIMTAAAKH---LTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDyILCd 180
Cdd:cd07125   243 AhPRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALR-LLY- 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 181 psIQNQIVEKLKKSLKefygeDAKKS----------RDYGRIISARHFQRVMGLIE---GQK--VAYGGTGDAATRYIAP 245
Cdd:cd07125   321 --LQEEIAERFIEMLK-----GAMASlkvgdpwdlsTDVGPLIDKPAGKLLRAHTElmrGEAwlIAPAPLDDGNGYFVAP 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 246 TILTDVDpqSPVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHIT 323
Cdd:cd07125   394 GIIEIVG--IFDLTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAI 471

                         330
                  ....*....|....*
gi 1054401713 324 LHSLPFGGVGNSGMG 338
Cdd:cd07125   472 VGRQPFGGWGLSGTG 486

ALDH_F7_AASADH

cd07130

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...

27-297

1.61e-29

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: 118.85 E-value: 1.61e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  27 IHSE-----------PLGVVLVIGTWNYP-----FNLTIqpmvgAIAAGNSVVLKPSELsenmASLLA----TIIPQYLD 86
Cdd:cd07130   117 IPSErpghrmmeqwnPLGVVGVITAFNFPvavwgWNAAI-----ALVCGNVVVWKPSPT----TPLTAiavtKIVARVLE 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  87 K-----DLYPVINGGVPETTELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 160
Cdd:cd07130   188 KnglpgAIASLVCGGADVGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVL 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 161 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG 234
Cdd:cd07130   268 FAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVrIGDPLDDGTLVGPLHTKAAVDNYLAAIEeaksqGGTVLFGG 347

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054401713 235 TG-DAATRYIAPTILTdVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN 297
Cdd:cd07130   348 KViDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTD 410

ALDH_RL0313

cd07148

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...

7-338

3.20e-29

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: 117.52 E-value: 3.20e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   7 EWAADE---------PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASLL 77
Cdd:cd07148    91 ELAADElgqlggreiPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA--LATPLSCL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  78 ATIipqyldkDLypVINGGVPE-----------TTELL--KERFDHILYTGSTGVGKIIMTAAAKHlTPVTLELGGKSPC 144
Cdd:cd07148   169 AFV-------DL--LHEAGLPEgwcqavpcenaVAEKLvtDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPV 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 145 YVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKL-KKSLKEFYGEDAKKSRDYGRIISARHFQRVMG 223
Cdd:cd07148   239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLaAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 224 LIE-----GQKVAYGGTGDAATRYiAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSND 298
Cdd:cd07148   319 WVNeavaaGARLLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDL 397

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1054401713 299 KVIKKMIAETSSGGVAANDvivhitlHS------LPFGGVGNSGMG 338
Cdd:cd07148   398 DVALKAVRRLDATAVMVND-------HTafrvdwMPFAGRRQSGYG 436

gabD1

PRK09406

succinic semialdehyde dehydrogenase; Reviewed

3-346

6.66e-29

succinic semialdehyde dehydrogenase; Reviewed

Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 116.76 E-value: 6.66e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   3 QKLPEWAADEPVEkTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPselsenmasllATIIP 82
Cdd:PRK09406   96 EHAEALLADEPAD-AAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH-----------ASNVP 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  83 Q---YLDkDLYPviNGGVPE---TTELL----------KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYV 146
Cdd:PRK09406  164 QtalYLA-DLFR--RAGFPDgcfQTLLVgsgaveailrDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 147 DKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI 225
Cdd:PRK09406  241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQV 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 226 E-----GQKVAYGGTG-DAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDK 299
Cdd:PRK09406  321 DdavaaGATILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054401713 300 VIKKMIAETSSGGVAANDVIVhiTLHSLPFGGVGNSGMG---SYHGKKSF 346
Cdd:PRK09406  401 EQERFIDDLEAGQVFINGMTV--SYPELPFGGVKRSGYGrelSAHGIREF 448

MMSDH

TIGR01722

methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...

15-341

7.06e-28

methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]

Pssm-ID: 130783 Cd Length: 477 Bit Score: 114.21 E-value: 7.06e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  15 EKTPQTQQD-ELYIHSEPLGVVLVIGTWNYP--FNLTIQPMvgAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLY 90
Cdd:TIGR01722 119 ETSTQVATRvDVYSIRQPLGVCAGITPFNFPamIPLWMFPI--AIACGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  91 PVINGGVPETTELLKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 169
Cdd:TIGR01722 197 NVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQ 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 170 TCVAPDYILCDPSIQN---QIVEKLKKsLKEFYGEDAkkSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATR 241
Cdd:TIGR01722 277 RCMAISAAVLVGAADEwvpEIRERAEK-IRIGPGDDP--GAEMGPLITPQAKDRVASLIaggaaEGAEVLLDGRGYKVDG 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 242 Y-----IAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN 316
Cdd:TIGR01722 354 YeegnwVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN 433

                         330       340
                  ....*....|....*....|....*.
gi 1054401713 317 DVI-VHITLHSlpFGGVGNSGMGSYH 341
Cdd:TIGR01722 434 VPIpVPLPYFS--FTGWKDSFFGDHH 457

D1pyr5carbox3

TIGR01238

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...

30-342

6.65e-24

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: 102.68 E-value: 6.65e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldkdlypvinGGVPETT-ELL---- 104
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQE-----------AGFPAGTiQLLpgrg 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 105 ---------KERFDHILYTGSTGVGKIIMTAAAKHL---TPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCV 172
Cdd:TIGR01238 228 advgaaltsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCS 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 173 APDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIEG----QKVAYGGTGDAATR-----Y 242
Cdd:TIGR01238 308 ALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAEAKQNLLAHIEHmsqtQKKIAQLTLDDSRAcqhgtF 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 243 IAPTI--LTDVDPqspvMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDV 318
Cdd:TIGR01238 388 VAPTLfeLDDIAE----LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRN 463

                         330       340
                  ....*....|....*....|....
gi 1054401713 319 IVHITLHSLPFGGVGNSGMGSYHG 342
Cdd:TIGR01238 464 QVGAVVGVQPFGGQGLSGTGPKAG 487

astD

PRK09457

succinylglutamic semialdehyde dehydrogenase; Reviewed

31-336

7.38e-24

succinylglutamic semialdehyde dehydrogenase; Reviewed

Pssm-ID: 181873 Cd Length: 487 Bit Score: 102.73 E-value: 7.38e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIipqYLDKDLYP-VIN--GGVPETTELL--K 105
Cdd:PRK09457  134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKL---WQQAGLPAgVLNlvQGGRETGKALaaH 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 106 ERFDHILYTGSTGVGKIIMTAAAKHltP---VTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 182
Cdd:PRK09457  211 PDIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQG 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 183 IQNQ-IVEKLKKSLKEF-YGE-DAKKSRDYGRIISARHFQrvmGLIEGQK--VAYGGTG-------DAATRYIAPTILtD 250
Cdd:PRK09457  289 AQGDaFLARLVAVAKRLtVGRwDAEPQPFMGAVISEQAAQ---GLVAAQAqlLALGGKSllemtqlQAGTGLLTPGII-D 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 251 VDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITlHSLPFG 330
Cdd:PRK09457  365 VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGAS-SAAPFG 443


                  ....*.
gi 1054401713 331 GVGNSG 336
Cdd:PRK09457  444 GVGASG 449

PLN02315

aldehyde dehydrogenase family 7 member

31-357

2.03e-22

aldehyde dehydrogenase family 7 member

Pssm-ID: 177949 Cd Length: 508 Bit Score: 98.37 E-value: 2.03e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYP-----FNLTIqpmvgAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP-----VINGGVPET 100
Cdd:PLN02315  154 PLGIVGVITAFNFPcavlgWNACI-----ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPgaiftSFCGGAEIG 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 101 TELLKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILC 179
Cdd:PLN02315  229 EAIAKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 180 DPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRI---ISARHFQRVMGLIEGQ--KVAYGGTG-DAATRYIAPTILtDVD 252
Cdd:PLN02315  309 HESIYDDVLEQLLTVYKQVkIGDPLEKGTLLGPLhtpESKKNFEKGIEIIKSQggKILTGGSAiESEGNFVQPTIV-EIS 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 253 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdviVHITLHSL----P 328
Cdd:PLN02315  388 PDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVN---VNIPTNGAeiggA 464

                         330       340
                  ....*....|....*....|....*....
gi 1054401713 329 FGGVGNSGMGSYHGKKSFETFSHRRSCLV 357
Cdd:PLN02315  465 FGGEKATGGGREAGSDSWKQYMRRSTCTI 493

PLN02419

methylmalonate-semialdehyde dehydrogenase [acylating]

24-354

2.48e-22

methylmalonate-semialdehyde dehydrogenase [acylating]

Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 98.67 E-value: 2.48e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  24 ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTEL 103
Cdd:PLN02419  242 DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 104 L--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILC-- 179
Cdd:PLN02419  322 IcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvg 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 180 -DPSIQNQIVEKlKKSLKEFYGedAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG-----TGDAATRYIAPTIL 248
Cdd:PLN02419  402 dAKSWEDKLVER-AKALKVTCG--SEPDADLGPVISKQAKERICRLIQsgvddGAKLLLDGrdivvPGYEKGNFIGPTIL 478

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 249 TDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdVIVHITLHSLP 328
Cdd:PLN02419  479 SGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN-VPIPVPLPFFS 557

                         330       340
                  ....*....|....*....|....*...
gi 1054401713 329 FGGVGNSGMG--SYHGKKSFETFSHRRS 354
Cdd:PLN02419  558 FTGNKASFAGdlNFYGKAGVDFFTQIKL 585

ALDH_F4-17_P5CDH

cd07123

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...

24-267

2.55e-22

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: 98.43 E-value: 2.55e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  24 ELYiHSEPLGVVlvIGTWN---Y-----------PFNLTiqpmvgAIAA---------GNSVVLKPSelseNMASLLATI 80
Cdd:cd07123   148 ELY-AQQPLSSP--AGVWNrleYrplegfvyavsPFNFT------AIGGnlagapalmGNVVLWKPS----DTAVLSNYL 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  81 IPQYLDKDLYP--VIN---GGVPETTE--LLKERFDHILYTGSTGVGKIIMTAAAKHLT-----P-VTLELGGKSPCYVD 147
Cdd:cd07123   215 VYKILEEAGLPpgVINfvpGDGPVVGDtvLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVH 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 148 KNCDLDVACRRIAWGKFMNSGQTCVAPD--YIlcdP-SIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMG 223
Cdd:cd07123   295 PSADVDSLVTATVRGAFEYQGQKCSAASraYV---PeSLWPEVKERLLEELKEIkMGDPDDFSNFMGAVIDEKAFDRIKG 371

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054401713 224 LIE------GQKVAYGGTGDAATRY-IAPTILTDVDPQSPVMQEEIFGPVL 267
Cdd:cd07123   372 YIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL 422

ALDH_KGSADH-like

cd07084

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...

11-342

6.80e-22

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: 96.54 E-value: 6.80e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  11 DEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKP----SELSENMASLL--ATIIPQy 84
Cdd:cd07084    80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhtavSIVMQIMVRLLhyAGLLPP- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  85 ldkDLYPVINGGVPETTELLKE-RFDHILYTGSTGVGKIImtAAAKHLTPVTLELGGKSPCYVDKNCD-LDVACRRIAWG 162
Cdd:cd07084   159 ---EDVTLINGDGKTMQALLLHpNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQD 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 163 KFMNSGQTCVAPDYILC--DPSIQnQIVEKLKkslkefygEDAKKSRDYGRIISARHFQRVMGLIE------GQKVAYGG 234
Cdd:cd07084   234 MTACSGQKCTAQSMLFVpeNWSKT-PLVEKLK--------ALLARRKLEDLLLGPVQTFTTLAMIAhmenllGSVLLFSG 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 235 T----GDAATRY---IAPTILTDVDP---QSPVMQEEIFGPVLPIVCVRSLEEA--IQFINQREKPLALYMFSSNDKVIK 302
Cdd:cd07084   305 KelknHSIPSIYgacVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQ 384

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1054401713 303 KMIAETSSGGVAandviVHITLhslpfgGVGNSGMGSYHG 342
Cdd:cd07084   385 ELIGNLWVAGRT-----YAILR------GRTGVAPNQNHG 413

putA

PRK11809

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...

31-338

2.14e-16

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

Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 81.17 E-value: 2.14e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyldkdlypvINGGVPE-TTELL----- 104
Cdd:PRK11809   768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL-----------LEAGVPAgVVQLLpgrge 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  105 --------KERFDHILYTGSTGVGKIIMTAAAKHL------TPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQT 170
Cdd:PRK11809   837 tvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR 916

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  171 CVAPDyILCdpsIQNQIVEK----LKKSLKEF-YGEDAKKSRDYGRIISA-------RHFQRVMGliEGQKV---AYGGT 235
Cdd:PRK11809   917 CSALR-VLC---LQDDVADRtlkmLRGAMAECrMGNPDRLSTDIGPVIDAeakanieRHIQAMRA--KGRPVfqaARENS 990

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  236 GDAAT-RYIAPTI--LTDVDPqspvMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 310
Cdd:PRK11809   991 EDWQSgTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHV 1066

                          330       340
                   ....*....|....*....|....*...
gi 1054401713  311 GGVAANDVIVHITLHSLPFGGVGNSGMG 338
Cdd:PRK11809  1067 GNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094

PRK11905

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

29-338

8.03e-15

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

Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 76.06 E-value: 8.03e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   29 SEPLGVVLVIGTWNYPfnLTIqpMVG----AIAAGNSVVLKPSELSENMASLLATIIPQyldkdlypvinGGVPETT-EL 103
Cdd:PRK11905   674 HKPLGPVVCISPWNFP--LAI--FTGqiaaALVAGNTVLAKPAEQTPLIAARAVRLLHE-----------AGVPKDAlQL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  104 L-------------KERFDHILYTGSTGVGKIIMTAAAKHLT-PVTL--ELGGKSPCYVDKNCDLDVACRRIAWGKFMNS 167
Cdd:PRK11905   739 LpgdgrtvgaalvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSA 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  168 GQTCVAPDyILCdpsIQNQIVEK----LKKSLKEFY-GEDAKKSRDYGRIISA-------RHFQRVMGliEGQKVAYGGT 235
Cdd:PRK11905   819 GQRCSALR-VLC---LQEDVADRvltmLKGAMDELRiGDPWRLSTDVGPVIDAeaqanieAHIEAMRA--AGRLVHQLPL 892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  236 GDAATR--YIAPTILtDVDPQSpVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSG 311
Cdd:PRK11905   893 PAETEKgtFVAPTLI-EIDSIS-DLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAG 970

                          330       340
                   ....*....|....*....|....*..
gi 1054401713  312 GVAANDVIVHITLHSLPFGGVGNSGMG 338
Cdd:PRK11905   971 NIYVNRNIIGAVVGVQPFGGEGLSGTG 997

ALDH_PAD-PaaZ

cd07127

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...

18-314

9.26e-12

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

Pssm-ID: 143445 Cd Length: 549 Bit Score: 66.35 E-value: 9.26e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  18 PQTQQDELYI----HSEPLGVVLVIG-----TWN-YPfnltiqPMVGAIAAGNSVVLKPSElsenmasllATIIPQYL-- 85
Cdd:cd07127   176 PQGKHDPLAMektfTVVPRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHP---------AAILPLAItv 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  86 ------------DKDLYPVI--NGGVPETTEL-LKERFDHILYTGSTGVGKIIMTAAAKHLtpVTLELGGKSPCYVDKNC 150
Cdd:cd07127   241 qvarevlaeagfDPNLVTLAadTPEEPIAQTLaTRPEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTD 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 151 DLDVACRRIAWGKFMNSGQTCVAPDYILCdPS--IQN--------QIVEKLKKSLKEFYGEDAKKSRDYG---------R 211
Cdd:cd07127   319 DLKAMLRNLAFSLSLYSGQMCTTPQNIYV-PRdgIQTddgrksfdEVAADLAAAIDGLLADPARAAALLGaiqspdtlaR 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 212 IISARHFQRVmgLIEGQKVAYGGTGDAATRyiAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQ--REK-P 288
Cdd:cd07127   398 IAEARQLGEV--LLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgA 473

                         330       340
                  ....*....|....*....|....*.
gi 1054401713 289 LALYMFSSNDKVIKKMIAETSSGGVA 314
Cdd:cd07127   474 MTVGVYSTDPEVVERVQEAALDAGVA 499

PutA2

COG4230

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

30-338

9.96e-11

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

Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 63.42 E-value: 9.96e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   30 EPLGVVLVIGTWNYPfnLTI---QpMVGAIAAGNSVVLKPSElsenMASLLATIIPQYLDKdlypvinGGVP-------- 98
Cdd:COG4230    679 RGRGVFVCISPWNFP--LAIftgQ-VAAALAAGNTVLAKPAE----QTPLIAARAVRLLHE-------AGVPadvlqllp 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   99 ---ETT--ELLK-ERFDHILYTGSTGVGKII-MTAAAKHLTPVTL--ELGGKSPCYVD------KNCDlDVacrrIAwGK 163
Cdd:COG4230    745 gdgETVgaALVAdPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDssalpeQVVD-DV----LA-SA 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  164 FMNSGQTCVAPDyILCdpsIQNQIVEK----LKKSLKEF-YGEDAKKSRDYGRIISA-------RHFQRVMGliEGQKVA 231
Cdd:COG4230    819 FDSAGQRCSALR-VLC---VQEDIADRvlemLKGAMAELrVGDPADLSTDVGPVIDAearanleAHIERMRA--EGRLVH 892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  232 YGGTGDAATR--YIAPTI--LTDVDpqspVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMI 305
Cdd:COG4230    893 QLPLPEECANgtFVAPTLieIDSIS----DLEREVFGPVLHVVRYKAdeLDKVIDAINATGYGLTLGVHSRIDETIDRVA 968

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1054401713  306 AETSSGGVAANDVIVHITLHSLPFGGVGNSGMG 338
Cdd:COG4230    969 ARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTG 1001

ALDH_KGSADH

cd07129

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...

31-286

1.69e-10

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: 62.17 E-value: 1.69e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIqpmVG-----AIAAGNSVVLK--PS--ELSEnmasLLATIIPQYLDKDLYP-----VINGG 96
Cdd:cd07129   105 PLGPVAVFGASNFPLAFSV---AGgdtasALAAGCPVVVKahPAhpGTSE----LVARAIRAALRATGLPagvfsLLQGG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  97 VPET-TELLKerfdH-----ILYTGSTGVGKIIMTAAAKHLT--PVTLELGGKSPCYVDKNCdldVACRRIAWGK-F--- 164
Cdd:cd07129   178 GREVgVALVK----HpaikaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFILPGA---LAERGEAIAQgFvgs 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 165 --MNSGQTCVAPDYILcdpSIQNQIVEKLKKSLKEFYGEDAKksrdyGRIIS---ARHFQRVMGLIEGQK----VAYGGT 235
Cdd:cd07129   251 ltLGAGQFCTNPGLVL---VPAGPAGDAFIAALAEALAAAPA-----QTMLTpgiAEAYRQGVEALAAAPgvrvLAGGAA 322

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054401713 236 GDAATRYiAPTILTdVDPQS----PVMQEEIFGPVLPIVCVRSLEEAIQFINQRE 286
Cdd:cd07129   323 AEGGNQA-APTLFK-VDAAAfladPALQEEVFGPASLVVRYDDAAELLAVAEALE 375

PRK11904

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

24-338

2.56e-10

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

Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 62.14 E-value: 2.56e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713   24 ELYIHsePLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSElsenMASLLATIIPQYLDKdlypvinGGVPETT-E 102
Cdd:PRK11904   679 ELRLH--GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE----QTPLIAAEAVKLLHE-------AGIPKDVlQ 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  103 LL-------------KERFDHILYTGSTGVGKII-MTAAAKHLTPVTL--ELGGKSPCYVDKNCDLDVACRRIAWGKFMN 166
Cdd:PRK11904   746 LLpgdgatvgaaltaDPRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRS 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  167 SGQTCVAPDyILCdpsIQNQIVEK----LKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE----GQKVAYGGTGD 237
Cdd:PRK11904   826 AGQRCSALR-VLF---VQEDIADRviemLKGAMAELkVGDPRLLSTDVGPVIDAEAKANLDAHIErmkrEARLLAQLPLP 901

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  238 AATR---YIAPTI--LTDVDpqspVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 310
Cdd:PRK11904   902 AGTEnghFVAPTAfeIDSIS----QLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRV 977

                          330       340
                   ....*....|....*....|....*...
gi 1054401713  311 GGVAANDVIVHITLHSLPFGGVGNSGMG 338
Cdd:PRK11904   978 GNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005

ALDH_F20_ACDH_EutE-like

cd07081

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...

15-304

7.32e-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: 57.28 E-value: 7.32e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  15 EKTPQT-QQDELY---IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYL----- 85
Cdd:cd07081    75 EKTCGVlTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaaga 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  86 DKDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKiimtAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGK 163
Cdd:cd07081   155 PENLIGWIDNPSIELAQRLmkFPGIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSK 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 164 FMNSGQTCVAPDYILCDPSIQNQIVEKLK-KSLKEFYGEDAKKSRDYgrIISARHFQR-VMGLIEGQKVAYGGTGDAATR 241
Cdd:cd07081   231 TFDNGVICASEQSVIVVDSVYDEVMRLFEgQGAYKLTAEELQQVQPV--ILKNGDVNRdIVGQDAYKIAAAAGLKVPQET 308

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054401713 242 YIAPTILTDVDPQSPVMQEEIfGPVLPIVCVRSLEEAIqfinqrEKPLALY----------MFSSNDKVIKKM 304
Cdd:cd07081   309 RILIGEVTSLAEHEPFAHEKL-SPVLAMYRAANFADAD------AKALALKleggcghtsaMYSDNIKAIENM 374

ALDH-like

cd07077

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...

14-197

5.80e-07

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

Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 51.07 E-value: 5.80e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  14 VEKTPQT---QQDELYIHSEPLGVVLVIGTWNYPFnLTIQPMVGAIAAGNSVVLKPSELSENMASLLA----TIIPQYLD 86
Cdd:cd07077    80 VGHIQDVllpDNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALAllfqAADAAHGP 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  87 KDLYPVINGGVPETTE-LLK-ERFDHILYTGSTGVGKiimtAAAKH--LTPVTLELGGKSPCYVDKNCDLDVACRRIAWG 162
Cdd:cd07077   159 KILVLYVPHPSDELAEeLLShPKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1054401713 163 KFMNsGQTCVAPDYILCDPSIQNQIVEKLKKSLKE 197
Cdd:cd07077   235 KFFD-QNACASEQNLYVVDDVLDPLYEEFKLKLVV 268

ALDH_F20_ACDH

cd07122

Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ...

30-303

1.24e-06

Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.

Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.18 E-value: 1.24e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  30 EPLGVVL-VIGTWNyP-----FNLTIqpmvgAIAAGNSVVLKPS----ELSENMASLL-ATIIPQYLDKDLYPVI-NGGV 97
Cdd:cd07122    94 EPVGVIAaLIPSTN-PtstaiFKALI-----ALKTRNAIIFSPHprakKCSIEAAKIMrEAAVAAGAPEGLIQWIeEPSI 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  98 PETTELLK-ERFDHILYTGSTGVGKiimtAAAKHLTPVtleLG---GKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVA 173
Cdd:cd07122   168 ELTQELMKhPDVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 174 PDYILCDPSIQNQIVEKLKKS----LKEfygEDAKKSRDY---------GRII--SARHFQRVMGLiegqKVAYGgtgda 238
Cdd:cd07122   241 EQSVIVDDEIYDEVRAELKRRgayfLNE---EEKEKLEKAlfddggtlnPDIVgkSAQKIAELAGI----EVPED----- 308

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054401713 239 aTRYIAPTIlTDVDPQSPVMQEEIFgPVLPIVCVRSLEEAIqfinqrEKPLALYMF----------SSNDKVIKK 303
Cdd:cd07122   309 -TKVLVAEE-TGVGPEEPLSREKLS-PVLAFYRAEDFEEAL------EKARELLEYggaghtavihSNDEEVIEE 374

LuxC

pfam05893

Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ...

21-307

1.57e-06

Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.

Pssm-ID: 399113 Cd Length: 401 Bit Score: 49.75 E-value: 1.57e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  21 QQDELYIHSEPLGVVLVIGTWNYPFnLTIQPMVGAIAAGNSVVLKPSELSENMAS-LLATIIPQYLDKDLYPVI-----N 94
Cdd:pfam05893  78 PTKPSYEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSSDPFTAAaLLASFADLDPTHPLADSLsvvywD 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  95 GGVPETTELLKERFDHILYTGstgvGKIIMTAAAKHLTPVT--LELGGK-SPCYVDKNCDLDVACRRIAWGKFMNSGQTC 171
Cdd:pfam05893 157 GGSTQLEDLIVANADVVIAWG----GEDAINAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAADDICVFDQQAC 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 172 VAPDYILCDPSIQNQI---VEKLKKSLK---EFYgEDAKKSRDYG-RIISARHFQRV-MGLIEGQKVaYGGTGDAATryi 243
Cdd:pfam05893 233 LSPQTVFVESDDKITPdefAERLAAALAkraRIL-PKAVLDIDEAaKISSDRAECKLdYAFAGERGV-WSDFHQRWT--- 307

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054401713 244 apTILTDVDPQSPvmqeEIFGPVLPIVCVRSLEEAIQFINQREKPL---ALYMFSSNDKVIKKMIAE 307
Cdd:pfam05893 308 --VIWSDGQEELN----SPLNRTVNVVPVPSLSDVVRYVSENRTYLqtcGLAPYSGRLPYLDRKLAL 368

ALDH_MaoC-N

cd07128

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...

33-310

5.78e-06

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: 48.03 E-value: 5.78e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  33 GVVLVIGTWNYPfnltIQPMVGAIA----AGNSVVLKPSELSENMASLLATIIpqyLDKDLYP-----VINGGVPETTEL 103
Cdd:cd07128   146 GVAVHINAFNFP----VWGMLEKFApallAGVPVIVKPATATAYLTEAVVKDI---VESGLLPegalqLICGSVGDLLDH 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 104 LKERfDHILYTGSTGVGKIIMT--AAAKHLTPVTLE--------LGgksPCYVDKNCDLDVACRRIAWGKFMNSGQTCVA 173
Cdd:cd07128   219 LGEQ-DVVAFTGSAATAAKLRAhpNIVARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTA 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 174 PDYILCDPSIQNQIVEKLKKSL-KEFYGEDAKKSRDYGRIISARHFQRVMG----LIEGQKVAYGGTGDAATR------- 241
Cdd:cd07128   295 IRRAFVPEARVDAVIEALKARLaKVVVGDPRLEGVRMGPLVSREQREDVRAavatLLAEAEVVFGGPDRFEVVgadaekg 374

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054401713 242 -YIAPTILT--DVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 310
Cdd:cd07128   375 aFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAP 446

ALDH_F12_P5CDH

cd07126

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...

31-234

1.44e-05

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.

Pssm-ID: 143444 Cd Length: 489 Bit Score: 46.72 E-value: 1.44e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  31 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKP----SELSENMASLLATIIPQYLDKDLypvINGGVPETTELLKE 106
Cdd:cd07126   142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVdskvSVVMEQFLRLLHLCGMPATDVDL---IHSDGPTMNKILLE 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 107 -RFDHILYTGSTGV---------GKIIMTAAA---KHLTPVTLELGgkspcYVDKNCDLDV-ACrriawgkfmnSGQTCV 172
Cdd:cd07126   219 aNPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDAyAC----------SGQKCS 283

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054401713 173 APDYILCDPS-IQNQIVEKLKKSLKEFYGEDAK----KSRDYGRIISarHFQRVMGlIEGQKVAYGG 234
Cdd:cd07126   284 AQSILFAHENwVQAGILDKLKALAEQRKLEDLTigpvLTWTTERILD--HVDKLLA-IPGAKVLFGG 347

PRK11903

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;

167-354

2.91e-04

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;

Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 42.77 E-value: 2.91e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 167 SGQTCVAPDYILCDPSIQNQIVEKLKKSL-KEFYGEDAKKSRDYGRIISARHFQRVM----GLIEGQKVAYGGTG----- 236
Cdd:PRK11903  292 SGQKCTAIRRIFVPEALYDAVAEALAARLaKTTVGNPRNDGVRMGPLVSRAQLAAVRaglaALRAQAEVLFDGGGfalvd 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 237 -DAATRY-IAPTIL--TDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAE--TSS 310
Cdd:PRK11903  372 aDPAVAAcVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALElaDSH 451

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054401713 311 GGVAA--NDVIVHITLHS--LP---FGGVGNSGMGSYHGKKSFETFSHRRS 354
Cdd:PRK11903  452 GRVHVisPDVAALHTGHGnvMPqslHGGPGRAGGGEELGGLRALAFYHRRS 502

PRK15398

aldehyde dehydrogenase;

53-279

4.14e-04

aldehyde dehydrogenase;

Pssm-ID: 237956 Cd Length: 465 Bit Score: 42.20 E-value: 4.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713  53 VGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP-----VINGGVPETTELLkerFDH-----ILYTGSTGVGKI 122
Cdd:PRK15398  151 ISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGGPenlvvTVAEPTIETAQRL---MKHpgialLVVTGGPAVVKA 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 123 IMT-------AAAkhltpvtlelgGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIV------- 188
Cdd:PRK15398  228 AMKsgkkaigAGA-----------GNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMrlmekng 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054401713 189 ---------EKLKKSL--------KEFYGEDAKKsrdygriisarhfqrvmgLIEgqkvAYGGTGDAATRyiapTILTDV 251
Cdd:PRK15398  297 avlltaeqaEKLQKVVlknggtvnKKWVGKDAAK------------------ILE----AAGINVPKDTR----LLIVET 350

                         250       260
                  ....*....|....*....|....*...
gi 1054401713 252 DPQSPVMQEEIFGPVLPIVCVRSLEEAI 279
Cdd:PRK15398  351 DANHPFVVTELMMPVLPVVRVKDVDEAI 378

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