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Conserved domains on  [gi|489529552|ref|WP_003434286|]
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aldo/keto reductase [Clostridioides difficile]

Protein Classification

aldo/keto reductase( domain architecture ID 11444628)

aldo/keto reductase is a soluble NAD(P)(H) oxidoreductase that catalyzes the reduction of aldehydes and ketones to their corresponding primary and secondary alcohols

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
6-373 4.14e-112

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


:

Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 331.40  E-value: 4.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPIKDEndvttidmEHLNKMVDTFLERGFTYFDTAYVYHmgKSEIALRESLvkRHKRESFTIATKLPLmALKK 85
Cdd:COG1453   16 LGFGGMRLPRKDE--------EEAEALIRRAIDNGINYIDTARGYG--DSEEFLGKAL--KGPRDKVILATKLPP-WVRD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  86 KEEQETIFNEQLEKCGVDYFDYYLLHNIGVSH-----------YEVAKK--------FdsfkfieekkkegkiknIGFSF 146
Cdd:COG1453   83 PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEdlekvlkpggaLEALEKakaegkirH-----------------IGFST 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 147 HDSAELLDKVLsEHPEVDFVQLQINYLDWDNESiqSRKCYEVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNdynPDMS 226
Cdd:COG1453  146 HGSLEVIKEAI-DTGDFDFVQLQYNYLDQDNQA--GEEALEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLC---PPLS 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 227 ISSWAIRFAASKDNVMMVLSGMSNMEQLLDNTGYMQNFKPFVQEEYNIIDEAVEIINESILIPCTACQYCVEgCPKNIAI 306
Cdd:COG1453  220 PAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLEPLTEEELAILERLAEELGELLKDFCTGCGYCMP-CPQGINI 298
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529552 307 PNYFALYNaEKQALNTGFSTQMVYYNNYTKTygKASDCIECKQCEESCPQHIKIIDALKNVAETFEK 373
Cdd:COG1453  299 PEVFRLYN-LARAYGMREYAKERYNALGPGA--KASACIECGACEERCPQGLDIPELLKEAHELLGG 362
 
Name Accession Description Interval E-value
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
6-373 4.14e-112

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 331.40  E-value: 4.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPIKDEndvttidmEHLNKMVDTFLERGFTYFDTAYVYHmgKSEIALRESLvkRHKRESFTIATKLPLmALKK 85
Cdd:COG1453   16 LGFGGMRLPRKDE--------EEAEALIRRAIDNGINYIDTARGYG--DSEEFLGKAL--KGPRDKVILATKLPP-WVRD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  86 KEEQETIFNEQLEKCGVDYFDYYLLHNIGVSH-----------YEVAKK--------FdsfkfieekkkegkiknIGFSF 146
Cdd:COG1453   83 PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEdlekvlkpggaLEALEKakaegkirH-----------------IGFST 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 147 HDSAELLDKVLsEHPEVDFVQLQINYLDWDNESiqSRKCYEVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNdynPDMS 226
Cdd:COG1453  146 HGSLEVIKEAI-DTGDFDFVQLQYNYLDQDNQA--GEEALEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLC---PPLS 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 227 ISSWAIRFAASKDNVMMVLSGMSNMEQLLDNTGYMQNFKPFVQEEYNIIDEAVEIINESILIPCTACQYCVEgCPKNIAI 306
Cdd:COG1453  220 PAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLEPLTEEELAILERLAEELGELLKDFCTGCGYCMP-CPQGINI 298
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529552 307 PNYFALYNaEKQALNTGFSTQMVYYNNYTKTygKASDCIECKQCEESCPQHIKIIDALKNVAETFEK 373
Cdd:COG1453  299 PEVFRLYN-LARAYGMREYAKERYNALGPGA--KASACIECGACEERCPQGLDIPELLKEAHELLGG 362
AKR_Fe-S_oxidoreductase cd19096
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...
4-266 7.68e-103

Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381322 [Multi-domain]  Cd Length: 255  Bit Score: 303.71  E-value: 7.68e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   4 KKLGFGLMRLPIKDENdvtTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKLPLMAL 83
Cdd:cd19096    1 SVLGFGTMRLPESDDD---SIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEAL-KEGPREKFYLATKLPPWSV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  84 KKKEEQETIFNEQLEKCGVDYFDYYLLHNIG-VSHYEVAKKFDSFKFIEEKKKEGKIKNIGFSFHDSAELLDKVLSEHPe 162
Cdd:cd19096   77 KSAEDFRRILEESLKRLGVDYIDFYLLHGLNsPEWLEKARKGGLLEFLEKAKKEGLIRHIGFSFHDSPELLKEILDSYD- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 163 VDFVQLQINYLDWDNEsiQSRKCYEVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNDYnpDMSISSWAIRFAASKDNVM 242
Cdd:cd19096  156 FDFVQLQYNYLDQENQ--AGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGA--PLSPAEWALRFLLSHPEVT 231
                        250       260
                 ....*....|....*....|....
gi 489529552 243 MVLSGMSNMEQLLDNTGYMQNFKP 266
Cdd:cd19096  232 TVLSGMSTPEQLDENIAAADEFEP 255
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
6-279 8.87e-56

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.


Pssm-ID: 425554 [Multi-domain]  Cd Length: 290  Bit Score: 184.44  E-value: 8.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552    6 LGFGLMRLPIKDEndvtTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKR-HKRESFTIATKL-----P 79
Cdd:pfam00248   1 IGLGTWQLGGGWG----PISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYpVKRDKVVIATKVpdgdgP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   80 LMALKKKEEQETIFNEQLEKCGVDYFDYYLLHNIGVSHY--EVAKKFDSfkfieeKKKEGKIKNIGFSFHDsAELLDKVL 157
Cdd:pfam00248  77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPieETWDALEE------LKKEGKIRAIGVSNFD-AEQIEKAL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  158 sEHPEVDFVQLQINYLDWdnESIQSRKCYEVAEKHNKPVIVMEPVKGGTLAK--------------------------IP 211
Cdd:pfam00248 150 -TKGKIPIVAVQVEYNLL--RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleAL 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489529552  212 EKAEKLLNDYNpdMSISSWAIRFAASKDNVMMVLSGMSNMEQLLDNTGYMQnfKPFVQEEYNIIDEAV 279
Cdd:pfam00248 227 EALEEIAKEHG--VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
289-366 1.21e-04

electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the C subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273888 [Multi-domain]  Cd Length: 435  Bit Score: 43.87  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  289 PCTACQYCVEGCPKNIaIP---NYFALYNAEKQALNTGFStqmvyynnytktygkasDCIECKQCEESCPQHIKIIDALK 365
Cdd:TIGR01945 364 PCIRCGKCVQVCPMNL-LPqqlNWLALADEFDEAEEHNLM-----------------DCIECGCCSYVCPSNIPLVQYIR 425

                  .
gi 489529552  366 N 366
Cdd:TIGR01945 426 Q 426
dkgA PRK11565
2,5-didehydrogluconate reductase DkgA;
37-111 3.19e-03

2,5-didehydrogluconate reductase DkgA;


Pssm-ID: 183203 [Multi-domain]  Cd Length: 275  Bit Score: 38.90  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKL-------PLMALKkkeeqetifnEQLEKCGVDYF 105
Cdd:PRK11565  38 LEVGYRSIDTAAIYKneegVGK---ALKEASVAR---EELFITTKLwnddhkrPREALE----------ESLKKLQLDYV 101

                 ....*.
gi 489529552 106 DYYLLH 111
Cdd:PRK11565 102 DLYLMH 107
 
Name Accession Description Interval E-value
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
6-373 4.14e-112

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 331.40  E-value: 4.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPIKDEndvttidmEHLNKMVDTFLERGFTYFDTAYVYHmgKSEIALRESLvkRHKRESFTIATKLPLmALKK 85
Cdd:COG1453   16 LGFGGMRLPRKDE--------EEAEALIRRAIDNGINYIDTARGYG--DSEEFLGKAL--KGPRDKVILATKLPP-WVRD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  86 KEEQETIFNEQLEKCGVDYFDYYLLHNIGVSH-----------YEVAKK--------FdsfkfieekkkegkiknIGFSF 146
Cdd:COG1453   83 PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEdlekvlkpggaLEALEKakaegkirH-----------------IGFST 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 147 HDSAELLDKVLsEHPEVDFVQLQINYLDWDNESiqSRKCYEVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNdynPDMS 226
Cdd:COG1453  146 HGSLEVIKEAI-DTGDFDFVQLQYNYLDQDNQA--GEEALEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLC---PPLS 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 227 ISSWAIRFAASKDNVMMVLSGMSNMEQLLDNTGYMQNFKPFVQEEYNIIDEAVEIINESILIPCTACQYCVEgCPKNIAI 306
Cdd:COG1453  220 PAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLEPLTEEELAILERLAEELGELLKDFCTGCGYCMP-CPQGINI 298
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529552 307 PNYFALYNaEKQALNTGFSTQMVYYNNYTKTygKASDCIECKQCEESCPQHIKIIDALKNVAETFEK 373
Cdd:COG1453  299 PEVFRLYN-LARAYGMREYAKERYNALGPGA--KASACIECGACEERCPQGLDIPELLKEAHELLGG 362
AKR_Fe-S_oxidoreductase cd19096
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...
4-266 7.68e-103

Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381322 [Multi-domain]  Cd Length: 255  Bit Score: 303.71  E-value: 7.68e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   4 KKLGFGLMRLPIKDENdvtTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKLPLMAL 83
Cdd:cd19096    1 SVLGFGTMRLPESDDD---SIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEAL-KEGPREKFYLATKLPPWSV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  84 KKKEEQETIFNEQLEKCGVDYFDYYLLHNIG-VSHYEVAKKFDSFKFIEEKKKEGKIKNIGFSFHDSAELLDKVLSEHPe 162
Cdd:cd19096   77 KSAEDFRRILEESLKRLGVDYIDFYLLHGLNsPEWLEKARKGGLLEFLEKAKKEGLIRHIGFSFHDSPELLKEILDSYD- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 163 VDFVQLQINYLDWDNEsiQSRKCYEVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNDYnpDMSISSWAIRFAASKDNVM 242
Cdd:cd19096  156 FDFVQLQYNYLDQENQ--AGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGA--PLSPAEWALRFLLSHPEVT 231
                        250       260
                 ....*....|....*....|....
gi 489529552 243 MVLSGMSNMEQLLDNTGYMQNFKP 266
Cdd:cd19096  232 TVLSGMSTPEQLDENIAAADEFEP 255
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
6-279 8.87e-56

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.


Pssm-ID: 425554 [Multi-domain]  Cd Length: 290  Bit Score: 184.44  E-value: 8.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552    6 LGFGLMRLPIKDEndvtTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKR-HKRESFTIATKL-----P 79
Cdd:pfam00248   1 IGLGTWQLGGGWG----PISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYpVKRDKVVIATKVpdgdgP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   80 LMALKKKEEQETIFNEQLEKCGVDYFDYYLLHNIGVSHY--EVAKKFDSfkfieeKKKEGKIKNIGFSFHDsAELLDKVL 157
Cdd:pfam00248  77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPieETWDALEE------LKKEGKIRAIGVSNFD-AEQIEKAL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  158 sEHPEVDFVQLQINYLDWdnESIQSRKCYEVAEKHNKPVIVMEPVKGGTLAK--------------------------IP 211
Cdd:pfam00248 150 -TKGKIPIVAVQVEYNLL--RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleAL 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489529552  212 EKAEKLLNDYNpdMSISSWAIRFAASKDNVMMVLSGMSNMEQLLDNTGYMQnfKPFVQEEYNIIDEAV 279
Cdd:pfam00248 227 EALEEIAKEHG--VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
AKR_SF cd06660
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
5-259 2.24e-30

Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.


Pssm-ID: 381296 [Multi-domain]  Cd Length: 232  Bit Score: 116.08  E-value: 2.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPikdendvTTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRHKRESFTIATKLPLMALK 84
Cdd:cd06660    2 RLGLGTMTFG-------GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRDDVVIATKGGHPPGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  85 K-------KEEQETIFNEQLEKCGVDYFDYYLLHNIGVSHY--EV---------AKKFdsfkfieekkkegkiKNIGFSF 146
Cdd:cd06660   75 DpsrsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPveETlealnelvrEGKI---------------RYIGVSN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 147 HDSAEL--LDKVLSEH--PEVDFVQLQINYLDWDnesIQSRKCYEVAEKHNKPVIVMEPVKGGtlakipekaekllndyn 222
Cdd:cd06660  140 WSAERLaeALAYAKAHglPGFAAVQPQYSLLDRS---PMEEELLDWAEENGLPLLAYSPLARG----------------- 199
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489529552 223 pdmsISSWAIRFAASKDNVMMVLSGMSNMEQLLDNTG 259
Cdd:cd06660  200 ----PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
AKR_unchar cd19100
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
1-257 9.25e-28

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381326 [Multi-domain]  Cd Length: 238  Bit Score: 109.11  E-value: 9.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   1 MEAKKLGFGLMRLPIKDENDVTtidmehlnKMVDTFLERGFTYFDTAYVYhmGKSEIALRESLvkRHKRESFTIATKLpl 80
Cdd:cd19100    9 LKVSRLGFGGGPLGRLSQEEAA--------AIIRRALDLGINYFDTAPSY--GDSEEKIGKAL--KGRRDKVFLATKT-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  81 MALKKKEEQETIfNEQLEKCGVDYFDYYLLHNIGVSH-----------YEVAKK--------Fdsfkfieekkkegkikn 141
Cdd:cd19100   75 GARDYEGAKRDL-ERSLKRLGTDYIDLYQLHAVDTEEdldqvfgpggaLEALLEakeegkirF----------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 142 IGFSFHDSAELLDkvLSEHPEVDFVQLQINYLDWDNESiQSRKCYEVAEKHNKPVIVMEPVKGGTLAKI-PEKAEKllnd 220
Cdd:cd19100  137 IGISGHSPEVLLR--ALETGEFDVVLFPINPAGDHIDS-FREELLPLAREKGVGVIAMKVLAGGRLLSGdPLDPEQ---- 209
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489529552 221 ynpdmsisswAIRFAASKDNVMMVLSGMSNMEQLLDN 257
Cdd:cd19100  210 ----------ALRYALSLPPVDVVIVGMDSPEELDEN 236
AKR_unchar cd19105
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
6-257 9.12e-25

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381331 [Multi-domain]  Cd Length: 250  Bit Score: 101.12  E-value: 9.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPIKDENdvttidmehlnkMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKLPL-MALK 84
Cdd:cd19105   16 LGFGGGGLPRESPE------------LLRRALDLGINYFDTAEGYGNGNSEEIIGEAL-KGLRRDKVFLATKASPrLDKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  85 KKEEQETIFNEQLEKCGVDYFDYYLLHNIGVSHYEV-----------AKK-----FdsfkfieekkkegkiknIGFSFHD 148
Cdd:cd19105   83 DKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLlneellealekLKKegkvrF-----------------IGFSTHD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 149 S-AELLDKVLsEHPEVDFVQLQINYLdwdNESIQSRKCYEVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNDynpdmSI 227
Cdd:cd19105  146 NmAEVLQAAI-ESGWFDVIMVAYNFL---NQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAKGF-----SL 216
                        250       260       270
                 ....*....|....*....|....*....|
gi 489529552 228 SSWAIRFAASKDNVMMVLSGMSNMEQLLDN 257
Cdd:cd19105  217 PQAALKWVLSNPRVDTVVPGMRNFAELEEN 246
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
5-284 7.60e-21

Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440431 [Multi-domain]  Cd Length: 316  Bit Score: 91.78  E-value: 7.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPikdeNDVTTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKLPLMALK 84
Cdd:COG0667   15 RLGLGTMTFG----GPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEAL-KGRPRDDVVIATKVGRRMGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  85 KKEEQ----ETIFnEQLEKC----GVDYFDYYLLHNIGVSHY--EVAKKFD---------SfkfieekkkegkiknIGFS 145
Cdd:COG0667   90 GPNGRglsrEHIR-RAVEASlrrlGTDYIDLYQLHRPDPDTPieETLGALDelvregkirY---------------IGVS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 146 FHDSAELLD--KVLSEHPEVDFVQLQINYLDWDNEsiqsRKCYEVAEKHNKPVIVMEPVKGGTLA-------KIPEK--- 213
Cdd:COG0667  154 NYSAEQLRRalAIAEGLPPIVAVQNEYSLLDRSAE----EELLPAARELGVGVLAYSPLAGGLLTgkyrrgaTFPEGdra 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 214 AEKLLNDYNPD-----------------MSISSWAIRFAASKDNVMMVLSGMSNMEQLLDNTGYMQNfkPFVQEEYNIID 276
Cdd:COG0667  230 ATNFVQGYLTErnlalvdalraiaaehgVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALD 307

                 ....*...
gi 489529552 277 EAVEIINE 284
Cdd:COG0667  308 AALAAVPA 315
AKR_AKR11C1 cd19086
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ...
5-259 3.17e-20

AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.


Pssm-ID: 381312 [Multi-domain]  Cd Length: 238  Bit Score: 88.30  E-value: 3.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPIKDENDVttiDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvkRHKRESFTIATKLPlMALK 84
Cdd:cd19086    5 EIGFGTWGLGGDWWGDV---DDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKAL--KGRRDKVVIATKFG-NRFD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  85 KKEEQETIFN-----EQLEKC----GVDYFDYYLLHNIGVSHY---------EVAKK-----Fdsfkfieekkkegkikn 141
Cdd:cd19086   79 GGPERPQDFSpeyirEAVEASlkrlGTDYIDLYQLHNPPDEVLdndelfealEKLKQegkirA----------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 142 IGFSFHDSAELLDkvLSEHPEVDFVQLQINYLDWDNEsiqsRKCYEVAEKHNKPVIVMEPVKGGTLA-KIPEkaekllnd 220
Cdd:cd19086  142 YGVSVGDPEEALA--ALRRGGIDVVQVIYNLLDQRPE----EELFPLAEEHGVGVIARVPLASGLLTgKLAQ-------- 207
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489529552 221 ynpdmsissWAIRFAASKDNVMMVLSGMSNMEQLLDNTG 259
Cdd:cd19086  208 ---------AALRFILSHPAVSTVIPGARSPEQVEENAA 237
AKR_unchar cd19097
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
31-257 4.26e-19

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381323 [Multi-domain]  Cd Length: 267  Bit Score: 86.04  E-value: 4.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  31 KMVDTFLERGFTYFDTAYVYhmGKSEIALRESLVKRHKresFTIATKLPLMALKKKEEQETI---FNEQLEKCGVDYFDY 107
Cdd:cd19097   30 KILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLDK---FKIITKLPPLKEDKKEDEAAIeasVEASLKRLKVDSLDG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 108 YLLHN---IGVSHYEVAKKFDSFKFIEEKKkegkikNIGFSFHDSAELLDkvLSEHPEVDFVQLQINYLD--WDNESIQS 182
Cdd:cd19097  105 LLLHNpddLLKHGGKLVEALLELKKEGLIR------KIGVSVYSPEELEK--ALESFKIDIIQLPFNILDqrFLKSGLLA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 183 RkcyevAEKHNKPVIV----------MEPVKggtLAKIPEKAEKLLNDYNP-----DMSISSWAIRFAASKDNVMMVLSG 247
Cdd:cd19097  177 K-----LKKKGIEIHArsvflqglllMEPDK---LPAKFAPAKPLLKKLHElakklGLSPLELALGFVLSLPEIDKIVVG 248
                        250
                 ....*....|
gi 489529552 248 MSNMEQLLDN 257
Cdd:cd19097  249 VDSLEQLKEI 258
AKR_AKR10A1_2 cd19082
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ...
5-111 4.47e-15

AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.


Pssm-ID: 381308 [Multi-domain]  Cd Length: 291  Bit Score: 74.90  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPikdendvTTIDMEHLNKMVDTFLERGFTYFDTAYVY----HMGKSEIALRESLVKRHKRESFTIATK--- 77
Cdd:cd19082    2 RIVLGTADFG-------TRIDEEEAFALLDAFVELGGNFIDTARVYgdwvERGASERVIGEWLKSRGNRDKVVIATKggh 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489529552  78 --LPLMALKK--KEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19082   75 pdLEDMSRSRlsPEDIRADLEESLERLGTDYIDLYFLH 112
AKR_unchar cd19103
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
22-112 2.82e-13

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381329 [Multi-domain]  Cd Length: 299  Bit Score: 69.67  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  22 TTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALREsLVKRHKRESFTIATKL-PLMALKKKEEQETIFNEQLEKC 100
Cdd:cd19103   27 NHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGE-FLKRYPREDYIISTKFtPQIAGQSADPVADMLEGSLARL 105
                         90
                 ....*....|..
gi 489529552 101 GVDYFDYYLLHN 112
Cdd:cd19103  106 GTDYIDIYWIHN 117
AKR_AKR3F1-like cd19072
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ...
5-276 5.25e-13

Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381298 [Multi-domain]  Cd Length: 263  Bit Score: 68.41  E-value: 5.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPIKDENDVTTIDmehlnkmvdTFLERGFTYFDTAYVYHMGKSEIALRESLVKRhKRESFTIATKLPLMALK 84
Cdd:cd19072   13 GIGGGMSKDYSDDKKAIEALR---------YAIELGINLIDTAEMYGGGHAEELVGKAIKGF-DREDLFITTKVSPDHLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  85 KKEEQETiFNEQLEKCGVDYFDYYLLH--NIGVSHYEVAKKFDsfkfieEKKKEGKIKNIGFSFHDSAEL--LDKVLSEH 160
Cdd:cd19072   83 YDDVIKA-AKESLKRLGTDYIDLYLIHwpNPSIPIEETLRAME------ELVEEGKIRYIGVSNFSLEELeeAQSYLKKG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 161 PeVDFVQLQINYLDWDNESiqsrKCYEVAEKHNKPVIVMEPVKGGTL--AKIPEKAEKLLNDYNpdMSISSWAIRFAASK 238
Cdd:cd19072  156 P-IVANQVEYNLFDREEES----GLLPYCQKNGIAIIAYSPLEKGKLsnAKGSPLLDEIAKKYG--KTPAQIALNWLISK 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489529552 239 DNVmMVLSGMSNMEQLLDNTGYMQnFKpFVQEEYNIID 276
Cdd:cd19072  229 PNV-IAIPKASNIEHLEENAGALG-WE-LSEEDLQRLD 263
AKR_unchar cd19104
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
37-254 1.64e-10

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381330 [Multi-domain]  Cd Length: 321  Bit Score: 61.51  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYHMGKSEIALRESLvkRHKRESFTIATK--LPLMALKK-KEEQETIFNEQLEKCGVDYFDYYLLHN- 112
Cdd:cd19104   42 LDLGINFFDTAPSYGDGKSEENLGRAL--KGLPAGPYITTKvrLDPDDLGDiGGQIERSVEKSLKRLKRDSVDLLQLHNr 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 113 ------------IGVSHY----EVAKKFDSFKFIEEKKKegkiknIGFSFHDSAELLDKVLsEHPEVDFVQLQINYLDW- 175
Cdd:cd19104  120 igderdkpvggtLSTTDVlglgGVADAFERLRSEGKIRF------IGITGLGNPPAIRELL-DSGKFDAVQVYYNLLNPs 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 176 -------DNESIQSRKCYEVAEKHNKPVIVMEPVKGGTLAKIP------------------EKAEK---LLNDYNPDMSI 227
Cdd:cd19104  193 aaearprGWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTTSLdrgreapptsdsdvaidfRRAAAfraLAREWGETLAQ 272
                        250       260
                 ....*....|....*....|....*..
gi 489529552 228 SswAIRFAASKDNVMMVLSGMSNMEQL 254
Cdd:cd19104  273 L--AHRFALSNPGVSTVLVGVKNREEL 297
AKR_unchar cd19099
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
5-258 6.49e-10

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381325 [Multi-domain]  Cd Length: 316  Bit Score: 59.64  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLpikDENDVTtiDMEHLNkMVDTFLERGFTYFDTAYVYHMGKSE----IALRESLVK-RHKRESFTIATKL- 78
Cdd:cd19099    5 SLGLGTYRG---DSDDET--DEEYRE-ALKAALDSGINVIDTAINYRGGRSErligKALRELIEKgGIKRDEVVIVTKAg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  79 -----------PLMALKKKEEQETI----------------FNEQLEKC----GVDYFDYYLLHN--IGVSHYeVAKKFD 125
Cdd:cd19099   79 yipgdgdeplrPLKYLEEKLGRGLIdvadsaglrhcispayLEDQIERSlkrlGLDTIDLYLLHNpeEQLLEL-GEEEFY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 126 SFKFIEEKKKEGKIK-----NIGFS------------FHDSAELL----DKVLSEHPEVDFVQLQINYLD---WDNESIQ 181
Cdd:cd19099  158 DRLEEAFEALEEAVAegkirYYGIStwdgfrappalpGHLSLEKLvaaaEEVGGDNHHFKVIQLPLNLLEpeaLTEKNTV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 182 SRKCY---EVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNdyNPDMSISSWAIRFAASKDNVMMVLSGMSNMEQLLDNT 258
Cdd:cd19099  238 KGEALsllEAAKELGLGVIASRPLNQGQLLGELRLADLLAL--PGGATLAQRALQFARSTPGVDSALVGMRRPEHVDENL 315
AKR_EcYajO-like cd19079
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ...
5-111 8.80e-10

Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.


Pssm-ID: 381305 [Multi-domain]  Cd Length: 312  Bit Score: 59.13  E-value: 8.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPIKDENDVTtIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRHKRESFTIATKL-PLMA- 82
Cdd:cd19079   14 RLCLGCMSFGDPKWRPWV-LDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRDEVVIATKVyFPMGd 92
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489529552  83 ------LKKKeeqeTIFNE---QLEKCGVDYFDYYLLH 111
Cdd:cd19079   93 gpngrgLSRK----HIMAEvdaSLKRLGTDYIDLYQIH 126
AKR_AKR3C2-3 cd19120
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ...
37-112 1.03e-09

Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.


Pssm-ID: 381346 [Multi-domain]  Cd Length: 269  Bit Score: 58.78  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKLplmALKKKEEQETiFNEQLEKCGVDYFDYYLLHN 112
Cdd:cd19120   35 LKAGFRHIDTAEMYGnekeVGE---ALKESGVPR---EDLFITTKV---SPGIKDPREA-LRKSLAKLGVDYVDLYLIHS 104
AKR_AKR1I_CgAKR1 cd19155
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ...
27-111 1.24e-09

Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.


Pssm-ID: 381381 [Multi-domain]  Cd Length: 307  Bit Score: 58.69  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  27 EHLNKMVDTFLERGFTYFDTAYVYhmgKSEIALRESLVK-----RHKRESFTIATKLPlMALKKKEEQETIFNEQLEKCG 101
Cdd:cd19155   25 EEIETAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKwidsgKVKREELFIVTKLP-PGGNRREKVEKFLLKSLEKLQ 100
                         90
                 ....*....|
gi 489529552 102 VDYFDYYLLH 111
Cdd:cd19155  101 LDYVDLYLIH 110
AKR_AKR7A1-5 cd19075
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ...
8-111 1.59e-09

AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.


Pssm-ID: 381301 [Multi-domain]  Cd Length: 304  Bit Score: 58.34  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   8 FGLMrlPIKDENDVTTIDMehLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRHKresFTIATKLPLMALK--K 85
Cdd:cd19075    5 LGTM--TFGSQGRFTTAEA--AAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERG---FKIDTKANPGVGGglS 77
                         90       100
                 ....*....|....*....|....*.
gi 489529552  86 KEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19075   78 PENVRKQLETSLKRLKVDKVDVFYLH 103
AKR_AKR11B3 cd19085
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ...
31-111 1.76e-09

Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.


Pssm-ID: 381311 [Multi-domain]  Cd Length: 292  Bit Score: 57.98  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  31 KMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvkRHKRESFTIATKLPLMALkKKEEQETIFNEQLEKCGVDYFDYYLL 110
Cdd:cd19085   27 ATIHAALDAGINFFDTAEAYGDGHSEEVLGKAL--KGRRDDVVIATKVSPDNL-TPEDVRKSCERSLKRLGTDYIDLYQI 103

                 .
gi 489529552 111 H 111
Cdd:cd19085  104 H 104
AKR_AKR1-5-like cd19071
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ...
5-111 1.86e-09

AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.


Pssm-ID: 381297 [Multi-domain]  Cd Length: 251  Bit Score: 57.49  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLpikDENDVTTIdmehlnkmVDTFLERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKLPl 80
Cdd:cd19071    3 LIGLGTYKL---KPEETAEA--------VLAALEAGYRHIDTAAAYGneaeVGE---AIRESGVPR---EELFITTKLW- 64
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489529552  81 MALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19071   65 PTDHGYERVREALEESLKDLGLDYLDLYLIH 95
Aldo_ket_red_shaker-like cd19074
Shaker potassium channel beta subunit family and similar proteins; This family includes ...
22-257 6.29e-09

Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381300 [Multi-domain]  Cd Length: 297  Bit Score: 56.45  E-value: 6.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  22 TTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKL--PLMA------LKKKEEQETIf 93
Cdd:cd19074   17 GQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKAL-KGWPRESYVISTKVfwPTGPgpndrgLSRKHIFESI- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  94 NEQLEKCGVDYFDYYLLH--NIGVSHYEVAKKFDSFKFIEEKKKegkiknIGFSfHDSAELLDKVLS-------EHPEVD 164
Cdd:cd19074   95 HASLKRLQLDYVDIYYCHryDPETPLEETVRAMDDLIRQGKILY------WGTS-EWSAEQIAEAHDlarqfglIPPVVE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 165 fvQLQINYLDWDNESiqsrKCYEVAEKHNKPVIVMEPVKGGTLA-----KIPE-------------KAEKLLNDYNPD-- 224
Cdd:cd19074  168 --QPQYNMLWREIEE----EVIPLCEKNGIGLVVWSPLAQGLLTgkyrdGIPPpsrsratdednrdKKRRLLTDENLEkv 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489529552 225 -----------MSISSWAIRFAASKDNVMMVLSGMSNMEQLLDN 257
Cdd:cd19074  242 kklkpiadelgLTLAQLALAWCLRNPAVSSAIIGASRPEQLEEN 285
AKR_AKR5A_5G cd19126
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ...
5-111 2.54e-08

AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.


Pssm-ID: 381352 [Multi-domain]  Cd Length: 254  Bit Score: 54.37  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPIKDENDvttidmehlnKMVDTFLERGFTYFDTAYVYHMGKSE-IALRESLVKRhkrESFTIATKLpLMAL 83
Cdd:cd19126   11 WLGLGVFQTPDGDETE----------RAVQTALENGYRSIDTAAIYKNEEGVgEAIRESGVPR---EELFVTTKL-WNDD 76
                         90       100
                 ....*....|....*....|....*...
gi 489529552  84 KKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19126   77 QRARRTEDAFQESLDRLGLDYVDLYLIH 104
AKR_AtPLR-like cd19093
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ...
33-111 3.01e-08

Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.


Pssm-ID: 381319 [Multi-domain]  Cd Length: 293  Bit Score: 54.54  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  33 VDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRHKRESFTIATKlpLMALKKKEEQETIFN---EQLEKCGVDYFDYYL 109
Cdd:cd19093   32 FDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRDEVVIATK--FAPLPWRLTRRSVVKalkASLERLGLDSIDLYQ 109

                 ..
gi 489529552 110 LH 111
Cdd:cd19093  110 LH 111
AKR_AKR5D1_E1 cd19132
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ...
5-111 3.76e-08

AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381358 [Multi-domain]  Cd Length: 255  Bit Score: 53.81  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLmrLPIKDENDVttidmehlnKMVDTFLERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKLPL 80
Cdd:cd19132    9 AIGFGT--YPLKGDEGV---------EAVVAALQAGYRLLDTAFNYEnegaVGE---AVRRSGVPR---EELFVTTKLPG 71
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489529552  81 MALKKKEEQETIfNEQLEKCGVDYFDYYLLH 111
Cdd:cd19132   72 RHHGYEEALRTI-EESLYRLGLDYVDLYLIH 101
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
290-358 4.61e-08

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 49.38  E-value: 4.61e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489529552  290 CTACQYCVEGCPKNIAIPNY-----FALYNAEKQALNTgfstqmvyynnytktYGKASDCIECKQCEESCPQHI 358
Cdd:pfam13534   2 CIQCGCCVDECPRYLLNGDEpkklmRAAYLGDLEELQA---------------NKVANLCSECGLCEYACPMGL 60
AKR_AKR11B1 cd19148
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ...
37-111 5.99e-08

Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381374 [Multi-domain]  Cd Length: 302  Bit Score: 53.46  E-value: 5.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYHMGKSEIALRESLVKRHKRESFTIATKLPLMALKKKE-----EQETIFNE---QLEKCGVDYFDYY 108
Cdd:cd19148   35 LDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRDRVVIATKVGLEWDEGGEvvrnsSPARIRKEvedSLRRLQTDYIDLY 114

                 ...
gi 489529552 109 LLH 111
Cdd:cd19148  115 QVH 117
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
5-111 6.64e-08

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440421 [Multi-domain]  Cd Length: 259  Bit Score: 53.14  E-value: 6.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPikdenDVTTIDMehlnkmVDTFLERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKLPL 80
Cdd:COG0656    7 ALGLGTWQLP-----GEEAAAA------VRTALEAGYRHIDTAAMYGneegVGE---AIAASGVPR---EELFVTTKVWN 69
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489529552  81 MALKKKEEQETiFNEQLEKCGVDYFDYYLLH 111
Cdd:COG0656   70 DNHGYDDTLAA-FEESLERLGLDYLDLYLIH 99
AKR_DrGR-like cd19136
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ...
6-116 9.52e-08

Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).


Pssm-ID: 381362 [Multi-domain]  Cd Length: 262  Bit Score: 52.63  E-value: 9.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRlpIKDEndvttidmEHLNKMVDTFLERGFTYFDTAYVYhmgKSEI----ALRESLVKRH-KRESFTIATKLPL 80
Cdd:cd19136    4 LGLGTFR--LRGE--------EEVRQAVDAALKAGYRLIDTASVY---RNEAdigkALRDLLPKYGlSREDIFITSKLAP 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489529552  81 MALKKKEEQETIfNEQLEKCGVDYFDYYLLHNIGVS 116
Cdd:cd19136   71 KDQGYEKARAAC-LGSLERLGTDYLDLYLIHWPGVQ 105
AKR_AKR11B1-like cd19084
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ...
37-259 1.26e-07

AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.


Pssm-ID: 381310 [Multi-domain]  Cd Length: 296  Bit Score: 52.53  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYHMGKSEIALRESLVKRhkRESFTIATKLPLMALKKKEEQ-----ETIFNE---QLEKCGVDYFDYY 108
Cdd:cd19084   35 IDLGINFFDTAPVYGFGHSEEILGKALKGR--RDDVVIATKCGLRWDGGKGVTkdlspESIRKEveqSLRRLQTDYIDLY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 109 LLHN--IGVSHYEVAKKFDsfkfieEKKKEGKIKNIGFSFHdSAELLDKvLSEHPEVDFVQLQINYLDWDNEsiqsRKCY 186
Cdd:cd19084  113 QIHWpdPNTPIEETAEALE------KLKKEGKIRYIGVSNF-SVEQLEE-ARKYGPIVSLQPPYSMLEREIE----EELL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 187 EVAEKHNKPVIVMEPVKGGTLA------------------------------KIPEKAEKLLNDYNpdMSISSWAIRFAA 236
Cdd:cd19084  181 PYCRENGIGVLPYGPLAQGLLTgkykkeptfppddrrsrfpffrgenfeknlEIVDKLKEIAEKYG--KSLAQLAIAWTL 258
                        250       260
                 ....*....|....*....|...
gi 489529552 237 SKDNVMMVLSGMSNMEQLLDNTG 259
Cdd:cd19084  259 AQPGVTSAIVGAKNPEQLEENAG 281
AKR_PsAKR cd19091
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ...
1-111 1.63e-07

Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.


Pssm-ID: 381317 [Multi-domain]  Cd Length: 319  Bit Score: 52.23  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   1 MEAKKLG----------FGLMRLPIKDEN--DVTTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvkRHK 68
Cdd:cd19091    1 MEYRTLGrsglkvselaLGTMTFGGGGGFfgAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKAL--KGR 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489529552  69 RESFTIATKLPL-MA-------LKKKEeqetIFNE---QLEKCGVDYFDYYLLH 111
Cdd:cd19091   79 RDDVLIATKVRGrMGegpndvgLSRHH----IIRAveaSLKRLGTDYIDLYQLH 128
AKR_BsYcsN_EcYdhF-like cd19092
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ...
1-111 1.87e-07

Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.


Pssm-ID: 381318 [Multi-domain]  Cd Length: 287  Bit Score: 51.79  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   1 MEAKKLGFGLMRLPikdENDVTTidmEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKR-HKRESFTIATKLP 79
Cdd:cd19092    4 LEVSRLVLGCMRLA---DWGESA---EELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNpGLREKIEIQTKCG 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489529552  80 LMALKKKEEQETIF------------NEQLEKCGVDYFDYYLLH 111
Cdd:cd19092   78 IRLGDDPRPGRIKHydtskehilasvEGSLKRLGTDYLDLLLLH 121
AKR_AKR11A1_11D1 cd19083
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ...
31-111 3.94e-07

AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).


Pssm-ID: 381309 [Multi-domain]  Cd Length: 307  Bit Score: 51.27  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  31 KMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKlplMALKKKEEQETIFNE------QLEKC---- 100
Cdd:cd19083   37 DLVREALDNGVNLLDTAFIYGLGRSEELVGEVL-KEYNRNEVVIATK---GAHKFGGDGSVLNNSpeflrsAVEKSlkrl 112
                         90
                 ....*....|.
gi 489529552 101 GVDYFDYYLLH 111
Cdd:cd19083  113 NTDYIDLYYIH 123
AKR_galDH cd19163
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ...
33-113 1.29e-06

L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).


Pssm-ID: 381389 [Multi-domain]  Cd Length: 293  Bit Score: 49.47  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  33 VDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKlplmALKKKEEQETIFN-----------EQLEKCG 101
Cdd:cd19163   39 VHEALDSGINYIDTAPWYGQGRSETVLGKAL-KGIPRDSYYLATK----VGRYGLDPDKMFDfsaeritksveESLKRLG 113
                         90
                 ....*....|..
gi 489529552 102 VDYFDYYLLHNI 113
Cdd:cd19163  114 LDYIDIIQVHDI 125
AKR_FDH cd19162
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ...
6-114 1.50e-06

D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.


Pssm-ID: 381388 [Multi-domain]  Cd Length: 290  Bit Score: 49.28  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFG---LMRLPIKDENDVTTidmehlnkMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATK----L 78
Cdd:cd19162    3 LGLGaasLGNLARAGEDEAAA--------TLDAAWDAGIRYFDTAPLYGLGLSERRLGAAL-ARHPRAEYVVSTKvgrlL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489529552  79 PLMALKKKEEQETIFN-----------EQLEKCGVDYFDYYLLHNIG 114
Cdd:cd19162   74 EPGAAGRPAGADRRFDfsadgirrsieASLERLGLDRLDLVFLHDPD 120
Fer4_9 pfam13187
4Fe-4S dicluster domain;
290-358 1.85e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 44.47  E-value: 1.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489529552  290 CTACQYCVEGCPKNIAIPNYFALYNAEKQALNtgfstqmvyynnytktygkasDCIECKQCEESCPQHI 358
Cdd:pfam13187   2 CTGCGACVAACPAGAIVPDLVGQTIRGDIAGL---------------------ACIGCGACVDACPRGA 49
AKR_AKR2E1-5 cd19116
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ...
37-111 4.39e-06

AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.


Pssm-ID: 381342 [Multi-domain]  Cd Length: 292  Bit Score: 47.66  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYhmGKSEI---ALREsLVKRH--KRESFTIATKLpLMALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19116   35 IEAGYRHIDTAYLY--GNEAEvgeAIRE-KIAEGvvKREDLFITTKL-WNSYHEREQVEPALRESLKRLGLDYVDLYLIH 110
AKR_AKR15A-like cd19090
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ...
7-257 5.08e-06

AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).


Pssm-ID: 381316 [Multi-domain]  Cd Length: 278  Bit Score: 47.55  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   7 GFGLMRLPIKDENDVTTIDmehlnkmvdTFLERGFTYFDTAYVYhmGKSEIALRESLvKRHKRESFTIATKL-PLMALKK 85
Cdd:cd19090    9 GLGGVFGGVDDDEAVATIR---------AALDLGINYIDTAPAY--GDSEERLGLAL-AELPREPLVLSTKVgRLPEDTA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  86 KEEQETI---FNEQLEKCGVDYFDYYLLHNIG-VSHYEVAKKFDSFKFIEEKKKEGKIKNIGFSFHDsAELLDKVLsEHP 161
Cdd:cd19090   77 DYSADRVrrsVEESLERLGRDRIDLLMIHDPErVPWVDILAPGGALEALLELKEEGLIKHIGLGGGP-PDLLRRAI-ETG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 162 EVDFVqlqINYLDWD--NESIQSRKCyEVAEKHNKPVIVMEPVKGGTLAKIP-------------------EKAEKLLND 220
Cdd:cd19090  155 DFDVV---LTANRYTllDQSAADELL-PAAARHGVGVINASPLGMGLLAGRPpervrytyrwlspelldraKRLYELCDE 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489529552 221 YNpdMSISSWAIRFAASKDNVMMVLSGMSNMEQLLDN 257
Cdd:cd19090  231 HG--VPLPALALRFLLRDPRISTVLVGASSPEELEQN 265
AKR_AKR5A1_2 cd19156
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ...
5-124 5.83e-06

AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.


Pssm-ID: 381382 [Multi-domain]  Cd Length: 266  Bit Score: 47.13  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPikdendvttiDMEHLNKMVDTFLERGFTYFDTAYVYhmgKSEI----ALRESLVKRhkrESFTIATKLpL 80
Cdd:cd19156   11 RLGLGVWRVQ----------DGAEAENAVKWAIEAGYRHIDTAAIY---KNEEgvgqGIRESGVPR---EEVFVTTKL-W 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489529552  81 MALKKKEEQETIFNEQLEKCGVDYFDYYLLhnigvsHYEVAKKF 124
Cdd:cd19156   74 NSDQGYESTLAAFEESLEKLGLDYVDLYLI------HWPVKGKF 111
AKR_AKR9C1 cd19081
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ...
6-259 8.82e-06

AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).


Pssm-ID: 381307 [Multi-domain]  Cd Length: 308  Bit Score: 46.82  E-value: 8.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPikdendvTTIDMEHLNKMVDTFLERGFTYFDTAYVY-------HMGKSEIALRESLVKRHKRESFTIATKL 78
Cdd:cd19081   12 LCLGTMVFG-------WTADEETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLKSRGKRDRVVIATKV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  79 --PLMALKKKEEQETIF---NEQLEKCGVDYFDYYLLH-------------------------NIGVSHYevakkfdsfk 128
Cdd:cd19081   85 gfPMGPNGPGLSRKHIRravEASLRRLQTDYIDLYQAHwddpatpleetlgalndlirqgkvrYIGASNY---------- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 129 fieekkkegkiknigfsfhdSAELLDKVLS---EHPEVDFVQLQINYldwdneSIQSRKCYE-----VAEKHNKPVIVME 200
Cdd:cd19081  155 --------------------SAWRLQEALElsrQHGLPRYVSLQPEY------NLVDRESFEgellpLCREEGIGVIPYS 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 201 PVKGGTL-------AKIP------EKAEKLLNDYN-------------PDMSISSWAIRFAASKDNVMMVLSGMSNMEQL 254
Cdd:cd19081  209 PLAGGFLtgkyrseADLPgstrrgEAAKRYLNERGlrildaldevaaeHGATPAQVALAWLLARPGVTAPIAGARTVEQL 288

                 ....*
gi 489529552 255 LDNTG 259
Cdd:cd19081  289 EDLLA 293
AKR_AKR11B2 cd19149
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ...
31-111 1.07e-05

Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.


Pssm-ID: 381375 [Multi-domain]  Cd Length: 315  Bit Score: 46.88  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  31 KMVDTFLERGFTYFDTAYVYHMGKSEIALRESLvkRHKRESFTIATKLPLM------ALKKKEEQETIFN---------- 94
Cdd:cd19149   37 RTIHAALDLGINLIDTAPAYGFGHSEEIVGKAI--KGRRDKVVLATKCGLRwdreggSFFFVRDGVTVYKnlspesiree 114
                         90
                 ....*....|....*....
gi 489529552  95 --EQLEKCGVDYFDYYLLH 111
Cdd:cd19149  115 veQSLKRLGTDYIDLYQTH 133
AKR_AKR9A_9B cd19080
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ...
31-111 1.17e-05

AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381306 [Multi-domain]  Cd Length: 307  Bit Score: 46.44  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  31 KMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRhkRESFTIATKLPLMAL----------KKKEEQEtiFNEQLEKC 100
Cdd:cd19080   35 AMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN--RDRIVLATKYTMNRRpgdpnaggnhRKNLRRS--VEASLRRL 110
                         90
                 ....*....|.
gi 489529552 101 GVDYFDYYLLH 111
Cdd:cd19080  111 QTDYIDLLYVH 121
AKR_AKR3F2_3 cd19073
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ...
33-111 1.41e-05

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381299 [Multi-domain]  Cd Length: 243  Bit Score: 45.72  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  33 VDTFLERGFTYFDTAYVYHmGKSEI--ALRESLVKRhkrESFTIATKLPLMALKKkEEQETIFNEQLEKCGVDYFDYYLL 110
Cdd:cd19073   20 VKEALELGYRHIDTAEIYN-NEAEVgeAIAESGVPR---EDLFITTKVWRDHLRP-EDLKKSVDRSLEKLGTDYVDLLLI 94

                 .
gi 489529552 111 H 111
Cdd:cd19073   95 H 95
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
275-369 1.93e-05

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 46.63  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 275 IDEAVEIINEsilipCTACQYCVEGCPKNIAIPNyfalynAEKQALNTGFStqmvyynNYTKTYgkaSDCIECKQCEESC 354
Cdd:cd01916  357 DEEFQELAAK-----CTDCGWCTRACPNSLRIKE------AMEAAKEGDFS-------GLADLF---DQCVGCGRCEQEC 415
                         90
                 ....*....|....*
gi 489529552 355 PQHIKIIDALKNVAE 369
Cdd:cd01916  416 PKEIPIINMIEKAAR 430
AKR_AKR5C2 cd19131
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ...
5-111 4.71e-05

Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.


Pssm-ID: 381357 [Multi-domain]  Cd Length: 256  Bit Score: 44.29  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPikdeNDVTTidmehlnKMVDTFLERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKLpL 80
Cdd:cd19131   12 QLGLGVWQVS----NDEAA-------SAVREALEVGYRSIDTAAIYGneegVGK---AIRASGVPR---EELFITTKL-W 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489529552  81 MALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19131   74 NSDQGYDSTLRAFDESLRKLGLDYVDLYLIH 104
AKR_AKR1G1_1I cd19111
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ...
27-111 5.75e-05

Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.


Pssm-ID: 381337 [Multi-domain]  Cd Length: 286  Bit Score: 44.41  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  27 EHLNKMVDTFLERGFTYFDTAYVYhmgKSEIALRESLvKRH------KRESFTIATKLPLMALK-KKEEQEtiFNEQLEK 99
Cdd:cd19111   17 EEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEAL-KWWlkngklKREEVFITTKLPPVYLEfKDTEKS--LEKSLEN 90
                         90
                 ....*....|..
gi 489529552 100 CGVDYFDYYLLH 111
Cdd:cd19111   91 LKLPYVDLYLIH 102
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
6-113 6.05e-05

AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.


Pssm-ID: 381304 [Multi-domain]  Cd Length: 301  Bit Score: 44.53  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRL-----PIKDENDVTtidmehlnKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRhkRESFTIATKLPL 80
Cdd:cd19078    7 IGLGCMGMshgygPPPDKEEMI--------ELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF--RDQVVIATKFGF 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489529552  81 MALKKKEEQ-------ETI---FNEQLEKCGVDYFDYYLLHNI 113
Cdd:cd19078   77 KIDGGKPGPlgldsrpEHIrkaVEGSLKRLQTDYIDLYYQHRV 119
AKR_AKR12A1_B1_C1 cd19087
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ...
32-113 6.21e-05

AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.


Pssm-ID: 381313 [Multi-domain]  Cd Length: 310  Bit Score: 44.49  E-value: 6.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  32 MVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRhkRESFTIATKL--P---------LMALKKKEEQEtifnEQLEKC 100
Cdd:cd19087   35 IMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR--RDDIVLATKVfgPmgddpndrgLSRRHIRRAVE----ASLRRL 108
                         90
                 ....*....|...
gi 489529552 101 GVDYFDYYLLHNI 113
Cdd:cd19087  109 QTDYIDLYQMHHF 121
AKR_AKR2C1 cd19114
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ...
40-111 6.64e-05

AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.


Pssm-ID: 381340 [Multi-domain]  Cd Length: 302  Bit Score: 44.09  E-value: 6.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529552  40 GFTYFDTAYVY----HMGKS-EIALRESLVKRhkrESFTIATKLpLMALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19114   30 GYRLIDGALLYgneaEVGRGiRKAIQEGLVKR---EDLFIVTKL-WNNFHGKDHVREAFDRQLKDYGLDYIDLYLIH 102
AKR_AKR1E1-2 cd19110
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ...
33-111 8.79e-05

AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.


Pssm-ID: 381336 [Multi-domain]  Cd Length: 301  Bit Score: 43.79  E-value: 8.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  33 VDTFLERGFTYFDTAYVYH------MGKSEiALRESLVkrhKRESFTIATKLpLMALKKKEEQETIFNEQLEKCGVDYFD 106
Cdd:cd19110   23 VKVAIDAGYRHFDCAYLYHnesevgAGIRE-KIKEGVV---RREDLFIVSKL-WCTCHKKSLVKTACTRSLKALKLNYLD 97

                 ....*
gi 489529552 107 YYLLH 111
Cdd:cd19110   98 LYLIH 102
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
290-358 1.02e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 39.99  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489529552  290 CTACQYCVEGCPkniaipNYFALYNAEKQALNTGFSTQMVYYNNYTKTYGKASDCIECKQCEESCPQHI 358
Cdd:pfam13183   2 CIRCGACLAACP------VYLVTGGRFPGDPRGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
AKR_AKR1G1_CeAKR cd19154
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ...
33-111 1.08e-04

Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381380 [Multi-domain]  Cd Length: 303  Bit Score: 43.55  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  33 VDTFLERGFTYFDTAYVYHmGKSEI--ALRESLVK-RHKRESFTIATKLPLMALKKKEEQETIfNEQLEKCGVDYFDYYL 109
Cdd:cd19154   31 VRTALKAGYRLIDTAFLYQ-NEEAIgeALAELLEEgVVKREDLFITTKLWTHEHAPEDVEEAL-RESLKKLQLEYVDLYL 108

                 ..
gi 489529552 110 LH 111
Cdd:cd19154  109 IH 110
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
289-366 1.21e-04

electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the C subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273888 [Multi-domain]  Cd Length: 435  Bit Score: 43.87  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  289 PCTACQYCVEGCPKNIaIP---NYFALYNAEKQALNTGFStqmvyynnytktygkasDCIECKQCEESCPQHIKIIDALK 365
Cdd:TIGR01945 364 PCIRCGKCVQVCPMNL-LPqqlNWLALADEFDEAEEHNLM-----------------DCIECGCCSYVCPSNIPLVQYIR 425

                  .
gi 489529552  366 N 366
Cdd:TIGR01945 426 Q 426
AKR_AKR9A1-2 cd19146
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ...
6-77 1.49e-04

Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.


Pssm-ID: 381372 [Multi-domain]  Cd Length: 326  Bit Score: 43.18  E-value: 1.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489529552   6 LGFGLMRLPIKDENDVTTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRHKRESFTIATK 77
Cdd:cd19146   14 LCLGAMSFGEAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEMVLATK 85
AKR_unchar cd19752
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
22-111 2.09e-04

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381391 [Multi-domain]  Cd Length: 291  Bit Score: 42.70  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  22 TTIDMEHLNKMVDTFLERGFTYFDTAYVY-------HMGKSEIALRESLVKRHKRESFTIATKL---PLMALKKKEEQE- 90
Cdd:cd19752   12 TRTDEETSFAILDRYVAAGGNFLDTANNYafwteggVGGESERLIGRWLKDRGNRDDVVIATKVgagPRDPDGGPESPEg 91
                         90       100
                 ....*....|....*....|....*...
gi 489529552  91 ----TIFNE---QLEKCGVDYFDYYLLH 111
Cdd:cd19752   92 lsaeTIEQEidkSLRRLGTDYIDLYYAH 119
AKR_AKR5G1-3 cd19157
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ...
6-111 2.27e-04

AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.


Pssm-ID: 381383 [Multi-domain]  Cd Length: 265  Bit Score: 42.38  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRlpIKDENDVTtidmehlnKMVDTFLERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKLpLM 81
Cdd:cd19157   13 LGLGVFK--VEEGSEVV--------NAVKTALKNGYRSIDTAAIYGneegVGK---GIKESGIPR---EELFITSKV-WN 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 489529552  82 ALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19157   76 ADQGYDSTLKAFEASLERLGLDYLDLYLIH 105
Aldo_ket_red_shaker cd19141
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ...
27-78 2.86e-04

Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381367 [Multi-domain]  Cd Length: 310  Bit Score: 42.43  E-value: 2.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489529552  27 EHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRH-KRESFTIATKL 78
Cdd:cd19141   30 EVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGwRRSSYVITTKI 82
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
289-358 3.58e-04

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 42.43  E-value: 3.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489529552 289 PCTACQYCVEGCPKNIaIPNYfaLYNAEKQalntgfstqmvyyNNYTKT--YGkASDCIECKQCEESCPQHI 358
Cdd:COG4656  365 PCIRCGRCVDACPMGL-LPQQ--LYWYARA-------------GDFDKAeeYN-LMDCIECGCCSYVCPSKI 419
AKR_AKR5F1 cd19133
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ...
6-111 3.67e-04

the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381359 [Multi-domain]  Cd Length: 255  Bit Score: 41.79  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPikdendvttiDMEHLNKMVDTFLERGFTYFDTAYVYhMGKSEI--ALRESLVKRhkrESFTIATKLPL--M 81
Cdd:cd19133   12 LGFGVFQIP----------DPEECERAVLEAIKAGYRLIDTAAAY-GNEEAVgrAIKKSGIPR---EELFITTKLWIqdA 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 489529552  82 ALKKKEEQetiFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19133   78 GYEKAKKA---FERSLKRLGLDYLDLYLIH 104
AKR_BaDH-like cd19129
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ...
6-111 3.71e-04

Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.


Pssm-ID: 381355 [Multi-domain]  Cd Length: 295  Bit Score: 42.06  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFG-LMRLPIKDENDVTTIdmehlnkmvdtfLERGFTYFDTAYVYHmGKSEI--ALRESLVK-RHKRESFTIATKLpLM 81
Cdd:cd19129    9 LGFGtLIPDPSATRNAVKAA------------LEAGFRHFDCAERYR-NEAEVgeAMQEVFKAgKIRREDLFVTTKL-WN 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 489529552  82 ALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19129   75 TNHRPERVKPAFEASLKRLQLDYLDLYLIH 104
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
290-360 4.10e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 38.56  E-value: 4.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489529552 290 CTACQYCVEGCPKN-IAIPNYFALYNAEKqalntgfstqmvyynnytktygkasdCIECKQCEESCPQH-IKI 360
Cdd:COG2768   13 CIGCGACVKVCPVGaISIEDGKAVIDPEK--------------------------CIGCGACIEVCPVGaIKI 59
AKR_AKR3F1 cd19137
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ...
27-111 6.68e-04

Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381363 [Multi-domain]  Cd Length: 260  Bit Score: 41.02  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  27 EHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESlVKRHKRESFTIATKLPLMALkKKEEQETIFNEQLEKCGVDYFD 106
Cdd:cd19137   26 EEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKA-IKDFPREDLFIVTKVWPTNL-RYDDLLRSLQNSLRRLDTDYID 103

                 ....*
gi 489529552 107 YYLLH 111
Cdd:cd19137  104 LYLIH 108
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
290-362 7.88e-04

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.38  E-value: 7.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489529552 290 CTACQYCVEGCPKNiaipnyfALYNAEKqalntgfSTQMVYYNnytktygkASDCIECKQCEESCPQH-IKIID 362
Cdd:COG1146   10 CIGCGACVEVCPVD-------VLELDEE-------GKKALVIN--------PEECIGCGACELVCPVGaITVED 61
AKR_AKR3A1-2 cd19117
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ...
31-111 8.89e-04

AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.


Pssm-ID: 381343 [Multi-domain]  Cd Length: 284  Bit Score: 40.56  E-value: 8.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  31 KMVDTFLERGFTYFDTAYVYhMGKSEI--ALRESLVKRhkrESFTIATKLplmALKKKEEQETIFNEQLEKCGVDYFDYY 108
Cdd:cd19117   31 KAVEAALKAGYRHIDTAAIY-GNEEEVgqGIKDSGVPR---EEIFITTKL---WCTWHRRVEEALDQSLKKLGLDYVDLY 103

                 ...
gi 489529552 109 LLH 111
Cdd:cd19117  104 LMH 106
AKR_AKR4A_4B cd19124
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ...
37-111 1.05e-03

AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.


Pssm-ID: 381350 [Multi-domain]  Cd Length: 281  Bit Score: 40.33  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYH----MGKS-EIALRESLVKrhKRESFTIATKL---------PLMALKKkeeqetifneQLEKCGV 102
Cdd:cd19124   30 IEVGYRHFDTAAAYGteeaLGEAlAEALRLGLVK--SRDELFVTSKLwcsdahpdlVLPALKK----------SLRNLQL 97

                 ....*....
gi 489529552 103 DYFDYYLLH 111
Cdd:cd19124   98 EYVDLYLIH 106
AKR_AKR5B1 cd19127
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ...
6-111 1.09e-03

AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.


Pssm-ID: 381353 [Multi-domain]  Cd Length: 268  Bit Score: 40.47  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPIKDENDVttidmehlnkmVDTFLERGFTYFDTAYVY----HMGKseiALRESLVKRhkrESFTIATKLpLM 81
Cdd:cd19127   12 LGLGVFQTPPEETADA-----------VATALADGYRLIDTAAAYgnerEVGE---GIRRSGVDR---SDIFVTTKL-WI 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 489529552  82 ALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19127   74 SDYGYDKALRGFDASLRRLGLDYVDLYLLH 103
AKR_AKR15A cd19152
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ...
37-78 1.19e-03

AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.


Pssm-ID: 381378 [Multi-domain]  Cd Length: 308  Bit Score: 40.29  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489529552  37 LERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIATKL 78
Cdd:cd19152   30 WDLGIRYFDTAPWYGAGLSEERLGAAL-RELGREDYVISTKV 70
AKR_AKR13B1 cd19088
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ...
6-257 1.26e-03

AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.


Pssm-ID: 381314 [Multi-domain]  Cd Length: 256  Bit Score: 39.89  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLPIKD--------ENDVTTIDmehlnkmvdTFLERGFTYFDTAYVYHMGKSEIALRESLVKRHKResFTIATK 77
Cdd:cd19088    4 LGYGAMRLTGPGiwgppadrEEAIAVLR---------RALELGVNFIDTADSYGPDVNERLIAEALHPYPDD--VVIATK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  78 LPLM---------ALKKKEEQETIfNEQLEKCGVDYFDYYLLHNIGvSHYEVAkkfDSFKFIEEKKKEGKIKNIGFSFHD 148
Cdd:cd19088   73 GGLVrtgpgwwgpDGSPEYLRQAV-EASLRRLGLDRIDLYQLHRID-PKVPFE---EQLGALAELQDEGLIRHIGLSNVT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 149 SAELldKVLSEHPEVDFVQLQINYLDWDNESIqsrkcYEVAEKHNKPVIVMEPVKGGTLAKIPEKAEKLLNDYnpDMSIS 228
Cdd:cd19088  148 VAQI--EEARAIVRIVSVQNRYNLANRDDEGV-----LDYCEAAGIAFIPWFPLGGGDLAQPGGLLAEVAARL--GATPA 218
                        250       260
                 ....*....|....*....|....*....
gi 489529552 229 SWAIRFAASKDNVMMVLSGMSNMEQLLDN 257
Cdd:cd19088  219 QVALAWLLARSPVMLPIPGTSSVEHLEEN 247
AKR_AKR3F2 cd19139
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ...
6-111 1.37e-03

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381365 [Multi-domain]  Cd Length: 248  Bit Score: 40.03  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   6 LGFGLMRLpiKDenDVTTidmehlnKMVDTFLERGFTYFDTAYVY----HMGKseiALRESLVKRHkrESFtIATKLPLM 81
Cdd:cd19139    4 FGLGTFRL--KD--DVVI-------DSVRTALELGYRHIDTAQIYdneaAVGQ---AIAESGVPRD--ELF-ITTKIWID 66
                         90       100       110
                 ....*....|....*....|....*....|
gi 489529552  82 ALKKKEEQETiFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19139   67 NLSKDKLLPS-LEESLEKLRTDYVDLTLIH 95
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
290-355 1.39e-03

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.35  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489529552  290 CTACQYCVEGCPKNIAIPNYFALYNAEKqalntgfstqmvyynnytKTYGKASDCIECKQCEESCP 355
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTK------------------TVVIDPERCVGCGACVAVCP 48
AKR_AKR2D1 cd19115
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ...
58-111 1.49e-03

AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.


Pssm-ID: 381341 [Multi-domain]  Cd Length: 311  Bit Score: 40.10  E-value: 1.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489529552  58 ALRESLVKRhkrESFTIATKLpLMALKKKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19115   62 AIKEGIVKR---EDLFIVSKL-WNTFHDGERVEPICRKQLADWGIDYFDLFLIH 111
AKR_unchar cd19102
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
37-111 1.65e-03

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381328 [Multi-domain]  Cd Length: 302  Bit Score: 39.96  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYHMGKSEIALRESLvkRHKRESFTIATKLPLM---------ALKKKEEQETIfNEQLEKCGVDYFDY 107
Cdd:cd19102   36 LDLGINWIDTAAVYGLGHSEEVVGRAL--KGLRDRPIVATKCGLLwdeegrirrSLKPASIRAEC-EASLRRLGVDVIDL 112

                 ....
gi 489529552 108 YLLH 111
Cdd:cd19102  113 YQIH 116
AKR_AKR13D1 cd19145
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ...
1-113 1.72e-03

AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.


Pssm-ID: 381371 [Multi-domain]  Cd Length: 304  Bit Score: 39.72  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   1 MEAKKLGFGLMRL-----PIKDENDVttIDMEHlnkmvdTFLERGFTYFDTAYVYHMGKSEIALRESLvKRHKRESFTIA 75
Cdd:cd19145   10 LEVSAQGLGCMGLsgdygAPKPEEEG--IALIH------HAFNSGVTFLDTSDIYGPNTNEVLLGKAL-KDGPREKVQLA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489529552  76 TKLPL-------MALKKKEEQ-ETIFNEQLEKCGVDYFDYYLLHNI 113
Cdd:cd19145   81 TKFGIheiggsgVEVRGDPAYvRAACEASLKRLDVDYIDLYYQHRI 126
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
271-356 2.00e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 37.76  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 271 EYNIIDEAVEIINESIlipCTACQYCVEGCPKNiAIPnyfalynaekqaLNTGFSTQMVYYNNYTktyGKASDCIECKQC 350
Cdd:cd10549   26 GPNGAIARGPEIDEDK---CVFCGACVEVCPTG-AIE------------LTPEGKEYVPKEKEAE---IDEEKCIGCGLC 86

                 ....*.
gi 489529552 351 EESCPQ 356
Cdd:cd10549   87 VKVCPV 92
AKR_AKR5C1 cd19130
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ...
5-111 2.21e-03

Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.


Pssm-ID: 381356 [Multi-domain]  Cd Length: 256  Bit Score: 39.51  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLPIKDENDVttidmehlnkmVDTFLERGFTYFDTAYVYhmGKSEIALRESLVKRHKRESFTIATKLpLMALK 84
Cdd:cd19130   12 QLGYGVFKVPPADTQRA-----------VATALEVGYRHIDTAAIY--GNEEGVGAAIAASGIPRDELFVTTKL-WNDRH 77
                         90       100
                 ....*....|....*....|....*..
gi 489529552  85 KKEEQETIFNEQLEKCGVDYFDYYLLH 111
Cdd:cd19130   78 DGDEPAAAFAESLAKLGLDQVDLYLVH 104
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
290-355 2.26e-03

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 36.26  E-value: 2.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489529552 290 CTACQYCVEGCPKNiAIpnyfalynaekqalntgfstQMVYYNNYTKTYGKASDCIECKQCEESCP 355
Cdd:COG1143    4 CIGCGLCVRVCPVD-AI--------------------TIEDGEPGKVYVIDPDKCIGCGLCVEVCP 48
AKR_AKR3D1 cd19121
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ...
31-111 2.46e-03

AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.


Pssm-ID: 381347 [Multi-domain]  Cd Length: 279  Bit Score: 39.44  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  31 KMVDTFLERGFTYFDTAYVYHmGKSEIA--LRESLVKRHKRESFTIATKLplMALKKKEEQETIfNEQLEKCGVDYFDYY 108
Cdd:cd19121   29 AAVAHALKIGYRHIDGALCYQ-NEDEVGegIKEAIAGGVKREDLFVTTKL--WSTYHRRVELCL-DRSLKSLGLDYVDLY 104

                 ...
gi 489529552 109 LLH 111
Cdd:cd19121  105 LVH 107
NapF COG1145
Ferredoxin [Energy production and conversion];
270-372 2.54e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 38.94  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552 270 EEYNIIDEAVEIINESIlipCTACQYCVEGCPKNiaipnyfALYNAEKQAlntgfstqMVYYNnytktygkASDCIECKQ 349
Cdd:COG1145  167 ELKIAIKKAKAVIDAEK---CIGCGLCVKVCPTG-------AIRLKDGKP--------QIVVD--------PDKCIGCGA 220
                         90       100
                 ....*....|....*....|...
gi 489529552 350 CEESCPqhikiIDALKNVAETFE 372
Cdd:COG1145  221 CVKVCP-----VGAISLEPKEIE 238
dkgA PRK11565
2,5-didehydrogluconate reductase DkgA;
37-111 3.19e-03

2,5-didehydrogluconate reductase DkgA;


Pssm-ID: 183203 [Multi-domain]  Cd Length: 275  Bit Score: 38.90  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  37 LERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKL-------PLMALKkkeeqetifnEQLEKCGVDYF 105
Cdd:PRK11565  38 LEVGYRSIDTAAIYKneegVGK---ALKEASVAR---EELFITTKLwnddhkrPREALE----------ESLKKLQLDYV 101

                 ....*.
gi 489529552 106 DYYLLH 111
Cdd:PRK11565 102 DLYLMH 107
AKR_CeZK1290-like cd19135
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ...
40-111 3.32e-03

Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.


Pssm-ID: 381361 [Multi-domain]  Cd Length: 265  Bit Score: 38.84  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  40 GFTYFDTAYVY----HMGKseiALRESLVKRHkrESFtIATKLplmalKKKEE--QETI--FNEQLEKCGVDYFDYYLLH 111
Cdd:cd19135   39 GYRHIDTAKRYgceeLLGK---AIKESGVPRE--DLF-LTTKL-----WPSDYgyESTKqaFEASLKRLGVDYLDLYLLH 107
AKR_AKR3B1-3 cd19118
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ...
33-111 3.67e-03

AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.


Pssm-ID: 381344 [Multi-domain]  Cd Length: 283  Bit Score: 38.93  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  33 VDTFLERGFTYFDTAYVYHmGKSEI--ALRESLVKRH--KRESFTIATKLpLMALKKKEEQETIFNEQLEKCGVDYFDYY 108
Cdd:cd19118   26 VKIALKAGYRHLDLAKVYQ-NQHEVgqALKELLKEEPgvKREDLFITSKL-WNNSHRPEYVEPALDDTLKELGLDYLDLY 103

                 ...
gi 489529552 109 LLH 111
Cdd:cd19118  104 LIH 106
AKR_AKR3F3 cd19140
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ...
5-121 3.89e-03

Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381366 [Multi-domain]  Cd Length: 253  Bit Score: 38.39  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552   5 KLGFGLMRLpikdendvttiDMEHLNKMVDTFLERGFTYFDTAYVYH----MGKseiALRESLVKRhkrESFTIATKLPL 80
Cdd:cd19140   10 ALGLGTYPL-----------TGEECTRAVEHALELGYRHIDTAQMYGneaqVGE---AIAASGVPR---DELFLTTKVWP 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489529552  81 MALKKKEEQETIfNEQLEKCGVDYFDYYLLH-------------------------NIGVSHYEVA 121
Cdd:cd19140   73 DNYSPDDFLASV-EESLRKLRTDYVDLLLLHwpnkdvplaetlgalneaqeaglarHIGVSNFTVA 137
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
18-77 5.73e-03

Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381373 [Multi-domain]  Cd Length: 319  Bit Score: 38.27  E-value: 5.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529552  18 ENDVTTIDMEHLNKMVDTFLERGFTYFDTAYVYHMGKSEIALRESLVKRHKRESFTIATK 77
Cdd:cd19147   25 SGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIVIATK 84
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
290-355 9.35e-03

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 34.15  E-value: 9.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489529552  290 CTACQYCVEGCPKNIAIPNYFALYNAEKQALntgfstqmvyynnytktyGKASDCIECKQCEESCP 355
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAIVERLEGEAVR------------------IGVWKCIGCGACVEACP 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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