|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-312 |
6.15e-167 |
|
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: 466.68 E-value: 6.15e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 2 EYVKLGDSDLMVSKVCLGCMGFGEAQKGmhSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYAKRE 81
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWR--PWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 82 DVIIATKFIPRTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNC 161
Cdd:cd19079 79 EVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 162 YAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKRLSED-IYAKG 240
Cdd:cd19079 159 YAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTtDTAKL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797152346 241 KYDITHDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19079 239 KYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKpgVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-319 |
1.29e-120 |
|
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: 349.48 E-value: 1.29e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFGEAQkgmhsWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKR 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGPW-----GGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGR-PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 81 EDVIIATKF-IPRTQEEIEQGIDAKqHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGIS 159
Cdd:COG0667 75 DDVVIATKVgRRMGPGPNGRGLSRE-HIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 160 NCYAWQIAKANEIakAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLA-----KHPGEESKRLSE 234
Cdd:COG0667 154 NYSAEQLRRALAI--AEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTgkyrrGATFPEGDRAAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 235 DIYAKGKYdithDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:COG0667 232 NFVQGYLT----ERNLALVDALRAIAAEHGVTPAQLALAWLLAQpgVTSVIPGARSPEQLEENLAAADLELSAEDLAALD 307
|
....*..
gi 1797152346 313 ELYKPHR 319
Cdd:COG0667 308 AALAAVP 314
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-312 |
2.48e-99 |
|
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: 294.90 E-value: 2.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 6 LGDSDLMVSKVCLGCMGFGEAQKgmhsWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyaKREDVII 85
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWG----WGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG--NRDRIVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 86 ATKFI-PRTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAW 164
Cdd:cd19080 77 ATKYTmNRRPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 165 QIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRL-AKHPGEESKRLSEDIYAKGKYD 243
Cdd:cd19080 157 VVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLtGKYQRGEEGRAGEAKGVTVGFG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797152346 244 ITHDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19080 237 KLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-314 |
3.47e-99 |
|
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: 294.87 E-value: 3.47e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFGEaqkgmhswTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyaKR 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGG--------RTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG--RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 81 EDVIIATKFIPRTQEEI-EQGIDAKqHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGIS 159
Cdd:cd19087 71 DDIVLATKVFGPMGDDPnDRGLSRR-HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 160 NCYAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALA----SGRLAKHPGEESKRLSED 235
Cdd:cd19087 150 NFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAggllTGKYGKGKRPESGRLVER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 236 IYAKGKYdiTHDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEE 313
Cdd:cd19087 230 ARYQARY--GLEEYRDIAERFEALAAEAGLTPASLALAWVLSHpaVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDE 307
|
.
gi 1797152346 314 L 314
Cdd:cd19087 308 L 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-314 |
5.40e-96 |
|
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: 286.82 E-value: 5.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFGEAQKGMHSW-TLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKeyAK 79
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFFGAWgGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALK--GR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 80 REDVIIATKFIPRTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGIS 159
Cdd:cd19091 79 RDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 160 NCYAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLA-KHPGEESKRLSEDIYA 238
Cdd:cd19091 159 NFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSgKYRRGQPAPEGSRLRR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 239 KGKYDITHDEDLA--IIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19091 239 TGFDFPPVDRERGydVVDALREIAKETGATPAQVALAWLLSRptVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-311 |
2.03e-87 |
|
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: 264.85 E-value: 2.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 5 KLGDSDLMVSKVCLGCMGFGeaqkgmhsWTLPYEESKKIIKYALDNGINFFDTA-------IGYQGGTSEAFLGKAIKEY 77
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFG--------WTADEETSFALLDAFVDAGGNFIDTAdvysawvPGNAGGESETIIGRWLKSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 78 AKREDVIIATKFIPRTQEEiEQGIDAKqHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIG 157
Cdd:cd19081 73 GKRDRVVIATKVGFPMGPN-GPGLSRK-HIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 158 ISNCYAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREE-EREMKQYCVAHNIAMTPYSALASGRLA-K-HPGEESKRLSE 234
Cdd:cd19081 151 ASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESfEGELLPLCREEGIGVIPYSPLAGGFLTgKyRSEADLPGSTR 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 235 DIYAKGKYdiTHDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYL 311
Cdd:cd19081 231 RGEAAKRY--LNERGLRILDALDEVAAEHGATPAQVALAWLLARpgVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-306 |
6.16e-85 |
|
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: 257.91 E-value: 6.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 11 LMVSKVCLGcmgfgeaqkgmhSWT-----LPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKREDVII 85
Cdd:cd19074 2 LKVSELSLG------------TWLtfggqVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGW-PRESYVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 86 ATK-FIPRTQEEIEQGIDAKqHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAW 164
Cdd:cd19074 69 STKvFWPTGPGPNDRGLSRK-HIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 165 QIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLA------KHPGEESKRLSEDIYA 238
Cdd:cd19074 148 QIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTgkyrdgIPPPSRSRATDEDNRD 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 239 KGKYDIThDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDE 306
Cdd:cd19074 228 KKRRLLT-DENLEKVKKLKPIADELGLTLAQLALAWCLRNpaVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-312 |
5.79e-84 |
|
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: 255.53 E-value: 5.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 10 DLMVSKVCLGCMGFGEAQKGMHSWtlpyEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYakREDVIIATKF 89
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWWGEVDD----QESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR--RDDVVIATKC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 90 IPRTQEEIEQGIDAK-QHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAK 168
Cdd:cd19084 75 GLRWDGGKGVTKDLSpESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 169 ANEIAKakgyeqFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALA----SGRLAKHPGEES-------KRLSEDIY 237
Cdd:cd19084 155 ARKYGP------IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAqgllTGKYKKEPTFPPddrrsrfPFFRGENF 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1797152346 238 AKGkydithdedLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19084 229 EKN---------LEIVDKLKEIAEKYGKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
21-315 |
1.43e-82 |
|
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: 251.85 E-value: 1.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 21 MGFGEAQKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYA-KREDVIIATKFIPRtQEEIEQ 99
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPvKRDKVVIATKVPDG-DGPWPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 100 GIdAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAKAKgye 179
Cdd:pfam00248 80 GG-SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIP--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 180 qFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHpGEESKRLSEDIYAKGKYDITHDEDLAIIHrVEEL 259
Cdd:pfam00248 156 -IVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGK-YTRDPDKGPGERRRLLKKGTPLNLEALEA-LEEI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1797152346 260 AEKKGVSMTEISLAWLL--TKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELY 315
Cdd:pfam00248 233 AKEHGVSPAQVALRWALskPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-297 |
1.55e-79 |
|
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: 242.04 E-value: 1.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 14 SKVCLGCMGFGeaqkgmhsWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYAKREDVIIATKFIPRT 93
Cdd:cd06660 1 SRLGLGTMTFG--------GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRDDVVIATKGGHPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 94 QEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIA 173
Cdd:cd06660 73 GGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 174 KAKGYEQFVSIQGHYNLIFREE-EREMKQYCVAHNIAMTPYSALASGrlakhpgeeskrlsediyakgkydithdedlai 252
Cdd:cd06660 153 KAHGLPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG--------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1797152346 253 ihrveelaekkgvsMTEISLAWLLTK--VTSPIIGATKPHHIDGAVK 297
Cdd:cd06660 200 --------------PAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
13-315 |
5.92e-77 |
|
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: 238.48 E-value: 5.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 13 VSKVCLGCMGFGEAQKGMHSwTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYAKREDVIIATKFI-- 90
Cdd:cd19146 11 VSPLCLGAMSFGEAWKSMMG-ECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEMVLATKYTtg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 91 --PRTQEEIE---QGIDAKQ-HIEncLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAW 164
Cdd:cd19146 90 yrRGGPIKIKsnyQGNHAKSlRLS--VEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 165 QIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLaKHPGEESKRLSEdiyakGKYDI 244
Cdd:cd19146 168 VVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQF-RTEEEFKRRGRS-----GRKGG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797152346 245 THDE-DLAIIHRVEELAEKKGVSMTEISLAWLLTKV--TSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELY 315
Cdd:cd19146 242 PQTEkERKVSEKLEKVAEEKGTAITSVALAYVMHKApyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAY 315
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-317 |
5.39e-76 |
|
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: 234.79 E-value: 5.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 13 VSKVCLGCMGFGEAQkgmhsWTLPY--EESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKeyAKREDVIIATKFI 90
Cdd:cd19085 1 VSRLGLGCWQFGGGY-----WWGDQddEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALK--GRRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 91 PR--TQEEIEQGIDAkqhienclngSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAK 168
Cdd:cd19085 74 PDnlTPEDVRKSCER----------SLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 169 ANEIAKakgyeqFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAK--HPGEESK---------RLSEDIY 237
Cdd:cd19085 144 ALDAGR------IDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGkfSSAEDFPpgdartrlfRHFEPGA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 238 AKgkydithdEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELY 315
Cdd:cd19085 218 EE--------ETFEALEKLKEIADELGVTMAQLALAWVLQQpgVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEIS 289
|
..
gi 1797152346 316 KP 317
Cdd:cd19085 290 DP 291
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-314 |
1.40e-72 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. 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: 381302 [Multi-domain] Cd Length: 303 Bit Score: 226.71 E-value: 1.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 2 EYVKLGDSDLMVSKVCLGCMGFGEAQKGMhswtlPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyaKRE 81
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYGPA-----DEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD--RRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 82 DVIIATKF-IPRTQEEIEQGIDAK-QHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGIS 159
Cdd:cd19076 74 EVVIATKFgIVRDPGSGFRGVDGRpEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 160 NCYAWQIAKANEIAKakgyeqFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLA---KHPGEESK------ 230
Cdd:cd19076 154 EASADTIRRAHAVHP------ITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTgaiKSPEDLPEddfrrn 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 231 --RLSEDIYAKgkydithdeDLAIIHRVEELAEKKGVSMTEISLAWLLTK----VtsPIIGATKPHHIDGAVKAVAVKLT 304
Cdd:cd19076 228 npRFQGENFDK---------NLKLVEKLEAIAAEKGCTPAQLALAWVLAQgddiV--PIPGTKRIKYLEENVGALDVVLT 296
|
330
....*....|
gi 1797152346 305 DEEiiyLEEL 314
Cdd:cd19076 297 PEE---LAEI 303
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-312 |
3.41e-68 |
|
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: 215.17 E-value: 3.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 13 VSKVCLGCMGFGEaQKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYAKREDVIIATKF--I 90
Cdd:cd19093 2 VSPLGLGTWQWGD-RLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRDEVVIATKFapL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 91 PRTQeeieqgidAKQHIENCLNGSLKRLDMDYVDLYILHM-WDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKA 169
Cdd:cd19093 81 PWRL--------TRRSVVKALKASLERLGLDSIDLYQLHWpGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 170 NEIAKAKGYEqFVSIQGHYNLIFRE-EEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKRlsEDIYAKGKYDITHDE 248
Cdd:cd19093 153 HKALKERGVP-LASNQVEYSLLYRDpEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPP--PGGRRRLFGRKNLEK 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797152346 249 DLAIIHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19093 230 VQPLLDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-315 |
8.87e-66 |
|
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: 209.20 E-value: 8.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 4 VKLGDSDLMVSkvclgCMGFGEAQKGMHSW--TLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKRE 81
Cdd:cd19083 2 VKLGKSDIDVN-----PIGLGTNAVGGHNLypNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEY-NRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 82 DVIIATKFIPRTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNC 161
Cdd:cd19083 76 EVVIATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 162 YAWQIAKANeiakAKGYEQfvSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKrLSEDIYAKGK 241
Cdd:cd19083 156 SLEQLKEAN----KDGYVD--VLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTK-FPDNDLRNDK 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 242 YDITHDEDLAIIHRVEEL---AEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELY 315
Cdd:cd19083 229 PLFKGERFSENLDKVDKLksiADEKGVTVAHLALAWYLTRpaIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDALF 307
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-306 |
2.28e-65 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 208.96 E-value: 2.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 13 VSKVCLGCMGFGEAQkgmhswTLpyEESKKIIKYALDNGINFFDTAIGY-------QGGTSEAFLGKAIKEYAKREDVII 85
Cdd:cd19094 1 VSEICLGTMTWGEQN------TE--AEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLKKKGNRDKVVL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 86 ATKFIPRTqEEIEQGIDA-----KQHIENCLNGSLKRLDMDYVDLYILHMWDYNTP------------------IEDIMA 142
Cdd:cd19094 73 ATKVAGPG-EGITWPRGGgtrldRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 143 ALHDVIRQGKVRYIGISNCYAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLA 222
Cdd:cd19094 152 ALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 223 ---KHPGEESKRLSEDIYAKGKYDITHDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVK 297
Cdd:cd19094 232 gkyLDGAARPEGGRLNLFPGYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRpfVTSTIIGATTLEQLKENID 311
|
....*....
gi 1797152346 298 AVAVKLTDE 306
Cdd:cd19094 312 AFDVPLSDE 320
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-315 |
3.91e-63 |
|
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: 202.52 E-value: 3.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 39 ESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYakREDVIIATK--FIPRTQEEIEQGIDAKQhIENCLNGSLK 116
Cdd:cd19102 27 DSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL--RDRPIVATKcgLLWDEEGRIRRSLKPAS-IRAECEASLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 117 RLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAKAKgyeqfvSIQGHYNLIFREEE 196
Cdd:cd19102 104 RLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIA------SLQPPYSLLRRGIE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 197 REMKQYCVAHNIAMTPYSALASGRLAKHPGEES-KRLSEDIYAKGKYDITHD---EDLAIIHRVEELAEKKGVSMTEISL 272
Cdd:cd19102 178 AEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERvASLPADDWRRRSPFFQEPnlaRNLALVDALRPIAERHGRTVAQLAI 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1797152346 273 AWLL--TKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELY 315
Cdd:cd19102 258 AWVLrrPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-298 |
6.48e-63 |
|
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: 201.24 E-value: 6.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 14 SKVCLGCMGFGeaqkgmhsWTLPYEESKKIIKYALDNGINFFDTAIGYQG----GTSEAFLGKAIKEYAKREDVIIATK- 88
Cdd:cd19082 1 SRIVLGTADFG--------TRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGNRDKVVIATKg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 89 --------FIPR-TQEEIEQgiDakqhiencLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGIS 159
Cdd:cd19082 73 ghpdledmSRSRlSPEDIRA--D--------LEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGAS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 160 NcyaW---QIAKANEIAKAKGYEQFVSIQGHYNLIFREEER-----------EMKQYCVAHNIAMTPYSALASGRLAKHP 225
Cdd:cd19082 143 N---WsteRIAEANAYAKAHGLPGFAASSPQWSLARPNEPPwpgptlvamdeEMRAWHEENQLPVFAYSSQARGFFSKRA 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1797152346 226 GEESKRLSEDiyaKGKYDitHDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKA 298
Cdd:cd19082 220 AGGAEDDSEL---RRVYY--SEENFERLERAKELAEEKGVSPTQIALAYVLNQpfPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-313 |
9.88e-61 |
|
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: 196.30 E-value: 9.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 10 DLMVSKVCLGCMGFGEAQKGMHSwtlpYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYakREDVIIATKF 89
Cdd:cd19078 1 GLEVSAIGLGCMGMSHGYGPPPD----KEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF--RDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 90 ---IPRTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNcyawqi 166
Cdd:cd19078 75 gfkIDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSE------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 167 AKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESK-----------RLSED 235
Cdd:cd19078 149 AGVETIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKfdegddraslpRFTPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 236 IYAKgkydithdeDLAIIHRVEELAEKKGVSMTEISLAWLLTK----VtsPIIGATKPHHIDGAVKAVAVKLTDEEIIYL 311
Cdd:cd19078 229 ALEA---------NQALVDLLKEFAEEKGATPAQIALAWLLAKkpwiV--PIPGTTKLSRLEENIGAADIELTPEELREI 297
|
..
gi 1797152346 312 EE 313
Cdd:cd19078 298 ED 299
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-306 |
7.93e-60 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. 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: 381369 [Multi-domain] Cd Length: 319 Bit Score: 194.35 E-value: 7.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGC-MGFGEAQKGmhswtlpyEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYA- 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDV--------DEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 79 KREDVIIATKFI------PRTQeeieQGIDAKQHIENClNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGK 152
Cdd:cd19143 73 PRSDYVVSTKIFwggggpPPND----RGLSRKHIVEGT-KASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 153 VRYIGISNCYAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREE-EREMKQYCVAHNIAMTPYSALASGRL-AKHPGE--E 228
Cdd:cd19143 148 AFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERvEVEYAPLYEKYGLGTTTWSPLASGLLtGKYNNGipE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 229 SKRLSEDIYaKGKYDITHDEDLAIIHRVEEL---AEKKGVSMTEISLAWLLT--KVTSPIIGATKPHHIDGAVKAVAV-- 301
Cdd:cd19143 228 GSRLALPGY-EWLKDRKEELGQEKIEKVRKLkpiAEELGCSLAQLAIAWCLKnpNVSTVITGATKVEQLEENLKALEVlp 306
|
....*
gi 1797152346 302 KLTDE 306
Cdd:cd19143 307 KLTPE 311
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-313 |
8.89e-60 |
|
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: 194.03 E-value: 8.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 3 YVKLGDSDLMVSKVCLGCMGFGeaqKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyaKRED 82
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIG---GGPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG--RRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 83 VIIATKF-----IPRTQEEIEQ-GID-----AKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQG 151
Cdd:cd19149 76 VVLATKCglrwdREGGSFFFVRdGVTvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 152 KVRYIGISNCYAWQIAKANEiakakgYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKR 231
Cdd:cd19149 156 KIRAIGASNVSVEQIKEYVK------AGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 232 LSEDIYAKGK-YDITHDED-LAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEE 307
Cdd:cd19149 230 DAGDARSGIPwFSPENREKvLALLEKWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARKPEQAEENAKAGDIRLSAED 309
|
....*.
gi 1797152346 308 IIYLEE 313
Cdd:cd19149 310 IATMRS 315
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-308 |
1.03e-59 |
|
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: 192.06 E-value: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 13 VSKVCLGCMGFGEaqkGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKREDVIIATKFIPR 92
Cdd:cd19072 4 VPVLGLGTWGIGG---GMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGF-DREDLFITTKVSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 93 TQeeieqgidAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNC------YAWQI 166
Cdd:cd19072 80 HL--------KYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFsleeleEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 167 AKANEIakakgyeqfVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESkrlsediyakgkydith 246
Cdd:cd19072 152 LKKGPI---------VANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL----------------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797152346 247 dedlaiihrVEELAEKKGVSMTEISLAWLLTK-VTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19072 206 ---------LDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDL 259
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-299 |
2.86e-58 |
|
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: 189.47 E-value: 2.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 14 SKVCLGCMGFGEaqkgmhswTLPYEESKKIIKYALDNGINFFDTA-------IGYQGGTSEAFLGKAIKEYAKREDVIIA 86
Cdd:cd19752 1 SELCLGTMYFGT--------RTDEETSFAILDRYVAAGGNFLDTAnnyafwtEGGVGGESERLIGRWLKDRGNRDDVVIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 87 TKF-----IPRTQEEIEQGIDAKQhIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNC 161
Cdd:cd19752 73 TKVgagprDPDGGPESPEGLSAET-IEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 162 YAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREEER----------EMKQYCVAH-NIAMTPYSALASGRLAKhpgeESK 230
Cdd:cd19752 152 AAWRLERARQIARQQGWAEFSAIQQRHSYLRPRPGAdfgvqrivtdELLDYASSRpDLTLLAYSPLLSGAYTR----PDR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797152346 231 RLSEDiyakgkYDitHDEDLAIIHRVEELAEKKGVSMTEISLAWLL--TKVTSPIIGATKPHHIDGAVKAV 299
Cdd:cd19752 228 PLPEQ------YD--GPDSDARLAVLEEVAGELGATPNQVVLAWLLhrTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-298 |
2.68e-56 |
|
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: 182.68 E-value: 2.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 11 LMVSKVCLGCMGFGEAQKGMHSwtlpYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyaKREDVIIATKFI 90
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWWGDVD----DAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG--RRDKVVIATKFG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 91 PRTQEEIEQGIDA-KQHIENCLNGSLKRLDMDYVDLYILHMWDYN-TPIEDIMAALHDVIRQGKVRYIGISncyawqIAK 168
Cdd:cd19086 75 NRFDGGPERPQDFsPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVS------VGD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 169 ANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHN---IAMTPysaLASGRLAkhpgeeskrlsediyakGKydit 245
Cdd:cd19086 149 PEEALAALRRGGIDVVQVIYNLLDQRPEEELFPLAEEHGvgvIARVP---LASGLLT-----------------GK---- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1797152346 246 hdedlaiihrveelaekkgvsMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKA 298
Cdd:cd19086 205 ---------------------LAQAALRFILSHpaVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
13-312 |
3.46e-55 |
|
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: 182.33 E-value: 3.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 13 VSKVCLGCMGFGEAQKG-MHSwtLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYAKREDVIIATKF-I 90
Cdd:cd19147 10 VSPLILGAMSIGDAWSGfMGS--MDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIVIATKFtT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 91 PRTQEEIEQGIDA------KQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAW 164
Cdd:cd19147 88 DYKAYEVGKGKAVnycgnhKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 165 QIAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRL-AKHPGEESKRLSEDIYAKGKYD 243
Cdd:cd19147 168 VVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFqSKKAVEERKKNGEGLRSFVGGT 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1797152346 244 ITHDEDLAIIHRVEELAEKKGV-SMTEISLAWLLTKVTS--PIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19147 248 EQTPEEVKISEALEKVAEEHGTeSVTAIALAYVRSKAPNvfPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-314 |
4.75e-55 |
|
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: 181.38 E-value: 4.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 10 DLMVSKVCLGCMGFG---EAQKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKREDVIIA 86
Cdd:cd19103 1 DKKLPKIALGTWSWGsggAGGDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRY-PREDYIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 87 TKFIPrtqeeieQGIDAKQH-IENCLNGSLKRLDMDYVDLYILHMwdyNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQ 165
Cdd:cd19103 80 TKFTP-------QIAGQSADpVADMLEGSLARLGTDYIDIYWIHN---PADVERWTPELIPLLKSGKVKHVGVSNHNLAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 166 IAKANEIAKAKGYEqFVSIQGHYNLIFREEERE-MKQYCVAHNIAMTPYSALASGRLAKHPGEEsKRLSEDIYAKGKYDI 244
Cdd:cd19103 150 IKRANEILAKAGVS-LSAVQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQGALSGKYDTK-HPLPEGSGRAETYNP 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 245 THDEDLAIIHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19103 228 LLPQLEELTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-308 |
2.67e-54 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 179.76 E-value: 2.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 3 YVKLGDSDLMVSKVCLGC-MGFGEAQkgmhswtlPYEESKKIIKYALDNGINFFDTAIGYQG--GTSEAFLGKAIKE--Y 77
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLwHNFGDYT--------SPEEARELLRTAFDLGITHFDLANNYGPppGSAEENFGRILKRdlR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 78 AKREDVIIATKFIPRTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIG 157
Cdd:cd19089 73 PYRDELVISTKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 158 ISNCYAWQIAKANEIAKAKGYeQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLA----KHPGEESKRLS 233
Cdd:cd19089 153 ISNYPGAKARRAIALLRELGV-PLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTdkylNGIPPDSRRAA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1797152346 234 EDIYAKGKYdIThDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAV-AVKLTDEEI 308
Cdd:cd19089 232 ESKFLTEEA-LT-PEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDprVTSVLIGASSPSQLEDNVAALkNLDFSEEEL 307
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-314 |
4.28e-52 |
|
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: 173.77 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 4 VKLGDSDLMVSKVCLGCMGFgeaqKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyAKREDV 83
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMGL----SGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKD-GPREKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 84 IIATKFIPRTQEEieQGIDAK---QHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISN 160
Cdd:cd19145 78 QLATKFGIHEIGG--SGVEVRgdpAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 161 cyawqiAKANEIAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKrLSEDIYAKg 240
Cdd:cd19145 156 ------ASADTIRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEEL-LENSDVRK- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 241 KYDITHDEDL----AIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEiiyLEEL 314
Cdd:cd19145 228 SHPRFQGENLeknkVLYERVEALAKKKGCTPAQLALAWVLHQgeDVVPIPGTTKIKNLNQNIGALSVKLTKED---LKEI 304
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
21-304 |
8.54e-51 |
|
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: 168.94 E-value: 8.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 21 MGFGeaqkGMHsWTLPY--------EESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYakREDVIIATKF-IP 91
Cdd:cd19088 4 LGYG----AMR-LTGPGiwgppadrEEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPY--PDDVVIATKGgLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 92 RTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNcyawqiAKANE 171
Cdd:cd19088 77 RTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSN------VTVAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 172 IAKAKGYEQFVSIQGHYNLIFREEErEMKQYCVAHNIAMTPYSALASGRLAKHPGEeskrlsediyakgkydithdedla 251
Cdd:cd19088 151 IEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLAQPGGL------------------------ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1797152346 252 iihrVEELAEKKGVSMTEISLAWLL--TKVTSPIIGATKPHHIDGAVKAVAVKLT 304
Cdd:cd19088 206 ----LAEVAARLGATPAQVALAWLLarSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-307 |
1.40e-49 |
|
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: 166.96 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 9 SDLMVSKVCLGCMGFGEaqkgmhsWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEY-AKREDVIIAT 87
Cdd:cd19092 2 EGLEVSRLVLGCMRLAD-------WGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNpGLREKIEIQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 88 KF-IPRTQEEIEQGI---DA-KQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCY 162
Cdd:cd19092 75 KCgIRLGDDPRPGRIkhyDTsKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 163 AWQIAK----------ANEIakakgyeQFvSIqGHYNLIFreeeREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKRL 232
Cdd:cd19092 155 PSQIELlqsyldqplvTNQI-------EL-SL-LHTEAID----DGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1797152346 233 SEDIyakgkydithdedlaiihrvEELAEKKGVSMTEISLAWLLT---KVtSPIIGATKPHHIDGAVKAVAVKLTDEE 307
Cdd:cd19092 222 RAAL--------------------EELAEEYGVTIEAIALAWLLRhpaRI-QPILGTTNPERIRSAVKALDIELTREE 278
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-316 |
9.50e-49 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 166.92 E-value: 9.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFGeaqkgmhswTLPYEESKKIIKYALDNGINFFDTAIGYqgGTSEAFLGKAIKEYakR 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLP---------RKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGP--R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 81 EDVIIATKFIPRTQeeieqgiDAKQhIENCLNGSLKRLDMDYVDLYILH----MWDYNTPIED--IMAALHDVIRQGKVR 154
Cdd:COG1453 68 DKVILATKLPPWVR-------DPED-MRKDLEESLKRLQTDYIDLYLIHglntEEDLEKVLKPggALEALEKAKAEGKIR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 155 YIGISNCYAWQIAKanEIAKAKGYEqFVSIQghYNLIFREEEREMK--QYCVAHNIAMTPYSALASGRLAKHPGEeskrl 232
Cdd:COG1453 140 HIGFSTHGSLEVIK--EAIDTGDFD-FVQLQ--YNYLDQDNQAGEEalEAAAEKGIGVIIMKPLKGGRLANPPEK----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 233 sediyakgkydithdedlaiihrVEELAEKKgVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAV--AVKLTDEEI 308
Cdd:COG1453 210 -----------------------LVELLCPP-LSPAEWALRFLLSHpeVTTVLSGMSTPEQLDENLKTAdnLEPLTEEEL 265
|
....*...
gi 1797152346 309 IYLEELYK 316
Cdd:COG1453 266 AILERLAE 273
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-299 |
6.32e-47 |
|
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: 160.41 E-value: 6.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 15 KVCLGCMGFGEAQKgmhSWTLpyEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIkeyAKREDVIIATKFIPRTQ 94
Cdd:cd19075 2 KIILGTMTFGSQGR---FTTA--EAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELG---LGERGFKIDTKANPGVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 95 eeieqGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAK 174
Cdd:cd19075 74 -----GGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 175 AKGYeqfvsI-----QGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKRLSE----------DIYaK 239
Cdd:cd19075 149 ENGW-----VlptvyQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGgrfdpnnalgKLY-R 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 240 GKYDitHDEDLAIIHRVEELAEKKGVSMTEISLAWLLTKvtSP---------IIGATKPHHIDGAVKAV 299
Cdd:cd19075 223 DRYW--KPSYFEALEKVEEAAEKEGISLAEAALRWLYHH--SAldgekgdgvILGASSLEQLEENLAAL 287
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-322 |
6.41e-45 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 155.68 E-value: 6.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFgEAQKGMHSwtlPYEESKKIIKYALDNGINFFDTAIGYqgGTSEAFLGKAIKE-YAK 79
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGL-SAFYGPPK---PDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQnPGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 80 REDVIIATKF-IPRTQEEIEQGIDAK-QHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIG 157
Cdd:cd19144 75 REKIFLATKFgIEKNVETGEYSVDGSpEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 158 ISNCyawqiaKANEIAKAKGYEQFVSIQGHYN---LIFREEEREMKQYCVAHNIAMTPYSALASGRLAK--------HPG 226
Cdd:cd19144 155 LSEC------SAETLRRAHAVHPIAAVQIEYSpfsLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGairspddfEEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 227 EESK---RLSEDIYAKgkydithdeDLAIIHRVEELAEKKGVSMTEISLAWLLTKVTS--PIIGATKPHHIDGAVKAVAV 301
Cdd:cd19144 229 DFRRmapRFQAENFPK---------NLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDiiPIPGTTKLKRLEENLGALKV 299
|
330 340
....*....|....*....|.
gi 1797152346 302 KLTDEEIIYLEELYKPHRLVG 322
Cdd:cd19144 300 KLTEEEEKEIREIAEEAEVVG 320
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-308 |
9.47e-44 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 152.17 E-value: 9.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 2 EYVKLGDSDLMVSKVCLGCM-GFGEAQKgmhswtlpYEESKKIIKYALDNGINFFDTAIGY--QGGTSEAFLGKAIKEYA 78
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWhNFGDVDR--------YENSRAMLRRAFDLGITHFDLANNYgpPPGSAEENFGRILKEDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 79 K--REDVIIATKFIPRTQEEIEQGIDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYI 156
Cdd:cd19151 73 KpyRDELIISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 157 GISNCYAWQIAKANEIAKAKGYEQFVSiQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKH-----PgEESKR 231
Cdd:cd19151 153 GISNYPPEEAREAAAILKDLGTPCLIH-QPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRylngiP-EDSRA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 232 LSEDIYAKgKYDIThDEDLAIIHRVEELAEKKGVSMTEISLAWLL--TKVTSPIIGATKPHHIDGAVKAVA-VKLTDEEI 308
Cdd:cd19151 231 AKGSSFLK-PEQIT-EEKLAKVRRLNEIAQARGQKLAQMALAWVLrnKRVTSVLIGASKPSQIEDAVGALDnREFSEEEL 308
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
22-320 |
1.16e-43 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 150.59 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 22 GFGeaqkgmhSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-AKREDVIIATKFIPRTQ--EEIE 98
Cdd:COG0656 9 GLG-------TWQLPGEEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAASgVPREELFVTTKVWNDNHgyDDTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 99 QGIDAkqhienclngSLKRLDMDYVDLYILHmWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAKAKgy 178
Cdd:COG0656 79 AAFEE----------SLERLGLDYLDLYLIH-WPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVK-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 179 eqFVSIQGHYNLIFReeEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEE 258
Cdd:COG0656 146 --PAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGKLLDDP-----------------------------VLAE 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1797152346 259 LAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRL 320
Cdd:COG0656 193 IAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-299 |
1.97e-42 |
|
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: 146.96 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFGEaqkgmhswtlpyeESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKR 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPR-------------ESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGL-RR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 81 EDVIIATKFIPRTQEeieqgiDAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPI---EDIMAALHDVIRQGKVRYIG 157
Cdd:cd19105 67 DKVFLATKASPRLDK------KDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 158 ISnCYAWQIAKANEIAKAKGYEqfvSIQGHYNLIFREEERE--MKQyCVAHNIAMTPYSALASGRLakhpgeeskrlsed 235
Cdd:cd19105 141 FS-THDNMAEVLQAAIESGWFD---VIMVAYNFLNQPAELEeaLAA-AAEKGIGVVAMKTLAGGYL-------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797152346 236 iyakgkyditHDEDLAIIhrveelaEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAV 299
Cdd:cd19105 202 ----------QPALLSVL-------KAKGFSLPQAALKWVLSNprVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-307 |
4.42e-42 |
|
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: 147.84 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 10 DLMVSKVCLGCMGFGEAQkgmhsWTLPYE-ESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYAKREDVIIATK 88
Cdd:cd19148 1 DLPVSRIALGTWAIGGWM-----WGGTDEkEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRDRVVIATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 89 FIPRTQEEIEQGIDA-KQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIA 167
Cdd:cd19148 76 VGLEWDEGGEVVRNSsPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 168 KANEIAKakgyeqFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLA-------KHPGEESKRlSEDIYAKG 240
Cdd:cd19148 156 TFRKVAP------LHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSgkmtkdtKFEGDDLRR-TDPKFQEP 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 241 KYdithDEDLAIIHRVEELAEKK-GVSMTEISLAWLLTKVTSPII--GATKPHHIDGAVKAVAVKLTDEE 307
Cdd:cd19148 229 RF----SQYLAAVEELDKLAQERyGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDED 294
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-228 |
1.78e-41 |
|
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: 144.16 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 3 YVKLGDSDLMVSKVCLGCMGFGEaqkgmhswtLPYEESKKIIKYALDNGINFFDTAIGYqgGTSEAFLGKAIKEYakRED 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR---------LSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKGR--RDK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 83 VIIATKFIPRTQEEieqgidAKQHIENclngSLKRLDMDYVDLYILH----MWDYNTPIED--IMAALHDVIRQGKVRYI 156
Cdd:cd19100 68 VFLATKTGARDYEG------AKRDLER----SLKRLGTDYIDLYQLHavdtEEDLDQVFGPggALEALLEAKEEGKIRFI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1797152346 157 GISnCYAWQIAKaneiaKAKGYEQFVSIQGHYNLIFREEEREMKQ---YCVAHNIAMTPYSALASGRLAKHPGEE 228
Cdd:cd19100 138 GIS-GHSPEVLL-----RALETGEFDVVLFPINPAGDHIDSFREEllpLAREKGVGVIAMKVLAGGRLLSGDPLD 206
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
13-315 |
1.07e-40 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 144.30 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 13 VSKVCLGCMGFgeaqkgmhSWT---LPYEESKKIIKYALDNGINFFDTAIGYqgGTSEAF-----LGKAIKEY-AKREDV 83
Cdd:cd19077 5 VGPIGLGLMGL--------TWRpnpTPDEEAFETMKAALDAGSNLWNGGEFY--GPPDPHanlklLARFFRKYpEYADKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 84 IIATKF-------IPRTQEEieqgiDAKQHIENCLngslKRLDM-DYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRY 155
Cdd:cd19077 75 VLSVKGgldpdtlRPDGSPE-----AVRKSIENIL----RALGGtKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 156 IGISNCYAWQIAKANEIAKakgyeqFVSIQGHYNLIFRE-EEREMKQYCVAHNIAMTPYSALASGRLA---KHPGEE--- 228
Cdd:cd19077 146 IGLSEVSAETIRRAHAVHP------IAAVEVEYSLFSREiEENGVLETCAELGIPIIAYSPLGRGLLTgriKSLADIpeg 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 229 -----SKRLSEDIYAKgkydithdeDLAIIHRVEELAEKKGVSMTEISLAWLLTKVTS---PIIGATKPHHIDGAVKAVA 300
Cdd:cd19077 220 dfrrhLDRFNGENFEK---------NLKLVDALQELAEKKGCTPAQLALAWILAQSGPkiiPIPGSTTLERVEENLKAAN 290
|
330
....*....|....*
gi 1797152346 301 VKLTDEEiiyLEELY 315
Cdd:cd19077 291 VELTDEE---LKEIN 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-306 |
1.54e-40 |
|
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: 143.08 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 14 SKVCLGCMGFGEAQKGmhswtLPYEESKKIIKYALDNGINFFDTAIGYqgGTSEAFLGKAIKEYaKREDVIIATKFIPRT 93
Cdd:cd19090 1 SALGLGTAGLGGVFGG-----VDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAEL-PREPLVLSTKVGRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 94 QEEIEQGIDA-KQHIENclngSLKRLDMDYVDLYILH-----MWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYA---W 164
Cdd:cd19090 73 EDTADYSADRvRRSVEE----SLERLGRDRIDLLMIHdpervPWVDILAPGGALEALLELKEEGLIKHIGLGGGPPdllR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 165 QIAKANEIAKAKGYeqfvsiqGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEeskrlsediYAKGKYDI 244
Cdd:cd19090 149 RAIETGDFDVVLTA-------NRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPE---------RVRYTYRW 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797152346 245 THDEDLAIIHRVEELAEKKGVSMTEISLAWLLT--KVTSPIIGATKPHHIDGAVKAVAVKLTDE 306
Cdd:cd19090 213 LSPELLDRAKRLYELCDEHGVPLPALALRFLLRdpRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-315 |
3.19e-39 |
|
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: 140.86 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 2 EYVKLGDSDLMVSKVCLGCMGFGEAqkgmhsWTL-PYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyaKR 80
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGGL------MGRtTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKG--LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 81 EDVIIATKfIPRTQEEIEqgiDAKQHIENCLNGSLKRLDMDYVDLYILH---------MWDYNTPIEDIM------AALH 145
Cdd:cd19104 73 AGPYITTK-VRLDPDDLG---DIGGQIERSVEKSLKRLKRDSVDLLQLHnrigderdkPVGGTLSTTDVLglggvaDAFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 146 DVIRQGKVRYIGISncyAWQIAKAneIAKAKGYEQFVSIQGHYNLI------------FREEEREMKQYCVAHNIAMTPY 213
Cdd:cd19104 149 RLRSEGKIRFIGIT---GLGNPPA--IRELLDSGKFDAVQVYYNLLnpsaaearprgwSAQDYGGIIDAAAEHGVGVMGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 214 SALASGRLAKHP--GEESKRLSEDIYAKgkydithDEDLAIihRVEELAEKKGVSMTEISLAWLLT--KVTSPIIGATKP 289
Cdd:cd19104 224 RVLAAGALTTSLdrGREAPPTSDSDVAI-------DFRRAA--AFRALAREWGETLAQLAHRFALSnpGVSTVLVGVKNR 294
|
330 340
....*....|....*....|....*..
gi 1797152346 290 HHIDGAVKAVAV-KLTDEEIIYLEELY 315
Cdd:cd19104 295 EELEEAVAAEAAgPLPAENLARLEALW 321
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
21-312 |
2.78e-38 |
|
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: 136.46 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 21 MGFGeaqkgmhSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKFIPRTQeeieq 99
Cdd:cd19071 4 IGLG-------TYKLKPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESGvPREELFITTKLWPTDH----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 100 gidAKQHIENCLNGSLKRLDMDYVDLYILH---MWDYNTPIEDIMA---ALHDVIRQGKVRYIGISNCYAWQIAKANEIA 173
Cdd:cd19071 69 ---GYERVREALEESLKDLGLDYLDLYLIHwpvPGKEGGSKEARLEtwrALEELVDEGLVRSIGVSNFNVEHLEELLAAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 174 KAKGyeqfVSIQGHYNLIFREeeREMKQYCVAHNIAMTPYSALASGR--LAKHPgeeskrlsediyakgkydithdedla 251
Cdd:cd19071 146 RIKP----AVNQIELHPYLQQ--KELVEFCKEHGIVVQAYSPLGRGRrpLLDDP-------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797152346 252 iihRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19071 194 ---VLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
29-308 |
2.99e-38 |
|
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: 135.86 E-value: 2.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-AKREDVIIATKfIPRtqeeieQGIDAKQHI 107
Cdd:cd19073 5 GLGTWQLRGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESgVPREDLFITTK-VWR------DHLRPEDLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 108 ENCLNgSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAKAK-GYEQfvsIQG 186
Cdd:cd19073 75 KSVDR-SLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPiAVNQ---VEF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 187 HYNLifreEEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEELAEKKGVS 266
Cdd:cd19073 151 HPFL----YQAELLEYCRENDIVITAYSPLARGEVLRDP-----------------------------VIQEIAEKYDKT 197
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1797152346 267 MTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19073 198 PAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDV 239
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
3-312 |
6.66e-37 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. 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: 381364 [Multi-domain] Cd Length: 266 Bit Score: 133.14 E-value: 6.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 3 YVKLGDSDLmVSKVCLGCMGFGEaqkGMHSWtlpyEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYakRED 82
Cdd:cd19138 2 TVTLPDGTK-VPALGQGTWYMGE---DPAKR----AQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGR--RDK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 83 VIIATKFIPRTQeeieqgidAKQHIENCLNGSLKRLDMDYVDLYILHmWDYNTPIEDIMAALHDVIRQGKVRYIGISNCY 162
Cdd:cd19138 72 VFLVSKVLPSNA--------SRQGTVRACERSLRRLGTDYLDLYLLH-WRGGVPLAETVAAMEELKKEGKIRAWGVSNFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 163 ------AWQIAKANEIAkakgyeqfvSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKRLSedi 236
Cdd:cd19138 143 tddmeeLWAVPGGGNCA---------ANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPTLK--- 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1797152346 237 yakgkydithdedlaiihrveELAEKKGVSMTEISLAWLL-TKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19138 211 ---------------------EIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
44-308 |
5.03e-36 |
|
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: 130.82 E-value: 5.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 44 IKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-AKREDVIIATKFIPRTQeeieqgidakqHIENCLNGSLKRLDMDY 122
Cdd:cd19120 31 VKLALKAGFRHIDTAEMYG---NEKEVGEALKESgVPREDLFITTKVSPGIK-----------DPREALRKSLAKLGVDY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 123 VDLYILHM--WDYN--TPIEDIMAALHDVIRQGKVRYIGISNcyaWQIAKANEIAKAKGYEQFVS-IQGHYNLIFREEEr 197
Cdd:cd19120 97 VDLYLIHSpfFAKEggPTLAEAWAELEALKDAGLVRSIGVSN---FRIEDLEELLDTAKIKPAVNqIEFHPYLYPQQPA- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 198 eMKQYCVAHNIAMTPYSALASgrlakhpgeeskrlsediyakgkydITHDEDLAIIHRVEELAEKKGVSMTEISLAWLLT 277
Cdd:cd19120 173 -LLEYCREHGIVVSAYSPLSP-------------------------LTRDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQ 226
|
250 260 270
....*....|....*....|....*....|.
gi 1797152346 278 KVTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19120 227 KGIVVVTTSSKEERMKEYLEAFDFELTEEEV 257
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-308 |
7.99e-36 |
|
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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 131.18 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 48 LDNGINFFDTAIGYqgGTSEAFLGKAIKEYAKR----EDVIIATKFIPRTQEeieQGIDaKQHIENCLNGSLKRLDMDYV 123
Cdd:cd19101 33 VDAGLTTFDCADIY--GPAEELIGEFRKRLRRErdaaDDVQIHTKWVPDPGE---LTMT-RAYVEAAIDRSLKRLGVDRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 124 DLYILHMWDYNTP-IEDIMAALHDVIRQGKVRYIGISNCYAWQIAkanEIAKAkGYEqFVSIQGHYNLIFREEEREMKQY 202
Cdd:cd19101 107 DLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLR---EILDA-GVP-IVSNQVQYSLLDRRPENGMAAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 203 CVAHNIAMTPYSALASGRLA-KHPGE-ESKRLSEDIYAKGKYDITHDE------------DLAIIhrveelAEKKGVSMT 268
Cdd:cd19101 182 CEDHGIKLLAYGTLAGGLLSeKYLGVpEPTGPALETRSLQKYKLMIDEwggwdlfqellrTLKAI------ADKHGVSIA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1797152346 269 EISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19101 256 NVAVRWVLDQpgVAGVIVGARNSEHIDDNVRAFSFRLDDEDR 297
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-304 |
1.30e-35 |
|
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: 131.03 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 3 YVKLGDSDLMVSkvclgCMGFGeaqkgmhSWT-----LPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEY 77
Cdd:cd19141 2 YRNLGKSGLRVS-----CLGLG-------TWVtfgsqISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 78 A-KREDVIIATKFIPRTQEEIEQGIDAKQHIENcLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYI 156
Cdd:cd19141 70 GwRRSSYVITTKIFWGGKAETERGLSRKHIIEG-LKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 157 GISNCYAWQIAKANEIAKakgyeQF-----VSIQGHYNLiFREEEREMKQYCVAHNI---AMTpYSALASGRLAKHPGE- 227
Cdd:cd19141 149 GTSRWSAMEIMEAYSVAR-----QFnlippIVEQAEYHL-FQREKVEMQLPELFHKIgvgAMT-WSPLACGILSGKYDDg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 228 --ESKRLSEDIYAKGKYDITHDE---DLAIIHRVEELAEKKGVSMTEISLAWLLT--KVTSPIIGATKPHHIDGAVKAVA 300
Cdd:cd19141 222 vpEYSRASLKGYQWLKEKILSEEgrrQQAKLKELQIIADRLGCTLPQLAIAWCLKneGVSSVLLGASSTEQLYENLQAIQ 301
|
....*.
gi 1797152346 301 V--KLT 304
Cdd:cd19141 302 VlpKLT 307
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
38-308 |
1.56e-35 |
|
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: 129.61 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 38 EESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKREDVIIATKFIPRTQEeieqgidaKQHIENCLNGSLKR 117
Cdd:cd19137 26 EEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDF-PREDLFIVTKVWPTNLR--------YDDLLRSLQNSLRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 118 LDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIakanEIAKAKGYEQFVSIQGHYNLIFRE-EE 196
Cdd:cd19137 97 LDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLL----EEAISKSQTPIVCNQVKYNLEDRDpER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 197 REMKQYCVAHNIAMTPYSALASGRLAKhpgeesKRLsediyakgkydithdedlaiihrVEELAEKKGVSMTEISLAWLL 276
Cdd:cd19137 173 DGLLEYCQKNGITVVAYSPLRRGLEKT------NRT-----------------------LEEIAKNYGKTIAQIALAWLI 223
|
250 260 270
....*....|....*....|....*....|....*
gi 1797152346 277 TK---VTSPIigATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19137 224 QKpnvVAIPK--AGRVEHLKENLKATEIKLSEEEM 256
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-301 |
2.40e-35 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 130.55 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSkvclgCMGFGeaqkgmhSWT-----LPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIK 75
Cdd:cd19159 1 MKYRNLGKSGLRVS-----CLGLG-------TWVtfggqISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 76 EYA-KREDVIIATKFIPRTQEEIEQGIdAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVR 154
Cdd:cd19159 69 KKGwRRSSLVITTKLYWGGKAETERGL-SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 155 YIGISNCYAWQIAKANEIAKAKGYEQFVSIQGHYNLiFREEEREMKQYCVAHNI---AMTpYSALASGRLAKHPGE---E 228
Cdd:cd19159 148 YWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHL-FQREKVEVQLPELYHKIgvgAMT-WSPLACGIISGKYGNgvpE 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1797152346 229 SKRLSEDIYAKGKYDITHDEDLAIIHRVEEL---AEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAV 301
Cdd:cd19159 226 SSRASLKCYQWLKERIVSEEGRKQQNKLKDLspiAERLGCTLPQLAVAWCLRNegVSSVLLGSSTPEQLIENLGAIQV 303
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
22-298 |
3.66e-35 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 128.12 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 22 GFGEAQKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYqgGTSEAFLGKAIKEYAkREDVIIATKfiprTQEEIEQGI 101
Cdd:cd19095 4 GLGTSGIGRVWGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLR-RDDLFIATK----VGTHGEGGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 102 DAKQ----HIENCLNGSLKRLDMDYVDLYILHM---WDYNtpiEDIMAALHDVIRQGKVRYIGISNcyawqiaKANEIAK 174
Cdd:cd19095 77 DRKDfspaAIRASIERSLRRLGTDYIDLLQLHGpsdDELT---GEVLETLEDLKAAGKVRYIGVSG-------DGEELEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 175 AKGYEQFVSIQGHYNLIFREEEREMKQycvAHN-----IAMTPysaLASGRLakHPGEESKRLSEDIYAkgkydithded 249
Cdd:cd19095 147 AIASGVFDVVQLPYNVLDREEEELLPL---AAEaglgvIVNRP---LANGRL--RRRVRRRPLYADYAR----------- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1797152346 250 laiihRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKA 298
Cdd:cd19095 208 -----RPEFAAEIGGATWAQAALRFVLSHpgVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-235 |
7.14e-35 |
|
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: 127.29 E-value: 7.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 14 SKVCLGCMGFGEAQKGmhswTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKREDVIIATKFIPRT 93
Cdd:cd19096 1 SVLGFGTMRLPESDDD----SIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEG-PREKFYLATKLPPWS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 94 QEEIEqgiDAKQHIENclngSLKRLDMDYVDLYILHM-----WDYNTPIEDIMAALHDVIRQGKVRYIGISNCyawqiAK 168
Cdd:cd19096 76 VKSAE---DFRRILEE----SLKRLGVDYIDFYLLHGlnspeWLEKARKGGLLEFLEKAKKEGLIRHIGFSFH-----DS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1797152346 169 ANEIAKAKGYEQFVSIQGHYNLIFREEEREMK--QYCVAHN---IAMTPysaLASGRLAKHPGEESKRLSED 235
Cdd:cd19096 144 PELLKEILDSYDFDFVQLQYNYLDQENQAGRPgiEYAAKKGmgvIIMEP---LKGGGLANNPPEALAILCGA 212
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-308 |
3.77e-32 |
|
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: 121.12 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFGeaqkGMHsWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEyAKR 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLG----GVF-GPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKG-IPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 81 EDVIIATKfIPRTQEEIEQGID-AKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIM----AALHDVIRQGKVRY 155
Cdd:cd19163 75 DSYYLATK-VGRYGLDPDKMFDfSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDQILnetlPALQKLKEEGKVRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 156 IGISNcYAWQIAKaNEIAKAKGYEQFVSIQGHYNLIFREEEREMkQYCVAHNIAMTPYSALASGRLAK------HPGees 229
Cdd:cd19163 154 IGITG-YPLDVLK-EVLERSPVKIDTVLSYCHYTLNDTSLLELL-PFFKEKGVGVINASPLSMGLLTErgppdwHPA--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 230 krlsediyakgkyditHDEDLAIIHRVEELAEKKGVSMTEISLAWLL--TKVTSPIIGATKPHHIDGAVKAVAVKLTDEE 307
Cdd:cd19163 228 ----------------SPEIKEACAKAAAYCKSRGVDISKLALQFALsnPDIATTLVGTASPENLRKNLEAAEEPLDAHL 291
|
.
gi 1797152346 308 I 308
Cdd:cd19163 292 L 292
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-316 |
6.73e-32 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 121.88 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCMGFGEAQKgmhswtlpYEESKKIIKYALDNGINFFDTAIGY--------QGGTsEAFLGK 72
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNS--------EADAHAQLDYAVAQGINLIDVAEMYpvpprpetQGLT-ETYIGN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 73 AIKEYAKREDVIIATKF---IPRTQEEI--EQGIDAKqHIENCLNGSLKRLDMDYVDLYILH--------------MWDY 133
Cdd:PRK10625 72 WLAKRGSREKLIIASKVsgpSRNNDKGIrpNQALDRK-NIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgySWTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 134 NTPIE---DIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAKAKGYEQFVSIQGHYNLIFREEE---REMKQYcvaHN 207
Cdd:PRK10625 151 SAPAVsllETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEvglAEVSQY---EG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 208 IAMTPYSALASGRL-------AKHPGEESKRLSEDIyakgKYDITHDEdLAIIHRVeELAEKKGVSMTEISLAWLLTK-- 278
Cdd:PRK10625 228 VELLAYSCLAFGTLtgkylngAKPAGARNTLFSRFT----RYSGEQTQ-KAVAAYV-DIAKRHGLDPAQMALAFVRRQpf 301
|
330 340 350
....*....|....*....|....*....|....*...
gi 1797152346 279 VTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYK 316
Cdd:PRK10625 302 VASTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-308 |
1.48e-31 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 120.25 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 3 YVKLGDSDLMVSKVCLGC-MGFGEAQkgmhswtlPYEESKKIIKYALDNGINFFDTAIGY--QGGTSEAFLGKAIKE--Y 77
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLwHNFGDDT--------PLETQRAILRTAFDLGITHFDLANNYgpPPGSAEENFGRILREdfA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 78 AKREDVIIATKfiprtqeeieQGID----------AKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDV 147
Cdd:cd19150 74 GYRDELIISTK----------AGYDmwpgpygewgSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 148 IRQGKVRYIGISNCYAWQIAKANEIAKAKGYEQFVSiQGHYNLIFR-EEEREMKQYCVAHNIAMTPYSALASGRLA-KHP 225
Cdd:cd19150 144 VRSGKALYVGISSYSPERTREAAAILRELGTPLLIH-QPSYNMLNRwVEESGLLDTLQELGVGCIAFTPLAQGLLTdKYL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 226 G--EESKRLSEDIYAKGKyDIThDEDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAV-A 300
Cdd:cd19150 223 NgiPEGSRASKERSLSPK-MLT-EANLNSIRALNEIAQKRGQSLAQMALAWVLRDgrVTSALIGASRPEQLEENVGALdN 300
|
....*...
gi 1797152346 301 VKLTDEEI 308
Cdd:cd19150 301 LTFSADEL 308
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-290 |
1.99e-31 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 120.26 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGcmgfgeaqkgmhSWT-----LPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIK 75
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLG------------TWStfstaISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 76 EYA-KREDVIIATKFIPRTQEEiEQGIDAKqHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVR 154
Cdd:cd19142 69 KKGwKRSSYIVSTKIYWSYGSE-ERGLSRK-HIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 155 YIGISNCYAWQIAKANEIAKakgyeQFVSI-----QGHYNLIFREE-EREMKQYCVAHNIAMTPYSALASGRLAKHPGEE 228
Cdd:cd19142 147 YWGTSRWSPVEIMEAFSIAR-----QFNCPtpiceQSEYHMFCREKmELYMPELYNKVGVGLITWSPLSLGLDPGISEET 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797152346 229 SKRLSEDIYAKGKYDI------THDEDLAIIHRVEEL---AEKKGVSMTEISLAWLLTK--VTSPIIGATKPH 290
Cdd:cd19142 222 RRLVTKLSFKSSKYKVgsdgngIHEETRRASHKLRELsliAERLGCDLTQLLIAWSLKNenVQCVLIGASSLE 294
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-287 |
2.14e-31 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 120.09 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSkvclgCMGFGeaqkgmhSWT-----LPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIK 75
Cdd:cd19160 3 MKYRNLGKSGLRVS-----CLGLG-------TWVtfgsqISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 76 EYA-KREDVIIATKFIPRTQEEIEQGIdAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVR 154
Cdd:cd19160 71 SKGwRRSSYVVTTKIYWGGQAETERGL-SRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 155 YIGISNCYAWQIAKANEIAKAKGYEQFVSIQGHYNLiFREEEREMKQYCVAHNI---AMTpYSALASGRL-AKHPGE--E 228
Cdd:cd19160 150 YWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHL-FQREKVEMQLPELYHKIgvgSVT-WSPLACGLItGKYDGRvpD 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797152346 229 SKRLSEDIYAKGKYDITHDEDLAIIHRVEEL---AEKKGVSMTEISLAWLLTK--VTSPIIGAT 287
Cdd:cd19160 228 TCRAAVKGYQWLKEKVQSEEGKKQQAKVKELhpiADRLGCTVAQLAIAWCLRSegVSSVLLGVS 291
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
29-320 |
8.11e-31 |
|
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: 117.60 E-value: 8.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-----AKREDVIIATKFIP--RTQEEIEQGi 101
Cdd:cd19111 8 GLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQ---NEKAIGEALKWWlkngkLKREEVFITTKLPPvyLEFKDTEKS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 102 dakqhiencLNGSLKRLDMDYVDLYILHM-WDYN------------TPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAK 168
Cdd:cd19111 84 ---------LEKSLENLKLPYVDLYLIHHpCGFVnkkdkgerelasSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 169 ANEIAKAKGYeqfvSIQGHYNLIFreEEREMKQYCVAHNIAMTPYSALASgrlakhPGEESKRLSEDiyakgKYDITHDE 248
Cdd:cd19111 155 ILAYAKVKPS----NLQLECHAYL--QQRELRKFCNKKNIVVTAYAPLGS------PGRANQSLWPD-----QPDLLEDP 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1797152346 249 dlaiihRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRL 320
Cdd:cd19111 218 ------TVLAIAKELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-313 |
1.33e-30 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 118.55 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSKVCLGCM-GFGEAQkgmhswtlPYEESKKIIKYALDNGINFFDTAIGY--QGGTSEAFLGKAIKE- 76
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWhNFGHVN--------ALESQRAILRKAFDLGITHFDLANNYgpPPGSAEENFGRLLREd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 77 -YAKREDVIIATKfiprtqeeieQGID----------AKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALH 145
Cdd:PRK09912 85 fAAYRDELIISTK----------AGYDmwpgpygsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 146 DVIRQGKVRYIGISNCYAWQIAKANEIAKAKGYEQFVSiQGHYNLIFREEEREMKQYCVAHN----IAMTPYS-ALASGR 220
Cdd:PRK09912 155 HAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIH-QPSYNLLNRWVDKSGLLDTLQNNgvgcIAFTPLAqGLLTGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 221 LAKHPGEESKRLSEDIYAKG-KYDITHDEDLAIIHRVEELAEKKGVSMTEISLAWLL--TKVTSPIIGATKPHHIDGAVK 297
Cdd:PRK09912 234 YLNGIPQDSRMHREGNKVRGlTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQ 313
|
330
....*....|....*..
gi 1797152346 298 AVA-VKLTDEEIIYLEE 313
Cdd:PRK09912 314 ALNnLTFSTEELAQIDQ 330
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
29-320 |
1.05e-29 |
|
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: 115.20 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-----AKREDVIIATKFIPrtqeeieqGIDA 103
Cdd:cd19154 16 GLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQ---NEEAIGEALAELleegvVKREDLFITTKLWT--------HEHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 104 KQHIENCLNGSLKRLDMDYVDLYILHM-W-------DYNT-----------PIEDIMAALHDVIRQGKVRYIGISNCYAW 164
Cdd:cd19154 85 PEDVEEALRESLKKLQLEYVDLYLIHApAafkddegESGTmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVSNFNND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 165 QIAKANEIAKAKGYEQFVSIQGHYnlifreEEREMKQYCVAHNIAMTPYSALASgrlakhPGEESKRLSeDIYAKGKYDI 244
Cdd:cd19154 165 QIQRILDNARVKPHNNQVECHLYF------PQKELVEFCKKHNISVTSYATLGS------PGRANFTKS-TGVSPAPNLL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797152346 245 THDedlaiihRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRL 320
Cdd:cd19154 232 QDP-------IVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
20-314 |
1.29e-29 |
|
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: 113.51 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 20 CMGFGeaqkgmhSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-AKREDVIIATKFIP---RTQe 95
Cdd:cd19140 10 ALGLG-------TYPLTGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASgVPRDELFLTTKVWPdnySPD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 96 eieqgiDAKQHIENclngSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAKA 175
Cdd:cd19140 79 ------DFLASVEE----SLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 176 KgyeqFVSIQGHYNLIFReeEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihR 255
Cdd:cd19140 149 P----LFTNQVEYHPYLD--QRKLLDAAREHGIALTAYSPLARGEVLKDP-----------------------------V 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 256 VEELAEKKGVSMTEISLAWLLTKVTSPII-GATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19140 194 LQEIGRKHGKTPAQVALRWLLQQEGVAAIpKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
29-320 |
5.72e-29 |
|
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: 113.00 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-----AKREDVIIATKfIPRTQEEIEQgida 103
Cdd:cd19155 16 GLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYR---NEAAIGNVLKKWidsgkVKREELFIVTK-LPPGGNRREK---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 104 kqhIENCLNGSLKRLDMDYVDLYILHM---------------------WDYNTPIEDIMAALHDVIRQGKVRYIGISNCY 162
Cdd:cd19155 88 ---VEKFLLKSLEKLQLDYVDLYLIHFpvgslskeddsgkldptgehkQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 163 AWQIAKANEIAKAKGyeqfVSIQGHYNLIFreEEREMKQYCVAHNIAMTPYSALASGRLAKhpgeeskrlsediYAKGKY 242
Cdd:cd19155 165 REQMARILKNARIKP----ANLQVELHVYL--QQKDLVDFCSTHSITVTAYAPLGSPGAAH-------------FSPGTG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 243 DITHDE-DLAIIHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRL 320
Cdd:cd19155 226 SPSGSSpDLLQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-297 |
6.71e-29 |
|
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: 113.18 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 38 EESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEY-----AKREDVIIATK--FIP-------RTQEEIEQGIDA 103
Cdd:cd19099 21 EEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekggIKRDEVVIVTKagYIPgdgdeplRPLKYLEEKLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 104 KQ----------------HIENCLNGSLKRLDMDYVDLYILH----------MWDYNTPIEDIMAALHDVIRQGKVRYIG 157
Cdd:cd19099 101 GLidvadsaglrhcispaYLEDQIERSLKRLGLDTIDLYLLHnpeeqllelgEEEFYDRLEEAFEALEEAVAEGKIRYYG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 158 ISnCYAWQIA-----------KANEIAKAKGYE--QFVSIQGHYNLIFREEEREMK----------QYCVAHNIAMTPYS 214
Cdd:cd19099 181 IS-TWDGFRAppalpghlsleKLVAAAEEVGGDnhHFKVIQLPLNLLEPEALTEKNtvkgealsllEAAKELGLGVIASR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 215 ALASGRLAKhpgeeskrlsediyakgkydithdedlaIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHI 292
Cdd:cd19099 260 PLNQGQLLG----------------------------ELRLADLLALPGGATLAQRALQFARSTpgVDSALVGMRRPEHV 311
|
....*
gi 1797152346 293 DGAVK 297
Cdd:cd19099 312 DENLA 316
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-301 |
8.50e-29 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 113.26 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSkvclgCMGFGeaqkgmhSWT-----LPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIK 75
Cdd:cd19158 1 QFYRNLGKSGLRVS-----CLGLG-------TWVtfggqITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 76 EYA-KREDVIIATKFIPRTQEEIEQGIdAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDVIRQGKVR 154
Cdd:cd19158 69 KKGwRRSSLVITTKIFWGGKAETERGL-SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 155 YIGISNCYAWQIAKANEIAKAKGYEQFVSIQGHYNLiFREEEREMKQYCVAHNI---AMTpYSALASGRLAKHPGE---E 228
Cdd:cd19158 148 YWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHM-FQREKVEVQLPELFHKIgvgAMT-WSPLACGIVSGKYDSgipP 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1797152346 229 SKRLSEDIYAKGKYDITHDE---DLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAV 301
Cdd:cd19158 226 YSRASLKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNegVSSVLLGASNAEQLMENIGAIQV 303
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-191 |
6.34e-27 |
|
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: 106.46 E-value: 6.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 14 SKVCLGCmgfgeAQKGM------HSWTLPYEESKKIIKYALDNGINFFDTAIGYqgGTSEAFLGKAIKEYakrEDVIIAT 87
Cdd:cd19097 1 SKLALGT-----AQFGLdygianKSGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL---DKFKIIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 88 KfIPRTQEEIEqgiDAKQHIENCLNGSLKRLDMDYVDLYILHMW-DYNTPIEDIMAALHDVIRQGKVRYIGISnCYAWqi 166
Cdd:cd19097 71 K-LPPLKEDKK---EDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS-VYSP-- 143
|
170 180
....*....|....*....|....*
gi 1797152346 167 akaNEIAKAKGYEQFVSIQGHYNLI 191
Cdd:cd19097 144 ---EELEKALESFKIDIIQLPFNIL 165
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
20-314 |
7.55e-25 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 101.45 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 20 CMGFGeaqkgmhSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE-----YAKREDVIIATKFIPrTQ 94
Cdd:cd19128 3 RLGFG-------TYKITESESKEAVKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEifkdgGVKREDLFITSKLWP-TM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 95 EEIEQgidakqhIENCLNGSLKRLDMDYVDLYILH---MWDYNT----------------PIEDIMAALHDVIRQGKVRY 155
Cdd:cd19128 72 HQPEN-------VKEQLLITLQDLQLEYLDLFLIHwplAFDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 156 IGISNCYAWQIAKANEIAKAKGYEQFVSIQGHYnlifrEEEREMKqYCVAHNIAMTPYSALAsGRlakhpgeeskrlsed 235
Cdd:cd19128 145 IGVSNYSTKLLTDLLNYCKIKPFMNQIECHPYF-----QNDKLIK-FCIENNIHVTAYRPLG-GS--------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 236 iYAKGKYDITHDEDLaiihrvEELAEKKGVSMTEISLAWLLTKVT---SPIIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:cd19128 203 -YGDGNLTFLNDSEL------KALATKYNTTPPQVIIAWHLQKWPknySVIPKSANKSRCQQNFDINDLALTKEDMDAIN 275
|
..
gi 1797152346 313 EL 314
Cdd:cd19128 276 TL 277
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
46-314 |
1.44e-23 |
|
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: 97.39 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 46 YAL-DNGINFFDTAIGYqgGTsEAFLGKAIKEYA-KREDVIIATKFIPrTQEEIEQGIDAKQhienclnGSLKRLDMDYV 123
Cdd:cd19135 33 YALkECGYRHIDTAKRY--GC-EELLGKAIKESGvPREDLFLTTKLWP-SDYGYESTKQAFE-------ASLKRLGVDYL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 124 DLYILHMWDYNTPIEDIMAALHDVIR-------QGKVRYIGISNcyaWQIAKANEIakakgyEQFVSIQGHYNL----IF 192
Cdd:cd19135 102 DLYLLHWPDCPSSGKNVKETRAETWRaleelydEGLCRAIGVSN---FLIEHLEQL------LEDCSVVPHVNQvefhPF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 193 REEErEMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEELAEKKGVSMTEISL 272
Cdd:cd19135 173 QNPV-ELIEYCRDNNIVFEGYCPLAKGKALEEP-----------------------------TVTELAKKYQKTPAQILI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1797152346 273 AWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19135 223 RWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
36-321 |
4.24e-22 |
|
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: 93.89 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 36 PYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-----AKREDVIIATKFiprtqeeieQGIDAKQH-IEN 109
Cdd:cd19116 23 DDEGVRQAVKHAIEAGYRHIDTAYLYG---NEAEVGEAIREKiaegvVKREDLFITTKL---------WNSYHEREqVEP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 110 CLNGSLKRLDMDYVDLYILHM-------WDYNTPIE---------DIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIA 173
Cdd:cd19116 91 ALRESLKRLGLDYVDLYLIHWpvafkenNDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 174 KAK-GYEQfvsIQGHYNLIfreeEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKRLSEdiyakgkydithdedlai 252
Cdd:cd19116 171 NIKpAVNQ---IEVHPTLT----QEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPRLDDP------------------ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 253 ihRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRLV 321
Cdd:cd19116 226 --TLVAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
29-314 |
7.02e-22 |
|
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: 92.42 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKFiprtqeeieqgidakqHI 107
Cdd:cd19139 5 GLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAESGvPRDELFITTKI----------------WI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 108 EN--------CLNGSLKRLDMDYVDLYILHmW---DYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAkak 176
Cdd:cd19139 66 DNlskdkllpSLEESLEKLRTDYVDLTLIH-WpspNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVV--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 177 GYEQFVSIQGHYNLIFreEEREMKQYCVAHNIAMTPYSALASGRLAKhpgeeskrlsediyakgkydithDEDLAIIhrv 256
Cdd:cd19139 142 GAGAIATNQIELSPYL--QNRKLVAHCKQHGIHVTSYMTLAYGKVLD-----------------------DPVLAAI--- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1797152346 257 eelAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19139 194 ---AERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
38-306 |
8.18e-22 |
|
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: 93.44 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 38 EESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYAkREDVIIATK----FIPRTQEE------IEQGIDAK--- 104
Cdd:cd19152 20 EEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG-REDYVISTKvgrlLVPLQEVEptfepgFWNPLPFDavf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 105 ----QHIENCLNGSLKRLDMDYVDLYILHMWDYNTP-----------IEDIMAALHDVIRQGKVRYIGI-SNcyAWQIA- 167
Cdd:cd19152 99 dysyDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREEGVIKAIGLgVN--DWEVIl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 168 KANEIAKAkgyeQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAkhpgeeskrlSEDIYAKGKYDITHD 247
Cdd:cd19152 177 RILEEADL----DWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLA----------GGDNFDYYEYGPAPP 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797152346 248 EDLAIIHRVEELAEKKGVSMTEISLAWLLTK--VTSPIIGATKPHHIDGAVKAVAVKLTDE 306
Cdd:cd19152 243 ELIARRDRIEALCEQHGVSLAAAALQFALAPpaVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-321 |
1.79e-21 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 92.47 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 1 MEYVKLGDSDLMVSkvclgcMGFGeaqkgmhSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAI-----K 75
Cdd:cd19123 1 MKTLPLSNGDLIPA------LGLG-------TWKSKPGEVGQAVKQALEAGYRHIDCAAIYG---NEAEIGAALaevfkE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 76 EYAKREDVIIATKFIPRTQeeieqgidAKQHIENCLNGSLKRLDMDYVDLYILHmW---------------DY----NTP 136
Cdd:cd19123 65 GKVKREDLWITSKLWNNSH--------APEDVLPALEKTLADLQLDYLDLYLMH-WpvalkkgvgfpesgeDLlslsPIP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 137 IEDIMAALHDVIRQGKVRYIGISNCYAWQIAKAneIAKAKGYEQFVSIQGHYNLifreEEREMKQYCVAHNIAMTPYSAL 216
Cdd:cd19123 136 LEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDL--LATARIKPAVNQVELHPYL----QQPELLAFCRDNGIHLTAYSPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 217 ASG-RLAKHPGEESKRLSEDiyakgkydithdedlAIIhrvEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGA 295
Cdd:cd19123 210 GSGdRPAAMKAEGEPVLLED---------------PVI---NKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQN 271
|
330 340
....*....|....*....|....*.
gi 1797152346 296 VKAVAVKLTDEEIIYLEELYKPHRLV 321
Cdd:cd19123 272 LEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
37-314 |
2.67e-21 |
|
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: 91.15 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 37 YEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE-----YAKREDVIIATKFIPRtqeeiEQGIDAKQhieNCL 111
Cdd:cd19136 14 EEEVRQAVDAALKAGYRLIDTASVYR---NEADIGKALRDllpkyGLSREDIFITSKLAPK-----DQGYEKAR---AAC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 112 NGSLKRLDMDYVDLYILHmWD--YNTPIEDIM---------AALHDVIRQGKVRYIGISNcYawqiakanEIAKAKGYEQ 180
Cdd:cd19136 83 LGSLERLGTDYLDLYLIH-WPgvQGLKPSDPRnaelrreswRALEDLYKEGKLRAIGVSN-Y--------TVRHLEELLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 181 FVSIQGHYNLI-F--REEEREMKQYCVAHNIAMTPYSALASGRLakhpgeesKRLSEDiyakgkydithdedlaiihRVE 257
Cdd:cd19136 153 YCEVPPAVNQVeFhpHLVQKELLKFCKDHGIHLQAYSSLGSGDL--------RLLEDP-------------------TVL 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1797152346 258 ELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19136 206 AIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
21-306 |
1.53e-20 |
|
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: 89.73 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 21 MGFGEAQKGMHSwTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKREDVIIATK---FIPRTQEEI 97
Cdd:cd19162 3 LGLGAASLGNLA-RAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARH-PRAEYVVSTKvgrLLEPGAAGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 98 EQGIDAKQH-----IENCLNGSLKRLDMDYVDLYILHMWD--YNTPIEDIMAALHDVIRQGKVRYIGISnCYAWQIAKAn 170
Cdd:cd19162 81 PAGADRRFDfsadgIRRSIEASLERLGLDRLDLVFLHDPDrhLLQALTDAFPALEELRAEGVVGAIGVG-VTDWAALLR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 171 eiAKAKGYEQFVSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEeskrlsEDIYakgKYDITHDEDL 250
Cdd:cd19162 159 --AARRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPA------GDRY---DYRPATPEVL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1797152346 251 AIIHRVEELAEKKGVSMTEISLAWLL--TKVTSPIIGATKPHHIDGAVKAVAVKLTDE 306
Cdd:cd19162 228 ARARRLAAVCRRYGVPLPAAALQFPLrhPAVASVVVGAASPAELRDNLALLRTPIPAE 285
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
29-321 |
1.71e-20 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 89.75 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYqggTSEAFLGKAIKE------YAKREDVIIATKFIprtqeeieqgiD 102
Cdd:cd19106 11 GLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVY---GNEQEVGEALKEkvgpgkAVPREDLFVTSKLW-----------N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 103 AKQH---IENCLNGSLKRLDMDYVDLYILHmWDY--------------------NTPIEDIMAALHDVIRQGKVRYIGIS 159
Cdd:cd19106 77 TKHHpedVEPALRKTLKDLQLDYLDLYLIH-WPYafergdnpfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 160 NCYAWQIAKANEIAKAKGYEQFVSIQGHYNlifreeEREMKQYCVAHNIAMTPYSALAS-GRLAKHPGEESkrLSEDiya 238
Cdd:cd19106 156 NFNSRQIDDILSVARIKPAVLQVECHPYLA------QNELIAHCKARGLVVTAYSPLGSpDRPWAKPDEPV--LLEE--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 239 kgkydithdedlaiiHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPH 318
Cdd:cd19106 225 ---------------PKVKALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNW 289
|
...
gi 1797152346 319 RLV 321
Cdd:cd19106 290 RYI 292
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
38-319 |
5.43e-20 |
|
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: 87.83 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 38 EESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYAK-REDVIIATKFIprtqeeieqgiDAKQHIENCL---NG 113
Cdd:cd19157 24 SEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKESGIpREELFITSKVW-----------NADQGYDSTLkafEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 114 SLKRLDMDYVDLYILHmWDYNTPIEDIMAALHDVIRQGKVRYIGISNcyaWQIAKANEI-AKAKGYEQFVSIQGHYNLIf 192
Cdd:cd19157 90 SLERLGLDYLDLYLIH-WPVKGKYKETWKALEKLYKDGRVRAIGVSN---FQVHHLEDLlADAEIVPMVNQVEFHPRLT- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 193 reeEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEELAEKKGVSMTEISL 272
Cdd:cd19157 165 ---QKELRDYCKKQGIQLEAWSPLMQGQLLDNP-----------------------------VLKEIAEKYNKSVAQVIL 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1797152346 273 AWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHR 319
Cdd:cd19157 213 RWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
27-225 |
1.46e-19 |
|
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: 86.27 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 27 QKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKFiprtqEEIEQGIDAKq 105
Cdd:cd19131 12 QLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRASGvPREELFITTKL-----WNSDQGYDST- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 106 hiENCLNGSLKRLDMDYVDLYILHmWDynTPIEDIMA----ALHDVIRQGKVRYIGISNcyaWQIAKANEIAKAKGYEQF 181
Cdd:cd19131 83 --LRAFDESLRKLGLDYVDLYLIH-WP--VPAQDKYVetwkALIELKKEGRVKSIGVSN---FTIEHLQRLIDETGVVPV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1797152346 182 VS-IQGHYnlifREEEREMKQYCVAHNIAMTPYSALASGRLAKHP 225
Cdd:cd19131 155 VNqIELHP----RFQQRELRAFHAKHGIQTESWSPLGQGGLLSDP 195
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
29-308 |
9.37e-19 |
|
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: 84.03 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPY-EESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKFIPRTQEEiEQGIDAKQH 106
Cdd:cd19126 13 GLGVFQTPDgDETERAVQTALENGYRSIDTAAIYK---NEEGVGEAIRESGvPREELFVTTKLWNDDQRA-RRTEDAFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 107 ienclngSLKRLDMDYVDLYILHmWDYNTPIEDIMAALHDVIRQGKVRYIGISNcyaWQIAKANEIAKAKGYEQFVS-IQ 185
Cdd:cd19126 89 -------SLDRLGLDYVDLYLIH-WPGKDKFIDTWKALEKLYASGKVKAIGVSN---FQEHHLEELLAHADVVPAVNqVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 186 GHYNLifreEEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEELAEKKGV 265
Cdd:cd19126 158 FHPYL----TQKELRGYCKSKGIVVEAWSPLGQGGLLSNP-----------------------------VLAAIGEKYGK 204
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1797152346 266 SMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19126 205 SAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDM 247
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
44-321 |
1.98e-18 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 83.53 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 44 IKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATK----------FIPRTQEeieqgidakqhiencln 112
Cdd:PRK11172 22 VKTALELGYRAIDTAQIYD---NEAAVGQAIAESGvPRDELFITTKiwidnlakdkLIPSLKE----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 113 gSLKRLDMDYVDLYILHmW---DYNTPIEDIMAALHDVIRQGKVRYIGISNcyaWQIAKANEIAKAKGYEQFVS--IQGH 187
Cdd:PRK11172 82 -SLQKLRTDYVDLTLIH-WpspNDEVSVEEFMQALLEAKKQGLTREIGISN---FTIALMKQAIAAVGAENIATnqIELS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 188 YNLifreEEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEELAEKKGVSM 267
Cdd:PRK11172 157 PYL----QNRKVVAFAKEHGIHVTSYMTLAYGKVLKDP-----------------------------VIARIAAKHNATP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1797152346 268 TEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRLV 321
Cdd:PRK11172 204 AQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
38-319 |
2.27e-18 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 83.70 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 38 EESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-----AKREDVIIATKFIPRTQEeieqgidakqHIENCLN 112
Cdd:cd19119 27 AEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAiddgsIKREELFITTKVWPTFYD----------EVERSLD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 113 GSLKRLDMDYVDLYILH-------------------------MWDYNTPIEDIMAALHDVIRQGKVRYIGISNcyaWQIA 167
Cdd:cd19119 94 ESLKALGLDYVDLLLVHwpvcfekdsddsgkpftpvnddgktRYAASGDHITTYKQLEKIYLDGRAKAIGVSN---YSIV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 168 KANEIAKAKGYEQFVS-IQGHYNLifreEEREMKQYCVAHNIAMTPYSALASGRLAKHPGEEskrlsediyakgkydith 246
Cdd:cd19119 171 YLERLIKECKVVPAVNqVELHPHL----PQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPL------------------ 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1797152346 247 dedlaiihrVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAvkLTDEEIIYLEELY--KPHR 319
Cdd:cd19119 229 ---------VKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVS--LTKEDLQKLDDIGekYPVR 292
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-159 |
2.69e-18 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 83.67 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 3 YVKLGDSDLMVSkvclgCMGFGEAQKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYA-KRE 81
Cdd:PLN02587 1 LRELGSTGLKVS-----SVGFGASPLGSVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGiPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 82 DVIIATKfIPRTQEeieqGID-AKQHIENCLNGSLKRLDMDYVDlyILHMWD-----YNTPIEDIMAALHDVIRQGKVRY 155
Cdd:PLN02587 76 KYVVSTK-CGRYGE----GFDfSAERVTKSVDESLARLQLDYVD--ILHCHDiefgsLDQIVNETIPALQKLKESGKVRF 148
|
....
gi 1797152346 156 IGIS 159
Cdd:PLN02587 149 IGIT 152
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
27-320 |
3.14e-18 |
|
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: 82.95 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 27 QKGMHSWTLPY-EESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKFIprtqeeieqgiDAK 104
Cdd:cd19156 11 RLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIRESGvPREEVFVTTKLW-----------NSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 105 QHIENCLNG---SLKRLDMDYVDLYILHmWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAKAKGYEQF 181
Cdd:cd19156 77 QGYESTLAAfeeSLEKLGLDYVDLYLIH-WPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 182 VSIQGHYNlifreeEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEELAE 261
Cdd:cd19156 156 IELHPLLT------QEPLRKFCKEKNIAVEAWSPLGQGKLLSNP-----------------------------VLKAIGK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 262 KKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRL 320
Cdd:cd19156 201 KYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
36-308 |
1.48e-17 |
|
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: 80.70 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 36 PYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKFIPR--TQEEIEQGIDAkqhiencln 112
Cdd:cd19133 21 DPEECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKSGiPREELFITTKLWIQdaGYEKAKKAFER--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 113 gSLKRLDMDYVDLYILHmWDYNtpiEDIMA--ALHDVIRQGKVRYIGISNCYAWQIA---KANEIAKAkgyeqfVS-IQG 186
Cdd:cd19133 89 -SLKRLGLDYLDLYLIH-QPFG---DVYGAwrAMEELYKEGKIRAIGVSNFYPDRLVdliLHNEVKPA------VNqIET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 187 HYNLIFREEEREMKQYcvahNIAMTPYSALASGRlakhpgeeskrlsediyakgkYDITHDEDLAiihrveELAEKKGVS 266
Cdd:cd19133 158 HPFNQQIEAVEFLKKY----GVQIEAWGPFAEGR---------------------NNLFENPVLT------EIAEKYGKS 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1797152346 267 MTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19133 207 VAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDM 248
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
38-307 |
1.48e-16 |
|
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: 78.46 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 38 EESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE------YAKREDVIIATKFIPRtqeeieqgiDA-KQHIENC 110
Cdd:cd19124 20 EDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlglVKSRDELFVTSKLWCS---------DAhPDLVLPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 111 LNGSLKRLDMDYVDLYILHmW-------DYNTPI--EDIM--------AALHDVIRQGKVRYIGISNCYAWQIAKANEIA 173
Cdd:cd19124 88 LKKSLRNLQLEYVDLYLIH-WpvslkpgKFSFPIeeEDFLpfdikgvwEAMEECQRLGLTKAIGVSNFSCKKLQELLSFA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 174 KakgyeqfvsI-----QGHYNLIFReeEREMKQYCVAHNIAMTPYSALasGRLAKHPGeeSKRLSEDiyakgkydithde 248
Cdd:cd19124 167 T---------IppavnQVEMNPAWQ--QKKLREFCKANGIHVTAYSPL--GAPGTKWG--SNAVMES------------- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 249 dlAIIHrveELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEE 307
Cdd:cd19124 219 --DVLK---EIAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEED 272
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
22-308 |
1.57e-16 |
|
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: 77.70 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 22 GFGeaqkgmhSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKfIPRTQEEIEQG 100
Cdd:cd19132 11 GFG-------TYPLKGDEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRSGvPREELFVTTK-LPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 101 IDakqhienCLNGSLKRLDMDYVDLYILHmWDynTPIEDIMA----ALHDVIRQGKVRYIGISNCYAWQIakaNEIAKAK 176
Cdd:cd19132 80 LR-------TIEESLYRLGLDYVDLYLIH-WP--NPSRDLYVeawqALIEAREEGLVRSIGVSNFLPEHL---DRLIDET 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 177 GYEQFVS-IQGHYNLifreEEREMKQYCVAHNIAMTPYSALASGrlakhpgeeSKRLSEDIyakgkydithdedlaiihr 255
Cdd:cd19132 147 GVTPAVNqIELHPYF----PQAEQRAYHREHGIVTQSWSPLGRG---------SGLLDEPV------------------- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1797152346 256 VEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19132 195 IKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDM 247
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
5-159 |
5.30e-16 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) 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(+). 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: 381379 [Multi-domain] Cd Length: 294 Bit Score: 77.19 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 5 KLGDSDLMVSKVCLGCMGFGeaqkGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEY-AKREDV 83
Cdd:cd19153 4 TLEIALGNVSPVGLGTAALG----GVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALqVPRSSY 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 84 IIATKFIPRTQEEIEQGIDAkqhIENCLNGSLKRLDMDYVDLYILH---MWDYNTPIEDIMAALHDVIRQGKVRYIGIS 159
Cdd:cd19153 80 TVATKVGRYRDSEFDYSAER---VRASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIKRIGIA 155
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
29-314 |
9.01e-16 |
|
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: 76.03 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY----AKREDVIIATKFIPRTQEEIEQGIDAk 104
Cdd:cd19121 16 GLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEAiaggVKREDLFVTTKLWSTYHRRVELCLDR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 105 qhienclngSLKRLDMDYVDLYILH------------------------MWDYNTPieDIMAALHDVIRQGKVRYIGISN 160
Cdd:cd19121 92 ---------SLKSLGLDYVDLYLVHwpvllnpngnhdlfptlpdgsrdlDWDWNHV--DTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 161 C---YAWQIAKANEIAKAKGyeqfvSIQGHYNLifreEEREMKQYCVAHNIAMTPYSALASgrlakhpgEESKRLSEDiy 237
Cdd:cd19121 161 YsipYLEELLKHATVVPAVN-----QVENHPYL----PQQELVDFCKEKGILIEAYSPLGS--------TGSPLISDE-- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1797152346 238 akgkydithdedlaiihRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKavAVKLTDEEIIYLEEL 314
Cdd:cd19121 222 -----------------PVVEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLE--IIDLDDEDMNKLNDI 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
29-319 |
2.18e-15 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 75.60 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE-----YAKREDVIIATKFIPRTQEEIeqgida 103
Cdd:cd19112 15 GLGVWRMEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAEafktgLVKREDLFITTKLWNSDHGHV------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 104 kqhIENCLNgSLKRLDMDYVDLYILH---------------------MW--DYNTPIEDIMAALHDVIRQGKVRYIGISN 160
Cdd:cd19112 86 ---IEACKD-SLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgVLdiDVTISLETTWHAMEKLVSAGLVRSIGISN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 161 CYAWQIAKANEIAKAKGYEQFVSIQGHYnlifreeERE-MKQYCVAHNIAMTPYSALASGRLAKHPGEESKRLSEDIyak 239
Cdd:cd19112 162 YDIFLTRDCLAYSKIKPAVNQIETHPYF-------QRDsLVKFCQKHGISVTAHTPLGGAAANAEWFGSVSPLDDPV--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 240 gkydithdedlaiihrVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHR 319
Cdd:cd19112 232 ----------------LKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
29-318 |
8.60e-15 |
|
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: 73.30 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATKfiprtqeeieqgIDAKQH- 106
Cdd:cd19117 18 GLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYG---NEEEVGQGIKDSGvPREEIFITTK------------LWCTWHr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 107 -IENCLNGSLKRLDMDYVDLYILHmW--------DYNTPIEDIMAALHD--------------VIRQGKVRYIGISNCYA 163
Cdd:cd19117 83 rVEEALDQSLKKLGLDYVDLYLMH-WpvpldpdgNDFLFKKDDGTKDHEpdwdfiktwelmqkLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 164 WQIAKANEIAKAKGYEQFVSIQGHYNLifreEEREMKQYCVAHNIAMTPYSALAS--GRLAKHPgeeskrlsediyakgk 241
Cdd:cd19117 162 KNLEKLLASPSAKIVPAVNQIELHPLL----PQPKLVDFCKSKGIHATAYSPLGStnAPLLKEP---------------- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1797152346 242 ydithdedlAIIhrveELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAvkLTDEEIIYLEELYKPH 318
Cdd:cd19117 222 ---------VII----KIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHKEY 283
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
21-307 |
1.06e-14 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 73.04 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 21 MGFG----EAQKGmhswtlpyeESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY------AKREDVIIATKfi 90
Cdd:cd19122 12 VGFGtfanEGAKG---------ETYAAVTKALDVGYRHLDCAWFYL---NEDEVGDAVRDFlkenpsVKREDLFICTK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 91 prTQEEIEQGIDAKQHIENclngSLKRLDMDYVDLYILHmW-------DYNTPI-----------------EDIMAALHD 146
Cdd:cd19122 78 --VWNHLHEPEDVKWSIDN----SLKNLKLDYIDLFLVH-WpiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRAMEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 147 VIRQGKVRYIGISNcyaWQIAKANEIAkakgyeQFVSIQGHYNLI----FREEErEMKQYCVAHNIAMTPYSALASGRLA 222
Cdd:cd19122 151 IYESGKAKAIGVSN---WTIPGLKKLL------SFAKVKPHVNQIeihpFLPNE-ELVDYCFSNDILPEAYSPLGSQNQV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 223 KHPGEeskRLSEDiyakgkydithdedlaiiHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKavAVK 302
Cdd:cd19122 221 PSTGE---RVSEN------------------PTLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFK--SIE 277
|
....*
gi 1797152346 303 LTDEE 307
Cdd:cd19122 278 LSDED 282
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
8-159 |
1.28e-14 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; 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: 381390 [Multi-domain] Cd Length: 298 Bit Score: 73.08 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 8 DSDLMVSKVCLGCMGFGEAQKgmhswTLPYE-ESKKIIKYALDNGINFFDTAIGYqgGTSEAFLGKAIKEYAK---REDV 83
Cdd:cd19164 8 LSLAGLPPLIFGAATFSYQYT-----TDPESiPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALRDefpRDTY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 84 IIATKFIPRTQEEIEQgidAKQHIENCLNGSLKRLDMDYVDLYILHMWDYNTPiEDIMAALHDVIR---QGKVRYIGIS 159
Cdd:cd19164 81 FIITKVGRYGPDDFDY---SPEWIRASVERSLRRLHTDYLDLVYLHDVEFVAD-EEVLEALKELFKlkdEGKIRNVGIS 155
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
29-314 |
3.20e-14 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 71.43 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYqggTSEAFLGKAI-KEYAKREDVIIATKFiprtqEEIEQGIDAKQhi 107
Cdd:cd19134 15 GLGVGELSDDEAERSVSAALEAGYRLIDTAAAY---GNEAAVGRAIaASGIPRGELFVTTKL-----ATPDQGFTASQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 108 ENClNGSLKRLDMDYVDLYILHmwdYNTPIE----DIMAALHDVIRQGKVRYIGISNCYAWQIakaNEIAKAKGYEQFVS 183
Cdd:cd19134 85 AAC-RASLERLGLDYVDLYLIH---WPAGREgkyvDSWGGLMKLREEGLARSIGVSNFTAEHL---ENLIDLTFFTPAVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 184 -IQGHYNLifreEEREMKQYCVAHNIAMTPYSALASGRLAKHPgeeskrlsediyakgkydithdedlaiihRVEELAEK 262
Cdd:cd19134 158 qIELHPLL----NQAELRKVNAQHGIVTQAYSPLGVGRLLDNP-----------------------------AVTAIAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1797152346 263 KGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19134 205 HGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGL 256
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
40-292 |
3.26e-14 |
|
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: 71.72 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 40 SKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY-----AKREDVIIATKfIPRTQEEIEQgidakqhIENCLNGS 114
Cdd:cd19129 21 TRNAVKAALEAGFRHFDCAERYR---NEAEVGEAMQEVfkagkIRREDLFVTTK-LWNTNHRPER-------VKPAFEAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 115 LKRLDMDYVDLYILH--------------------MWDYNTPIEDIMAALHDVIRQGKVRYIGISNCYAWQIAKANEIAK 174
Cdd:cd19129 90 LKRLQLDYLDLYLIHtpfafqpgdeqdprdangnvIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 175 AKgyEQFVSIQGHYNLifreEEREMKQYCVAHNIAMTPYSALAsgrlakHpGEESKRLSEDIyakgkydIThdedlAIIH 254
Cdd:cd19129 170 IK--PAVVQVESHPYL----PEWELLDFCKNHGIVLQAFAPLG------H-GMEPKLLEDPV-------IT-----AIAR 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1797152346 255 RVEElaekkgvSMTEISLAWLLTKVTSPIIGATKPHHI 292
Cdd:cd19129 225 RVNK-------TPAQVLLAWAIQRGTALLTTSKTPSRI 255
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
29-321 |
3.54e-14 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 71.61 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE-----YAKREDVIIATKFIPRTqeeieqgiDA 103
Cdd:cd19125 15 GLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYG---NEKEIGKALKKlfedgVVKREDLFITSKLWCTD--------HA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 104 KQHIENCLNGSLKRLDMDYVDLYILHmWDYN---------------TPIEDIMAALHDVIRQGKVRYIGISNcyaWQIAK 168
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIH-WPVRlkkgahmpepeevlpPDIPSTWKAMEKLVDSGKVRAIGVSN---FSVKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 169 ANEIAKAKGYEQFVSiQGHYNLIFREEerEMKQYCVAHNIAMTPYSALASgrlakhpgeeskrlSEDIYAKGkyDITHDE 248
Cdd:cd19125 160 LEDLLAVARVPPAVN-QVECHPGWQQD--KLHEFCKSKGIHLSAYSPLGS--------------PGTTWVKK--NVLKDP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797152346 249 dlaiihRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELyKPHRLV 321
Cdd:cd19125 221 ------IVTKVAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI-EQQRRV 286
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-289 |
4.87e-14 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 71.59 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 14 SKVCLGCMGFGeaqkGMHSwTLPYEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYaKREDVIIATK----F 89
Cdd:cd19161 1 SELGLGTAGLG----NLYT-AVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK-PRDEFVLSTKvgrlL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 90 IPRTQEEIEQGID-------------AKQHIENCLNGSLKRLDMDYVDLYILHMWDY------NTPIEDIMA------AL 144
Cdd:cd19161 75 KPAREGSVPDPNGfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVythgdrKERHHFAQLmsggfkAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 145 HDVIRQGKVRYIGIS-NcyAWQIakaneIAKAKGYEQF--VSIQGHYNLIFREEEREMKQYCVAHNIAMTPYSALASGRL 221
Cdd:cd19161 155 EELKKAGVIKAFGLGvN--EVQI-----CLEALDEADLdcFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGIL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797152346 222 AKHPGEEskrlsediyakGKYDIThDEDLAIIHRVEEL---AEKKGVSMTEISLAWLL--TKVTSPIIGATKP 289
Cdd:cd19161 228 ATGTKSG-----------AKFNYG-DAPAEIISRVMEIekiCDAYNVPLAAAALQFPLrhPAVASVLTGARNP 288
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
27-314 |
7.17e-14 |
|
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: 70.52 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 27 QKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEY------AKREDVIIATKFIPRTQeeieqg 100
Cdd:cd19118 9 AIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQ---NQHEVGQALKELlkeepgVKREDLFITSKLWNNSH------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 101 idAKQHIENCLNGSLKRLDMDYVDLYILHmW-------------------------DYNTPIEDIMAALHDVIRQGKVRY 155
Cdd:cd19118 80 --RPEYVEPALDDTLKELGLDYLDLYLIH-WpvafkptgdlnpltavptnggevdlDLSVSLVDTWKAMVELKKTGKVKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 156 IGISNcyaWQIAKANEIAKAKGYEQFVS-IQGHYNLIfreeEREMKQYCVAHNIAMTPYSAL---ASG--RLAKHPGees 229
Cdd:cd19118 157 IGVSN---FSIDHLQAIIEETGVVPAVNqIEAHPLLL----QDELVDYCKSKNIHITAYSPLgnnLAGlpLLVQHPE--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 230 krlsediyakgkydithdedlaiihrVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKavAVKLTDEEII 309
Cdd:cd19118 227 --------------------------VKAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFN 278
|
....*
gi 1797152346 310 YLEEL 314
Cdd:cd19118 279 AVTAL 283
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
21-312 |
1.43e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 70.00 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 21 MGFGEAQ-KGMHSWTLP--YEESKKIIKYALDNGINFFDTAIGYQGGTSEAFLGKAIKEYakREDVIIATK--------- 88
Cdd:PRK10376 20 LGYGAMQlAGPGVFGPPkdRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPY--PDDLTIVTKvgarrgedg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 89 -FIP-RTQEEIEQGIdakqHiENCLNGSLKRLDMdyVDLYIlhMWDYNTP----IEDIMAALHDVIRQGKVRYIGISNCY 162
Cdd:PRK10376 98 sWLPaFSPAELRRAV----H-DNLRNLGLDVLDV--VNLRL--MGDGHGPaegsIEEPLTVLAELQRQGLVRHIGLSNVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 163 AWQIAKANEIAKakgyeqFVSIQGHYNLIFREEEREMKQYcVAHNIAMTPY------SALASGRLAkhpgeeskrlsedi 236
Cdd:PRK10376 169 PTQVAEARKIAE------IVCVQNHYNLAHRADDALIDAL-ARDGIAYVPFfplggfTPLQSSTLS-------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 237 yakgkydithdedlaiihrveELAEKKGVSMTEISLAWLLTKvtSP----IIGATKPHHIDGAVKAVAVKLTDEEIIYLE 312
Cdd:PRK10376 228 ---------------------DVAASLGATPMQVALAWLLQR--SPnillIPGTSSVAHLRENLAAAELVLSEEVLAELD 284
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
29-160 |
3.72e-13 |
|
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: 68.59 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KREDVIIATK-FIPrtqeeiEQGIDAKQH 106
Cdd:cd19127 13 GLGVFQTPPEETADAVATALADGYRLIDTAAAYG---NEREVGEGIRRSGvDRSDIFVTTKlWIS------DYGYDKALR 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1797152346 107 ienCLNGSLKRLDMDYVDLYILHmWDYNTPIEDIMAALHDVIR---QGKVRYIGISN 160
Cdd:cd19127 84 ---GFDASLRRLGLDYVDLYLLH-WPVPNDFDRTIQAYKALEKllaEGRVRAIGVSN 136
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
47-317 |
2.38e-12 |
|
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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 66.60 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 47 ALDNGINFFDTAIGYqgGTSEAFLGKAIKEYA-KREDVIIATKFIPRTQEEIEqgIDAKQHIENclNGSLKRLDM----- 120
Cdd:cd19098 44 AWAAGVRYFDAARSY--GRAEEFLGSWLRSRNiAPDAVFVGSKWGYTYTADWQ--VDAAVHEVK--DHSLARLLKqweet 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 121 -----DYVDLYILHMWDYNTPI---EDIMAALHDVIRQGkvRYIGISNCYAWQ---IAKANEIAkAKGYEQFVSIQGHYN 189
Cdd:cd19098 118 rsllgKHLDLYQIHSATLESGVledADVLAALAELKAEG--VKIGLSLSGPQQaetLRRALEIE-IDGARLFDSVQATWN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 190 LIfreEEREMKQYCVAHNIAMTPY--SALASGRLAKHPgeeskrlsediyakgkydiTHDEDLAIIHRVEELAEKKGVSM 267
Cdd:cd19098 195 LL---EQSAGEALEEAHEAGMGVIvkEALANGRLTDRN-------------------PSPELAPLMAVLKAVADRLGVTP 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1797152346 268 TEISLAWLLTKVTSPII--GATKPHHIDGAVKAVAVKLTDEEIIYLEELYKP 317
Cdd:cd19098 253 DALALAAVLAQPFVDVVlsGAATPEQLRSNLRALDVSLDLELLAALADLAEP 304
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
4-276 |
3.43e-12 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 65.86 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 4 VKLGDSDLMvskvclgcmgfgeAQKGMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKEYA-KRED 82
Cdd:PRK11565 7 IKLQDGNVM-------------PQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEASvAREE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 83 VIIATKFIPrtqeeieqgiDAKQHIENCLNGSLKRLDMDYVDLYILHmWDYnTPIEDIMAALHDVI---RQGKVRYIGIS 159
Cdd:PRK11565 71 LFITTKLWN----------DDHKRPREALEESLKKLQLDYVDLYLMH-WPV-PAIDHYVEAWKGMIelqKEGLIKSIGVC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 160 NcyaWQIAKANEIAKAKGYEQFVS-IQGHYNLifreEEREMKQYCVAHNIAMTPYSALASGrlakhpgeeskrlsediyA 238
Cdd:PRK11565 139 N---FQIHHLQRLIDETGVTPVINqIELHPLM----QQRQLHAWNATHKIQTESWSPLAQG------------------G 193
|
250 260 270
....*....|....*....|....*....|....*...
gi 1797152346 239 KGKYdithdeDLAIIHRveeLAEKKGVSMTEISLAWLL 276
Cdd:PRK11565 194 KGVF------DQKVIRD---LADKYGKTPAQIVIRWHL 222
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
29-308 |
5.53e-11 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 62.44 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE-----YAKREDVIIATKFIPRTQEeieqgida 103
Cdd:cd19107 8 GLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQ---NENEVGEAIQEkikeqVVKREDLFIVSKLWCTFHE-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 104 KQHIENCLNGSLKRLDMDYVDLYILHmW--------DY------------NTPIEDIMAALHDVIRQGKVRYIGISNCYA 163
Cdd:cd19107 77 KGLVKGACQKTLSDLKLDYLDLYLIH-WptgfkpgkELfpldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFNH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 164 WQIAKaneIAKAKG--YEQFVS-IQGHYNLifreEEREMKQYCVAHNIAMTPYSALAS-GRLAKHPGEESkrLSEDiyak 239
Cdd:cd19107 156 LQIER---ILNKPGlkYKPAVNqIECHPYL----TQEKLIQYCQSKGIVVTAYSPLGSpDRPWAKPEDPS--LLED---- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797152346 240 gkydithdedlaiiHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19107 223 --------------PKIKEIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDM 277
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
22-216 |
5.82e-11 |
|
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: 62.44 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 22 GFGeaqkgmhSWTLPYEESKKIIKYALDNGINFFDTAIGYqGGTSEAFLG--KAIKE-YAKREDVIIATKfiprtqeeIE 98
Cdd:cd19115 17 GFG-------LWKVNNDTCADQVYNAIKAGYRLFDGACDY-GNEVEAGQGvaRAIKEgIVKREDLFIVSK--------LW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 99 QGIDAKQHIENCLNGSLKRLDMDYVDLYILHM----------------WDY--------NTPIEDIMAALHDVIRQGKVR 154
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFpialkyvdpavryppgWFYdgkkvefsNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1797152346 155 YIGISNCYAWQIAKANEIAKAKgyEQFVSIQGHYNLifreEEREMKQYCVAHNIAMTPYSAL 216
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYARIR--PATLQIEHHPYL----TQPRLVKYAQKEGIAVTAYSSF 216
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
29-215 |
1.14e-10 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 61.69 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYqGGTSEAFLG--KAIKE-YAKREDVIIATKfiprtqeeIEQGIDAKQ 105
Cdd:cd19113 15 GFGCWKLDNATAADQIYQAIKAGYRLFDGAEDY-GNEKEVGEGvnRAIDEgLVKREELFLTSK--------LWNNFHDPK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 106 HIENCLNGSLKRLDMDYVDLYILHM------------------------WDY-NTPIEDIMAALHDVIRQGKVRYIGISN 160
Cdd:cd19113 86 NVETALNKTLSDLKLDYVDLFLIHFpiafkfvpieekyppgfycgdgdnFVYeDVPILDTWKALEKLVDAGKIKSIGVSN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1797152346 161 CYAWQIAKANEIAKAKgyEQFVSIQGHYNLifreEEREMKQYCVAHNIAMTPYSA 215
Cdd:cd19113 166 FPGALILDLLRGATIK--PAVLQIEHHPYL----QQPKLIEYAQKAGITITAYSS 214
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
27-308 |
1.32e-10 |
|
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: 60.69 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 27 QKGMHSWTLPYEESKKIIKYALDNGINFFDTA--IGYQGGTSEAFLGKAIKeyakREDVIIATKFIPRTQ--EEIEQGID 102
Cdd:cd19130 12 QLGYGVFKVPPADTQRAVATALEVGYRHIDTAaiYGNEEGVGAAIAASGIP----RDELFVTTKLWNDRHdgDEPAAAFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 103 AkqhienclngSLKRLDMDYVDLYILHmwdYNTPIEDIM----AALHDVIRQGKVRYIGISNcyaWQIAKANEIAKAKGY 178
Cdd:cd19130 88 E----------SLAKLGLDQVDLYLVH---WPTPAAGNYvhtwEAMIELRAAGRTRSIGVSN---FLPPHLERIVAATGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 179 EQFVS-IQGHYNLifreEEREMKQYCVAHNIAMTPYSALASGRLAKHPGeeskrlsediyakgkydithdedlaiihrVE 257
Cdd:cd19130 152 VPAVNqIELHPAY----QQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPP-----------------------------VG 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1797152346 258 ELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEI 308
Cdd:cd19130 199 AIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEI 249
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
29-320 |
1.64e-10 |
|
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: 61.13 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYQGgTSEAFLG--KAIKEYA-KREDVIIATKFIPRTQEeieqgidaKQ 105
Cdd:cd19110 8 GLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHN-ESEVGAGirEKIKEGVvRREDLFIVSKLWCTCHK--------KS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 106 HIENCLNGSLKRLDMDYVDLYILHmWDY--------------------NTPIEDIMAALHDVIRQGKVRYIGISNCYAWQ 165
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIH-WPMgfkpgepdlpldrsgmvipsDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 166 IAKANEIAKAKGYEQFVSIQGHYNLifreEEREMKQYCVAHNIAMTPYSALASgrlakhpgeeskrlsediyAKGKYDIT 245
Cdd:cd19110 158 LERLLNKPGLRVKPVTNQIECHPYL----TQKKLISFCQSRNVSVTAYRPLGG-------------------SCEGVDLI 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1797152346 246 HDedlAIIHRVeelAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRL 320
Cdd:cd19110 215 DD---PVIQRI---AKKHGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRL 283
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
34-321 |
8.32e-09 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 55.96 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 34 TLPYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE-----YAKREDVIIATKFIPRTQEeieqgidaKQHIE 108
Cdd:cd19109 17 TTPKGACAEAVKVAIDTGYRHIDGAYIYQ---NEHEVGQAIREkiaegKVKREDIFYCGKLWNTCHP--------PELVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 109 NCLNGSLKRLDMDYVDLYILHMWDYNTPIEDIMAALHDvirqGKVRYIGISNCYAWQ---IAKANEIAKAKGYEQFVSIQ 185
Cdd:cd19109 86 PTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDEN----GKWLYHKTNLCATWEaleACKDAGLVKSIGVSNFNRRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 186 ghYNLIFRE------------------EEREMKQYCVAHNIAMTPYSALASGRLAKHPGEESKRLSEDiyakgkydithd 247
Cdd:cd19109 162 --LELILNKpglkhkpvsnqvechpyfTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLED------------ 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797152346 248 edlaiiHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEELYKPHRLV 321
Cdd:cd19109 228 ------PLLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYV 295
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
29-314 |
1.16e-08 |
|
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: 55.26 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 29 GMHSWTLPYEESKKIIKYALDNGINFFDTAIGYqggTSEAFLGKAIKE-----YAKREDVIIATKfiprtqeeIEQGIDA 103
Cdd:cd19114 8 GFGTAKIKANETEEVIYNAIKVGYRLIDGALLY---GNEAEVGRGIRKaiqegLVKREDLFIVTK--------LWNNFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 104 KQHIENCLNGSLKRLDMDYVDLYILH----------------MWDY---------NTPIEDIMAALHDVIRQGKVRYIGI 158
Cdd:cd19114 77 KDHVREAFDRQLKDYGLDYIDLYLIHfpipaayvdpaenypfLWKDkelkkfpleQSPMQECWREMEKLVDAGLVRNIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 159 SNCYAWQIAKANEIAKAKgyEQFVSIQGHYNLifreEEREMKQYCVAHNIAMTPYSALASGRLAKHPgEESKRLSediya 238
Cdd:cd19114 157 ANFNVQLILDLLTYAKIK--PAVLQIEHHPYL----QQKRLIDWAKKQGIQITAYSSFGNAVYTKVT-KHLKHFT----- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797152346 239 kgkydithdeDLAIIHRVEELAEKKGVSMTEISLAWLLTKVTSPIIGATKPHHIDGAVKAVAVKLTDEEIIYLEEL 314
Cdd:cd19114 225 ----------NLLEHPVVKKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYEL 290
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
36-129 |
1.43e-08 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 55.31 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797152346 36 PYEESKKIIKYALDNGINFFDTAIGYQggtSEAFLGKAIKE-----YAKREDVIIATK-----FIPrtqeeieqgidakQ 105
Cdd:cd19108 25 PKSKALEATKLAIDAGFRHIDSAYLYQ---NEEEVGQAIRSkiadgTVKREDIFYTSKlwctfHRP-------------E 88
|
90 100
....*....|....*....|....
gi 1797152346 106 HIENCLNGSLKRLDMDYVDLYILH 129
Cdd:cd19108 89 LVRPALEKSLKKLQLDYVDLYLIH 112
|
|
| |
