|
Name |
Accession |
Description |
Interval |
E-value |
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-306 |
6.23e-156 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 437.28 E-value: 6.23e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRMN--QKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQ 78
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGewDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 79 SKTGIVPG--------KRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNF 150
Cdd:COG4989 81 TKCGIRLPseardnrvKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 151 DTAQFKLLQSCLSQRLMFNQLQFSLKHTGMIDFGMhmnmvdkpsvdrdsqfLDYARLHKVTVQAWSPFQYGMFEGTFidN 230
Cdd:COG4989 161 TPSQFELLQSALDQPLVTNQIELSLLHTDAFDDGT----------------LDYCQLNGITPMAWSPLAGGRLFGGF--D 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492021191 231 DGFPKLNQELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEWYDLYLAA-GNYLP 306
Cdd:COG4989 223 EQFPRLRAALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTREEWYELYEAArGHEVP 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
11-302 |
5.24e-137 |
|
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: 388.84 E-value: 5.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 11 LSIPAMALGIMRMNQKSVPEAQVA--IQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQSKTGIVPG-- 86
Cdd:cd19092 4 LEVSRLVLGCMRLADWGESAEELLslIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGIRLGdd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 ------KRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQS 160
Cdd:cd19092 84 prpgriKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIELLQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 161 CLSQRLMFNQLQFSLKHTGMIDFGMhmnmvdkpsvdrdsqfLDYARLHKVTVQAWSPFQYGMFEGTFIDNdgFPKLNQEL 240
Cdd:cd19092 164 YLDQPLVTNQIELSLLHTEAIDDGT----------------LDYCQLLDITPMAWSPLGGGRLFGGFDER--FQRLRAAL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492021191 241 QKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEWYDLYLAAG 302
Cdd:cd19092 226 EELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWYEIYEAAR 287
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-294 |
8.76e-69 |
|
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: 216.58 E-value: 8.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRM----NQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqiKREEMF 76
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFggpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGR--PRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 77 IQSKTGIVPGK---RYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTA 153
Cdd:COG0667 79 IATKVGRRMGPgpnGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 154 QFKLLQ--SCLSQRLMFNQLQFSLkhtgmidfgmhmnmvdkpsVDRDS--QFLDYARLHKVTVQAWSPFQYGMFEGTFID 229
Cdd:COG0667 159 QLRRALaiAEGLPPIVAVQNEYSL-------------------LDRSAeeELLPAARELGVGVLAYSPLAGGLLTGKYRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 230 NDGFP-------------------KLNQELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLT 290
Cdd:COG0667 220 GATFPegdraatnfvqgylternlALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELS 299
|
....
gi 492021191 291 RQEW 294
Cdd:COG0667 300 AEDL 303
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-294 |
2.89e-60 |
|
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: 193.68 E-value: 2.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 16 MALGIMRMNQKSVP----EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQSKTGIVPG-KRYD 90
Cdd:pfam00248 1 IGLGTWQLGGGWGPiskeEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGpWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 91 FSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQfklLQSCLSQRLM--- 167
Cdd:pfam00248 81 GSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQ---IEKALTKGKIpiv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 168 FNQLQFSLkhtgmidfgmhMNMVDkpsvdrDSQFLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGFP------------- 234
Cdd:pfam00248 158 AVQVEYNL-----------LRRRQ------EEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGpgerrrllkkgtp 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492021191 235 ---KLNQELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEW 294
Cdd:pfam00248 221 lnlEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEV 283
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
3-297 |
2.45e-58 |
|
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: 188.89 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 3 RIKMGCttlsipaMALGIMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqiKREEMFIQSKTG 82
Cdd:cd19084 6 RIGLGT-------WAIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKCG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 83 IVP----GKRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLL 158
Cdd:cd19084 76 LRWdggkGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 159 QSCLsqRLMFNQLQFSLkhtgmidfgmhmnmvdkpsVDRD--SQFLDYARLHKVTVQAWSPFQYGMF------EGTFIDN 230
Cdd:cd19084 156 RKYG--PIVSLQPPYSM-------------------LEREieEELLPYCRENGIGVLPYGPLAQGLLtgkykkEPTFPPD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 231 D---GFPKLNQE-----------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEWYD 296
Cdd:cd19084 215 DrrsRFPFFRGEnfeknleivdkLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKE 294
|
.
gi 492021191 297 L 297
Cdd:cd19084 295 I 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-283 |
8.90e-58 |
|
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: 185.41 E-value: 8.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 14 PAMALGIMRM-NQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQiKREEMFIQSKTGIVPGK---RY 89
Cdd:cd06660 1 SRLGLGTMTFgGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGGHPPGGdpsRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 90 DFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLS----QR 165
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 166 LMFNQLQFSLkhtgmidfgMHMNMVDKpsvdrdsQFLDYARLHKVTVQAWSPFQYGMfegtfidndgfpklnqelqklad 245
Cdd:cd06660 160 FAAVQPQYSL---------LDRSPMEE-------ELLDWAEENGLPLLAYSPLARGP----------------------- 200
|
250 260 270
....*....|....*....|....*....|....*...
gi 492021191 246 kyevgkNAIAAAWILRHPANIQMLVGSMNPQHIRDSAK 283
Cdd:cd06660 201 ------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
4-293 |
1.57e-50 |
|
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: 169.38 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 4 IKMGCTTLSIPAMALGI------MRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAfsqmqIK--REEM 75
Cdd:cd19149 2 RKLGKSGIEASVIGLGTwaigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKA-----IKgrRDKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 76 FIQSKTGIV------------PGK--RYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGK 141
Cdd:cd19149 77 VLATKCGLRwdreggsfffvrDGVtvYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 142 VRFFGVSNFDTAQFKLLQSCLSqrLMFNQLQFSlkhtgMIDFGMhmnmvdkpsvdrDSQFLDYARLHKVTVQAWSPFQYG 221
Cdd:cd19149 157 IRAIGASNVSVEQIKEYVKAGQ--LDIIQEKYS-----MLDRGI------------EKELLPYCKKNNIAFQAYSPLEQG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 222 MFEGTFIDNDGFPK--------------------LNQELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDS 281
Cdd:cd19149 218 LLTGKITPDREFDAgdarsgipwfspenrekvlaLLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEEN 297
|
330
....*....|..
gi 492021191 282 AKGAKIRLTRQE 293
Cdd:cd19149 298 AKAGDIRLSAED 309
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-293 |
1.35e-46 |
|
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: 157.78 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNQKSVP------EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqIKREEMFIQSKtgivp 85
Cdd:cd19072 3 EVPVLGLGTWGIGGGMSKdysddkKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKG--FDREDLFITTK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 86 gkrydFSKEH-----ILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQS 160
Cdd:cd19072 76 -----VSPDHlkyddVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 161 CLSQ-RLMFNQLQFSLkhtgmidfgmhmnmvdkpsVDRD--SQFLDYARLHKVTVQAWSPFQYGMFEGTFIDNdgfpkln 237
Cdd:cd19072 151 YLKKgPIVANQVEYNL-------------------FDREeeSGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSP------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492021191 238 qELQKLADKYEVGKNAIAAAWILRHPaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19072 205 -LLDEIAKKYGKTPAQIALNWLISKP-NVIAIPKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
30-283 |
2.08e-45 |
|
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: 153.79 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 30 EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqiKREEMFIQSKTGIV----PGKRYDFSKEHILHSVDEILE 105
Cdd:cd19086 25 EAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFGNRfdggPERPQDFSPEYIREAVEASLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 106 RMQLDYLDSLVLHRP-DALMDPEEVAEAFDQLQAAGKVRFFGVS--NFDTAQFkllqsclsqrlmfnqlqfsLKHTGMID 182
Cdd:cd19086 102 RLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYGVSvgDPEEALA-------------------ALRRGGID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 183 FGMH-MNMVDKPSVDrdsQFLDYARLHKVTVQAWSPFQYGMFEGtfidndgfpklnqelqKLAdkyevgknAIAAAWILR 261
Cdd:cd19086 163 VVQViYNLLDQRPEE---ELFPLAEEHGVGVIARVPLASGLLTG----------------KLA--------QAALRFILS 215
|
250 260
....*....|....*....|..
gi 492021191 262 HPANIQMLVGSMNPQHIRDSAK 283
Cdd:cd19086 216 HPAVSTVIPGARSPEQVEENAA 237
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-293 |
2.96e-45 |
|
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: 155.85 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRMNQK----------SVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqi 70
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGggffgawggvDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 71 KREEMFIQSKTGIVPGK---RYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGV 147
Cdd:cd19091 78 RRDDVLIATKVRGRMGEgpnDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 148 SNFDTAQFKLLQScLSQRLMF-----NQLQFSLkhtgmidfgmhmnmvdkpsVDRDSQF--LDYARLHKVTVQAWSPFQY 220
Cdd:cd19091 158 SNFSAWQIMKALG-ISERRGLarfvaLQAYYSL-------------------LGRDLEHelMPLALDQGVGLLVWSPLAG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 221 GMFEG-------------TFIDNDGFPKLNQE--------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIR 279
Cdd:cd19091 218 GLLSGkyrrgqpapegsrLRRTGFDFPPVDRErgydvvdaLREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLE 297
|
330
....*....|....
gi 492021191 280 DSAKGAKIRLTRQE 293
Cdd:cd19091 298 DNLGAAGLSLTPEE 311
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-293 |
7.51e-44 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 150.21 E-value: 7.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNQKsvpEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKtgiVPGKryDF 91
Cdd:COG0656 4 EIPALGLGTWQLPGE---EAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAASGVPREELFVTTK---VWND--NH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 92 SKEHILHSVDEILERMQLDYLDSLVLHRPdALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLSQRLMFNQL 171
Cdd:COG0656 73 GYDDTLAAFEESLERLGLDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 172 QFSLKHtgmidfgmhmnmvdkpsvdRDSQFLDYARLHKVTVQAWSPFQYG-MFEgtfidndgfpklNQELQKLADKYevG 250
Cdd:COG0656 152 ELHPYL-------------------QQRELLAFCREHGIVVEAYSPLGRGkLLD------------DPVLAEIAEKH--G 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492021191 251 KNA--IAAAWILRHpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:COG0656 199 KTPaqVVLRWHLQR--GVVVIPKSVTPERIRENLDAFDFELSDED 241
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-296 |
1.03e-43 |
|
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: 151.57 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRM-NQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqiKREEMFIQS 79
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFgGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 80 KTGIVPGKRYD---FSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFdtAQFK 156
Cdd:cd19087 78 KVFGPMGDDPNdrgLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNF--AAWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 157 LLQSC-LSQRLMFN-----QLQFSLkhtgmidfgmhmnmvdkpsVDR--DSQFLDYARLHKVTVQAWSPFQYGMFEG--- 225
Cdd:cd19087 156 IAKAQgIAARRGLLrfvseQPMYNL-------------------LKRqaELEILPAARAYGLGVIPYSPLAGGLLTGkyg 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 226 ------------------TFIDNDGFPKLnQELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKI 287
Cdd:cd19087 217 kgkrpesgrlveraryqaRYGLEEYRDIA-ERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI 295
|
....*....
gi 492021191 288 RLTrQEWYD 296
Cdd:cd19087 296 TLT-PELLA 303
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
13-297 |
2.97e-43 |
|
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: 148.94 E-value: 2.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSVPEAQV--AIQAAYDAGINFIDSADIYGGGKSEEIFGQAfsqMQIKREEMFIQSKtgIVPGkryD 90
Cdd:cd19138 11 VPALGQGTWYMGEDPAKRAQEieALRAGIDLGMTLIDTAEMYGDGGSEELVGEA---IRGRRDKVFLVSK--VLPS---N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 91 FSKEHILHSVDEILERMQLDYLDSLVLHRPDAlMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLSQRLM-FN 169
Cdd:cd19138 83 ASRQGTVRACERSLRRLGTDYLDLYLLHWRGG-VPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCaAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 170 QLQFSLKHTGmIDFGMhmnmvdkpsvdrdsqfLDYARLHKVTVQAWSPFQygmfEGTFIDNDGFPklNQELQKLADKYEV 249
Cdd:cd19138 162 QVLYNLGSRG-IEYDL----------------LPWCREHGVPVMAYSPLA----QGGLLRRGLLE--NPTLKEIAARHGA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 492021191 250 GKNAIAAAWILRHPANIQmLVGSMNPQHIRDSAKGAKIRLTRQEWYDL 297
Cdd:cd19138 219 TPAQVALAWVLRDGNVIA-IPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-294 |
4.44e-43 |
|
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: 149.75 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 34 AIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqikREEMFIQSKTGIVPGK----RYDFSKEHILHSVDEILERMQL 109
Cdd:cd19102 31 AIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATKCGLLWDEegriRRSLKPASIRAECEASLRRLGV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 110 DYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQfklLQSCLSQR-LMFNQLQFSLkhtgmidfgmhmn 188
Cdd:cd19102 108 DVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQ---MKRCQAIHpIASLQPPYSL------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 189 mvdkpsVDRD--SQFLDYARLHKVTVQAWSPFQYGMFEG--------TFIDNDG------F--PKLNQ------ELQKLA 244
Cdd:cd19102 172 ------LRRGieAEILPFCAEHGIGVIVYSPMQSGLLTGkmtpervaSLPADDWrrrspfFqePNLARnlalvdALRPIA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 492021191 245 DKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEW 294
Cdd:cd19102 246 ERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEEL 295
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
24-290 |
1.41e-42 |
|
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: 148.12 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 24 NQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqIKREEMFIQSK----TGIVPGKRyDFSKEHILHS 99
Cdd:cd19074 17 GQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKG--WPRESYVISTKvfwpTGPGPNDR-GLSRKHIFES 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 100 VDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQF-KLLQSCLSQRLMF---NQLQFsl 175
Cdd:cd19074 94 IHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIaEAHDLARQFGLIPpvvEQPQY-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 176 khtgmidfgmhmNMVDKPSVDrdsQFLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGFP------------KLN------ 237
Cdd:cd19074 172 ------------NMLWREIEE---EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPsrsratdednrdKKRrlltde 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 492021191 238 -----QELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLT 290
Cdd:cd19074 237 nlekvKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLS 294
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
34-289 |
3.18e-42 |
|
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: 147.35 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 34 AIQAAYDAGINFIDSADIYGGGKSEEIFGQAfsqMQIKREEMFIQSKTGIVPGKRYDFSKehilhSVDEILERMQLDYLD 113
Cdd:cd19085 28 TIHAALDAGINFFDTAEAYGDGHSEEVLGKA---LKGRRDDVVIATKVSPDNLTPEDVRK-----SCERSLKRLGTDYID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 114 SLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQfklLQSCLS-QRLMFNQLQFSLKHTGmIDFGMhmnmvdk 192
Cdd:cd19085 100 LYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQ---LEEALDaGRIDSNQLPYNLLWRA-IEYEI------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 193 psvdrdsqfLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGFP---------------------KLNQELQKLADKYEVGK 251
Cdd:cd19085 169 ---------LPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPpgdartrlfrhfepgaeeetfEALEKLKEIADELGVTM 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 492021191 252 NAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRL 289
Cdd:cd19085 240 AQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLEL 277
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-293 |
1.25e-39 |
|
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: 139.15 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGimrMNQKSVPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKtgiVPGKryDFS 92
Cdd:cd19071 1 MPLIGLG---TYKLKPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESGVPREELFITTK---LWPT--DHG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLHRPDALMDP------EEVAEAFDQLQAAGKVRFFGVSNFDTAQF-KLLQSClSQR 165
Cdd:cd19071 70 YERVREALEESLKDLGLDYLDLYLIHWPVPGKEGgskearLETWRALEELVDEGLVRSIGVSNFNVEHLeELLAAA-RIK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 166 LMFNQLQFSLKHTgmidfgmhmnmvdkpsvdrDSQFLDYARLHKVTVQAWSPFqyGMFEGTFIDNDgfpklnqELQKLAD 245
Cdd:cd19071 149 PAVNQIELHPYLQ-------------------QKELVEFCKEHGIVVQAYSPL--GRGRRPLLDDP-------VLKEIAK 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 492021191 246 KYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19071 201 KYGKTPAQVLLRWALQR--GVVVIPKSSNPERIKENLDVFDFELSEED 246
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-293 |
8.12e-39 |
|
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: 138.87 E-value: 8.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 2 KRIKMGCTTLSIPAMALGIM---RMNQKSV----PEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqIKREE 74
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMsfgDPKWRPWvldeEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEF-APRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 75 MFIQSKTGIVPGKRYD---FSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFD 151
Cdd:cd19079 80 VVIATKVYFPMGDGPNgrgLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 152 TAQF-KLLQscLSQRLMFnqlqfslkhTGMIDFGMHMNMVDKpsvDRDSQFLDYARLHKVTVQAWSPFQYGM-------- 222
Cdd:cd19079 160 AWQFaKALH--LAEKNGW---------TKFVSMQNHYNLLYR---EEEREMIPLCEEEGIGVIPWSPLARGRlarpwgdt 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 223 -------FEGTFIDNDGFPKLNQE----LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTR 291
Cdd:cd19079 226 terrrstTDTAKLKYDYFTEADKEivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSE 305
|
..
gi 492021191 292 QE 293
Cdd:cd19079 306 EE 307
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-297 |
1.81e-38 |
|
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: 137.36 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSV--------PEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQiKREEMFIQSKtgiV 84
Cdd:cd19093 2 VSPLGLGTWQWGDRLWwgygeygdEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATK---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 85 PGKRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDA-LMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLS 163
Cdd:cd19093 78 APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 164 QR---LMFNQLQFSLKHTGMIDFGMhmnmvdkpsvdrdsqfLDYARLHKVTVQAWSPFQYGMFEG--------TFIDNDG 232
Cdd:cd19093 158 ERgvpLASNQVEYSLLYRDPEQNGL----------------LPACDELGITLIAYSPLAQGLLTGkyspenppPGGRRRL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492021191 233 FPKLN--------QELQKLADKYEVGKNAIAAAWILRHPANIqmLVGSMNPQHIRDSAKGAKIRLTRQEWYDL 297
Cdd:cd19093 222 FGRKNlekvqpllDALEEIAEKYGKTPAQVALNWLIAKGVVP--IPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
7-294 |
2.05e-37 |
|
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: 135.03 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 7 GCTTLSIPAMALGIMRMNQKSVPEAQVAIQAAY-DAGINFIDSADIYG-------GGKSEEIFGQAFSQmQIKREEMFIQ 78
Cdd:cd19081 3 GRTGLSVSPLCLGTMVFGWTADEETSFALLDAFvDAGGNFIDTADVYSawvpgnaGGESETIIGRWLKS-RGKRDRVVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 79 SKTGIVPG-KRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQF-K 156
Cdd:cd19081 82 TKVGFPMGpNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLqE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 157 LLQSCLSQRL-MFNQLQfslkhtgmidfgMHMNMVDKPSVDRDsqFLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGFPK 235
Cdd:cd19081 162 ALELSRQHGLpRYVSLQ------------PEYNLVDRESFEGE--LLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492021191 236 -----------LN-------QELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEW 294
Cdd:cd19081 228 strrgeaakryLNerglrilDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEV 304
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-148 |
7.07e-37 |
|
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: 131.94 E-value: 7.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRMNQKSVPeaqvAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSqmQIKREEMFIQSK 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESPE----LLRRALDLGINYFDTAEGYGNGNSEEIIGEALK--GLRRDKVFLATK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492021191 81 tgiVPGKRYDFSKEHILHSVDEILERMQLDYLDSLVLHR---PDALMDPEEVAEAFDQLQAAGKVRFFGVS 148
Cdd:cd19105 75 ---ASPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGvdtPEERLLNEELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-293 |
1.49e-36 |
|
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: 131.54 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSVP------EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFsqMQIKREEMFIQSKtgIVPG 86
Cdd:cd19137 4 IPALGLGTWGIGGFLTPdysrdeEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAI--KDFPREDLFIVTK--VWPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 kryDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLSQRL 166
Cdd:cd19137 80 ---NLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 167 MFNQLQFslkhtgmidfgmhmNMVDKPSVDRDsqFLDYARLHKVTVQAWSPFQYGMFegtfidndgfpKLNQELQKLADK 246
Cdd:cd19137 157 VCNQVKY--------------NLEDRDPERDG--LLEYCQKNGITVVAYSPLRRGLE-----------KTNRTLEEIAKN 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492021191 247 YEVGKNAIAAAWILRHPaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19137 210 YGKTIAQIALAWLIQKP-NVVAIPKAGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-283 |
7.08e-36 |
|
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: 129.28 E-value: 7.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 14 PAMALGIMR--MNQKSVPEAQVA--IQAAYDAGINFIDSADIYGGgkSEEIFGQAFSQMQikREEMFIQSKTGIV---PG 86
Cdd:cd19095 1 SVLGLGTSGigRVWGVPSEAEAArlLNTALDLGINLIDTAPAYGR--SEERLGRALAGLR--RDDLFIATKVGTHgegGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 KRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAqfkllqsclsqrl 166
Cdd:cd19095 77 DRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEE------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 167 mfnqLQFSLKhTGMIDFGM-HMNMVDKpsvdRDSQFLDYARLHKVTVQAWSPFQYG-MFEGTFIDNDgfPKLNQELQKLA 244
Cdd:cd19095 144 ----LEAAIA-SGVFDVVQlPYNVLDR----EEEELLPLAAEAGLGVIVNRPLANGrLRRRVRRRPL--YADYARRPEFA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 492021191 245 DKYEVGKNAIAA-AWILRHPANIQMLVGSMNPQHIRDSAK 283
Cdd:cd19095 213 AEIGGATWAQAAlRFVLSHPGVSSAIVGTTNPEHLEENLA 252
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
27-286 |
7.25e-35 |
|
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: 127.67 E-value: 7.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 27 SVPEAQVAIQAAYDAGINFIDSADIYGGgkSEEIFGQAFSQmqIKREEMFIQSKTGIVPGKRYDFSKEHILHSVDEILER 106
Cdd:cd19090 18 DDDEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAE--LPREPLVLSTKVGRLPEDTADYSADRVRRSVEESLER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 107 MQLDYLDSLVLHRPD-----ALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAqfkLLQSCLSqrlmfnqlqfslkhTGMI 181
Cdd:cd19090 94 LGRDRIDLLMIHDPErvpwvDILAPGGALEALLELKEEGLIKHIGLGGGPPD---LLRRAIE--------------TGDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 182 DFGM---HMNMVDKPSVDrdsQFLDYARLHKVTVQAWSPFQYGMF------EGTFIDNDGFPKLNQELQKL---ADKYEV 249
Cdd:cd19090 157 DVVLtanRYTLLDQSAAD---ELLPAAARHGVGVINASPLGMGLLagrppeRVRYTYRWLSPELLDRAKRLyelCDEHGV 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 492021191 250 GKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAK 286
Cdd:cd19090 234 PLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
37-285 |
2.41e-34 |
|
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: 126.51 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 37 AAYDAGINFIDSADIYGG----GKSEEIFGQAFSQmQIKREEMFIQSK---TGIVPGKRYDFSKEHILHSVDEILERMQL 109
Cdd:cd19082 25 AFVELGGNFIDTARVYGDwverGASERVIGEWLKS-RGNRDKVVIATKgghPDLEDMSRSRLSPEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 110 DYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLS----QRLMFNQLQFSLkhtgmidfgM 185
Cdd:cd19082 104 DYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKahglPGFAASSPQWSL---------A 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 186 HMNM---VDKPSVDRDSQFLDYARLHKVTVQAWSPFQYGMFEGTfiDNDGFPKLNQE---------------LQKLADKY 247
Cdd:cd19082 175 RPNEppwPGPTLVAMDEEMRAWHEENQLPVFAYSSQARGFFSKR--AAGGAEDDSELrrvyyseenferlerAKELAEEK 252
|
250 260 270
....*....|....*....|....*....|....*...
gi 492021191 248 EVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGA 285
Cdd:cd19082 253 GVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-290 |
3.49e-34 |
|
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: 125.02 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSV------PEAQVA-IQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqiKREEMFIQSKTGIVP 85
Cdd:cd19088 1 VSRLGYGAMRLTGPGIwgppadREEAIAvLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 86 GK----RYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSC 161
Cdd:cd19088 78 TGpgwwGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 162 LsqRLMFNQLQFSLKHTGmidfgmhmnmvdkpsvdrDSQFLDYARLHKVTVQAWSPFqygmfeGTFidNDGFPKlnQELQ 241
Cdd:cd19088 158 V--RIVSVQNRYNLANRD------------------DEGVLDYCEAAGIAFIPWFPL------GGG--DLAQPG--GLLA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492021191 242 KLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLT 290
Cdd:cd19088 208 EVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-293 |
5.93e-34 |
|
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: 124.31 E-value: 5.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKtgiVPGKRYDfs 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANA---VKEALELGYRHIDTAEIYN---NEAEVGEAIAESGVPREDLFITTK---VWRDHLR-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTaqfKLLQSCLSQ---RLMFN 169
Cdd:cd19073 70 PEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTI---ELLEEALDIsplPIAVN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 170 QLQFSlkhtgmidfgmhmnmvdkPSVDRdSQFLDYARLHKVTVQAWSPFQYG-MFEgtfidndgfpklNQELQKLADKYE 248
Cdd:cd19073 147 QVEFH------------------PFLYQ-AELLEYCRENDIVITAYSPLARGeVLR------------DPVIQEIAEKYD 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492021191 249 VGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19073 196 KTPAQVALRWLVQK--GIVVIPKASSEDHLKENLAIFDWELTSED 238
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-287 |
1.37e-33 |
|
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: 125.02 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALG--IMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQ 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGswVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 79 SK-----TGIVPGKRYdFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTA 153
Cdd:cd19143 81 TKifwggGGPPPNDRG-LSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 154 QfkllqsclsqrlmfnqlqfsLKHTGMI--DFGMHMNMVDKPS---VDRDSQFLDYARLHK-----VTVqaWSPFQYGMF 223
Cdd:cd19143 160 Q--------------------IEEAHEIadRLGLIPPVMEQPQynlFHRERVEVEYAPLYEkyglgTTT--WSPLASGLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 224 EGTFidNDGFP-----------------------KLNQ--ELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHI 278
Cdd:cd19143 218 TGKY--NNGIPegsrlalpgyewlkdrkeelgqeKIEKvrKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQL 295
|
....*....
gi 492021191 279 RDSAKGAKI 287
Cdd:cd19143 296 EENLKALEV 304
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
30-280 |
2.45e-33 |
|
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: 123.96 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 30 EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQiKREEMFIQSKTGIV--PGKRY--DFSKEHILHSVDEILE 105
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKVGLEwdEGGEVvrNSSPARIRKEVEDSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 106 RMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSclSQRLMFNQLQFSLkhtgmidFgm 185
Cdd:cd19148 105 RLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRK--VAPLHTVQPPYNL-------F-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 186 hmnmvdKPSVDRDsqFLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGF---------PKLNQ-----------ELQKLAD 245
Cdd:cd19148 174 ------EREIEKD--VLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFegddlrrtdPKFQEprfsqylaaveELDKLAQ 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 492021191 246 KYeVGKNAIAAA--WILRHPANIQMLVGSMNPQHIRD 280
Cdd:cd19148 246 ER-YGKSVIHLAvrWLLDQPGVSIALWGARKPEQLDA 281
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-285 |
6.01e-33 |
|
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: 122.83 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 14 PAMALGIMRMNQKSVPEAQVAIQAAY-DAGINFIDSADIYG-------GGKSEEIFGQAFSQmQIKREEMFIQSKTGIVP 85
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYvAAGGNFLDTANNYAfwteggvGGESERLIGRWLKD-RGNRDDVVIATKVGAGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 86 GK-------RYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDT------ 152
Cdd:cd19752 80 RDpdggpesPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAwrlera 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 153 ---------AQFkllqSCLsqrlmfnQLQFS-LKHTGMIDFGMHMNMvdkpsvdrDSQFLDYARLHK-VTVQAWSPFQYG 221
Cdd:cd19752 160 rqiarqqgwAEF----SAI-------QQRHSyLRPRPGADFGVQRIV--------TDELLDYASSRPdLTLLAYSPLLSG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492021191 222 MFegtfiDNDGFPKLNQE-----------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGA 285
Cdd:cd19752 221 AY-----TRPDRPLPEQYdgpdsdarlavLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
35-293 |
1.83e-32 |
|
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: 121.76 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 35 IQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqiKREEMFIQSKTGIV---PGKRYDFSKEHILHSVDEILERMQLDY 111
Cdd:cd19083 39 VREALDNGVNLLDTAFIYGLGRSEELVGEVLKEY--NRNEVVIATKGAHKfggDGSVLNNSPEFLRSAVEKSLKRLNTDY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 112 LDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFK---------LLQSClsqrlmFNQLQfslkhtgmid 182
Cdd:cd19083 117 IDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKeankdgyvdVLQGE------YNLLQ---------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 183 fgmhmnmvdkpsVDRDSQFLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGFP--KLNQE------------------LQK 242
Cdd:cd19083 181 ------------REAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPdnDLRNDkplfkgerfsenldkvdkLKS 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492021191 243 LADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19083 249 IADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-293 |
5.63e-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: 120.35 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALG---IMRM-NQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSqmQIKREEMF 76
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGaspLGGVfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALK--GIPRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 77 IQSKTG---IVPGKRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAE----AFDQLQAAGKVRFFGVSN 149
Cdd:cd19163 79 LATKVGrygLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDQILNetlpALQKLKEEGKVRFIGITG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 150 FDTAQFKLLQSCLSqrlmfNQLQFSLKHTgmidfgmHMNMVDkpsvDRDSQFLDYARLHKVTVQAWSPFQYGMF--EGTF 227
Cdd:cd19163 159 YPLDVLKEVLERSP-----VKIDTVLSYC-------HYTLND----TSLLELLPFFKEKGVGVINASPLSMGLLteRGPP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 228 IDNDGFPKLNQELQKLAD---KYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19163 223 DWHPASPEIKEACAKAAAyckSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPLDAHL 291
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-283 |
6.21e-32 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 121.85 E-value: 6.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGgkSEEIFGQAFSQMqikREEMFIQSK 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALKGP---RDKVILATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 81 TGIvpgkrYDFSKEHILHSVDEILERMQLDYLDSLVLHRP------DALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQ 154
Cdd:COG1453 76 LPP-----WVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLnteedlEKVLKPGGALEALEKAKAEGKIRHIGFSTHGSLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 155 fkLLQSCLsqrlmfnqlqfslkHTGMIDFGM-HMNMVDKPSVDRDsQFLDYARLHKVTVQAWSPFQYGMfegtfidndgf 233
Cdd:COG1453 151 --VIKEAI--------------DTGDFDFVQlQYNYLDQDNQAGE-EALEAAAEKGIGVIIMKPLKGGR----------- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492021191 234 pkLNQELQKLADKYEVGKNAIAAA--WILRHPANIQMLVGSMNPQHIRDSAK 283
Cdd:COG1453 203 --LANPPEKLVELLCPPLSPAEWAlrFLLSHPEVTTVLSGMSTPEQLDENLK 252
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-279 |
6.23e-31 |
|
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: 116.59 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKsvpEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTGIVpgkryDFS 92
Cdd:cd19140 8 IPALGLGTYPLTGE---ECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASGVPRDELFLTTKVWPD-----NYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLSQRLMFNQLQ 172
Cdd:cd19140 77 PDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 173 FslkHtgmidfgmhmnmvdkPSVDRDSqFLDYARLHKVTVQAWSPFQygmfegtfidnDGFPKLNQELQKLADKYEVGKN 252
Cdd:cd19140 157 Y---H---------------PYLDQRK-LLDAAREHGIALTAYSPLA-----------RGEVLKDPVLQEIGRKHGKTPA 206
|
250 260
....*....|....*....|....*..
gi 492021191 253 AIAAAWILRHPaNIQMLVGSMNPQHIR 279
Cdd:cd19140 207 QVALRWLLQQE-GVAAIPKATNPERLE 232
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-293 |
1.49e-30 |
|
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: 116.55 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 2 KRIKMGCTTLSIPAMALGIMRMNQKSVP----EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqiKREEMFI 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYGPadeeESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 78 QSKTGIV----PGKRY-DFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDT 152
Cdd:cd19076 78 ATKFGIVrdpgSGFRGvDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 153 AQFKLLQSClsQRLMFNQLQFSLKhtgmidfgmhmnmvdkpSVDRDSQFLDYARLHKVTVQAWSPFQYGMFEGTFIDNDG 232
Cdd:cd19076 158 DTIRRAHAV--HPITAVQSEYSLW-----------------TRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPED 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 233 FP--------------------KLNQELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQ 292
Cdd:cd19076 219 LPeddfrrnnprfqgenfdknlKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPE 298
|
.
gi 492021191 293 E 293
Cdd:cd19076 299 E 299
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
7-293 |
3.56e-29 |
|
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: 113.12 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 7 GCTTLSIPAMALGIMR-MNQKSVPEAQVAI-QAAYDAGINFIDSADIYGG--GKSEEIFGQAFSQ-MQIKREEMFIQSKT 81
Cdd:cd19089 5 GRSGLHLPAISLGLWHnFGDYTSPEEARELlRTAFDLGITHFDLANNYGPppGSAEENFGRILKRdLRPYRDELVISTKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 82 GI--VPGKRYDF-SKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLL 158
Cdd:cd19089 85 GYgmWPGPYGDGgSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 159 QSCLSQR---LMFNQLQFSLkhtgmidfgmhmnmvdkpsVDRDSQ--FLDYARLHKVTVQAWSPFQYGMFEGTFID---- 229
Cdd:cd19089 165 IALLRELgvpLIIHQPRYSL-------------------LDRWAEdgLLEVLEEAGIGFIAFSPLAQGLLTDKYLNgipp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 230 ------NDGF-------PKLNQELQKLadkyevgkNAIAA-----------AWILRHPANIQMLVGSMNPQHIRDSAKGA 285
Cdd:cd19089 226 dsrraaESKFlteealtPEKLEQLRKL--------NKIAAkrgqslaqlalSWVLRDPRVTSVLIGASSPSQLEDNVAAL 297
|
....*....
gi 492021191 286 K-IRLTRQE 293
Cdd:cd19089 298 KnLDFSEEE 306
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-297 |
3.17e-28 |
|
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: 110.14 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 14 PAMALG---IMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqiKREEMFIQSKTG--IVPG-- 86
Cdd:cd19162 1 PRLGLGaasLGNLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARH--PRAEYVVSTKVGrlLEPGaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 -------KRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDpEEVAEAF---DQLQAAGKVRFFGVSNFDTAQfk 156
Cdd:cd19162 79 grpagadRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLL-QALTDAFpalEELRAEGVVGAIGVGVTDWAA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 157 LLQscLSQRLMFNQLQFSLKHTgmidfgmhmnMVDKPSVDRdsqFLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGF--- 233
Cdd:cd19162 156 LLR--AARRADVDVVMVAGRYT----------LLDRRAATE---LLPLCAAKGVAVVAAGVFNSGILATDDPAGDRYdyr 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 234 ---PKLNQELQKLAD---KYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEWYDL 297
Cdd:cd19162 221 patPEVLARARRLAAvcrRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAEFWAEL 290
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-297 |
3.44e-28 |
|
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: 110.40 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 10 TLSIPAMALGIMRMN-----QKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqiKREEMFIQSKTG-- 82
Cdd:cd19078 1 GLEVSAIGLGCMGMShgygpPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGfk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 83 IVPGKRY----DFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFD------- 151
Cdd:cd19078 78 IDGGKPGplglDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGvetirra 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 152 ------TAqfklLQSclsqrlmfnqlQFSLkhtgmidfgmhmnMVDKPsvdrDSQFLDYARLHKVTVQAWSPFQYGMFEG 225
Cdd:cd19078 158 havcpvTA----VQS-----------EYSM-------------MWREP----EKEVLPTLEELGIGFVPFSPLGKGFLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 226 ------TFIDND---GFPKLNQE-----------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGA 285
Cdd:cd19078 206 kidentKFDEGDdraSLPRFTPEaleanqalvdlLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAA 285
|
330
....*....|..
gi 492021191 286 KIRLTRQEWYDL 297
Cdd:cd19078 286 DIELTPEELREI 297
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-280 |
5.66e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 108.34 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 3 RIKMGCTTLSIPAMALGIMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYggGKSEEIFGQAFSQmqiKREEMFIQSKTG 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATKTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 83 ivpGKRYDFSKEHIlhsvDEILERMQLDYLDSLVLH------RPDALMDPEEVAEAFDQLQAAGKVRFFGVS--NFDTAQ 154
Cdd:cd19100 76 ---ARDYEGAKRDL----ERSLKRLGTDYIDLYQLHavdteeDLDQVFGPGGALEALLEAKEEGKIRFIGISghSPEVLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 155 fKLLqsclsQRLMFNQLQFSLkhtgmidfgmhmNMVDKPSVDRDSQFLDYARLHKVTVqawspfqYGM--FEGTFIDNDG 232
Cdd:cd19100 149 -RAL-----ETGEFDVVLFPI------------NPAGDHIDSFREELLPLAREKGVGV-------IAMkvLAGGRLLSGD 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 492021191 233 FPKLNQELQkladkyevgknaiaaaWILRHPANIQMLVGSMNPQHIRD 280
Cdd:cd19100 204 PLDPEQALR----------------YALSLPPVDVVIVGMDSPEELDE 235
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
30-290 |
1.73e-27 |
|
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: 108.46 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 30 EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQaFsqMQIKREEMFIQSK-TGIVPGKRYDFSKEH---ILHSVDEILE 105
Cdd:cd19080 32 EARAMFDAYVEAGGNFIDTANNYTNGTSERLLGE-F--IAGNRDRIVLATKyTMNRRPGDPNAGGNHrknLRRSVEASLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 106 RMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNF--------DT-AQFKLLQsclsqrlMFNQLQfslk 176
Cdd:cd19080 109 RLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTpawvvaraNTlAELRGWS-------PFVALQ---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 177 htgmidfgMHMNMVDKpSVDRDsqFLDYARLHKVTVQAWSPFQYGMFEG------------TFIDNDGFPKLN------- 237
Cdd:cd19080 178 --------IEYSLLER-TPERE--LLPMARALGLGVTPWSPLGGGLLTGkyqrgeegrageAKGVTVGFGKLTernwaiv 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 492021191 238 QELQKLADkyEVGKNA--IAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLT 290
Cdd:cd19080 247 DVVAAVAE--ELGRSAaqVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLS 299
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-293 |
1.02e-26 |
|
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: 105.78 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGI-MRMNQKSVPEAQV----AIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKtgivpg 86
Cdd:cd19120 3 KIPAIAFGTgTAWYKSGDDDIQRdlvdSVKLALKAGFRHIDTAEMYG---NEKEVGEALKESGVPREDLFITTK------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 krYDFSKEHILHSVDEILERMQLDYLDSLVLHRP----DALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFK-LLQSC 161
Cdd:cd19120 74 --VSPGIKDPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEeLLDTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 162 LSqRLMFNQLQFSlkhtgmidfgmhmnmvdkPSV-DRDSQFLDYARLHKVTVQAWSPFQygmfegTFIDNDGFPkLNQEL 240
Cdd:cd19120 152 KI-KPAVNQIEFH------------------PYLyPQQPALLEYCREHGIVVSAYSPLS------PLTRDAGGP-LDPVL 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 492021191 241 QKLADKYEVGKNAIAAAWilrhpaNIQMLVG----SMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19120 206 EKIAEKYGVTPAQVLLRW------ALQKGIVvvttSSKEERMKEYLEAFDFELTEEE 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-293 |
1.50e-26 |
|
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: 106.37 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRMN-----QKSVPEAQVAIQAAYDAGINFIDSADIYGggKSEEIFGQAFSQMQIKREEM 75
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSafygpPKPDEERFAVLDAAFELGCTFWDTADIYG--DSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 76 FIQSKTGI---VPGKRY--DFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSnf 150
Cdd:cd19144 79 FLATKFGIeknVETGEYsvDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 151 DTAQFKLLQSCLSQRLMFNQLQFSlkhtgmiDFGMHmnmVDKPSVDrdsqFLDYARLHKVTVQAWSPFQYGMFEGTFIDN 230
Cdd:cd19144 157 ECSAETLRRAHAVHPIAAVQIEYS-------PFSLD---IERPEIG----VLDTCRELGVAIVAYSPLGRGFLTGAIRSP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 231 DGF---------PKLNQE-----------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLT 290
Cdd:cd19144 223 DDFeegdfrrmaPRFQAEnfpknlelvdkIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLT 302
|
...
gi 492021191 291 RQE 293
Cdd:cd19144 303 EEE 305
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-283 |
1.75e-26 |
|
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: 105.86 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 17 ALGI----MRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQM----QIKREEMFIQSKTGIVPGK- 87
Cdd:cd19099 5 SLGLgtyrGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDEVVIVTKAGYIPGDg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 88 ---------------------------RYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDP----------EEVA 130
Cdd:cd19099 85 deplrplkyleeklgrglidvadsaglRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLElgeeefydrlEEAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 131 EAFDQLQAAGKVRFFGVS--NFDTAQFKLLQSCLSQRLMFNQLQFSLK--HTGMIDFGMHMNM----VDKPSVDRDSQ-F 201
Cdd:cd19099 165 EALEEAVAEGKIRYYGIStwDGFRAPPALPGHLSLEKLVAAAEEVGGDnhHFKVIQLPLNLLEpealTEKNTVKGEALsL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 202 LDYARLHKVTVQAWSPFqygmfegtfidNDGFPKLNQELQKLADKYEVGKNA-IAAAWILRHPANIQMLVGSMNPQHIRD 280
Cdd:cd19099 245 LEAAKELGLGVIASRPL-----------NQGQLLGELRLADLLALPGGATLAqRALQFARSTPGVDSALVGMRRPEHVDE 313
|
...
gi 492021191 281 SAK 283
Cdd:cd19099 314 NLA 316
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-293 |
4.53e-26 |
|
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: 104.60 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 29 PEAQVAIQAAYDAGINFIDSADIYGGgkSEEIFGQAFSQMQIKREEMF-IQSKTGIVP-GKRYDFSKEHILHSVDEILER 106
Cdd:cd19101 23 DAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRRERDAADdVQIHTKWVPdPGELTMTRAYVEAAIDRSLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 107 MQLDYLDSLVLHRPDaLMDP--EEVAEAFDQLQAAGKVRFFGVSNFDTAQfklLQSCLSQ--RLMFNQLQFSL----KHT 178
Cdd:cd19101 101 LGVDRLDLVQFHWWD-YSDPgyLDAAKHLAELQEEGKIRHLGLTNFDTER---LREILDAgvPIVSNQVQYSLldrrPEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 179 GMIDF----GMHM-------------NMVDKPSVDRDSqfLDYARL--HKVTVQAWSPFqygmfegtfidnDGFPKLNQE 239
Cdd:cd19101 177 GMAALcedhGIKLlaygtlaggllseKYLGVPEPTGPA--LETRSLqkYKLMIDEWGGW------------DLFQELLRT 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 492021191 240 LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19101 243 LKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDED 296
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-148 |
7.66e-26 |
|
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: 104.27 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 29 PEAQV-AIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQmqiKREEMFIQSKTGIVPGKRYDFsKEHILHSVDEILERM 107
Cdd:cd19104 31 REEQIaAVRRALDLGINFFDTAPSYGDGKSEENLGRALKG---LPAGPYITTKVRLDPDDLGDI-GGQIERSVEKSLKRL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 492021191 108 QLDYLDSLVLHR---------------PDALMDPEEVAEAFDQLQAAGKVRFFGVS 148
Cdd:cd19104 107 KRDSVDLLQLHNrigderdkpvggtlsTTDVLGLGGVADAFERLRSEGKIRFIGIT 162
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
18-290 |
5.16e-25 |
|
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: 102.26 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 18 LGIMRM-NQKSVPEAQVAIQAAYDAGINFIDSADIY-------GGGKSEEIFGQAFsQMQIKREEMFIQSK-TGivPGKR 88
Cdd:cd19094 6 LGTMTWgEQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWL-KKKGNRDKVVLATKvAG--PGEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 YDF--------SKEHILHSVDEILERMQLDYLDSLVLHRPD------------------ALMDPEEVAEAFDQLQAAGKV 142
Cdd:cd19094 83 ITWprgggtrlDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVKAGKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 143 RFFGVSNfDTAqFKLLQSC-LSQ-----RLMFNQLQFSLkhtgmidfgMHMNmvdkpsvdRDSQFLDYARLHKVTVQAWS 216
Cdd:cd19094 163 RHIGLSN-ETP-WGVMKFLeLAEqlglpRIVSIQNPYSL---------LNRN--------FEEGLAEACHRENVGLLAYS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 217 PFQYGMFEGTFIDNDGFPK---LN------------------QELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNP 275
Cdd:cd19094 224 PLAGGVLTGKYLDGAARPEggrLNlfpgymaryrspqaleavAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTL 303
|
330
....*....|....*
gi 492021191 276 QHIRDSAKGAKIRLT 290
Cdd:cd19094 304 EQLKENIDAFDVPLS 318
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-280 |
2.82e-24 |
|
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: 98.79 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 14 PAMALGIMRM---NQKSVPEAQVA--IQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqiKREEMFIQSKTGIVPGKR 88
Cdd:cd19096 1 SVLGFGTMRLpesDDDSIDEEKAIemIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEG--PREKFYLATKLPPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 YDFSKEHIlhsvDEILERMQLDYLDSLVLH---RPD--ALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQF--KLLQSc 161
Cdd:cd19096 79 AEDFRRIL----EESLKRLGVDYIDFYLLHglnSPEwlEKARKGGLLEFLEKAKKEGLIRHIGFSFHDSPELlkEILDS- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 162 lsqrlmfnqlqfslkhtGMIDF-GMHMNMVDKPSVDRdSQFLDYARLHKVTVQAWSPFQYGMfegtfidndgFPKLNQEL 240
Cdd:cd19096 154 -----------------YDFDFvQLQYNYLDQENQAG-RPGIEYAAKKGMGVIIMEPLKGGG----------LANNPPEA 205
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 492021191 241 QKLADKYEVGKNAIAAAWILRHPaNIQMLVGSM-NPQHIRD 280
Cdd:cd19096 206 LAILCGAPLSPAEWALRFLLSHP-EVTTVLSGMsTPEQLDE 245
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-282 |
6.24e-23 |
|
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: 96.32 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 7 GCTTLSIPAMALGIMRM--NQKSVPEAQVAIQAAYDAGINFIDSADIYG--GGKSEEIFGQAFSQ-MQIKREEMFIQSKT 81
Cdd:cd19151 6 GRSGLKLPAISLGLWHNfgDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdLKPYRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 82 G--IVPGKRYDF-SKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQ---- 154
Cdd:cd19151 86 GytMWPGPYGDWgSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEarea 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 155 FKLLQScLSQRLMFNQLQFSLkhtgmidfgmhmnmvdkpsVDR--DSQFLDYARLHKVTVQAWSPFQYGMFEGTFIdnDG 232
Cdd:cd19151 166 AAILKD-LGTPCLIHQPKYSM-------------------FNRwvEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYL--NG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492021191 233 FPK----------LNQE------------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSA 282
Cdd:cd19151 224 IPEdsraakgssfLKPEqiteeklakvrrLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAV 295
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
13-279 |
1.05e-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: 95.43 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMnqKSVPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQA----FSQMQIKREEMFIQSKTGIvpgkr 88
Cdd:cd19116 11 IPAIALGTWKL--KDDEGVRQAVKHAIEAGYRHIDTAYLYG---NEAEVGEAirekIAEGVVKREDLFITTKLWN----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 YDFSKEHILHSVDEILERMQLDYLDSLVLHRPDAL----------------MDPEEVAEAFDQLQAAGKVRFFGVSNFDT 152
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFkenndsesngdgslsdIDYLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 153 AQFKLLQSCLSQRLMFNQLQFslkhtgmidfgmHMNMVDKPSVdrdsqflDYARLHKVTVQAWSPFqyGMFEGTFIDNDG 232
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEV------------HPTLTQEKLV-------AYCQSNGIVVMAYSPF--GRLVPRGQTNPP 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 492021191 233 fPKLNQE-LQKLADKYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIR 279
Cdd:cd19116 220 -PRLDDPtLVAIAKKYGKTTAQIVLRYLIDR--GVVPIPKSSNKKRIK 264
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-293 |
1.52e-22 |
|
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: 95.21 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 6 MGCTTLSIPAMALG--IMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQSKtgI 83
Cdd:cd19141 5 LGKSGLRVSCLGLGtwVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK--I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 84 VPGKRYD----FSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQ 159
Cdd:cd19141 83 FWGGKAEtergLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 160 SCLSQrlmFNQLQFSLKHTGMIDFGMHMNMVDKPSVdrdsqfldyarLHKVTVQA--WSPFQYGMFEGTFIDN------- 230
Cdd:cd19141 163 SVARQ---FNLIPPIVEQAEYHLFQREKVEMQLPEL-----------FHKIGVGAmtWSPLACGILSGKYDDGvpeysra 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 231 --DGFPKLN---------------QELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIR--LTR 291
Cdd:cd19141 229 slKGYQWLKekilseegrrqqaklKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLpkLTP 308
|
..
gi 492021191 292 QE 293
Cdd:cd19141 309 NI 310
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-293 |
1.70e-22 |
|
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: 94.71 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 24 NQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSqmQIKREEMFIQSKtgIVPGKRYDfSKEHILHSVDEI 103
Cdd:cd19103 27 NHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLK--RYPREDYIISTK--FTPQIAGQ-SADPVADMLEGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 104 LERMQLDYLDSLVLHRPdalMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLSQ---RLMFNQLQFSLKHTGM 180
Cdd:cd19103 102 LARLGTDYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKagvSLSAVQNHYSLLYRSS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 181 IDFGMhmnmvdkpsvdrdsqfLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGFP-----------------KLNQELQKL 243
Cdd:cd19103 179 EEAGI----------------LDYCKENGITFFAYMVLEQGALSGKYDTKHPLPegsgraetynpllpqleELTAVMAEI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492021191 244 ADKYEVGKNAIAAAW-ILRhpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19103 243 GAKHGASIAQVAIAWaIAK---GTTPIIGVTKPHHVEDAARAASITLTDDE 290
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
7-150 |
2.89e-22 |
|
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: 94.14 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 7 GCTTLSIPAMALGIMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQSKTGIVPG 86
Cdd:cd19153 11 NVSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYRD 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 87 KRYDFSKEHILHSVDEILERMQLDYLDSLVLH-----RPDALMDpeEVAEAFDQLQAAGKVRFFGVSNF 150
Cdd:cd19153 91 SEFDYSAERVRASVATSLERLHTTYLDVVYLHdiefvDYDTLVD--EALPALRTLKDEGVIKRIGIAGY 157
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-280 |
3.38e-22 |
|
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: 93.10 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNQKsvpEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKtgiVPGKRYDF 91
Cdd:cd19132 6 QIPAIGFGTYPLKGD---EGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRSGVPREELFVTTK---LPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 92 skEHILHSVDEILERMQLDYLDSLVLHRPDALMDPE-EVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQsclsqrlmfnq 170
Cdd:cd19132 77 --EEALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLDRLI----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 171 lqfslKHTGMI----DFGMHmnmvdkPSVDRDSQfLDYARLHKVTVQAWSPFQYGMFEGTfidndgfpklNQELQKLADK 246
Cdd:cd19132 144 -----DETGVTpavnQIELH------PYFPQAEQ-RAYHREHGIVTQSWSPLGRGSGLLD----------EPVIKAIAEK 201
|
250 260 270
....*....|....*....|....*....|....
gi 492021191 247 YEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRD 280
Cdd:cd19132 202 HGKTPAQVVLRWHVQL--GVVPIPKSANPERQRE 233
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-283 |
4.51e-22 |
|
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: 93.08 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMnqKSVPEAQVAIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQM----QIKREEMFIQSKTGivpgkR 88
Cdd:cd19136 1 MPILGLGTFRL--RGEEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDLlpkyGLSREDIFITSKLA-----P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 YDFSKEHILHSVDEILERMQLDYLDSLVLHRPD-ALMDPE---------EVAEAFDQLQAAGKVRFFGVSNFDTAQFKLL 158
Cdd:cd19136 71 KDQGYEKARAACLGSLERLGTDYLDLYLIHWPGvQGLKPSdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 159 QSCLSQRLMFNQLQFslkhtgmidfgmHMNMVDKpsvdrdsQFLDYARLHKVTVQAWSPFqyGMFEGTFIDNDgfpklnq 238
Cdd:cd19136 151 LKYCEVPPAVNQVEF------------HPHLVQK-------ELLKFCKDHGIHLQAYSSL--GSGDLRLLEDP------- 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492021191 239 ELQKLADKYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSAK 283
Cdd:cd19136 203 TVLAIAKKYGRTPAQVLLRWALQQ--GIGVIPKSTNPERIAENIK 245
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-282 |
5.90e-22 |
|
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: 92.84 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 8 CTTLS----IPAMALGIMRmnqksVPEAQVAIQA---AYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSK 80
Cdd:cd19157 1 TVTLNngvkMPWLGLGVFK-----VEEGSEVVNAvktALKNGYRSIDTAAIYG---NEEGVGKGIKESGIPREELFITSK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 81 TGivpgkRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDpEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQS 160
Cdd:cd19157 73 VW-----NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKY-KETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 161 CLSQRLMFNQLQFslkhtgmidfgmHMNMVDKpsvdrdsQFLDYARLHKVTVQAWSPfqygMFEGTFIDNDgfpklnqEL 240
Cdd:cd19157 147 DAEIVPMVNQVEF------------HPRLTQK-------ELRDYCKKQGIQLEAWSP----LMQGQLLDNP-------VL 196
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 492021191 241 QKLADKYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSA 282
Cdd:cd19157 197 KEIAEKYNKSVAQVILRWDLQN--GVVTIPKSIKEHRIIENA 236
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
13-280 |
6.87e-22 |
|
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: 92.25 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSvpEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTGIvpgkrYDFS 92
Cdd:cd19133 9 MPILGFGVFQIPDPE--ECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKSGIPREELFITTKLWI-----QDAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLHRPDAlmDPEEVAEAFDQLQAAGKVRFFGVSNFDtaqfkllqsclSQRLMfnqlq 172
Cdd:cd19133 79 YEKAKKAFERSLKRLGLDYLDLYLIHQPFG--DVYGAWRAMEELYKEGKIRAIGVSNFY-----------PDRLV----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 173 fslkhtgmiDFGMHmNMVdKPSVDR------DSQFLDYARLHK--VTVQAWSPF---QYGMFEgtfidndgfpklNQELQ 241
Cdd:cd19133 141 ---------DLILH-NEV-KPAVNQiethpfNQQIEAVEFLKKygVQIEAWGPFaegRNNLFE------------NPVLT 197
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 492021191 242 KLADKYevGKNaiAAAWILRHpaNIQ----MLVGSMNPQHIRD 280
Cdd:cd19133 198 EIAEKY--GKS--VAQVILRW--LIQrgivVIPKSVRPERIAE 234
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
14-150 |
1.70e-21 |
|
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: 92.23 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 14 PAMALGIMRMN----QKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQafsqMQIKREEMFIQSKTGIVPGKry 89
Cdd:cd19075 1 PKIILGTMTFGsqgrFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGE----LGLGERGFKIDTKANPGVGG-- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492021191 90 DFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNF 150
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNY 135
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
12-247 |
1.52e-20 |
|
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: 88.58 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMrmnQKSVPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTgivpgKRYDF 91
Cdd:cd19131 9 TIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRASGVPREELFITTKL-----WNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 92 SKEHILHSVDEILERMQLDYLDSLVLHRPDALMDP-EEVAEAFDQLQAAGKVRFFGVSNFDTAQFkllqsclsQRLMfnq 170
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDKyVETWKALIELKKEGRVKSIGVSNFTIEHL--------QRLI--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 171 lqfslKHTGMIdfgmhmnmvdkPSVDR--------DSQFLDYARLHKVTVQAWSPF-QYGMFEGTFIdndgfpklnqelQ 241
Cdd:cd19131 147 -----DETGVV-----------PVVNQielhprfqQRELRAFHAKHGIQTESWSPLgQGGLLSDPVI------------G 198
|
....*.
gi 492021191 242 KLADKY 247
Cdd:cd19131 199 EIAEKH 204
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
28-156 |
1.67e-20 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 89.45 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 28 VPE--AQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQSKTGivpgkRY----DFSKEHILHSVD 101
Cdd:PLN02587 28 VSEedAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKCG-----RYgegfDFSAERVTKSVD 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 492021191 102 EILERMQLDYLDSLVLHRPD-ALMDP--EEVAEAFDQLQAAGKVRFFGVSNFDTAQFK 156
Cdd:PLN02587 103 ESLARLQLDYVDILHCHDIEfGSLDQivNETIPALQKLKESGKVRFIGITGLPLAIFT 160
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
16-293 |
9.25e-20 |
|
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: 87.29 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 16 MALGIMRMNQKSVP----EAQVAIQAAYDAGINFIDSADIYGGGK---SEEIFGQAFSQMQIKREEMFIQSKTGIVPG-K 87
Cdd:cd19077 8 IGLGLMGLTWRPNPtpdeEAFETMKAALDAGSNLWNGGEFYGPPDphaNLKLLARFFRKYPEYADKVVLSVKGGLDPDtL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 88 RYDFSKEHILHSVDEILERM-QLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQ-----SC 161
Cdd:cd19077 88 RPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHavhpiAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 162 LsqrlmfnQLQFSLKHTGMIDFGMhmnmvdkpsvdrdsqfLDYARLHKVTVQAWSPFQYGMFEGTFIDNDGFP------- 234
Cdd:cd19077 168 V-------EVEYSLFSREIEENGV----------------LETCAELGIPIIAYSPLGRGLLTGRIKSLADIPegdfrrh 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492021191 235 -------------KLNQELQKLADKYEVGKNAIAAAWILR-HPANIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19077 225 ldrfngenfeknlKLVDALQELAEKKGCTPAQLALAWILAqSGPKIIPIPGSTTLERVEENLKAANVELTDEE 297
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-280 |
9.77e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 86.43 E-value: 9.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 16 MALGIMRMNQKsVPEAQVA--IQAAYDAGINFIDSADIYGggKSEEIFGQAFSQMQikreEMFIQSKTGIVPGKRYDfSK 93
Cdd:cd19097 12 LDYGIANKSGK-PSEKEAKkiLEYALKAGINTLDTAPAYG--DSEKVLGKFLKRLD----KFKIITKLPPLKEDKKE-DE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 94 EHILHSVDEILERMQLDYLDSLVLHRPDAL-MDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLlqscLSQRLMFN--Q 170
Cdd:cd19097 84 AAIEASVEASLKRLKVDSLDGLLLHNPDDLlKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEK----ALESFKIDiiQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 171 LQFSLkhtgmidfgmhmnmvdkpsVDR---DSQFLDYARLHKVTVQAWSPFQYGMFegtFIDNDGFPKLNQE-------L 240
Cdd:cd19097 160 LPFNI-------------------LDQrflKSGLLAKLKKKGIEIHARSVFLQGLL---LMEPDKLPAKFAPakpllkkL 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 492021191 241 QKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRD 280
Cdd:cd19097 218 HELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKE 257
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
13-293 |
1.06e-19 |
|
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: 86.42 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSvpEAQVAIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQMQIKREEMFIQSKTGivpgkRYDFS 92
Cdd:cd19156 9 MPRLGLGVWRVQDGA--EAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKLW-----NSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLHRP--DALMDpeeVAEAFDQLQAAGKVRFFGVSNFDTAQFK-LLQSClSQRLMFN 169
Cdd:cd19156 79 YESTLAAFEESLEKLGLDYVDLYLIHWPvkGKFKD---TWKAFEKLYKEKKVRAIGVSNFHEHHLEeLLKSC-KVAPMVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 170 QLQfslkhtgmidfgMHMNMVDKPsvdrdsqFLDYARLHKVTVQAWSPFQYGmfegtfidndgfpKL--NQELQKLADKY 247
Cdd:cd19156 155 QIE------------LHPLLTQEP-------LRKFCKEKNIAVEAWSPLGQG-------------KLlsNPVLKAIGKKY 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 492021191 248 evGKNA--IAAAWILRHpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19156 203 --GKSAaqVIIRWDIQH--GIITIPKSVHEERIQENFDVFDFELTAEE 246
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
27-148 |
3.43e-19 |
|
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: 85.79 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 27 SVPEAQvAIQAAYDAGINFIDSADIYGggKSEEIFGQAFSQMQIK--REEMFIQSKTGIVPGKRYDFSKEHILHSVDEIL 104
Cdd:cd19164 33 SIPPVD-IVRRALELGIRAFDTSPYYG--PSEIILGRALKALRDEfpRDTYFIITKVGRYGPDDFDYSPEWIRASVERSL 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 492021191 105 ERMQLDYLDSLVLHrpDA-LMDPEEVAEAFD---QLQAAGKVRFFGVS 148
Cdd:cd19164 110 RRLHTDYLDLVYLH--DVeFVADEEVLEALKelfKLKDEGKIRNVGIS 155
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-293 |
3.83e-19 |
|
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: 85.27 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 14 PAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQM----QIKREEMFIQSKtgIVPgkrY 89
Cdd:cd19128 2 PRLGFGTYKITESESKEA---VKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEIfkdgGVKREDLFITSK--LWP---T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 90 DFSKEHILHSVDEILERMQLDYLDSLVLH-----RPDALMDP--------------EEVAEAFDQLQAAGKVRFFGVSNF 150
Cdd:cd19128 71 MHQPENVKEQLLITLQDLQLEYLDLFLIHwplafDMDTDGDPrddnqiqslskkplEDTWRAMEQCVDEKLTKNIGVSNY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 151 DTAQF-KLLQSCLSQRLMfNQLQFSLKHtgmidfgmhmnmvdkpsvdRDSQFLDYARLHKVTVQAWSPFQygmfeGTFID 229
Cdd:cd19128 151 STKLLtDLLNYCKIKPFM-NQIECHPYF-------------------QNDKLIKFCIENNIHVTAYRPLG-----GSYGD 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492021191 230 NDGFPKLNQELQKLADKYEVGKNAIAAAWIL-RHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19128 206 GNLTFLNDSELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNFDINDLALTKED 270
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-281 |
4.04e-19 |
|
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: 85.91 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALG--IMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQ 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGtwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 79 SKT---GIVPGKRyDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFdtAQF 155
Cdd:cd19158 81 TKIfwgGKAETER-GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW--SSM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 156 KLLQSCLSQRlmfnqlQFSLKHTGMIDFGMHMNMVDKPSVDRDSQFldyarlHKVTVQA--WSPFQYGMFEGTFidNDGF 233
Cdd:cd19158 158 EIMEAYSVAR------QFNLIPPICEQAEYHMFQREKVEVQLPELF------HKIGVGAmtWSPLACGIVSGKY--DSGI 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492021191 234 PKLN--------------------------QELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDS 281
Cdd:cd19158 224 PPYSraslkgyqwlkdkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMEN 297
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
13-282 |
5.74e-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: 84.41 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMnqKSVPEAQVAIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQMQIKREEMFIQSKTGivpgkRYDFS 92
Cdd:cd19126 9 MPWLGLGVFQT--PDGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKLW-----NDDQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLHRP--DALMDpeeVAEAFDQLQAAGKVRFFGVSNFDTAQF-KLLQSClSQRLMFN 169
Cdd:cd19126 79 ARRTEDAFQESLDRLGLDYVDLYLIHWPgkDKFID---TWKALEKLYASGKVKAIGVSNFQEHHLeELLAHA-DVVPAVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 170 QLQFSlkhtgmidfgmhmnmvdkPSVDRDSqFLDYARLHKVTVQAWSPF-QYGMFEgtfidndgfpklNQELQKLADKYe 248
Cdd:cd19126 155 QVEFH------------------PYLTQKE-LRGYCKSKGIVVEAWSPLgQGGLLS------------NPVLAAIGEKY- 202
|
250 260 270
....*....|....*....|....*....|....*.
gi 492021191 249 vGKNA--IAAAWILRHpaNIQMLVGSMNPQHIRDSA 282
Cdd:cd19126 203 -GKSAaqVVLRWDIQH--GVVTIPKSVHASRIKENA 235
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-278 |
5.93e-19 |
|
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: 85.48 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALG--IMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQ 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGtwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 79 SKT---GIVPGKRyDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQF 155
Cdd:cd19159 81 TKLywgGKAETER-GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 156 KLLQSCLSQrlmFNQLQFSLKHTgmidfGMHMNMVDKPSVDRDSQFldyarlHKVTVQA--WSPFQYGMFEGTF------ 227
Cdd:cd19159 160 MEAYSVARQ---FNMIPPVCEQA-----EYHLFQREKVEVQLPELY------HKIGVGAmtWSPLACGIISGKYgngvpe 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 228 ----------------IDNDGFPKLNQ--ELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHI 278
Cdd:cd19159 226 ssraslkcyqwlkeriVSEEGRKQQNKlkDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 294
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
13-293 |
7.54e-19 |
|
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: 84.77 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMrmnqKSVP-EAQVAIQAAYDAGINFIDSADIYGggKSEEI---FGQAFSQMQIKREEMFIQSKTgivpgkr 88
Cdd:cd19123 12 IPALGLGTW----KSKPgEVGQAVKQALEAGYRHIDCAAIYG--NEAEIgaaLAEVFKEGKVKREDLWITSKL------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 ydFSKEH----ILHSVDEILERMQLDYLDSLVLHRPDAL---------------MDPEEVAE---AFDQLQAAGKVRFFG 146
Cdd:cd19123 79 --WNNSHapedVLPALEKTLADLQLDYLDLYLMHWPVALkkgvgfpesgedllsLSPIPLEDtwrAMEELVDKGLCRHIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 147 VSNFDTaqfKLLQSCLSQRLMFNQlqfslkhtgmidfgmhMNMVDKPSVDRDSQFLDYARLHKVTVQAWSPFQYGMfEGT 226
Cdd:cd19123 157 VSNFSV---KKLEDLLATARIKPA----------------VNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGD-RPA 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 227 FIDNDGFPKLNQE--LQKLADKYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19123 217 AMKAEGEPVLLEDpvINKIAEKHGASPAQVLIAWAIQR--GTVVIPKSVNPERIQQNLEAAEVELDASD 283
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
12-293 |
1.03e-18 |
|
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: 83.81 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRmnqksVPEAQV--AIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTGivpgkRY 89
Cdd:cd19130 9 SIPQLGYGVFK-----VPPADTqrAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASGIPRDELFVTTKLW-----ND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 90 DFSKEHILHSVDEILERMQLDYLDSLVLHRP-DALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCLSQRLMF 168
Cdd:cd19130 76 RHDGDEPAAAFAESLAKLGLDQVDLYLVHWPtPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 169 NQLQfslkhtgmidfgMHMNMVDKPSVdrdsqflDYARLHKVTVQAWSPfqygMFEGTFIDndgfpklNQELQKLADKYE 248
Cdd:cd19130 156 NQIE------------LHPAYQQRTIR-------DWAQAHDVKIEAWSP----LGQGKLLG-------DPPVGAIAAAHG 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492021191 249 VGKNAIAAAWILRHPANIqmLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19130 206 KTPAQIVLRWHLQKGHVV--FPKSVRRERMEDNLDVFDFDLTDTE 248
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
13-248 |
2.67e-18 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 82.81 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMrmnQKSVPEAQVAIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQMQIKREEMFIQSKTgivpgkrYDFS 92
Cdd:PRK11565 15 MPQLGLGVW---QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-------WNDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLHRPDALMDpeEVAEAFDQ---LQAAGKVRFFGVSNFDTAQFkllqsclsQRLMfn 169
Cdd:PRK11565 82 HKRPREALEESLKKLQLDYVDLYLMHWPVPAID--HYVEAWKGmieLQKEGLIKSIGVCNFQIHHL--------QRLI-- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 170 qlqfslKHTGMIDFgmhMNMVDKPSVDRDSQFLDYARLHKVTVQAWSPFQYGMfEGTFiDndgfpklNQELQKLADKYE 248
Cdd:PRK11565 150 ------DETGVTPV---INQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGG-KGVF-D-------QKVIRDLADKYG 210
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
26-297 |
3.14e-18 |
|
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: 83.14 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 26 KSVPEAQV--AIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQikREEMFIQSKTG--IVPGKR------------- 88
Cdd:cd19161 15 TAVSNADAdaTLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKVGrlLKPAREgsvpdpngfvdpl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 -----YDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVA------------EAFDQLQAAGKVRFFGVSNFD 151
Cdd:cd19161 93 pfeivYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKErhhfaqlmsggfKALEELKKAGVIKAFGLGVNE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 152 TaqfkllQSCLsqRLMfNQLQFSLkhtgMIDFGMHmNMVDKPSVDRdsqFLDYARLHKVTVQAWSPFQYGMF------EG 225
Cdd:cd19161 173 V------QICL--EAL-DEADLDC----FLLAGRY-SLLDQSAEEE---FLPRCEQRGTSLVIGGVFNSGILatgtksGA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492021191 226 TFIDNDGFP-KLNQ--ELQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEWYDL 297
Cdd:cd19161 236 KFNYGDAPAeIISRvmEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIPEELWQAL 310
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
11-279 |
3.19e-18 |
|
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: 82.45 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 11 LSIPAMALGIMrmnQKSVPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTGIVpgkryD 90
Cdd:cd19127 7 VEMPALGLGVF---QTPPEETADAVATALADGYRLIDTAAAYG---NEREVGEGIRRSGVDRSDIFVTTKLWIS-----D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 91 FSKEHILHSVDEILERMQLDYLDSLVLHRPDAlMDPEEVAEAF---DQLQAAGKVRFFGVSNFDTAQFKllqsclsqRLM 167
Cdd:cd19127 76 YGYDKALRGFDASLRRLGLDYVDLYLLHWPVP-NDFDRTIQAYkalEKLLAEGRVRAIGVSNFTPEHLE--------RLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 168 fnqlqfslKHTGMIDfgmHMNMVDKPSVDRDSQFLDYARLHKVTVQAWSPFQYGMFEGTfIDNDGFPKLNQE--LQKLAD 245
Cdd:cd19127 147 --------DATTVVP---AVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGA-SGPTGPGDVLQDptITGLAE 214
|
250 260 270
....*....|....*....|....*....|....*.
gi 492021191 246 KYevGKNA--IAAAWILRHpaNIQMLVGSMNPQHIR 279
Cdd:cd19127 215 KY--GKTPaqIVLRWHLQN--GVSAIPKSVHPERIA 246
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
7-293 |
3.87e-18 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 83.50 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 7 GCTTLSIPAMALGIMR-MNQKSVPEAQVAI-QAAYDAGINFIDSADIYG--GGKSEEIFGQAFSQ-MQIKREEMFIQSKT 81
Cdd:PRK09912 19 GKSGLRLPALSLGLWHnFGHVNALESQRAIlRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdFAAYRDELIISTKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 82 GivpgkrYDF---------SKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDT 152
Cdd:PRK09912 99 G------YDMwpgpygsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 153 AQFKLLQSCLSQ---RLMFNQLQFSLKHtgmidfgmhmNMVDKpsvdrdSQFLDYARLHKVTVQAWSPFQYGMFEGTFId 229
Cdd:PRK09912 173 ERTQKMVELLREwkiPLLIHQPSYNLLN----------RWVDK------SGLLDTLQNNGVGCIAFTPLAQGLLTGKYL- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 230 nDGFP---KLNQE----------------------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKG 284
Cdd:PRK09912 236 -NGIPqdsRMHREgnkvrgltpkmlteanlnslrlLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQA 314
|
330
....*....|
gi 492021191 285 AK-IRLTRQE 293
Cdd:PRK09912 315 LNnLTFSTEE 324
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-293 |
5.75e-18 |
|
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: 81.25 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTGIVpgkryDFS 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDS---VRTALELGYRHIDTAQIYD---NEAAVGQAIAESGVPRDELFITTKIWID-----NLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 93 KEHILHSVDEILERMQLDYLDSLVLH--RPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCL-SQRLMFN 169
Cdd:cd19139 70 KDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVgAGAIATN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 170 QLQFSlkhtgmidfgmhmnmvdkPSVdRDSQFLDYARLHKVTVQAWSPFQYGMfegtFIDNDgfpklnqELQKLADKYEV 249
Cdd:cd19139 150 QIELS------------------PYL-QNRKLVAHCKQHGIHVTSYMTLAYGK----VLDDP-------VLAAIAERHGA 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 492021191 250 GKNAIAAAWILrhpaNIQMLV--GSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19139 200 TPAQIALAWAM----ARGYAVipSSTKREHLRSNLLALDLTLDADD 241
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
11-158 |
8.60e-18 |
|
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: 81.69 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 11 LSIPAMALGIMRMNQKSVpeaQVAIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQM----QIKREEMFIQSKTGIVPG 86
Cdd:cd19154 10 VKMPLIGLGTWQSKGAEG---ITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELleegVVKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 KRYDfskehILHSVDEILERMQLDYLDSLVLHRPDAL-------------------MDPEEVAEAFDQLQAAGKVRFFGV 147
Cdd:cd19154 84 APED-----VEEALRESLKKLQLEYVDLYLIHAPAAFkddegesgtmengmsihdaVDVEDVWRGMEKVYDEGLTKAIGV 158
|
170
....*....|.
gi 492021191 148 SNFDTAQFKLL 158
Cdd:cd19154 159 SNFNNDQIQRI 169
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
7-283 |
7.34e-17 |
|
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: 79.42 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 7 GCTTLSIPAMALGIMRMNQKSVP-EAQVAI-QAAYDAGINFIDSADIYG--GGKSEEIFGQAFSQ-MQIKREEMFIQSKT 81
Cdd:cd19150 6 GKSGLKLPALSLGLWHNFGDDTPlETQRAIlRTAFDLGITHFDLANNYGppPGSAEENFGRILREdFAGYRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 82 G--IVPGKRYDF-SKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLL 158
Cdd:cd19150 86 GydMWPGPYGEWgSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 159 QSCLSQR---LMFNQLQFSLKHTGMIDFGMhmnmvdkpsvdrdsqfLDYARLHKVTVQAWSPFQYGMFEGTFIdnDGFPK 235
Cdd:cd19150 166 AAILRELgtpLLIHQPSYNMLNRWVEESGL----------------LDTLQELGVGCIAFTPLAQGLLTDKYL--NGIPE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 236 ---------LNQE------------LQKLADKYEVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAK 283
Cdd:cd19150 228 gsraskersLSPKmlteanlnsiraLNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVG 296
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-150 |
8.02e-17 |
|
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: 79.43 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALGIMRMNQKSVPEAQVA--IQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQ 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEeiVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492021191 79 SK----TGivPGKRyDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNF 150
Cdd:cd19142 81 TKiywsYG--SEER-GLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRW 153
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-283 |
6.03e-16 |
|
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: 76.38 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 9 TTLSIPAMALGIMRmnqkSVP-EAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTgivpgk 87
Cdd:cd19117 10 TGAEIPAVGLGTWQ----SKPnEVAKAVEAALKAGYRHIDTAAIYG---NEEEVGQGIKDSGVPREEIFITTKL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 88 rYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALM---------------------DPEEVAEAFDQLQAAGKVRFFG 146
Cdd:cd19117 77 -WCTWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDpdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 147 VSNFDTAQFKLLQSCLSQRLM--FNQLQfslkhtgmidfgMHMNMvdkPSvdrdSQFLDYARLHKVTVQAWSPFqygmfe 224
Cdd:cd19117 156 VSNFSIKNLEKLLASPSAKIVpaVNQIE------------LHPLL---PQ----PKLVDFCKSKGIHATAYSPL------ 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 225 gtfiDNDGFPKLNQE-LQKLADKYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSAK 283
Cdd:cd19117 211 ----GSTNAPLLKEPvIIKIAKKHGKTPAQVIISWGLQR--GYSVLPKSVTPSRIESNFK 264
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
30-147 |
1.19e-15 |
|
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: 75.72 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 30 EAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSqmQIKREEMFIQSKTG--IVPGK------------------RY 89
Cdd:cd19152 21 EAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALR--ELGREDYVISTKVGrlLVPLQeveptfepgfwnplpfdaVF 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 90 DFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQ-----------LQAAGKVRFFGV 147
Cdd:cd19152 99 DYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQaikgafraleeLREEGVIKAIGL 167
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-279 |
1.63e-15 |
|
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: 75.14 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMrmnQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKseEIfGQAFSQMQ-----IKREEMFIQSKTGivpg 86
Cdd:cd19118 6 KIPAIGLGTW---QAEPGEVGAAVKIALKAGYRHLDLAKVYQNQH--EV-GQALKELLkeepgVKREDLFITSKLW---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 kRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDAL-------------MDPEEVA-----------EAFDQLQAAGKV 142
Cdd:cd19118 76 -NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFkptgdlnpltavpTNGGEVDldlsvslvdtwKAMVELKKTGKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 143 RFFGVSNFDTAQFKLLQSCLSQRLMFNQLQfslkhtgmidfgMHmnmvdkPSVDRDsQFLDYARLHKVTVQAWSPFqygm 222
Cdd:cd19118 155 KSIGVSNFSIDHLQAIIEETGVVPAVNQIE------------AH------PLLLQD-ELVDYCKSKNIHITAYSPL---- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492021191 223 fegtfiDND--GFPKL--NQELQKLADKYEVGKNAIAAAWILRhpANIQMLVGSMNPQHIR 279
Cdd:cd19118 212 ------GNNlaGLPLLvqHPEVKAIAAKLGKTPAQVLIAWGIQ--RGHSVIPKSVTPSRIR 264
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
12-279 |
5.00e-15 |
|
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: 73.92 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIYGGGKseEI---FGQAFSQMQIKREEMFIQSKTgivpgKR 88
Cdd:cd19125 10 KIPAVGLGTWQADPGVVGNA---VKTAIKEGYRHIDCAAIYGNEK--EIgkaLKKLFEDGVVKREDLFITSKL-----WC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 YDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMD------PEEVAE--------AFDQLQAAGKVRFFGVSNFDTAQ 154
Cdd:cd19125 80 TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKgahmpePEEVLPpdipstwkAMEKLVDSGKVRAIGVSNFSVKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 155 F-KLLQSClsqRLM--FNQLQfslkhtgmidfgMHmnmvdkPSVdRDSQFLDYARLHKVTVQAWSPFqyGMFEGTFIDnd 231
Cdd:cd19125 160 LeDLLAVA---RVPpaVNQVE------------CH------PGW-QQDKLHEFCKSKGIHLSAYSPL--GSPGTTWVK-- 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 492021191 232 gfPKL--NQELQKLADKYEVGKNAIAAAWilrhpaNIQM----LVGSMNPQHIR 279
Cdd:cd19125 214 --KNVlkDPIVTKVAEKLGKTPAQVALRW------GLQRgtsvLPKSTNEERIK 259
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
12-278 |
5.80e-15 |
|
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: 73.35 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMnqkSVPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTGiVPGKRYDF 91
Cdd:cd19134 10 TMPVIGLGVGEL---SDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKLA-TPDQGFTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 92 SKEHILHSvdeiLERMQLDYLDSLVLHRPDAlmDPEEVAEAFD---QLQAAGKVRFFGVSNFDTAQFKLLQSCLSQRLMF 168
Cdd:cd19134 83 SQAACRAS----LERLGLDYVDLYLIHWPAG--REGKYVDSWGglmKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 169 NQLQfslkhtgmidfgMHmnmvdkPSVDRDsQFLDYARLHKVTVQAWSPFQYgmfeGTFIDNDgfpklnqELQKLADKYE 248
Cdd:cd19134 157 NQIE------------LH------PLLNQA-ELRKVNAQHGIVTQAYSPLGV----GRLLDNP-------AVTAIAAAHG 206
|
250 260 270
....*....|....*....|....*....|....
gi 492021191 249 VGKNAIAAAWilrhpaNIQM----LVGSMNPQHI 278
Cdd:cd19134 207 RTPAQVLLRW------SLQLgnvvISRSSNPERI 234
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
11-156 |
1.06e-14 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 72.36 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 11 LSIPAMALGIMRMNqksvpeAQVAI---QAAYDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKTGIVpgk 87
Cdd:PRK11172 1 MSIPAFGLGTFRLK------DQVVIdsvKTALELGYRAIDTAQIYD---NEAAVGQAIAESGVPRDELFITTKIWID--- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492021191 88 ryDFSKEHILHSVDEILERMQLDYLDSLVLH--RPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQFK 156
Cdd:PRK11172 69 --NLAKDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMK 137
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-148 |
1.08e-14 |
|
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: 72.85 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 3 RIKMGCTTLSIPAMALGIMRMNQ---KSVPEAQV--AIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqiKREEMFI 77
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGdygAPKPEEEGiaLIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDG--PREKVQL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492021191 78 QSKTGIV----PGKRYDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVS 148
Cdd:cd19145 80 ATKFGIHeiggSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLS 154
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-154 |
1.96e-14 |
|
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: 72.15 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMrmnQKSVPEAQVAIQAAYDAGINFIDSADIYgggKSEEIFGQA----FSQMQIKREEMFIQSKtgiVPgkR 88
Cdd:cd19111 4 MPVIGLGTY---QSPPEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEAlkwwLKNGKLKREEVFITTK---LP--P 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 89 YDFSKEHILHSVDEILERMQLDYLDSLVLH-------------RPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQ 154
Cdd:cd19111 73 VYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-280 |
3.80e-14 |
|
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: 71.55 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 1 MKRIKMGCTTLSIPAMALG--IMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIKREEMFIQ 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGtwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 79 SKT---GIVPGKRyDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSNFDTAQf 155
Cdd:cd19160 83 TKIywgGQAETER-GLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 156 kLLQSCLSQRlmfnqlQFSLKHTGMIDFGMHMNMVDKPSVDRDSQFldyarlHKVTVQA--WSPFQYGMFEGTFIDN--- 230
Cdd:cd19160 161 -IMEAYSVAR------QFNLIPPVCEQAEYHLFQREKVEMQLPELY------HKIGVGSvtWSPLACGLITGKYDGRvpd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 231 ------DGFPKLNQ---------------ELQKLADKYEVGKNAIAAAWILR-------------------HPANIQMLv 270
Cdd:cd19160 228 tcraavKGYQWLKEkvqseegkkqqakvkELHPIADRLGCTVAQLAIAWCLRsegvssvllgvssaeqlieNLGSIQVL- 306
|
330
....*....|
gi 492021191 271 GSMNPQHIRD 280
Cdd:cd19160 307 SQLTPQTVME 316
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
12-293 |
4.05e-14 |
|
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: 71.36 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIYGGGKS-EEIFGQAFSQMQIKREEMFIQsktgivpGKRYD 90
Cdd:cd19112 10 KMPVIGLGVWRMEPGEIKEL---ILNAIKIGYRHFDCAADYKNEKEvGEALAEAFKTGLVKREDLFIT-------TKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 91 FSKEHILHSVDEILERMQLDYLDSLVLHRP-----------DALMDPEEVAE------------AFDQLQAAGKVRFFGV 147
Cdd:cd19112 80 SDHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttGSALGEDGVLDidvtislettwhAMEKLVSAGLVRSIGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 148 SNFDTAqfkLLQSCLSQRLM---FNQLQfslkhtgmidfgMHmnmvdkPSVDRDSqFLDYARLHKVTVQAWSPFQygmfe 224
Cdd:cd19112 160 SNYDIF---LTRDCLAYSKIkpaVNQIE------------TH------PYFQRDS-LVKFCQKHGISVTAHTPLG----- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492021191 225 GTFIDNDGF----PKLNQELQKLADKYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19112 213 GAAANAEWFgsvsPLDDPVLKDLAKKYGKSAAQIVLRWGIQR--NTAVIPKSSKPERLKENIDVFDFQLSKED 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
11-262 |
8.87e-14 |
|
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: 70.05 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 11 LSIPAMALGIMRMNQKSVPEAQVAIQaayDAGINFIDSADIYGggkSEEIFGQAFSQMQIKREEMFIQSKtgIVPGkryD 90
Cdd:cd19135 11 VEMPILGLGTSHSGGYSHEAVVYALK---ECGYRHIDTAKRYG---CEELLGKAIKESGVPREDLFLTTK--LWPS---D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 91 FSKEHILHSVDEILERMQLDYLDSLVLHRPDAlMDP--------EEVAEAFDQLQAAGKVRFFGVSNFDTAQFKLLQSCL 162
Cdd:cd19135 80 YGYESTKQAFEASLKRLGVDYLDLYLLHWPDC-PSSgknvketrAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 163 SQRLMFNQLQFSLkhtgmidfgmhmnmvdkpsVDRDSQFLDYARLHKVTVQAWSPFQYGMFegtfidndgfpkLNQE-LQ 241
Cdd:cd19135 159 SVVPHVNQVEFHP-------------------FQNPVELIEYCRDNNIVFEGYCPLAKGKA------------LEEPtVT 207
|
250 260
....*....|....*....|.
gi 492021191 242 KLADKYEVGKNAIAAAWILRH 262
Cdd:cd19135 208 ELAKKYQKTPAQILIRWSIQN 228
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-297 |
2.66e-13 |
|
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: 69.06 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNQKSVP-EAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAF----SQMQIKREEMFIQSKTgivpg 86
Cdd:cd19109 3 SIPIIGLGTYSEPKTTPKgACAEAVKVAIDTGYRHIDGAYIYQ---NEHEVGQAIrekiAEGKVKREDIFYCGKL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 krydFSKEHILHSVDEILER----MQLDYLDSLVLHRPDALMDPEEVA-------------------EAFDQLQAAGKVR 143
Cdd:cd19109 75 ----WNTCHPPELVRPTLERtlkvLQLDYVDLYIIEMPMAFKPGDEIYprdengkwlyhktnlcatwEALEACKDAGLVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 144 FFGVSNFDTAQFKLLQSclsqrlmfnqlQFSLKHTGMidfgmhMNMVDKPSVDRDSQFLDYARLHKVTVQAWSPFQYGMf 223
Cdd:cd19109 151 SIGVSNFNRRQLELILN-----------KPGLKHKPV------SNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCR- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 224 EGTFIDNDGFPKLNQE-LQKLADKYevgkNAIAAAWILRHpaNIQ----MLVGSMNPQHIRDSAKGAKIRLTRQEWYDL 297
Cdd:cd19109 213 DPIWVNVSSPPLLEDPlLNSIGKKY----NKTAAQVVLRF--NIQrgvvVIPKSFNPERIKENFQIFDFSLTEEEMKDI 285
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-293 |
2.80e-13 |
|
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: 68.68 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 9 TTLSIPAMALGIMRMNQKSVPEAQVaIQAAYDAGINFIDSADIYGggkSEEIFGQA----FSQMQIKREEMFIQSKtgiV 84
Cdd:cd19119 8 TGASIPALGLGTASPHEDRAEVKEA-VEAAIKEGYRHIDTAYAYE---TEDFVGEAikraIDDGSIKREELFITTK---V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 85 PGKRYDfskeHILHSVDEILERMQLDYLDSLVLHRPDALM-DPEEVAEAF---------------------DQLQA---A 139
Cdd:cd19119 81 WPTFYD----EVERSLDESLKALGLDYVDLLLVHWPVCFEkDSDDSGKPFtpvnddgktryaasgdhittyKQLEKiylD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 140 GKVRFFGVSNFDTAQFK-LLQSCLSQRLMfNQLQfslkhtgmidfgMHMNMvdkPSVDrdsqFLDYARLHKVTVQAWSPF 218
Cdd:cd19119 157 GRAKAIGVSNYSIVYLErLIKECKVVPAV-NQVE------------LHPHL---PQMD----LRDFCFKHGILVTAYSPL 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492021191 219 QYGmfegtfidndGFPKL-NQELQKLADKYEVGKNAIAAAWILRHpaNIQMLVGSMNPQHIRDSAKgaKIRLTRQE 293
Cdd:cd19119 217 GSH----------GAPNLkNPLVKKIAEKYNVSTGDILISYHVRQ--GVIVLPKSLKPVRIVSNGK--IVSLTKED 278
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
39-149 |
1.72e-12 |
|
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: 66.68 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 39 YDAGINFIDSADIYGGGKSEEIFGQAFSQMQIkREEMFIQSK--TGIVPGK----RYDFSKEHI--LH-SVDEILERMQL 109
Cdd:cd19146 45 YEQGGNFIDTANNYQGEESERWVGEWMASRGN-RDEMVLATKytTGYRRGGpikiKSNYQGNHAksLRlSVEASLKKLQT 123
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 492021191 110 DYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSN 149
Cdd:cd19146 124 SYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSD 163
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
13-297 |
8.14e-12 |
|
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: 64.59 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIY------GGGKSEEIfgqafSQMQIKREEMFIQSKTGIVPG 86
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEA---VKVAIDAGYRHFDCAYLYhnesevGAGIREKI-----KEGVVRREDLFIVSKLWCTCH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 KrydfsKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPE-------------------EVAEAFDQLQAAGKVRFFGV 147
Cdd:cd19110 76 K-----KSLVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEpdlpldrsgmvipsdtdflDTWEAMEDLVIEGLVKNIGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 148 SNFDTAQFKLL--QSCLSQRLMFNQLQfslkhtgmidfgMHMNMVDKpsvdrdsQFLDYARLHKVTVQAWSPFQygmfeG 225
Cdd:cd19110 151 SNFNHEQLERLlnKPGLRVKPVTNQIE------------CHPYLTQK-------KLISFCQSRNVSVTAYRPLG-----G 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492021191 226 TfidNDGFPKL-NQELQKLADKYevGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQEWYDL 297
Cdd:cd19110 207 S---CEGVDLIdDPVIQRIAKKH--GKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
9-149 |
1.13e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 64.49 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 9 TTLSIPAMALGIMRM-NQKSVPEAQVAIQAAYDAGINFIDSADIY-------GGGKSEEIFGqAFSQMQIKREEMFIQSK 80
Cdd:PRK10625 9 SSLEVSTLGLGTMTFgEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIG-NWLAKRGSREKLIIASK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 81 ---------TGIVPGKRYDfsKEHILHSVDEILERMQLDYLDSLVLHRPD-----------------ALMDPEEVAEAFD 134
Cdd:PRK10625 88 vsgpsrnndKGIRPNQALD--RKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPAVSLLETLDALA 165
|
170
....*....|....*
gi 492021191 135 QLQAAGKVRFFGVSN 149
Cdd:PRK10625 166 EQQRAGKIRYIGVSN 180
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
13-293 |
1.71e-11 |
|
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: 63.44 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSvPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFSQ-----MQIKREEMFIQSKTGIVpgk 87
Cdd:cd19124 5 MPVIGMGTASDPPSP-EDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlgLVKSRDELFVTSKLWCS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 88 ryDFSKEHILHSVDEILERMQLDYLDSLVLHRPDAL----------------MDPEEVAEAFDQLQAAGKVRFFGVSNFD 151
Cdd:cd19124 78 --DAHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLkpgkfsfpieeedflpFDIKGVWEAMEECQRLGLTKAIGVSNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 152 TAQFKLLQSCLSQRLMFNQLQFSLKHtgmidfgmhmnmvdkpsvdRDSQFLDYARLHKVTVQAWSPF-QYGMFEGT--FI 228
Cdd:cd19124 156 CKKLQELLSFATIPPAVNQVEMNPAW-------------------QQKKLREFCKANGIHVTAYSPLgAPGTKWGSnaVM 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492021191 229 DNDgfpklnqELQKLADKYevGKNA--IAAAWILRHpaNIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19124 217 ESD-------VLKEIAAAK--GKTVaqVSLRWVYEQ--GVSLVVKSFNKERMKQNLDIFDWELTEED 272
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-254 |
4.35e-11 |
|
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: 62.16 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 9 TTLSIPAMALGIMrmnQKSVPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQ----AFSQMqIKREEMFIQSKTGIV 84
Cdd:cd19121 8 TGASIPAVGLGTW---QAKAGEVKAAVAHALKIGYRHIDGALCYQ---NEDEVGEgikeAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 85 PGKRydfskehILHSVDEILERMQLDYLDSLVLHRPdALMDPEEVAEAF-----------------------DQLQAAGK 141
Cdd:cd19121 81 YHRR-------VELCLDRSLKSLGLDYVDLYLVHWP-VLLNPNGNHDLFptlpdgsrdldwdwnhvdtwkqmEKVLKTGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 142 VRFFGVSNFDTAQFKLLqsclsqrlmfnqlqfsLKHTGMIDfgmHMNMVDKPSVDRDSQFLDYARLHKVTVQAWSPFqyG 221
Cdd:cd19121 153 TKAIGVSNYSIPYLEEL----------------LKHATVVP---AVNQVENHPYLPQQELVDFCKEKGILIEAYSPL--G 211
|
250 260 270
....*....|....*....|....*....|...
gi 492021191 222 MFEGTFIDNDGfpklnqeLQKLADKYEVGKNAI 254
Cdd:cd19121 212 STGSPLISDEP-------VVEIAKKHNVGPGTV 237
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-154 |
5.00e-11 |
|
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: 62.40 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 9 TTLSIPAMALGimrmNQKSVP-EAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAF-----SQMQIKREEMFIQSK-- 80
Cdd:cd19106 3 TGQKMPLIGLG----TWKSKPgQVKAAVKYALDAGYRHIDCAAVYG---NEQEVGEALkekvgPGKAVPREDLFVTSKlw 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 81 -TGIVPgkrydfskEHILHSVDEILERMQLDYLDSLVLHRPDAL-------------------MDPEEVAEAFDQLQAAG 140
Cdd:cd19106 76 nTKHHP--------EDVEPALRKTLKDLQLDYLDLYLIHWPYAFergdnpfpknpdgtirydsTHYKETWKAMEKLVDKG 147
|
170
....*....|....
gi 492021191 141 KVRFFGVSNFDTAQ 154
Cdd:cd19106 148 LVKAIGLSNFNSRQ 161
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
18-293 |
1.37e-10 |
|
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: 60.99 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 18 LGIMRMNQksvpeAQVAIQAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMQIkREEMFIQSKTGIV-------PGKRYD 90
Cdd:cd19147 28 MGSMDKEQ-----AFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKN-RDQIVIATKFTTDykayevgKGKAVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 91 FSKEH--ILH-SVDEILERMQLDYLDSLVLHRPDALMDPEEVAEAFDQLQAAGKVRFFGVSN-----------FDTAQFK 156
Cdd:cd19147 102 YCGNHkrSLHvSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDtpawvvsaanyYATAHGK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 157 LLQSCLSQRlmFNQLQFSLKHTgMIDFGMHMNMVDKP-SVDRDSQFLDyarlhKVTVQAWSPFQYGMFEGTFIDN--DGF 233
Cdd:cd19147 182 TPFSVYQGR--WNVLNRDFERD-IIPMARHFGMALAPwDVLGGGKFQS-----KKAVEERKKNGEGLRSFVGGTEqtPEE 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492021191 234 PKLNQELQKLADKY-EVGKNAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19147 254 VKISEALEKVAEEHgTESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEE 314
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
13-293 |
4.37e-10 |
|
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: 59.46 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMrmnQKSVPEAQVAIQAAYDAGINFIDSADIYGGGKS-EEIFGQAFSQMQIKREEMFIQSKtgiVP--GKRY 89
Cdd:cd19155 12 MPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAiGNVLKKWIDSGKVKREELFIVTK---LPpgGNRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 90 DFSKEHILHSvdeiLERMQLDYLDSLVLHRP---------DALMDPEEVAE------------AFDQLQAAGKVRFFGVS 148
Cdd:cd19155 86 EKVEKFLLKS----LEKLQLDYVDLYLIHFPvgslskeddSGKLDPTGEHKqdyttdlldiwkAMEAQVDQGLTRSIGLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 149 NFDTAQF-KLLQSClsqRLMFNQLQFSLkhtgmidfgmHMNMVDKpsvdrdsQFLDYARLHKVTVQAWSPF----QYGMF 223
Cdd:cd19155 162 NFNREQMaRILKNA---RIKPANLQVEL----------HVYLQQK-------DLVDFCSTHSITVTAYAPLgspgAAHFS 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492021191 224 EGTFIDNDGFPKLNQ--ELQKLADKYEVGKNAIAAAWILRhpANIQMLVGSMNPQHIRDSAKGAKIRLTRQE 293
Cdd:cd19155 222 PGTGSPSGSSPDLLQdpVVKAIAERHGKSPAQVLLRWLMQ--RGVVVIPKSTNAARIKENFQVFDFELTEAD 291
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
12-154 |
6.55e-10 |
|
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: 58.78 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNQKSVPEAQVAIQAAYDAGINFIDSADIYGggkSEEIFGQAFsQMQI-----KREEMFIQSKTGIVpg 86
Cdd:cd19108 10 FIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQ---NEEEVGQAI-RSKIadgtvKREDIFYTSKLWCT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 87 kryDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVA-------------------EAFDQLQAAGKVRFFGV 147
Cdd:cd19108 84 ---FHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFpkdengklifdtvdlcatwEAMEKCKDAGLAKSIGV 160
|
....*..
gi 492021191 148 SNFDTAQ 154
Cdd:cd19108 161 SNFNRRQ 167
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-280 |
2.42e-09 |
|
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: 57.08 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMrmnqksVPEAQV---AIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQM----QIKREEMFIQSK---TG 82
Cdd:cd19129 6 IPALGFGTL------IPDPSAtrnAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagKIRREDLFVTTKlwnTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 83 IVPgkrydfskEHILHSVDEILERMQLDYLDSLVLHRPDAL-----MDPE---------------EVAEAFDQLQAAGKV 142
Cdd:cd19129 77 HRP--------ERVKPAFEASLKRLQLDYLDLYLIHTPFAFqpgdeQDPRdangnviyddgvtllDTWRAMERLVDEGRC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 143 RFFGVSNFDTAQFKllqsclsqrlmfnqlqfSLKHTGMIdfgmhmnmvdKPSVDR--------DSQFLDYARLHKVTVQA 214
Cdd:cd19129 149 KAIGLSDVSLEKLR-----------------EIFEAARI----------KPAVVQveshpylpEWELLDFCKNHGIVLQA 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492021191 215 WSPFQYGMfegtfidndgFPKLNQELQKLADKYEVGKNA--IAAAW-ILRHPAniqMLVGSMNPQHIRD 280
Cdd:cd19129 202 FAPLGHGM----------EPKLLEDPVITAIARRVNKTPaqVLLAWaIQRGTA---LLTTSKTPSRIRE 257
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
29-290 |
1.33e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 54.98 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 29 PEAQVAI-QAAYDAGINFIDSADIYGGGKSEEIFGQAFSQMqikREEMFIQSKTGIVPGKR----YDFSKEHILHSVDEI 103
Cdd:PRK10376 39 RDAAIAVlREAVALGVNHIDTSDFYGPHVTNQLIREALHPY---PDDLTIVTKVGARRGEDgswlPAFSPAELRRAVHDN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 104 LERMQLDYLDSLVLHRPDALMDPEE--VAEAFD---QLQAAGKVRFFGVSNFDTAQFKLLQS-----CLsqrlmfnQLQF 173
Cdd:PRK10376 116 LRNLGLDVLDVVNLRLMGDGHGPAEgsIEEPLTvlaELQRQGLVRHIGLSNVTPTQVAEARKiaeivCV-------QNHY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 174 SLKHTGmidfgmhmnmvdkpsvdrDSQFLDyaRLHKVTVqAWSP-FQYGmfegtfidndGFPKLNQE-LQKLADKYEVGK 251
Cdd:PRK10376 189 NLAHRA------------------DDALID--ALARDGI-AYVPfFPLG----------GFTPLQSStLSDVAASLGATP 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 492021191 252 NAIAAAWILRHPANIQMLVGSMNPQHIRDSAKGAKIRLT 290
Cdd:PRK10376 238 MQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLS 276
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
13-154 |
1.20e-07 |
|
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: 52.04 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGimrmNQKSVP-EAQVAIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQM----QIKREEMFIQSKTGIVpgk 87
Cdd:cd19107 4 MPILGLG----TWKSPPgQVTEAVKVAIDAGYRHIDCAYVY---QNENEVGEAIQEKikeqVVKREDLFIVSKLWCT--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 88 ryDFSKEHILHSVDEILERMQLDYLDSLVLHRPDALMDPEEVA-------------------EAFDQLQAAGKVRFFGVS 148
Cdd:cd19107 74 --FHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFpldesgnvipsdttfldtwEAMEELVDEGLVKAIGVS 151
|
....*.
gi 492021191 149 NFDTAQ 154
Cdd:cd19107 152 NFNHLQ 157
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-183 |
1.44e-07 |
|
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: 51.85 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 9 TTLSIPAMALGIMrMNQKSVPEAQVAIQAAYDAGINFIDSADIYgggKSEEIFGQAFSQM-----QIKREEMFIQSKTGi 83
Cdd:cd19122 5 NGVKIPAVGFGTF-ANEGAKGETYAAVTKALDVGYRHLDCAWFY---LNEDEVGDAVRDFlkenpSVKREDLFICTKVW- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 84 vpgkRYDFSKEHILHSVDEILERMQLDYLDSLVLHRP-----------------------DALMDPEEVAEAFDQLQAAG 140
Cdd:cd19122 80 ----NHLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPiaaekndqrspklgpdgkyvilkDLTENPEPTWRAMEEIYESG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492021191 141 KVRFFGVSNFDTAQFKLLQSCLSQRLMFNQLQFS--LKHTGMIDF 183
Cdd:cd19122 156 KAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHpfLPNEELVDY 200
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-260 |
1.67e-07 |
|
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: 51.79 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 13 IPAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIYGggkSEEIFG----QAFSQMQIKREEMFIQSKTGivpgkr 88
Cdd:cd19114 4 MPLVGFGTAKIKANETEEV---IYNAIKVGYRLIDGALLYG---NEAEVGrgirKAIQEGLVKREDLFIVTKLW------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 89 YDF-SKEHILHSVDEILERMQLDYLDSLVLHRPDALM-------------DPEEVAEAFDQ------------LQAAGKV 142
Cdd:cd19114 72 NNFhGKDHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdpaenypflwkDKELKKFPLEQspmqecwremekLVDAGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 143 RFFGVSNFDTaqfkllqsclsqRLMFNQLQFSLKHTGMIDFGMHmnmvdkPSVDRDsQFLDYARLHKVTVQAWSPFQYGM 222
Cdd:cd19114 152 RNIGIANFNV------------QLILDLLTYAKIKPAVLQIEHH------PYLQQK-RLIDWAKKQGIQITAYSSFGNAV 212
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250 260 270 280
....*....|....*....|....*....|....*....|
gi 492021191 223 FEGTFIDNDGFPKL--NQELQKLADKYEVGKNAIAAAWIL 260
Cdd:cd19114 213 YTKVTKHLKHFTNLleHPVVKKLADKHKRDTGQVLLRWAV 252
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| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
11-218 |
1.89e-06 |
|
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: 48.60 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 11 LSIPAMALGIMRMNQKSVPEAqvaIQAAYDAGINFIDSADIYGGGKS-EEIFGQAFSQMQIKREEMFIQSKtgiVPGKRY 89
Cdd:cd19113 9 YKMPSVGFGCWKLDNATAADQ---IYQAIKAGYRLFDGAEDYGNEKEvGEGVNRAIDEGLVKREELFLTSK---LWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 90 DfsKEHILHSVDEILERMQLDYLDSLVLHRPDAL--------------------MDPEEVA-----EAFDQLQAAGKVRF 144
Cdd:cd19113 83 D--PKNVETALNKTLSDLKLDYVDLFLIHFPIAFkfvpieekyppgfycgdgdnFVYEDVPildtwKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492021191 145 FGVSNFDTAQFK-LLQSClsqRLMFNQLQFSlkhtgmidfgmHMNMVDKPsvdrdsQFLDYARLHKVTVQAWSPF 218
Cdd:cd19113 161 IGVSNFPGALILdLLRGA---TIKPAVLQIE-----------HHPYLQQP------KLIEYAQKAGITITAYSSF 215
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| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-289 |
9.99e-04 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 40.02 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 36 QAAYDAGINFIDSADIYggGKSEEIFGQAFSQMQIKREEMFIQSKTGI-------VPGKRY---DFSKEHILHSVDEILE 105
Cdd:cd19098 42 DAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSKWGYtytadwqVDAAVHevkDHSLARLLKQWEETRS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 106 RMQlDYLDSLVLHRPDA---LMDPEEVAEAFDQLQAAG--------------------KVRFFGVSNFDTAQ--FKLL-Q 159
Cdd:cd19098 120 LLG-KHLDLYQIHSATLesgVLEDADVLAALAELKAEGvkiglslsgpqqaetlrralEIEIDGARLFDSVQatWNLLeQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 160 SCLSQRLMfnqlqfsLKHTGmidfgmhMNMVDKpsvdrdsQFLDYARLHKVtvqawspfqygmfegtfIDNDGFPKLNQE 239
Cdd:cd19098 199 SAGEALEE-------AHEAG-------MGVIVK-------EALANGRLTDR-----------------NPSPELAPLMAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492021191 240 LQKLADKYEVGKNAIAAAWILRHP-ANIqMLVGSMNPQHIRDSAKGAKIRL 289
Cdd:cd19098 241 LKAVADRLGVTPDALALAAVLAQPfVDV-VLSGAATPEQLRSNLRALDVSL 290
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| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
12-154 |
2.13e-03 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 39.33 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 12 SIPAMALGIMRMNqKSVPEAQV--AIQAAYdagiNFIDSADIYGggkSEEIFGQ----AFSQMQIKREEMFIQSKtgiVP 85
Cdd:cd19115 12 DMPLVGFGLWKVN-NDTCADQVynAIKAGY----RLFDGACDYG---NEVEAGQgvarAIKEGIVKREDLFIVSK---LW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492021191 86 GKRYDfsKEHILHSVDEILERMQLDYLDSLVLHRPDAL--MDP----------------------EEVAEAFDQLQAAGK 141
Cdd:cd19115 81 NTFHD--GERVEPICRKQLADWGIDYFDLFLIHFPIALkyVDPavryppgwfydgkkvefsnapiQETWTAMEKLVDKGL 158
|
170
....*....|...
gi 492021191 142 VRFFGVSNFdTAQ 154
Cdd:cd19115 159 ARSIGVSNF-SAQ 170
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