|
Name |
Accession |
Description |
Interval |
E-value |
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-385 |
0e+00 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 574.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMRLPviedgTIDEERATRQVRYAIDHGVNYIDTAWPYHmgESEPFLGRALtDGYREKIKL 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLP-----RKDEEEAEALIRRAIDNGINYIDTARGYG--DSEEFLGKAL-KGPRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 81 ATKLPSWlVENREDMDRFLNTQLERLNTDHIDYYLLHSL-AGEVWDK-LEPLGVIDFLNKAKDDGRITNAGFSFHGPIED 158
Cdd:COG1453 73 ATKLPPW-VRDPEDMRKDLEESLKRLQTDYIDLYLIHGLnTEEDLEKvLKPGGALEALEKAKAEGKIRHIGFSTHGSLEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 159 FKRIVDAYPWTFCQIQYNFMDERNQAGTEGLKYAASKGLGVIVMEPLLGGNLASPvPAEVKDIWdeaETKRTPAEWALRW 238
Cdd:COG1453 152 IKEAIDTGDFDFVQLQYNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLANP-PEKLVELL---CPPLSPAEWALRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 239 VWNHPEVTVVLSGMNEESHIEENLKIASEAYPnsLTDTEMQLVNRVEQKYRQLVKIGCTGCRYCMPCPSGVNIPECFEIY 318
Cdd:COG1453 228 LLSHPEVTTVLSGMSTPEQLDENLKTADNLEP--LTEEELAILERLAEELGELLKDFCTGCGYCMPCPQGINIPEVFRLY 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499626852 319 NNLHMFGNVEGARFKYAvrmsgvftNTEPGGFASQCTECGQCMEKCPQNLKIPDLLKAVEEDLEGPD 385
Cdd:COG1453 306 NLARAYGMREYAKERYN--------ALGPGAKASACIECGACEERCPQGLDIPELLKEAHELLGGLP 364
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-270 |
7.70e-141 |
|
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: 401.17 E-value: 7.70e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 14 SILGFGCMRLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATKLPSWLVENRE 93
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLPPWSVKSAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 94 DMDRFLNTQLERLNTDHIDYYLLHSL-AGEVWDKLEPLGVIDFLNKAKDDGRITNAGFSFHGPIEDFKRIVDAYPWTFCQ 172
Cdd:cd19096 81 DFRRILEESLKRLGVDYIDFYLLHGLnSPEWLEKARKGGLLEFLEKAKKEGLIRHIGFSFHDSPELLKEILDSYDFDFVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 173 IQYNFMDERNQAGTEGLKYAASKGLGVIVMEPLLGGNLASPVPAEVKDIWDEaetKRTPAEWALRWVWNHPEVTVVLSGM 252
Cdd:cd19096 161 LQYNYLDQENQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGA---PLSPAEWALRFLLSHPEVTTVLSGM 237
|
250
....*....|....*...
gi 499626852 253 NEESHIEENLKIASEAYP 270
Cdd:cd19096 238 STPEQLDENIAAADEFEP 255
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-265 |
1.06e-65 |
|
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: 209.75 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMRLPVIEDGTIdeeratrqvRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKL 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESPELL---------RRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 81 ATKLPSWLVEN-REDMDRFLNTQLERLNTDHIDYYLLHSLAGEVWDKLEPlGVIDFLNKAKDDGRITNAGFSFHGPIEDF 159
Cdd:cd19105 72 ATKASPRLDKKdKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNE-ELLEALEKLKKEGKVRFIGFSTHDNMAEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 160 -KRIVDAYPWTFCQIQYNFM---DERNQAgtegLKYAASKGLGVIVMEPLLGGNLASPVPAEVKdiwdeaETKRTPAEWA 235
Cdd:cd19105 151 lQAAIESGWFDVIMVAYNFLnqpAELEEA----LAAAAEKGIGVVAMKTLAGGYLQPALLSVLK------AKGFSLPQAA 220
|
250 260 270
....*....|....*....|....*....|
gi 499626852 236 LRWVWNHPEVTVVLSGMNEESHIEENLKIA 265
Cdd:cd19105 221 LKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-263 |
4.00e-65 |
|
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: 207.72 E-value: 4.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 3 YRKIPKNGDKLSILGFGCMRLpviedGTIDEERATRQVRYAIDHGVNYIDTAWPYhmGESEPFLGRALTdGYREKIKLAT 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL-----GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALK-GRRDKVFLAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 83 KLPSWlveNREDMDRFLNTQLERLNTDHIDYYLLHSL--AGEVWDKLEPLGVIDFLNKAKDDGRITNAGFSFHGPiEDFK 160
Cdd:cd19100 73 KTGAR---DYEGAKRDLERSLKRLGTDYIDLYQLHAVdtEEDLDQVFGPGGALEALLEAKEEGKIRFIGISGHSP-EVLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 161 RIVDAYPWTFCQIQYNF-MDERNQAGTEGLKYAASKGLGVIVMEPLLGGNLASPVPAEVKDiwdeaetkrtpaewALRWV 239
Cdd:cd19100 149 RALETGEFDVVLFPINPaGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQ--------------ALRYA 214
|
250 260
....*....|....*....|....
gi 499626852 240 WNHPEVTVVLSGMNEESHIEENLK 263
Cdd:cd19100 215 LSLPPVDVVIVGMDSPEELDENLA 238
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-284 |
4.20e-55 |
|
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: 184.23 E-value: 4.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMRLPvIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKL 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFG-GPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 81 ATK--LPSWLVENREDMDR-----FLNTQLERLNTDHIDYYLLHSlagevWDKLEPL-GVIDFLNKAKDDGRITNAGFSF 152
Cdd:COG0667 80 ATKvgRRMGPGPNGRGLSRehirrAVEASLRRLGTDYIDLYQLHR-----PDPDTPIeETLGALDELVREGKIRYIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 153 HGPiEDFKRIVDA----YPWTFCQIQYNFMDeRnQAGTEGLKYAASKGLGVIVMEPLLGGNLA----------------- 211
Cdd:COG0667 155 YSA-EQLRRALAIaeglPPIVAVQNEYSLLD-R-SAEEELLPAARELGVGVLAYSPLAGGLLTgkyrrgatfpegdraat 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 212 ----SPVPAEVKDIWDE-----AETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASeaypNSLTDTEMQLVN 282
Cdd:COG0667 232 nfvqGYLTERNLALVDAlraiaAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAAD----LELSAEDLAALD 307
|
..
gi 499626852 283 RV 284
Cdd:COG0667 308 AA 309
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-266 |
2.35e-52 |
|
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: 176.35 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 16 LGFGCMRLPvIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTD--GYREKIKLATKLPSWLVEN-- 91
Cdd:pfam00248 1 IGLGTWQLG-GGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDypVKRDKVVIATKVPDGDGPWps 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 92 ---REDMDRFLNTQLERLNTDHIDYYLLHSlagevWDKLEP-LGVIDFLNKAKDDGRITNAGFSFHgPIEDFKRIVDA-- 165
Cdd:pfam00248 80 ggsKENIRKSLEESLKRLGTDYIDLYYLHW-----PDPDTPiEETWDALEELKKEGKIRAIGVSNF-DAEQIEKALTKgk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 166 YPWTFCQIQYNFMDERNQAGTegLKYAASKGLGVIVMEPLLGG-------------------NLASPVPAEVK--DIWDE 224
Cdd:pfam00248 154 IPIVAVQVEYNLLRRRQEEEL--LEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrLLKKGTPLNLEalEALEE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499626852 225 --AETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIAS 266
Cdd:pfam00248 232 iaKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE 275
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-263 |
6.88e-51 |
|
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: 170.78 E-value: 6.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 14 SILGFGCMRLpvieDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRAL-TDGYREKIKLATK--LPSWLVE 90
Cdd:cd06660 1 SRLGLGTMTF----GGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLkGRGNRDDVVIATKggHPPGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 91 NREDMDRF-----LNTQLERLNTDHIDYYLLHSlagevWDKLEPLG-VIDFLNKAKDDGRITNAGFSFHgPIEDFKRIVD 164
Cdd:cd06660 77 SRSRLSPEhirrdLEESLRRLGTDYIDLYYLHR-----DDPSTPVEeTLEALNELVREGKIRYIGVSNW-SAERLAEALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 165 A------YPWTFCQIQYNFMDeRNQAGTEGLKYAASKGLGVIVMEPLLGGnlaspvpaevkdiwdeaetkrtPAEWALRW 238
Cdd:cd06660 151 YakahglPGFAAVQPQYSLLD-RSPMEEELLDWAEENGLPLLAYSPLARG----------------------PAQLALAW 207
|
250 260
....*....|....*....|....*
gi 499626852 239 VWNHPEVTVVLSGMNEESHIEENLK 263
Cdd:cd06660 208 LLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-263 |
7.60e-51 |
|
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: 170.74 E-value: 7.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 12 KLSILGFGCMRLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALtDGYREKIKLATKLPSWLVEN 91
Cdd:cd19086 2 EVSEIGFGTWGLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKAL-KGRRDKVVIATKFGNRFDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 92 REDMDRF--------LNTQLERLNTDHIDYYLLHSLAGEVWDKLEplgVIDFLNKAKDDGRITNAGFSFhGPIEDFKRIV 163
Cdd:cd19086 81 PERPQDFspeyireaVEASLKRLGTDYIDLYQLHNPPDEVLDNDE---LFEALEKLKQEGKIRAYGVSV-GDPEEALAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 164 DAYPWTFCQIQYNFMDERnqAGTEGLKYAASKGLGVIVMEPLLGGNLASpvpaevkdiwdeaetkrTPAEWALRWVWNHP 243
Cdd:cd19086 157 RRGGIDVVQVIYNLLDQR--PEEELFPLAEEHGVGVIARVPLASGLLTG-----------------KLAQAALRFILSHP 217
|
250 260
....*....|....*....|
gi 499626852 244 EVTVVLSGMNEESHIEENLK 263
Cdd:cd19086 218 AVSTVIPGARSPEQVEENAA 237
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-263 |
2.67e-47 |
|
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: 162.02 E-value: 2.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 14 SILGFGCMRLPVIeDGTIDEERATRQVRYAIDHGVNYIDTAWPYhmGESEPFLGRALTDGYREKIKLATK-------LPS 86
Cdd:cd19095 1 SVLGLGTSGIGRV-WGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDDLFIATKvgthgegGRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVENREDMDRFLNTQLERLNTDHIDYYLLHSLAGEVWDKleplGVIDFLNKAKDDGRITNAGFSFHGPieDFKRIVDAY 166
Cdd:cd19095 78 RKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTG----EVLETLEDLKAAGKVRYIGVSGDGE--ELEAAIASG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 167 PWTFCQIQYNFMDernQAGTEGLKYAASKGLGVIVMEPLLGGNLASPVP-------AEVKDIWDEAETKRTPAEWALRWV 239
Cdd:cd19095 152 VFDVVQLPYNVLD---REEEELLPLAAEAGLGVIVNRPLANGRLRRRVRrrplyadYARRPEFAAEIGGATWAQAALRFV 228
|
250 260
....*....|....*....|....
gi 499626852 240 WNHPEVTVVLSGMNEESHIEENLK 263
Cdd:cd19095 229 LSHPGVSSAIVGTTNPEHLEENLA 252
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-282 |
3.41e-39 |
|
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: 141.89 E-value: 3.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 12 KLSILGFGCMRLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALtDGYREKIKLATKL------- 84
Cdd:cd19084 3 KVSRIGLGTWAIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKAL-KGRRDDVVIATKCglrwdgg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 85 --------PSWLVENREDmdrflntQLERLNTDHIDYYLLHSlagevWDKLEPLG-VIDFLNKAKDDGRITNAGFSFHGP 155
Cdd:cd19084 82 kgvtkdlsPESIRKEVEQ-------SLRRLQTDYIDLYQIHW-----PDPNTPIEeTAEALEKLKKEGKIRYIGVSNFSV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 156 iEDFKRIVDAYPWTFCQIQYNfMDERNqAGTEGLKYAASKGLGVIVMEPLLGGNLA-----SPVPA-------------- 216
Cdd:cd19084 150 -EQLEEARKYGPIVSLQPPYS-MLERE-IEEELLPYCRENGIGVLPYGPLAQGLLTgkykkEPTFPpddrrsrfpffrge 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499626852 217 ------EVKDIWDE-AETK-RTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLkiasEAYPNSLTDTEMQLVN 282
Cdd:cd19084 227 nfeknlEIVDKLKEiAEKYgKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENA----GALDWELTEEELKEID 296
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-273 |
4.61e-37 |
|
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: 135.76 E-value: 4.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 14 SILGFGCMRLPViEDGTIDEERATRQVRYAIDHGVNYIDTAWPYhmGESEPFLGRALTDGYREKIKLATK---LPSWLV- 89
Cdd:cd19090 1 SALGLGTAGLGG-VFGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPREPLVLSTKvgrLPEDTAd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 90 ENREDMDRFLNTQLERLNTDHIDYYLLHS-LAGEVWDKLEPLGVIDFLNKAKDDGRITNAGFSFhGPIEDFKRIVDAypW 168
Cdd:cd19090 78 YSADRVRRSVEESLERLGRDRIDLLMIHDpERVPWVDILAPGGALEALLELKEEGLIKHIGLGG-GPPDLLRRAIET--G 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 169 TF-CQIQYNFMDERNQ-AGTEGLKYAASKGLGVIVMEPLLGGNLASPVPAEVKDIWDEAETKRTPA-----EW------- 234
Cdd:cd19090 155 DFdVVLTANRYTLLDQsAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYRWLSPELLDRakrlyELcdehgvp 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499626852 235 ----ALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAYPNSL 273
Cdd:cd19090 235 lpalALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEEL 277
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-279 |
2.13e-36 |
|
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: 134.22 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMRLPVIEdGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKL 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVF-GPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSYYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 81 ATKLPSWLVENREDMD-------RFLNTQLERLNTDHIDYYLLHSLagEVWDKLEPlgVID----FLNKAKDDGRITNAG 149
Cdd:cd19163 80 ATKVGRYGLDPDKMFDfsaeritKSVEESLKRLGLDYIDIIQVHDI--EFAPSLDQ--ILNetlpALQKLKEEGKVRFIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 150 FSfhG-PIEDFKRIVDAYP------WTFCqiQYNFMDernQAGTEGLKYAASKGLGVIVMEPLLGGNLAS-------PVP 215
Cdd:cd19163 156 IT--GyPLDVLKEVLERSPvkidtvLSYC--HYTLND---TSLLELLPFFKEKGVGVINASPLSMGLLTErgppdwhPAS 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499626852 216 AEVKDIWDEAETKRTP-----AEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAypnsLTDTEMQ 279
Cdd:cd19163 229 PEIKEACAKAAAYCKSrgvdiSKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEP----LDAHLLA 293
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-270 |
5.88e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 132.27 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 29 GTIDEERATRQVRYAIDHGVNYIDTAWPYhmGESEPFLGRALTDGyrEKIKLATKLPSWLVENREDMDRF---LNTQLER 105
Cdd:cd19097 21 GKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL--DKFKIITKLPPLKEDKKEDEAAIeasVEASLKR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 106 LNTDHIDYYLLHSlagevWDKLEPLG--VIDFLNKAKDDGRITNAGFSFHGPiEDFKRIVDAYPWTFCQIQYNFMDERNQ 183
Cdd:cd19097 97 LKVDSLDGLLLHN-----PDDLLKHGgkLVEALLELKKEGLIRKIGVSVYSP-EELEKALESFKIDIIQLPFNILDQRFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 184 AgTEGLKYAASKGLGVIV----------MEPllggNLASPVPAEVKDIWDE-----AETKRTPAEWALRWVWNHPEVTVV 248
Cdd:cd19097 171 K-SGLLAKLKKKGIEIHArsvflqglllMEP----DKLPAKFAPAKPLLKKlhelaKKLGLSPLELALGFVLSLPEIDKI 245
|
250 260
....*....|....*....|..
gi 499626852 249 LSGMNEESHIEENLKIASEAYP 270
Cdd:cd19097 246 VVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-264 |
5.46e-35 |
|
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: 129.66 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 10 GDKLSILGFGCMRL-PVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATKLPSWL 88
Cdd:cd19072 1 GEEVPVLGLGTWGIgGGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTKVSPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 89 VeNREDMDRFLNTQLERLNTDHIDYYLLHSlageVWDKLEPLGVIDFLNKAKDDGRITNAGFS-FHgpIEDFKR---IVD 164
Cdd:cd19072 81 L-KYDDVIKAAKESLKRLGTDYIDLYLIHW----PNPSIPIEETLRAMEELVEEGKIRYIGVSnFS--LEELEEaqsYLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 165 AYPWTFCQIQYNFMDERNQAGTegLKYAASKGLGVIVMEPLLGGNLAS-PVPAEVKDIWDEAEtkRTPAEWALRWVWNHP 243
Cdd:cd19072 154 KGPIVANQVEYNLFDREEESGL--LPYCQKNGIAIIAYSPLEKGKLSNaKGSPLLDEIAKKYG--KTPAQIALNWLISKP 229
|
250 260
....*....|....*....|.
gi 499626852 244 EVtVVLSGMNEESHIEENLKI 264
Cdd:cd19072 230 NV-IAIPKASNIEHLEENAGA 249
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-279 |
3.70e-34 |
|
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: 128.92 E-value: 3.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 3 YRKIPKNGDKLSILGFGCMRLP-VIEDGTIDEERATrqVRYAIDHGVNYIDTAWPYHMGESEPFLGRALtDGYREKIKLA 81
Cdd:cd19104 2 YRRFGRTGLKVSELTFGGGGIGgLMGRTTREEQIAA--VRRALDLGINFFDTAPSYGDGKSEENLGRAL-KGLPAGPYIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 82 TK--LPSwlvENREDM----DRFLNTQLERLNTDHIDYYLLHSLAGEVWDK-----------LEPLGVIDFLNKAKDDGR 144
Cdd:cd19104 79 TKvrLDP---DDLGDIggqiERSVEKSLKRLKRDSVDLLQLHNRIGDERDKpvggtlsttdvLGLGGVADAFERLRSEGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 145 ITNAGFSFHGPIEDFKRIVDAYPWTFCQIQYNFMD----------ERNQAGTEGLKYAASKGLGVIVMEPLLGGNLASPV 214
Cdd:cd19104 156 IRFIGITGLGNPPAIRELLDSGKFDAVQVYYNLLNpsaaearprgWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTTSL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 215 --PAEVKDIWDEAETK----------------RTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAypnSLTDT 276
Cdd:cd19104 236 drGREAPPTSDSDVAIdfrraaafralarewgETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAG---PLPAE 312
|
...
gi 499626852 277 EMQ 279
Cdd:cd19104 313 NLA 315
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-284 |
8.21e-33 |
|
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: 125.42 E-value: 8.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCM-----RLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTdGYR 75
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMtfgggGGFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALK-GRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 76 EKIKLATKLPSWLVEN-------REDMDRFLNTQLERLNTDHIDYYLLHSlagevWDKLEPlgVIDFLnKAKDD----GR 144
Cdd:cd19091 80 DDVLIATKVRGRMGEGpndvglsRHHIIRAVEASLKRLGTDYIDLYQLHG-----FDALTP--LEETL-RALDDlvrqGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 145 ITNAGFS-FHG-PIEDFKRIVDAYPWT-FC--QIQYNFMD---ERnqagtEGLKYAASKGLGVIVMEPLLGGNL------ 210
Cdd:cd19091 152 VRYIGVSnFSAwQIMKALGISERRGLArFValQAYYSLLGrdlEH-----ELMPLALDQGVGLLVWSPLAGGLLsgkyrr 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 211 ASPVPA---------------EVK--DIWDE-----AETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEa 268
Cdd:cd19091 227 GQPAPEgsrlrrtgfdfppvdRERgyDVVDAlreiaKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL- 305
|
330
....*....|....*.
gi 499626852 269 ypnSLTDTEMQLVNRV 284
Cdd:cd19091 306 ---SLTPEEIARLDKV 318
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-263 |
3.33e-32 |
|
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: 123.58 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 12 KLSILGFGCMRLPviEDGTIDEErATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALT------DGYREKIKLATK-- 83
Cdd:cd19099 2 TLSSLGLGTYRGD--SDDETDEE-YREALKAALDSGINVIDTAINYRGGRSERLIGKALReliekgGIKRDEVVIVTKag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 84 -LPSWLVENREDMDRFLNTQ-----------------------------LERLNTDHIDYYLLHS--------LAGEVWD 125
Cdd:cd19099 79 yIPGDGDEPLRPLKYLEEKLgrglidvadsaglrhcispayledqiersLKRLGLDTIDLYLLHNpeeqllelGEEEFYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 126 KLEplGVIDFLNKAKDDGRI------TNAGFS------FHGPIEDFKRIVDAYP-----WTFCQIQYN-FMDE----RNQ 183
Cdd:cd19099 159 RLE--EAFEALEEAVAEGKIryygisTWDGFRappalpGHLSLEKLVAAAEEVGgdnhhFKVIQLPLNlLEPEalteKNT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 184 AGTEG---LKYAASKGLGVIVMEPLLGGNLASPVPAEVKDIWDEAetkRTPAEWALRWVWNHPEVTVVLSGMNEESHIEE 260
Cdd:cd19099 237 VKGEAlslLEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGG---ATLAQRALQFARSTPGVDSALVGMRRPEHVDE 313
|
...
gi 499626852 261 NLK 263
Cdd:cd19099 314 NLA 316
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
3-279 |
1.85e-30 |
|
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: 118.84 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 3 YRKIPKNGDKLSILGFGCMRLPVIEDG--TIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTD-GYREKIK 79
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCMSFGDPKWRpwVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEfAPRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLpswlvenREDMDRFLNTQ--------------LERLNTDHIDYYLLHslageVWD----KLEPLGVidfLNKAKD 141
Cdd:cd19079 82 IATKV-------YFPMGDGPNGRglsrkhimaevdasLKRLGTDYIDLYQIH-----RWDyetpIEETLEA---LHDVVK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 142 DGRITNAGFS--FHGPIEDFKRIVDAYPWT-FCQIQ--YNFM---DERnqagtEGLKYAASKGLGVIVMEPLLGGNLASP 213
Cdd:cd19079 147 SGKVRYIGASsmYAWQFAKALHLAEKNGWTkFVSMQnhYNLLyreEER-----EMIPLCEEEGIGVIPWSPLARGRLARP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 214 ----------------------------VPAEVKDIwdEAETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLkia 265
Cdd:cd19079 222 wgdtterrrsttdtaklkydyfteadkeIVDRVEEV--AKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAV--- 296
|
330
....*....|....
gi 499626852 266 sEAYPNSLTDTEMQ 279
Cdd:cd19079 297 -AALDIKLSEEEIK 309
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-266 |
3.29e-30 |
|
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: 117.69 E-value: 3.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 13 LSILGFGCMRLPVIED-GTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALtDGYREKIKLATKLpsWLVEN 91
Cdd:cd19085 1 VSRLGLGCWQFGGGYWwGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKAL-KGRRDDVVIATKV--SPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 92 R-EDMDRFLNTQLERLNTDHIDYYLLHSLAGEVwdKLEPlgVIDFLNKAKDDGRITNAGFSFHGPiEDFKRIVDAYPWTF 170
Cdd:cd19085 78 TpEDVRKSCERSLKRLGTDYIDLYQIHWPSSDV--PLEE--TMEALEKLKEEGKIRAIGVSNFGP-AQLEEALDAGRIDS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 171 CQIQYNFMdERNqAGTEGLKYAASKGLGVI----VMEPLLGGNLASP--VP------------------------AEVKD 220
Cdd:cd19085 153 NQLPYNLL-WRA-IEYEILPFCREHGIGVLayspLAQGLLTGKFSSAedFPpgdartrlfrhfepgaeeetfealEKLKE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499626852 221 IWDEAetKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIAS 266
Cdd:cd19085 231 IADEL--GVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVD 274
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-265 |
2.09e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 113.15 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 29 GTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTdGYREKIKLATKL-PSWLVENR-------EDMDRFLN 100
Cdd:cd19102 21 GPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK-GLRDRPIVATKCgLLWDEEGRirrslkpASIRAECE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 101 TQLERLNTDHIDYYLLHSLAG-----EVWDKLEPLgvidflnkaKDDGRITNAGFS-FhgPIEDFKRIVDAYPWTFCQIQ 174
Cdd:cd19102 100 ASLRRLGVDVIDLYQIHWPDPdepieEAWGALAEL---------KEEGKVRAIGVSnF--SVDQMKRCQAIHPIASLQPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 175 YNFMdeRNQAGTEGLKYAASKGLGVIVMEPLLGGNLASPVPAEV--KDIWDE---------------------------A 225
Cdd:cd19102 169 YSLL--RRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERvaSLPADDwrrrspffqepnlarnlalvdalrpiaE 246
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499626852 226 ETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIA 265
Cdd:cd19102 247 RHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAA 286
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-266 |
5.18e-27 |
|
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: 108.07 E-value: 5.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 16 LGFGCMRL--PVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDgYREKIKLATKL-------PS 86
Cdd:cd19088 4 LGYGAMRLtgPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP-YPDDVVIATKGglvrtgpGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVENR-EDMDRFLNTQLERLNTDHIDYYLLHSLAGEVwDKLEPLGVIDflnKAKDDGRITNAGFSfHGPIEDFKRIVDA 165
Cdd:cd19088 83 WGPDGSpEYLRQAVEASLRRLGLDRIDLYQLHRIDPKV-PFEEQLGALA---ELQDEGLIRHIGLS-NVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 166 YPWTFCQIQYNFMDeRNQAGTegLKYAASKGLGVIVMEPLLGGNLASPvpaevKDIWDEAETKR--TPAEWALRWVWNHP 243
Cdd:cd19088 158 VRIVSVQNRYNLAN-RDDEGV--LDYCEAAGIAFIPWFPLGGGDLAQP-----GGLLAEVAARLgaTPAQVALAWLLARS 229
|
250 260
....*....|....*....|...
gi 499626852 244 EVTVVLSGMNEESHIEENLKIAS 266
Cdd:cd19088 230 PVMLPIPGTSSVEHLEENLAAAG 252
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-263 |
1.20e-24 |
|
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: 102.65 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMRLpvieDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTdGYREKIKL 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNF----GGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIA-GRRDDIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 81 ATKLpswlvenREDMDRFLNTQ--------------LERLNTDHIDYYLLHSLAGEV-WDklEPLGVIDFLNKAkddGRI 145
Cdd:cd19087 76 ATKV-------FGPMGDDPNDRglsrrhirraveasLRRLQTDYIDLYQMHHFDRDTpLE--ETLRALDDLVRQ---GKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 146 TNAGFS-FHG-PIEDFKRIVDAYPWT-FCQIQ--YNFMDErnQAGTEGLKYAASKGLGVIVMEPLLGGNLA--------- 211
Cdd:cd19087 144 RYIGVSnFAAwQIAKAQGIAARRGLLrFVSEQpmYNLLKR--QAELEILPAARAYGLGVIPYSPLAGGLLTgkygkgkrp 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 212 ---SPVPAEVKDI--WDE-------------AETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLK 263
Cdd:cd19087 222 esgRLVERARYQAryGLEeyrdiaerfealaAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLA 291
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-290 |
5.68e-24 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 99.74 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRlpviedgtIDEERATRQVRYAIDHGVNYIDTAwpyHMGESEPFLGRALTD-GY-REKIKLATKLps 86
Cdd:COG0656 1 NGVEIPALGLGTWQ--------LPGEEAAAAVRTALEAGYRHIDTA---AMYGNEEGVGEAIAAsGVpREELFVTTKV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WlVEN--REDMDRFLNTQLERLNTDHIDYYLLHSLAG----EVWDKLEplgvidflnKAKDDGRITNAGFS-FHgpIEDF 159
Cdd:COG0656 68 W-NDNhgYDDTLAAFEESLERLGLDYLDLYLIHWPGPgpyvETWRALE---------ELYEEGLIRAIGVSnFD--PEHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 160 KRIVDAypwtfC-------QIQYN-FMDERNQagtegLKYAASKGlgvIVME---PLLGGN-LASPVpaeVKDIwdeAET 227
Cdd:COG0656 136 EELLAE-----TgvkpavnQVELHpYLQQREL-----LAFCREHG---IVVEaysPLGRGKlLDDPV---LAEI---AEK 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499626852 228 -KRTPAEWALRWVWNHPevTVVLSGMNEESHIEENLKIASEaypnSLTDTEMQLVNRVEQKYRQ 290
Cdd:COG0656 197 hGKTPAQVVLRWHLQRG--VVVIPKSVTPERIRENLDAFDF----ELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
31-281 |
1.51e-23 |
|
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: 99.80 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 31 IDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATKLPSWLVENREDMD---RFLNTQLE--- 104
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVIATKGAHKFGGDGSVLNnspEFLRSAVEksl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 105 -RLNTDHIDYYLLHSLAGEVwDKLEPLGVidfLNKAKDDGRITNAGFSfHGPIEDFKR-----IVDAYpwtfcQIQYNFM 178
Cdd:cd19083 110 kRLNTDYIDLYYIHFPDGET-PKAEAVGA---LQELKDEGKIRAIGVS-NFSLEQLKEankdgYVDVL-----QGEYNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 179 DERNQAGTegLKYAASKGLGVIVMEPLLGGNLA---------------SPVP--------------AEVKDIWDEAETkr 229
Cdd:cd19083 180 QREAEEDI--LPYCVENNISFIPYFPLASGLLAgkytkdtkfpdndlrNDKPlfkgerfsenldkvDKLKSIADEKGV-- 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499626852 230 TPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKiaseAYPNSLTDTEMQLV 281
Cdd:cd19083 256 TVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLK----ALDVTLTEEEIAFI 303
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
15-266 |
6.59e-23 |
|
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: 96.93 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 15 ILGFGcMRLPVIEDGT--IDEERATRQ-----VRYAIDHGVNYIDTAWPYHMGESEPFLGRALtDGYREKIKLATK-LPS 86
Cdd:cd19138 4 TLPDG-TKVPALGQGTwyMGEDPAKRAqeieaLRAGIDLGMTLIDTAEMYGDGGSEELVGEAI-RGRRDKVFLVSKvLPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 wlveN--REDMDRFLNTQLERLNTDHIDYYLLHslagevWDKLEPLG-VIDFLNKAKDDGRITNAGFSFHGP--IEDFKR 161
Cdd:cd19138 82 ----NasRQGTVRACERSLRRLGTDYLDLYLLH------WRGGVPLAeTVAAMEELKKEGKIRAWGVSNFDTddMEELWA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 162 IVDAYPWTFCQIQYNFMDErnqaGTEG--LKYAASKGLGVIVMEPLLGGNLASPVPAE---VKDIWDEAETkrTPAEWAL 236
Cdd:cd19138 152 VPGGGNCAANQVLYNLGSR----GIEYdlLPWCREHGVPVMAYSPLAQGGLLRRGLLEnptLKEIAARHGA--TPAQVAL 225
|
250 260 270
....*....|....*....|....*....|
gi 499626852 237 RWVWNHPEVTVVLSGMNEEsHIEENLKIAS 266
Cdd:cd19138 226 AWVLRDGNVIAIPKSGSPE-HARENAAAAD 254
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-282 |
9.94e-23 |
|
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: 96.01 E-value: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 15 ILGFGCMRLpviedgtiDEERATRQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDGY--REKIKLATKLPSWLvENR 92
Cdd:cd19071 3 LIGLGTYKL--------KPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESGvpREELFITTKLWPTD-HGY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 93 EDMDRFLNTQLERLNTDHIDYYLLHS-LAG----------EVWDKLEplgvidflnKAKDDGRITNAGFS-FHgpIEDFK 160
Cdd:cd19071 71 ERVREALEESLKDLGLDYLDLYLIHWpVPGkeggskearlETWRALE---------ELVDEGLVRSIGVSnFN--VEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 161 RIVDA---YPwTFCQIQYN-FMDERnqagtEGLKYAASKGlgvIVME---PLLGGN---LASPVpaeVKDIwdeAE-TKR 229
Cdd:cd19071 140 ELLAAariKP-AVNQIELHpYLQQK-----ELVEFCKEHG---IVVQaysPLGRGRrplLDDPV---LKEI---AKkYGK 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499626852 230 TPAEWALRWVWNHPevTVVLSGMNEESHIEENLKIASEaypnSLTDTEMQLVN 282
Cdd:cd19071 205 TPAQVLLRWALQRG--VVVIPKSSNPERIKENLDVFDF----ELSEEDMAAID 251
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
9-282 |
2.57e-22 |
|
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: 96.13 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLpviedG-TIDEERATRQVRYAIDHGVNYIDTA-----W-PYH-MGESEPFLGRALTD-GYREKIK 79
Cdd:cd19081 5 TGLSVSPLCLGTMVF-----GwTADEETSFALLDAFVDAGGNFIDTAdvysaWvPGNaGGESETIIGRWLKSrGKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLPSWLVENREDMDRFLNTQ-----LERLNTDHIDYYLLHSlagevWDKLEPLG-VIDFLNKAKDDGRITNAGFS-F 152
Cdd:cd19081 80 IATKVGFPMGPNGPGLSRKHIRRaveasLRRLQTDYIDLYQAHW-----DDPATPLEeTLGALNDLIRQGKVRYIGASnY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 153 HGpiEDFKRIVDA------YPWTFCQIQYNFMDernQAGTEG--LKYAASKGLGVIVMEPLLGGNLA------------S 212
Cdd:cd19081 155 SA--WRLQEALELsrqhglPRYVSLQPEYNLVD---RESFEGelLPLCREEGIGVIPYSPLAGGFLTgkyrseadlpgsT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 213 PVPAEVKDIWDE-------------AETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEaypnSLTDTEMQ 279
Cdd:cd19081 230 RRGEAAKRYLNErglrildaldevaAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL----RLTDEEVA 305
|
...
gi 499626852 280 LVN 282
Cdd:cd19081 306 RLD 308
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-290 |
5.33e-22 |
|
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: 94.61 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 10 GDKLSILGFGC-MRLPVIEDGTIDEErATRQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRAL--TDGYREKIKLATKLps 86
Cdd:cd19120 1 GSKIPAIAFGTgTAWYKSGDDDIQRD-LVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALkeSGVPREDLFITTKV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 wlVENREDMDRFLNTQLERLNTDHIDYYLLHSLA---------GEVWDKLEplgvidflnKAKDDGRITNAGFS-FHgpI 156
Cdd:cd19120 75 --SPGIKDPREALRKSLAKLGVDYVDLYLIHSPFfakeggptlAEAWAELE---------ALKDAGLVRSIGVSnFR--I 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 157 EDFKRIVDA--YPWTFCQIQYNfmdERNQAGTEGL-KYAASKGlgvIVME---PL--LGGNLASPVPAEVKDIwdEAETK 228
Cdd:cd19120 142 EDLEELLDTakIKPAVNQIEFH---PYLYPQQPALlEYCREHG---IVVSaysPLspLTRDAGGPLDPVLEKI--AEKYG 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499626852 229 RTPAEWALRWVWNHpEVTVVLSGMNEEsHIEENLKIASeaypNSLTDTEMQLVNRVEQKYRQ 290
Cdd:cd19120 214 VTPAQVLLRWALQK-GIVVVTTSSKEE-RMKEYLEAFD----FELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-262 |
8.09e-22 |
|
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: 94.60 E-value: 8.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 12 KLSILGFGCM----RLpVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTD-GYREKIKLATK-LP 85
Cdd:cd19093 1 EVSPLGLGTWqwgdRL-WWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKElGDRDEVVIATKfAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 86 SWLVENREDMDRFLNTQLERLNTDHIDYYLLHSLAGevWDKLEPlGVIDFLNKAKDDGRITNAGFSFHGPiEDFKRIVDA 165
Cdd:cd19093 80 LPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGP--WYSQIE-ALMDGLADAVEEGLVRAVGVSNYSA-DQLRRAHKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 166 -----YPWTFCQIQYNFMdERNQAGTEGLKYAASKGLGVIVMEPLLGGNLA-------------------------SPVP 215
Cdd:cd19093 156 lkergVPLASNQVEYSLL-YRDPEQNGLLPACDELGITLIAYSPLAQGLLTgkyspenpppggrrrlfgrknlekvQPLL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499626852 216 AEVKDIwdEAETKRTPAEWALRWVWNHPevTVVLSGMNEESHIEENL 262
Cdd:cd19093 235 DALEEI--AEKYGKTPAQVALNWLIAKG--VVPIPGAKNAEQAEENA 277
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-276 |
1.32e-21 |
|
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: 93.81 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 10 GDKLSILGFGCMrlpVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATKLpSWLV 89
Cdd:cd19074 1 GLKVSELSLGTW---LTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKV-FWPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 90 eNREDMDRFL---------NTQLERLNTDHIDYYLLHSlagevWDKLEPLG-VIDFLNKAKDDGRITNAGFSFHGP--IE 157
Cdd:cd19074 77 -GPGPNDRGLsrkhifesiHASLKRLQLDYVDIYYCHR-----YDPETPLEeTVRAMDDLIRQGKILYWGTSEWSAeqIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 158 DFKRIVDAYPWTFC---QIQYNfMDERnQAGTEGLKYAASKGLGVIVMEPLLGGNLA------SPVP----AEVKDIWDE 224
Cdd:cd19074 151 EAHDLARQFGLIPPvveQPQYN-MLWR-EIEEEVIPLCEKNGIGLVVWSPLAQGLLTgkyrdgIPPPsrsrATDEDNRDK 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499626852 225 A--------------------ETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKiaseAYPNSLTDT 276
Cdd:cd19074 229 KrrlltdenlekvkklkpiadELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVK----ASGVKLSPE 296
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-263 |
1.73e-21 |
|
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: 93.88 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 3 YRKIPKNGDKLSILGFGCMRL---PVieDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTdGYREKIK 79
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIgggPW--WGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIK-GRRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLPswLVENREDMDRFLNTQ--------------------LERLNTDHIDYYLLHslagevW-DKLEPLG-VIDFLN 137
Cdd:cd19149 78 LATKCG--LRWDREGGSFFFVRDgvtvyknlspesireeveqsLKRLGTDYIDLYQTH------WqDVETPIEeTMEALE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 138 KAKDDGRITNAGFSFHGPiEDFKRIVDAYPWTFCQIQYNFMDERnqAGTEGLKYAASKGLGVIVMEPLLGGNLASPV--- 214
Cdd:cd19149 150 ELKRQGKIRAIGASNVSV-EQIKEYVKAGQLDIIQEKYSMLDRG--IEKELLPYCKKNNIAFQAYSPLEQGLLTGKItpd 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499626852 215 ------PAEVKDIWDEAETKR------------------TPAEWALRWVWNHPEVTVVLSGMNEESHIEENLK 263
Cdd:cd19149 227 refdagDARSGIPWFSPENREkvlallekwkplcekygcTLAQLVIAWTLAQPGITSALCGARKPEQAEENAK 299
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
29-284 |
1.86e-21 |
|
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: 93.53 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 29 GTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTD-GYREKIKLATKL---------------PSWLVENR 92
Cdd:cd19148 20 GGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEyGKRDRVVIATKVglewdeggevvrnssPARIRKEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 93 EDmdrflntQLERLNTDHIDYYLLHslagevW-DKLEPlgvID----FLNKAKDDGRITNAGFSFHGP--IEDFKRIVda 165
Cdd:cd19148 100 ED-------SLRRLQTDYIDLYQVH------WpDPLVP---IEetaeALKELLDEGKIRAIGVSNFSPeqMETFRKVA-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 166 yPWTFCQIQYNFMdERnQAGTEGLKYAASKGLGVIVMEPLL---------------GGNLASPVP-------------AE 217
Cdd:cd19148 162 -PLHTVQPPYNLF-ER-EIEKDVLPYARKHNIVTLAYGALCrgllsgkmtkdtkfeGDDLRRTDPkfqeprfsqylaaVE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499626852 218 VKDIWDEAETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEEnlkiASEAYPNSLTDTEMQLVNRV 284
Cdd:cd19148 239 ELDKLAQERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDA----VDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
3-279 |
2.03e-21 |
|
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: 93.43 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 3 YRKIPKNGDKLSILGFGCMRLPVIEdGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGyREKIKLAT 82
Cdd:cd19076 2 TRKLGTQGLEVSALGLGCMGMSAFY-GPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDR-RDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 83 KLPswLVENREDMDRFLNTQ-----------LERLNTDHIDYYLLHSLAGEVwdklePLG-VIDFLNKAKDDGRITNAGF 150
Cdd:cd19076 80 KFG--IVRDPGSGFRGVDGRpeyvraaceasLKRLGTDVIDLYYQHRVDPNV-----PIEeTVGAMAELVEEGKVRYIGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 151 SFHGPiEDFKRIVDAYPWTFCQIQYNfMDERNqAGTEGLKYAASKGLGVIVMEPL----LGGNLASPV-----------P 215
Cdd:cd19076 153 SEASA-DTIRRAHAVHPITAVQSEYS-LWTRD-IEDEVLPTCRELGIGFVAYSPLgrgfLTGAIKSPEdlpeddfrrnnP 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499626852 216 AEVKDIWDE-----------AETKR-TPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEaypnSLTDTEMQ 279
Cdd:cd19076 230 RFQGENFDKnlklvekleaiAAEKGcTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDV----VLTPEELA 301
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-286 |
3.75e-21 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 92.92 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 3 YRKIPKNGDKLSILGFGCMRLPVIEdGTIDEERATRQVRYAIDHGVNYIDTAwPYHMGE-SEPFLGRALTDGY--REKIK 79
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSVF-GPVSEEDAIASVREAFRLGINFFDTS-PYYGGTlSEKVLGKALKALGipREKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLPSWlVE----NREDMDRFLNTQLERLNTDHIDYYLLHSLAGEVWDKL--EplgVIDFLNKAKDDGRITNAGFSfh 153
Cdd:PLN02587 79 VSTKCGRY-GEgfdfSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIvnE---TIPALQKLKESGKVRFIGIT-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 154 G-PIEDFKRIVDAYP-------WTFCQIQYNfmderNQAGTEGLKYAASKGLGVIVMEPLLGGNLAS-------PVPAEV 218
Cdd:PLN02587 153 GlPLAIFTYVLDRVPpgtvdviLSYCHYSLN-----DSSLEDLLPYLKSKGVGVISASPLAMGLLTEngppewhPAPPEL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499626852 219 KDIWDEA-----ETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAypnSLTDTEMQLVNRVEQ 286
Cdd:PLN02587 228 KSACAAAathckEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATEL---ETSGIDEELLSEVEA 297
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
7-279 |
1.68e-20 |
|
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: 91.13 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 7 PKNGDKLSILGFGCMRLpviedGT-----IDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRaLTDGYREKIKLA 81
Cdd:cd19080 4 GRSGLRVSPLALGTMTF-----GTewgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGE-FIAGNRDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 82 TKLpSWLVEN---------REDMDRFLNTQLERLNTDHIDYYLLHslageVWDKLEPlgvIDFLNKAKDD----GRITNA 148
Cdd:cd19080 78 TKY-TMNRRPgdpnaggnhRKNLRRSVEASLRRLQTDYIDLLYVH-----AWDFTTP---VEEVMRALDDlvraGKVLYV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 149 GFSfhgpieDF--------KRIVDAYPWT-FC--QIQYNFMD---ERnqagtEGLKYAASKGLGVIVMEPLLGGNLASP- 213
Cdd:cd19080 149 GIS------DTpawvvaraNTLAELRGWSpFValQIEYSLLErtpER-----ELLPMARALGLGVTPWSPLGGGLLTGKy 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 214 ---------------------------VPAEVKDIwdEAETKRTPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIAS 266
Cdd:cd19080 218 qrgeegrageakgvtvgfgklternwaIVDVVAAV--AEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALD 295
|
330
....*....|...
gi 499626852 267 EaypnSLTDTEMQ 279
Cdd:cd19080 296 L----TLSPEQLA 304
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-282 |
2.34e-20 |
|
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: 89.55 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 10 GDKLSILGFGCMRLPVIE--DGTIDEErATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATK-LPS 86
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLtpDYSRDEE-MVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTKvWPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLveNREDMDRFLNTQLERLNTDHIDYYLLHSLAGEVwdklePLG-VIDFLNKAKDDGRITNAGFS-FHgpIEDFKRIVD 164
Cdd:cd19137 80 NL--RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNI-----PLEeTLSAMAEGVRQGLIRYIGVSnFN--RRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 165 --AYPWTFCQIQYNFMDeRNQAGTEGLKYAASKGLGVIVMEPLLGGnlASPVPAEVKDIwdEAETKRTPAEWALRWVWNH 242
Cdd:cd19137 151 ksQTPIVCNQVKYNLED-RDPERDGLLEYCQKNGITVVAYSPLRRG--LEKTNRTLEEI--AKNYGKTIAQIALAWLIQK 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499626852 243 PEVTVVLSGMNEEsHIEENLKiaseAYPNSLTDTEMQLVN 282
Cdd:cd19137 226 PNVVAIPKAGRVE-HLKENLK----ATEIKLSEEEMKLLD 260
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-282 |
1.11e-19 |
|
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: 87.33 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 15 ILGFGCMRLpviedgtiDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALT--DGYREKIKLATKLPSWLVENr 92
Cdd:cd19073 3 ALGLGTWQL--------RGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAesGVPREDLFITTKVWRDHLRP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 93 EDMDRFLNTQLERLNTDHIDYYLLHSLAGEVwDKLEPLGVidfLNKAKDDGRITNAGFS-FHgpIEDFKRIVDAYPWTFC 171
Cdd:cd19073 71 EDLKKSVDRSLEKLGTDYVDLLLIHWPNPTV-PLEETLGA---LKELKEAGKVKSIGVSnFT--IELLEEALDISPLPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 172 QIQYNFMDERNQAgtEGLKYAASKGLGVIVMEPLLGGN-LASPVPAEVKDiwdeaETKRTPAEWALRWVWNHPevTVVLS 250
Cdd:cd19073 145 VNQVEFHPFLYQA--ELLEYCRENDIVITAYSPLARGEvLRDPVIQEIAE-----KYDKTPAQVALRWLVQKG--IVVIP 215
|
250 260 270
....*....|....*....|....*....|..
gi 499626852 251 GMNEESHIEENLKIASEaypnSLTDTEMQLVN 282
Cdd:cd19073 216 KASSEDHLKENLAIFDW----ELTSEDVAKID 243
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
4-262 |
5.19e-19 |
|
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: 87.11 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 4 RKIPKNGDKLSILGFGCMRLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYhmGESEPFLGR--ALTDGYREKIKLA 81
Cdd:cd19144 4 RTLGRNGPSVPALGFGAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRwfKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 82 TKL---------PSWLVENREDMDRFLNTQLERLNTDHIDYYLLHSLAGEVwdklePL-GVIDFLNKAKDDGRITNAGFS 151
Cdd:cd19144 82 TKFgieknvetgEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKT-----PIeKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 152 fHGPIEDFKRIVDAYPWTFCQIQYN--FMD-ERNQAGTegLKYAASKGLGVIVMEPL----LGGNLASPVPAEVKD---- 220
Cdd:cd19144 157 -ECSAETLRRAHAVHPIAAVQIEYSpfSLDiERPEIGV--LDTCRELGVAIVAYSPLgrgfLTGAIRSPDDFEEGDfrrm 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499626852 221 ------------------IWDEAETKR-TPAEWALRWVWNHPEVTVVLSGMNEESHIEENL 262
Cdd:cd19144 234 aprfqaenfpknlelvdkIKAIAKKKNvTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENL 294
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-263 |
8.40e-19 |
|
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: 85.69 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 8 KNGDKLSILGFGCMRLPvieDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRAL--TDGYREKIKLATK-- 83
Cdd:cd19092 1 PEGLEVSRLVLGCMRLA---DWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALalNPGLREKIEIQTKcg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 84 --LPSwlvENREDMDRFLNTQ-----------LERLNTDHIDYYLLHSLagevwDKL-EPLGVIDFLNKAKDDGRITNAG 149
Cdd:cd19092 78 irLGD---DPRPGRIKHYDTSkehilasvegsLKRLGTDYLDLLLLHRP-----DPLmDPEEVAEAFDELVKSGKVRYFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 150 FSFHGP--IEDFKRIVDaYPWTFCQIQYNFMDERN-QAGTegLKYAASKGLGVIVMEPLLGGNLASP-------VPAEVK 219
Cdd:cd19092 150 VSNFTPsqIELLQSYLD-QPLVTNQIELSLLHTEAiDDGT--LDYCQLLDITPMAWSPLGGGRLFGGfderfqrLRAALE 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499626852 220 DIWDEAETkrTPAEWALRWVWNHP-EVTVVLSGMNEEsHIEENLK 263
Cdd:cd19092 227 ELAEEYGV--TIEAIALAWLLRHPaRIQPILGTTNPE-RIRSAVK 268
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-266 |
4.14e-18 |
|
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: 83.92 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 14 SILGFGCMRLpviedGTIDEERATRQV--RYaIDHGVNYIDTA-----W--PYHMGESEPFLGRALTD-GYREKIKLATK 83
Cdd:cd19752 1 SELCLGTMYF-----GTRTDEETSFAIldRY-VAAGGNFLDTAnnyafWteGGVGGESERLIGRWLKDrGNRDDVVIATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 84 L------PSWLVENREDMD-----RFLNTQLERLNTDHIDYYLLHslageVWDKLEPLG-VIDFLNKAKDDGRITNAGFS 151
Cdd:cd19752 75 VgagprdPDGGPESPEGLSaetieQEIDKSLRRLGTDYIDLYYAH-----VDDRDTPLEeTLEAFNELVKAGKVRAIGAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 152 FHGP--IEDFKRIVDAYPW-TFCQIQ-----------YNFMDERNqAGTEGLKYAASKG-LGVIVMEPLLGGNLASPvPA 216
Cdd:cd19752 150 NFAAwrLERARQIARQQGWaEFSAIQqrhsylrprpgADFGVQRI-VTDELLDYASSRPdLTLLAYSPLLSGAYTRP-DR 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499626852 217 EVKDIWDEAETKR--------------TPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIAS 266
Cdd:cd19752 228 PLPEQYDGPDSDArlavleevagelgaTPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
14-284 |
1.96e-17 |
|
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: 82.61 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 14 SILGFGCMRLpviedGT-IDEERATRQVRYAIDHGVNYIDTAWPY-------HMGESEPFLGRAL-TDGYREKIKLATKL 84
Cdd:cd19094 2 SEICLGTMTW-----GEqNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLkKKGNRDKVVLATKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 85 --PS----WLVENREDMDRF-----LNTQLERLNTDHIDYYLLH--------SLAGEVWDKLEPLGVIDF------LNKA 139
Cdd:cd19094 77 agPGegitWPRGGGTRLDREnireaVEGSLKRLGTDYIDLYQLHwpdrytplFGGGYYTEPSEEEDSVSFeeqleaLGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 140 KDDGRITNAG-----------FSFHGPIEDFKRIVdaypwtFCQIQYNFMderNQAGTEGLKYAASK-GLGVIVMEPLLG 207
Cdd:cd19094 157 VKAGKIRHIGlsnetpwgvmkFLELAEQLGLPRIV------SIQNPYSLL---NRNFEEGLAEACHReNVGLLAYSPLAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 208 GNL--------ASPVPAEVKDIW----------DEAETKR----------TPAEWALRWVWNHPEVTVVLSGMNEESHIE 259
Cdd:cd19094 228 GVLtgkyldgaARPEGGRLNLFPgymaryrspqALEAVAEyvklarkhglSPAQLALAWVRSRPFVTSTIIGATTLEQLK 307
|
330 340
....*....|....*....|....*
gi 499626852 260 ENLKiaseAYPNSLTDTEMQLVNRV 284
Cdd:cd19094 308 ENID----AFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-263 |
8.49e-17 |
|
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: 80.38 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 3 YRKIPKNGDKLSILGFGCMRLPvieDGTIDEERATRQVRYAIDHGVNYIDTAWPY--HMGESEPFLGRALTD---GYREK 77
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNF---GDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdlrPYRDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 78 IKLATK-------LP--SWLveNREDMDRFLNTQLERLNTDHIDYYLLHSLagevwDKLEPLGV-IDFLNKAKDDGRITN 147
Cdd:cd19089 78 LVISTKagygmwpGPygDGG--SRKYLLASLDQSLKRMGLDYVDIFYHHRY-----DPDTPLEEtMTALADAVRSGKALY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 148 AGFSFHGPiEDFKRIVD-----AYPWTFCQIQYNFMDERNQAGTegLKYAASKGLGVIVMEPLLGGNLA----------S 212
Cdd:cd19089 151 VGISNYPG-AKARRAIAllrelGVPLIIHQPRYSLLDRWAEDGL--LEVLEEAGIGFIAFSPLAQGLLTdkylngippdS 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499626852 213 PVPAEVKDIWDEAET---------------KR--TPAEWALRWVWNHPEVTVVLSGMNEESHIEENLK 263
Cdd:cd19089 228 RRAAESKFLTEEALTpekleqlrklnkiaaKRgqSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVA 295
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
16-273 |
1.10e-16 |
|
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: 79.71 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 16 LGFGCMRLPVIedGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATKLPSWLVENRE-- 93
Cdd:cd19162 3 LGLGAASLGNL--ARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVGRLLEPGAAgr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 94 --DMDRFLN-----------TQLERLNTDHIDYYLLHSLAGEVWDKLEplGVIDFLNKAKDDGRITNAGFSFhGPIEDFK 160
Cdd:cd19162 81 paGADRRFDfsadgirrsieASLERLGLDRLDLVFLHDPDRHLLQALT--DAFPALEELRAEGVVGAIGVGV-TDWAALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 161 RIVDAYPWTFCQI--QYNFMDERnqAGTEGLKYAASKGLGVIVMEPLLGGNLAS-----------PVPAEVKD----IWD 223
Cdd:cd19162 158 RAARRADVDVVMVagRYTLLDRR--AATELLPLCAAKGVAVVAAGVFNSGILATddpagdrydyrPATPEVLArarrLAA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499626852 224 EAETKRTP-AEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAYPNSL 273
Cdd:cd19162 236 VCRRYGVPlPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAEF 286
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
6-283 |
1.88e-16 |
|
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: 78.45 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 6 IPKNGDKLSILGFGCMRLpviedgtiDEERATRQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDG--YREKIKLATK 83
Cdd:cd19140 1 VTVNGVRIPALGLGTYPL--------TGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASgvPRDELFLTTK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 84 LpsWLVENRedMDRFLNT---QLERLNTDHIDYYLLHSLAGEVwdklePLG-VIDFLNKAKDDGRITNAGFS-FhgPIED 158
Cdd:cd19140 70 V--WPDNYS--PDDFLASveeSLRKLRTDYVDLLLLHWPNKDV-----PLAeTLGALNEAQEAGLARHIGVSnF--TVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 159 FKRIVDAYPW-TFC-QIQYN-FMDERNQagtegLKYAASKGLGVIVMEPLLGGNLAS-PVPAEVKDIWDeaetkRTPAEW 234
Cdd:cd19140 139 LREAVELSEApLFTnQVEYHpYLDQRKL-----LDAAREHGIALTAYSPLARGEVLKdPVLQEIGRKHG-----KTPAQV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499626852 235 ALRWVWNHPEVtVVLSGMNEESHIEENLKIaseaYPNSLTDTEMQLVNR 283
Cdd:cd19140 209 ALRWLLQQEGV-AAIPKATNPERLEENLDI----FDFTLSDEEMARIAA 252
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
9-285 |
3.54e-16 |
|
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: 77.48 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgtiDEERATRQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDG--YREKIKLATKLps 86
Cdd:cd19126 5 NGTRMPWLGLGVFQTP-------DGDETERAVQTALENGYRSIDTAAIYK---NEEGVGEAIRESgvPREELFVTTKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVENRED--MDRFlNTQLERLNTDHIDYYLLHSLAG----EVWDKLEPLgvidflnkaKDDGRITNAGFS-FHGP-IED 158
Cdd:cd19126 73 WNDDQRARrtEDAF-QESLDRLGLDYVDLYLIHWPGKdkfiDTWKALEKL---------YASGKVKAIGVSnFQEHhLEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 159 FKRIVDAYPwTFCQIQYN-FMDERnqagtEGLKYAASKGLGVIVMEPLLGGNLAS-PVPAEVkdiwdeAET-KRTPAEWA 235
Cdd:cd19126 143 LLAHADVVP-AVNQVEFHpYLTQK-----ELRGYCKSKGIVVEAWSPLGQGGLLSnPVLAAI------GEKyGKSAAQVV 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499626852 236 LRWVWNHPEVTVVLSGmnEESHIEENLKIaseaYPNSLTDTEMQLVNRVE 285
Cdd:cd19126 211 LRWDIQHGVVTIPKSV--HASRIKENADI----FDFELSEDDMTAIDALN 254
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
12-279 |
1.90e-15 |
|
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: 76.12 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 12 KLSILGFGCMRLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTdGYREKIKLATKL------- 84
Cdd:cd19078 3 EVSAIGLGCMGMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALK-PFRDQVVIATKFgfkidgg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 85 -PSWLVEN--REDMDRFLNTQLERLNTDHIDYYLLHSLagevwDKLEPL----GVIDFLnkaKDDGRITNAGFSFHGPiE 157
Cdd:cd19078 82 kPGPLGLDsrPEHIRKAVEGSLKRLQTDYIDLYYQHRV-----DPNVPIeevaGTMKEL---IKEGKIRHWGLSEAGV-E 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 158 DFKRIVDAYPWTFCQIQYNFMDERNQagTEGLKYAASKGLGVIVMEPLLGGNLASPVPAEVK------------------ 219
Cdd:cd19078 153 TIRRAHAVCPVTAVQSEYSMMWREPE--KEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKfdegddraslprftpeal 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499626852 220 -------DIWDE-AETKR-TPAEWALRWVWNHPEVTVVLSGMNEESHIEENLkiasEAYPNSLTDTEMQ 279
Cdd:cd19078 231 eanqalvDLLKEfAEEKGaTPAQIALAWLLAKKPWIVPIPGTTKLSRLEENI----GAADIELTPEELR 295
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-290 |
2.07e-15 |
|
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: 76.17 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLpviedgtIDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY------REKIKLAT 82
Cdd:cd19116 7 DGNEIPAIALGTWKL-------KDDEGVRQAVKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKIaegvvkREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 83 KLpsW-LVENREDMDRFLNTQLERLNTDHIDYYLLHSLAG--EVWDKLEPLGV----IDFLN------KAKDDGRITNAG 149
Cdd:cd19116 77 KL--WnSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAfkENNDSESNGDGslsdIDYLEtwrgmeDLVKLGLTRSIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 150 FS-FHgpIEDFKRIvdaypWTFCQI-----QYNFMDERNQAgtEGLKYAASKGLGVIVMEPlLGGNLASPVPAEVKDIWD 223
Cdd:cd19116 155 VSnFN--SEQINRL-----LSNCNIkpavnQIEVHPTLTQE--KLVAYCQSNGIVVMAYSP-FGRLVPRGQTNPPPRLDD 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499626852 224 EAETK------RTPAEWALRWVWNHPEVTVVLSgmNEESHIEENLKIaseaYPNSLTDTEMQLVNRVEQKYRQ 290
Cdd:cd19116 225 PTLVAiakkygKTTAQIVLRYLIDRGVVPIPKS--SNKKRIKENIDI----FDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-145 |
2.48e-15 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 75.67 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 14 SILGFGCMRLpvieDGTIDEERATRQVRYAIDHGVNYIDTAWPY----HMGESEPFLGRALTD-GYREKIKLATK----- 83
Cdd:cd19082 1 SRIVLGTADF----GTRIDEEEAFALLDAFVELGGNFIDTARVYgdwvERGASERVIGEWLKSrGNRDKVVIATKgghpd 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499626852 84 ----LPSWLveNREDMDRFLNTQLERLNTDHIDYYLLHSlagevwDKLE-PLG-VIDFLNKAKDDGRI 145
Cdd:cd19082 77 ledmSRSRL--SPEDIRADLEESLERLGTDYIDLYFLHR------DDPSvPVGeIVDTLNELVRAGKI 136
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-262 |
5.69e-15 |
|
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: 74.78 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 4 RKIPKNGDKLSILGFGCMRLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATK 83
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 84 LPSWLVEN-----REDMDRF---LNTQLERLNTDHIDYYLLHSLagevwDKLEPLGV-IDFLNKAKDDGRITNAGFSFHG 154
Cdd:cd19145 83 FGIHEIGGsgvevRGDPAYVraaCEASLKRLDVDYIDLYYQHRI-----DTTVPIEItMGELKKLVEEGKIKYIGLSEAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 155 PiEDFKRIVDAYPWTFCQIQYNFMDErnQAGTEGLKYAASKGLGVIVMEPLLGGNLAS-PVPAEVKD------------- 220
Cdd:cd19145 158 A-DTIRRAHAVHPITAVQLEWSLWTR--DIEEEIIPTCRELGIGIVPYSPLGRGFFAGkAKLEELLEnsdvrkshprfqg 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499626852 221 ------------IWDEAETKR-TPAEWALRWVWNHPEVTVVLSGMNEESHIEENL 262
Cdd:cd19145 235 enleknkvlyerVEALAKKKGcTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNI 289
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
9-289 |
4.85e-14 |
|
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: 71.65 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgtiDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY--REKIKLATKLps 86
Cdd:cd19157 6 NGVKMPWLGLGVFKVE-------EGSEVVNAVKTALKNGYRSIDTAAIY---GNEEGVGKGIKESGipREELFITSKV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WlvENREDMDRFL---NTQLERLNTDHIDYYLLH----SLAGEVWDKLEPLgvidflnkaKDDGRITNAGFS-FH-GPIE 157
Cdd:cd19157 74 W--NADQGYDSTLkafEASLERLGLDYLDLYLIHwpvkGKYKETWKALEKL---------YKDGRVRAIGVSnFQvHHLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 158 DFKRIVDAYPwTFCQIQYN-FMDErnqagTEGLKYAASKGLGVIVMEPLLGGNLAS-PVpaeVKDIwdeAET-KRTPAEW 234
Cdd:cd19157 143 DLLADAEIVP-MVNQVEFHpRLTQ-----KELRDYCKKQGIQLEAWSPLMQGQLLDnPV---LKEI---AEKyNKSVAQV 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499626852 235 ALRWVWNHPEVTVVLSgMNEEsHIEENlkiaSEAYPNSLTDTEMQLVNRVEQKYR 289
Cdd:cd19157 211 ILRWDLQNGVVTIPKS-IKEH-RIIEN----ADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-272 |
1.21e-13 |
|
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: 71.03 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 4 RKIPKNGDKLSILGFGCMRLPVIEDGTIDEERATRQVRYAIDHGVNYIDTAwPYHMGE-SEPFLGRALTDGY--REKIKL 80
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTS-PYYGAEsSEAVLGKALAALQvpRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 81 ATKLPSWLVE----NREDMDRFLNTQLERLNTDHIDYYLLHSLAGEVWDKLePLGVIDFLNKAKDDGRITNAGFSFHgPI 156
Cdd:cd19153 82 ATKVGRYRDSefdySAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTL-VDEALPALRTLKDEGVIKRIGIAGY-PL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 157 EDFKRIVD-AYPWTFCQIQ----YNFMDERNQAGTEGLKYAasKGLGVIVMEPLLGGNLASPVP-------------AEV 218
Cdd:cd19153 160 DTLTRATRrCSPGSLDAVLsychLTLQDARLESDAPGLVRG--AGPHVINASPLSMGLLTSQGPppwhpasgelrhyAAA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499626852 219 KDIWDEAETKRTPaEWALRW-VWNHPEVTVVLSGMNEESHIEENLKIASEAYPNS 272
Cdd:cd19153 238 ADAVCASVEASLP-DLALQYsLAAHAGVGTVLLGPSSLAQLRSMLAAVDAVASLG 291
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-278 |
3.24e-13 |
|
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: 69.17 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgTIDEERATRQvryAIDHGVNYIDTAWPYHmgeSEPFLGRAL--TDGYREKIKLATKLps 86
Cdd:cd19130 6 DGNSIPQLGYGVFKVP-----PADTQRAVAT---ALEVGYRHIDTAAIYG---NEEGVGAAIaaSGIPRDELFVTTKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVENR-EDMDRFLNTQLERLNTDHIDYYLLH------SLAGEVWDKLEPLgvidflnkaKDDGRITNAGFSFHGPiEDF 159
Cdd:cd19130 73 WNDRHDgDEPAAAFAESLAKLGLDQVDLYLVHwptpaaGNYVHTWEAMIEL---------RAAGRTRSIGVSNFLP-PHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 160 KRIVDAYPWT--FCQIQ-YNFMDERnqagtEGLKYAASKGLGVIVMEPLLGGNL--ASPVPAEVkdiwdeAETKRTPAEW 234
Cdd:cd19130 143 ERIVAATGVVpaVNQIElHPAYQQR-----TIRDWAQAHDVKIEAWSPLGQGKLlgDPPVGAIA------AAHGKTPAQI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499626852 235 ALRWVWNHPEvtVVLSGMNEESHIEENLKIaseaYPNSLTDTEM 278
Cdd:cd19130 212 VLRWHLQKGH--VVFPKSVRRERMEDNLDV----FDFDLTDTEI 249
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-282 |
4.61e-13 |
|
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: 68.89 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLpviedGTIDEEratrQVRYAIDH-GVNYIDTAWPYhmgESEPFLGRALTDG--YREKIKLATKLp 85
Cdd:cd19135 9 NGVEMPILGLGTSHS-----GGYSHE----AVVYALKEcGYRHIDTAKRY---GCEELLGKAIKESgvPREDLFLTTKL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 86 sWLVE--NREDMDRFLNtQLERLNTDHIDYYLLH------------SLAGEVWDKLEPLgvidflnkaKDDGRITNAGFS 151
Cdd:cd19135 76 -WPSDygYESTKQAFEA-SLKRLGVDYLDLYLLHwpdcpssgknvkETRAETWRALEEL---------YDEGLCRAIGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 152 FHGpIEDFKRIVDaypwtFCQI-----QYNFMDERNQAgtEGLKYAASKGlgvIVME---PLLGGN-LASPVPAEVKdiw 222
Cdd:cd19135 145 NFL-IEHLEQLLE-----DCSVvphvnQVEFHPFQNPV--ELIEYCRDNN---IVFEgycPLAKGKaLEEPTVTELA--- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 223 deAETKRTPAEWALRWVWNHPEVTVVLSgmNEESHIEENLKIaseaYPNSLTDTEMQLVN 282
Cdd:cd19135 211 --KKYQKTPAQILIRWSIQNGVVTIPKS--TKEERIKENCQV----FDFSLSEEDMATLD 262
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-279 |
6.24e-13 |
|
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: 69.16 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMrlpVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGY--REKI 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSW---VTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGwpRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 79 KLATKLpSWLVENREDMDRFLNTQ---------LERLNTDHIDYYLLHslagevwdKLEPLGVIDFLNKAKDDgrITNAG 149
Cdd:cd19143 78 VVSTKI-FWGGGGPPPNDRGLSRKhivegtkasLKRLQLDYVDLVFCH--------RPDPATPIEETVRAMND--LIDQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 150 FSFH-GP-------IEDFKRIVDAY---PWTFCQIQYNfMDERNQAGTEGLKYAASKGLGVIVMEPLLGGNL----ASPV 214
Cdd:cd19143 147 KAFYwGTsewsaqqIEEAHEIADRLgliPPVMEQPQYN-LFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLtgkyNNGI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 215 PA-------EVKDIWDEAETKR-------------------TPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKiASEA 268
Cdd:cd19143 226 PEgsrlalpGYEWLKDRKEELGqekiekvrklkpiaeelgcSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLK-ALEV 304
|
330
....*....|.
gi 499626852 269 YPnSLTDTEMQ 279
Cdd:cd19143 305 LP-KLTPEVME 314
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-279 |
6.04e-12 |
|
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: 65.29 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgtiDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDG--YREKIKLATKLps 86
Cdd:cd19133 5 NGVEMPILGFGVFQIP-------DPEECERAVLEAIKAGYRLIDTAAAY---GNEEAVGRAIKKSgiPREELFITTKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVE-NREDMDRFLNTQLERLNTDHIDYYLLHSLAGEV---WDKLEplgvidflnKAKDDGRITNAGFS-FHGpiedfKR 161
Cdd:cd19133 73 WIQDaGYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDVygaWRAME---------ELYKEGKIRAIGVSnFYP-----DR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 162 IVDAYPwtFC-------QIQYNFMDERNQAgtegLKYAASKGlgvIVME---PLLGGN---LASPVPAEVKDIWDeaetk 228
Cdd:cd19133 139 LVDLIL--HNevkpavnQIETHPFNQQIEA----VEFLKKYG---VQIEawgPFAEGRnnlFENPVLTEIAEKYG----- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499626852 229 RTPAEWALRwvWNHPEVTVVLSGMNEESHIEENLKIaseaYPNSLTDTEMQ 279
Cdd:cd19133 205 KSVAQVILR--WLIQRGIVVIPKSVRPERIAENFDI----FDFELSDEDME 249
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-117 |
7.89e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 66.03 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMRLPviEDGTidEERATRQVRYAIDHGVNYIDTAWPYHM-------GESEPFLGRALTD- 72
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFG--EQNS--EADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKr 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499626852 73 GYREKIKLATKL--PSWLVEN---------REDMDRFLNTQLERLNTDHIDYYLLH 117
Cdd:PRK10625 77 GSREKLIIASKVsgPSRNNDKgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVH 132
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
40-151 |
7.98e-12 |
|
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: 65.38 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 40 VRYAIDHGVNYIDTAwPYHmGESEPFLGRAL---TDGY-REKIKLATKL-----------PSWLvenREDMDRflntQLE 104
Cdd:cd19164 40 VRRALELGIRAFDTS-PYY-GPSEIILGRALkalRDEFpRDTYFIITKVgrygpddfdysPEWI---RASVER----SLR 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499626852 105 RLNTDHIDYYLLHSLagEVWDKLEPLGVIDFLNKAKDDGRITNAGFS 151
Cdd:cd19164 111 RLHTDYLDLVYLHDV--EFVADEEVLEALKELFKLKDEGKIRNVGIS 155
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-117 |
1.42e-11 |
|
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: 64.66 E-value: 1.42e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499626852 43 AIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATKLPSWLVENRED-MDRFLNTQLERLNTDHIDYYLLH 117
Cdd:cd19103 41 AMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIISTKFTPQIAGQSADpVADMLEGSLARLGTDYIDIYWIH 116
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-284 |
1.26e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 61.84 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 29 GTIDEERATRQVRYAIDHGVNYIDTAWPYhmGESEPFLGRALTD-----GYREKIKLATKL---PSWLVENREDMDRFLN 100
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRlrrerDAADDVQIHTKWvpdPGELTMTRAYVEAAID 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 101 TQLERLNTDHIDYYLLHSlagevWDKLEP--LGVIDFLNKAKDDGRITNAG---FsfhgPIEDFKRIVDA-YPWTFCQIQ 174
Cdd:cd19101 96 RSLKRLGVDRLDLVQFHW-----WDYSDPgyLDAAKHLAELQEEGKIRHLGltnF----DTERLREILDAgVPIVSNQVQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 175 YNFMDERNQAGTegLKYAASKGLGVIVMEPLLGGNLAS-----PVPaevkdIWDEAET------KRTPAEW--------- 234
Cdd:cd19101 167 YSLLDRRPENGM--AALCEDHGIKLLAYGTLAGGLLSEkylgvPEP-----TGPALETrslqkyKLMIDEWggwdlfqel 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499626852 235 ------------------ALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAypnsLTDTEMQLVNRV 284
Cdd:cd19101 240 lrtlkaiadkhgvsianvAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFR----LDDEDRAAIDAV 303
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-263 |
1.31e-10 |
|
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: 61.80 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 18 FGCMRLPVIEdGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGyrEKIKLATKLPSWL--VENREDM 95
Cdd:cd19075 5 LGTMTFGSQG-RFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGE--RGFKIDTKANPGVggGLSPENV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 96 DRFLNTQLERLNTDHIDYYLLHS------LAgevwdklEPLGVIDFLNKAkddGRITNAGFSFHGP--IEDFKRIVDAYP 167
Cdd:cd19075 82 RKQLETSLKRLKVDKVDVFYLHApdrstpLE-------ETLAAIDELYKE---GKFKEFGLSNYSAweVAEIVEICKENG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 168 W---TFCQIQYNFMDeRnQAGTE--------GLK-YAASkglgvivmePLLGGNLASPVPAEVK---------------- 219
Cdd:cd19075 152 WvlpTVYQGMYNAIT-R-QVETElfpclrklGIRfYAYS---------PLAGGFLTGKYKYSEDkagggrfdpnnalgkl 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499626852 220 --------------DIWDEA--ETKRTPAEWALRWVWNHPEV------TVVLsGMNEESHIEENLK 263
Cdd:cd19075 221 yrdrywkpsyfealEKVEEAaeKEGISLAEAALRWLYHHSALdgekgdGVIL-GASSLEQLEENLA 285
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
31-276 |
2.17e-10 |
|
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: 61.09 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 31 IDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATKL-----------PS--WLVENREDMD- 96
Cdd:cd19152 17 VSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVgrllvplqevePTfePGFWNPLPFDa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 97 ----------RFLNTQLERLNTDHIDYYLLH----SLAGEVWDKLEPLGVID-F--LNKAKDDGRITNAGFSFH--GPIE 157
Cdd:cd19152 97 vfdysydgilRSIEDSLQRLGLSRIDLLSIHdpdeDLAGAESDEHFAQAIKGaFraLEELREEGVIKAIGLGVNdwEVIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 158 DFKRIVDaYPWTFCQIQYNFMDErnQAGTEGLKYAASKGLGVIVMEPLLGGNLAS----------PVPAEVKD----IWD 223
Cdd:cd19152 177 RILEEAD-LDWVMLAGRYTLLDH--SAARELLPECEKRGVKVVNAGPFNSGFLAGgdnfdyyeygPAPPELIArrdrIEA 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499626852 224 EAETKRTP-AEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAYPNSLTDT 276
Cdd:cd19152 254 LCEQHGVSlAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAAFWEE 307
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-263 |
3.30e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 60.82 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 43 AIDHGVNYIDTAWPYhmGESEPFLGRALTdgyREKIKLA----------TKLPSWLV-----ENREDMDRFLNTQLER-- 105
Cdd:cd19098 44 AWAAGVRYFDAARSY--GRAEEFLGSWLR---SRNIAPDavfvgskwgyTYTADWQVdaavhEVKDHSLARLLKQWEEtr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 106 -LNTDHIDYYLLHSLAGE--VwdkLEPLGVIDFLNKAKDDGriTNAGFSFHGPIEDFK-------RIVDAYPWTFCQIQY 175
Cdd:cd19098 119 sLLGKHLDLYQIHSATLEsgV---LEDADVLAALAELKAEG--VKIGLSLSGPQQAETlrraleiEIDGARLFDSVQATW 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 176 NFMDernQAGTEGLKYAASKGLGVIVMEPLLGGNLASPVP-AEVKDIWDE--AETKR---TPAEWALRWVWNHPEVTVVL 249
Cdd:cd19098 194 NLLE---QSAGEALEEAHEAGMGVIVKEALANGRLTDRNPsPELAPLMAVlkAVADRlgvTPDALALAAVLAQPFVDVVL 270
|
250
....*....|....
gi 499626852 250 SGMNEESHIEENLK 263
Cdd:cd19098 271 SGAATPEQLRSNLR 284
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
16-273 |
3.55e-10 |
|
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: 60.80 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 16 LGFGCMRL-----PViedgTIDEERATRQVryAIDHGVNYIDTAWPYHMGESEPFLGRALTDGYREKIKLATK------- 83
Cdd:cd19161 3 LGLGTAGLgnlytAV----SNADADATLDA--AWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKvgrllkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 84 -------LPSWLVE---NREDMD-------RFLNTQLERLNTDHIDYYLLHSL--------AGEVWDKLEPLGVIDFLNK 138
Cdd:cd19161 77 aregsvpDPNGFVDplpFEIVYDysydgimRSFEDSLQRLGLNRIDILYVHDIgvythgdrKERHHFAQLMSGGFKALEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 139 AKDDGRITNAGFSfhgpIEDFKRIVDA---YPWTFCQIQ--YNFMDERnqAGTEGLKYAASKGLGVIVMEPLLGGNLAS- 212
Cdd:cd19161 157 LKKAGVIKAFGLG----VNEVQICLEAldeADLDCFLLAgrYSLLDQS--AEEEFLPRCEQRGTSLVIGGVFNSGILATg 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499626852 213 ----------PVPAEV-------KDIWDEAETKrtPAEWALRWVWNHPEVTVVLSGMNEESHIEENLKIASEAYPNSL 273
Cdd:cd19161 231 tksgakfnygDAPAEIisrvmeiEKICDAYNVP--LAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIPEEL 306
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-289 |
6.36e-10 |
|
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: 59.45 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgtiDEERATRQVRYAIDHGVNYIDTAWPYHMGESepfLGRALTDG--YREKIKLATKLps 86
Cdd:cd19156 5 NGVEMPRLGLGVWRVQ-------DGAEAENAVKWAIEAGYRHIDTAAIYKNEEG---VGQGIRESgvPREEVFVTTKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVEN-REDMDRFLNTQLERLNTDHIDYYLLHSLAG----EVWDKLEPLgvidflnkaKDDGRITNAGFS-FHG-PIEDF 159
Cdd:cd19156 73 WNSDQgYESTLAAFEESLEKLGLDYVDLYLIHWPVKgkfkDTWKAFEKL---------YKEKKVRAIGVSnFHEhHLEEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 160 KRIVDAYPWTFcqiQYNFMDERNQAGTEglKYAASKGLGVIVMEPLLGGNLAS-PVPAEVKDIWDeaetkRTPAEWALRW 238
Cdd:cd19156 144 LKSCKVAPMVN---QIELHPLLTQEPLR--KFCKEKNIAVEAWSPLGQGKLLSnPVLKAIGKKYG-----KSAAQVIIRW 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499626852 239 VWNHPEVTVVLSGmnEESHIEENLKIaseaYPNSLTDTEMQLVNRVEQKYR 289
Cdd:cd19156 214 DIQHGIITIPKSV--HEERIQENFDV----FDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
22-289 |
7.05e-10 |
|
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: 59.73 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 22 RLPVIEDGT--IDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTD------GYREKIKLATKLPSWLVEnRE 93
Cdd:cd19154 11 KMPLIGLGTwqSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAElleegvVKREDLFITTKLWTHEHA-PE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 94 DMDRFLNTQLERLNTDHIDYYLLH----------SLAGEVWDKLEPlGVIDF------LNKAKDDGRITNAGFS-FHgpI 156
Cdd:cd19154 87 DVEEALRESLKKLQLEYVDLYLIHapaafkddegESGTMENGMSIH-DAVDVedvwrgMEKVYDEGLTKAIGVSnFN--N 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 157 EDFKRIVDA------------YPWTFCQIQYNFMDERNQAGTeglKYAAskgLGVI--VMEPLLGGNLASPVPAE---VK 219
Cdd:cd19154 164 DQIQRILDNarvkphnnqvecHLYFPQKELVEFCKKHNISVT---SYAT---LGSPgrANFTKSTGVSPAPNLLQdpiVK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 220 DIwdEAETKRTPAEWALRWVWNHPEVTVVLSGmnEESHIEENLKIaseaYPNSLTDTEMQLVNRVEQKYR 289
Cdd:cd19154 238 AI--AEKHGKTPAQVLLRYLLQRGIAVIPKSA--TPSRIKENFNI----FDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-281 |
1.13e-09 |
|
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: 58.54 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgtiDEErATRQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDG--YREKIKLATKLps 86
Cdd:cd19131 6 DGNTIPQLGLGVWQVS-------NDE-AASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRASgvPREELFITTKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVEN-REDMDRFLNTQLERLNTDHIDYYLLH------SLAGEVWDKLEplgvidflnKAKDDGRITNAGFS-FHgpIED 158
Cdd:cd19131 73 WNSDQgYDSTLRAFDESLRKLGLDYVDLYLIHwpvpaqDKYVETWKALI---------ELKKEGRVKSIGVSnFT--IEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 159 FKRIVDAYPWT--FCQIQ-YNFMDERnqagtEGLKYAASKGLGVIVMEPLL-GGNLASPVPAEVKDiwdeaETKRTPAEW 234
Cdd:cd19131 142 LQRLIDETGVVpvVNQIElHPRFQQR-----ELRAFHAKHGIQTESWSPLGqGGLLSDPVIGEIAE-----KHGKTPAQV 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499626852 235 ALRWvwnHPEV-TVVLSGMNEESHIEENLKIaseaYPNSLTDTEMQLV 281
Cdd:cd19131 212 VIRW---HLQNgLVVIPKSVTPSRIAENFDV----FDFELDADDMQAI 252
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
22-278 |
1.35e-09 |
|
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: 58.66 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 22 RLPVIEDGTIDE--ERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY------REKIKLATKLPSwlVENR- 92
Cdd:cd19111 3 PMPVIGLGTYQSppEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKWWLkngklkREEVFITTKLPP--VYLEf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 93 EDMDRFLNTQLERLNTDHIDYYLLHSLAGEVWDKLEPL------GVIDF---LNKAKDDGRITNAGFSFHGPiEDFKRIV 163
Cdd:cd19111 78 KDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGErelassDVTSVwraMEALVSEGKVKSIGLSNFNP-RQINKIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 164 dAYPWTF---CQIQYNFMDERNqagtEGLKYAASKGLGVIVMEPLLGGNLA-----SPVPAEVKD---IWDEAETKRTPA 232
Cdd:cd19111 157 -AYAKVKpsnLQLECHAYLQQR----ELRKFCNKKNIVVTAYAPLGSPGRAnqslwPDQPDLLEDptvLAIAKELDKTPA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499626852 233 EWALRWVWNHPevTVVLSGMNEESHIEENLkiasEAYPNSLTDTEM 278
Cdd:cd19111 232 QVLLRFVLQRG--TGVLPKSTNKERIEENF----EVFDFELTEEHF 271
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
22-286 |
1.56e-09 |
|
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: 58.05 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 22 RLPVIEDGT--IDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY--REKIKLATKLPSwLVENREDMDR 97
Cdd:cd19132 6 QIPAIGFGTypLKGDEGVEAVVAALQAGYRLLDTAFNY---ENEGAVGEAVRRSGvpREELFVTTKLPG-RHHGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 98 FLNTQLERLNTDHIDYYLLH------SLAGEVWDKLeplgvIDflnkAKDDGRITNAGFSFHGPiEDFKRIVDA---YPw 168
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHwpnpsrDLYVEAWQAL-----IE----AREEGLVRSIGVSNFLP-EHLDRLIDEtgvTP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 169 TFCQIQY--NFmderNQAgtEGLKYAASKGlgvIVME---PLLGGN--LASPVPAEVKDiwdeaETKRTPAEWALRWvwn 241
Cdd:cd19132 151 AVNQIELhpYF----PQA--EQRAYHREHG---IVTQswsPLGRGSglLDEPVIKAIAE-----KHGKTPAQVVLRW--- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499626852 242 HPEVTVV-LSGMNEESHIEENLkiasEAYPNSLTDTEMQLVNRVEQ 286
Cdd:cd19132 214 HVQLGVVpIPKSANPERQRENL----AIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-278 |
1.95e-09 |
|
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: 58.40 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPVIEDGTIDEErATRQVRYAIDHGVNYIDTAWPYhmGESEPF-----LGRALT--DGYREKIKLA 81
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPNPTPDEE-AFETMKAALDAGSNLWNGGEFY--GPPDPHanlklLARFFRkyPEYADKVVLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 82 TK---LPSWLVE--NREDMDRFLNTQLERLN-TDHIDYYllhsLAGEVWDKLEPLGVIDFLNKAKDDGRITNAGFSfHGP 155
Cdd:cd19077 78 VKgglDPDTLRPdgSPEAVRKSIENILRALGgTKKIDIF----EPARVDPNVPIEETIKALKELVKEGKIRGIGLS-EVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 156 IEDFKRIVDAYPWTFCQIQYNFMD-ERNQAGTegLKYAASKGLGVIVMEPL----LGGNLASpvPAEVKDIW-------- 222
Cdd:cd19077 153 AETIRRAHAVHPIAAVEVEYSLFSrEIEENGV--LETCAELGIPIIAYSPLgrglLTGRIKS--LADIPEGDfrrhldrf 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499626852 223 ----------------DEAETKR-TPAEWALRWV--WNHPEVtVVLSGMNEESHIEENLKIASEaypnSLTDTEM 278
Cdd:cd19077 229 ngenfeknlklvdalqELAEKKGcTPAQLALAWIlaQSGPKI-IPIPGSTTLERVEENLKAANV----ELTDEEL 298
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
296-367 |
3.43e-09 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 52.17 E-value: 3.43e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499626852 296 CTGCRYCMP-CPSGVNIPECFEIYNNLHMFGNvegarfkyavrmsgvftntepggfasQCTECGQCMEKCPQN 367
Cdd:pfam13187 2 CTGCGACVAaCPAGAIVPDLVGQTIRGDIAGL--------------------------ACIGCGACVDACPRG 48
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-212 |
5.61e-09 |
|
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: 57.09 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCmrLPVIEDGtIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDG--YREKI 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGT--WSTFSTA-ISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKgwKRSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 79 KLATKL-----PSWLVENREDMDRFLNTQLERLNTDHIDYYLLHSLagevwDKLEPL-GVIDFLNKAKDDGRITNAGFSF 152
Cdd:cd19142 78 IVSTKIywsygSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKA-----DPMCPMeEVVRAMSYLIDNGLIMYWGTSR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499626852 153 HGPIEdfkrIVDAY--------PWTFC-QIQYNfMDERNQAGTEGLKYAASKGLGVIVMEPLLGGNLAS 212
Cdd:cd19142 153 WSPVE----IMEAFsiarqfncPTPICeQSEYH-MFCREKMELYMPELYNKVGVGLITWSPLSLGLDPG 216
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-289 |
7.81e-09 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 56.38 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgtidEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY------REKIKLAT 82
Cdd:cd19155 8 NGEKMPVVGLGTWQSS--------PEEIETAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKWIdsgkvkREELFIVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 83 KLPswLVENR-EDMDRFLNTQLERLNTDHIDYYLLHSLAG-------EVWDKLEPLGVIDF----------LNKAKDDGR 144
Cdd:cd19155 77 KLP--PGGNRrEKVEKFLLKSLEKLQLDYVDLYLIHFPVGslskeddSGKLDPTGEHKQDYttdlldiwkaMEAQVDQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 145 ITNAGFS-FH----GPIEDFKRIVDAYPWTFCQIQYNFMDERNQAGTEGLKYAASKGLGVIVMEPLLGGnlASPVPAEVK 219
Cdd:cd19155 155 TRSIGLSnFNreqmARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPG--TGSPSGSSP 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499626852 220 DIWDEAETKR-------TPAEWALRWVWNHPevTVVLSGMNEESHIEENLKIaseaYPNSLTDTEMQLVNRVEQKYR 289
Cdd:cd19155 233 DLLQDPVVKAiaerhgkSPAQVLLRWLMQRG--VVVIPKSTNAARIKENFQV----FDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
9-283 |
1.02e-08 |
|
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: 55.88 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPVIEdgtideerATRQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDG--YREKIKLATKLps 86
Cdd:cd19127 5 NGVEMPALGLGVFQTPPEE--------TADAVATALADGYRLIDTAAAYG---NEREVGEGIRRSgvDRSDIFVTTKL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVE-NREDMDRFLNTQLERLNTDHIDYYLLHSLAGEVWDKlePLGVIDFLNKAKDDGRITNAGFSFHGPiEDFKRIVDA 165
Cdd:cd19127 72 WISDyGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDR--TIQAYKALEKLLAEGRVRAIGVSNFTP-EHLERLIDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 166 ------------YPWtFCQIQYNFMDERNQAGTEglkyAASKGLGVIVMEPllGGNLASPVPAEVKDIWDEAET-KRTPA 232
Cdd:cd19127 149 ttvvpavnqvelHPY-FSQKDLRAFHRRLGIVTQ----AWSPIGGVMRYGA--SGPTGPGDVLQDPTITGLAEKyGKTPA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499626852 233 EWALRWVWNHpEVTVVLSGMNEEsHIEENLKIaseaYPNSLTDTEMQLVNR 283
Cdd:cd19127 222 QIVLRWHLQN-GVSAIPKSVHPE-RIAENIDI----FDFALSAEDMAAIDA 266
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-298 |
1.14e-08 |
|
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: 55.93 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMrlpviedgtIDEERATRQ-VRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY------REKIKLA 81
Cdd:cd19129 2 GSGAIPALGFGTL---------IPDPSATRNaVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVFkagkirREDLFVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 82 TKLpsWLVENR-EDMDRFLNTQLERLNTDHIDYYLLHS--------------LAGEV-----------WDKLEPLgvidf 135
Cdd:cd19129 70 TKL--WNTNHRpERVKPAFEASLKRLQLDYLDLYLIHTpfafqpgdeqdprdANGNViyddgvtlldtWRAMERL----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 136 lnkaKDDGRITNAGFSFHG-----PIEDFKRI------VDAYPWTfcqIQYNFMDERNQAGTEGLKYAAskgLGViVMEP 204
Cdd:cd19129 143 ----VDEGRCKAIGLSDVSleklrEIFEAARIkpavvqVESHPYL---PEWELLDFCKNHGIVLQAFAP---LGH-GMEP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 205 LLggnLASPVPAEVKdiwdeAETKRTPAEWALRWVWNHPevTVVLSGMNEESHIEENLKIAseaypnSLTDTEMQLVNR- 283
Cdd:cd19129 212 KL---LEDPVITAIA-----RRVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIRENFDIS------TLPEDAMREINEg 275
|
330
....*....|....*..
gi 499626852 284 VEQKYR--QLVKIGCTG 298
Cdd:cd19129 276 IKTRYRfnSVVETGVPG 292
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
15-284 |
1.72e-08 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 54.95 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 15 ILGFGCMRLPviedgtiDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY------REKIKLATKL-PSw 87
Cdd:cd19136 3 ILGLGTFRLR-------GEEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDLLpkyglsREDIFITSKLaPK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 88 lvENREDMDR-FLNTQLERLNTDHIDYYLLH---------------SLAGEVWDKLEplgvidflnKAKDDGRITNAGFS 151
Cdd:cd19136 72 --DQGYEKARaACLGSLERLGTDYLDLYLIHwpgvqglkpsdprnaELRRESWRALE---------DLYKEGKLRAIGVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 152 -F---HgpIEDFKRivdaypwtFCQI-----QYNFMDERNQagTEGLKYAASKGLGVIVMEPLLGGNLASPVPAEVKDIw 222
Cdd:cd19136 141 nYtvrH--LEELLK--------YCEVppavnQVEFHPHLVQ--KELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAI- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499626852 223 dEAETKRTPAEWALRWVWNHpEVTVVLSGMNEEsHIEENLKIASeaypNSLTDTEMQLVNRV 284
Cdd:cd19136 208 -AKKYGRTPAQVLLRWALQQ-GIGVIPKSTNPE-RIAENIKVFD----FELSEEDMAELNAL 262
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-288 |
2.46e-08 |
|
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: 54.81 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRlpviedgTIDEErATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDG--YREKIKLATKLps 86
Cdd:cd19117 10 TGAEIPAVGLGTWQ-------SKPNE-VAKAVEAALKAGYRHIDTAAIY---GNEEEVGQGIKDSgvPREEIFITTKL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 87 WLVENReDMDRFLNTQLERLNTDHIDYYLLH---SL--AGEVWDKLEPLGVIDFLN------------KAKDDGRITNAG 149
Cdd:cd19117 77 WCTWHR-RVEEALDQSLKKLGLDYVDLYLMHwpvPLdpDGNDFLFKKDDGTKDHEPdwdfiktwelmqKLPATGKVKAIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 150 FS-FHGP-IEDF-----KRIVDAYPwtfcQIQYNFMDERNqagtEGLKYAASKGLGVIVMEPLlgGNLASPVPAEvKDIW 222
Cdd:cd19117 156 VSnFSIKnLEKLlaspsAKIVPAVN----QIELHPLLPQP----KLVDFCKSKGIHATAYSPL--GSTNAPLLKE-PVII 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499626852 223 DEAETK-RTPAEWALRWVWNHPevTVVLSGMNEESHIEENLKIAseaypnSLTDTEMQLVNRVEQKY 288
Cdd:cd19117 225 KIAKKHgKTPAQVIISWGLQRG--YSVLPKSVTPSRIESNFKLF------TLSDEEFKEIDELHKEY 283
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
9-289 |
2.50e-08 |
|
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: 54.72 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLpviedgtiDEERATRQVRYAIDHGVNYIDTAWPYhMGESEpfLGRALTDGY------REKIKLAT 82
Cdd:cd19123 8 NGDLIPALGLGTWKS--------KPGEVGQAVKQALEAGYRHIDCAAIY-GNEAE--IGAALAEVFkegkvkREDLWITS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 83 KLpsWLVENR-EDMDRFLNTQLERLNTDHIDYYLLH-SLA----------GEVWDKLEPLGVIDF---LNKAKDDGRITN 147
Cdd:cd19123 77 KL--WNNSHApEDVLPALEKTLADLQLDYLDLYLMHwPVAlkkgvgfpesGEDLLSLSPIPLEDTwraMEELVDKGLCRH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 148 AG---FSFHgPIEDFKRIVDAYPwtfcqiqynfmdERNQ-------AGTEGLKYAASKGLGVIVMEPLLGGNLASPVPAE 217
Cdd:cd19123 155 IGvsnFSVK-KLEDLLATARIKP------------AVNQvelhpylQQPELLAFCRDNGIHLTAYSPLGSGDRPAAMKAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 218 VKD-------IWDEAETKR-TPAEWALRWVWnHPEVTVVLSGMNEEsHIEENLKiASEAypnSLTDTEMQLVNRVEQKYR 289
Cdd:cd19123 222 GEPvlledpvINKIAEKHGaSPAQVLIAWAI-QRGTVVIPKSVNPE-RIQQNLE-AAEV---ELDASDMATIAALDRHHR 295
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
23-282 |
8.59e-08 |
|
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: 52.94 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 23 LPVIEDGT--IDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDG--YREKIKLATKLpsWLVENREDMDR- 97
Cdd:cd19134 11 MPVIGLGVgeLSDDEAERSVSAALEAGYRLIDTAAAY---GNEAAVGRAIAASgiPRGELFVTTKL--ATPDQGFTASQa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 98 FLNTQLERLNTDHIDYYLLHSLAGEVWDKLEPLGVidfLNKAKDDGRITNAGFS-FHGpiEDFKRIVDAYPWTFCQIQYN 176
Cdd:cd19134 86 ACRASLERLGLDYVDLYLIHWPAGREGKYVDSWGG---LMKLREEGLARSIGVSnFTA--EHLENLIDLTFFTPAVNQIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 177 FMDERNQAgtEGLKYAASKGLGVIVMEPLLGGNLASpvPAEVKDIwdEAETKRTPAEWALRwvWNHPEVTVVLSGMNEES 256
Cdd:cd19134 161 LHPLLNQA--ELRKVNAQHGIVTQAYSPLGVGRLLD--NPAVTAI--AAAHGRTPAQVLLR--WSLQLGNVVISRSSNPE 232
|
250 260
....*....|....*....|....*.
gi 499626852 257 HIEENLKIaseaYPNSLTDTEMQLVN 282
Cdd:cd19134 233 RIASNLDV----FDFELTADHMDALD 254
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
296-368 |
1.50e-07 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 47.84 E-value: 1.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499626852 296 CTGCRYCMP-CPSgvnipecFEIYNNlhmfgnvEGARFKYAVRMsGVFTNTEPGGFASQCTECGQCMEKCPQNL 368
Cdd:pfam13534 2 CIQCGCCVDeCPR-------YLLNGD-------EPKKLMRAAYL-GDLEELQANKVANLCSECGLCEYACPMGL 60
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-284 |
1.99e-07 |
|
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: 52.14 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 16 LGFGCMRLPviedgtidEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRAL-----TDGY-REKIKLATKLPSWLV 89
Cdd:cd19128 4 LGFGTYKIT--------ESESKEAVKNAIKAGYRHIDCAYYY---GNEAFIGIAFseifkDGGVkREDLFITSKLWPTMH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 90 ENREDMDRFLNTqLERLNTDHIDYYLLH-SLAgevWDKLEPLGVIDFLNKAK-----------------DDGRITNAGFS 151
Cdd:cd19128 73 QPENVKEQLLIT-LQDLQLEYLDLFLIHwPLA---FDMDTDGDPRDDNQIQSlskkpledtwrameqcvDEKLTKNIGVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 152 FHG-----------PIEDFKRIVDAYPWtfcqiqynFMDERNqagtegLKYAASKGLGVIVMEPLLG----GNLASPVPA 216
Cdd:cd19128 149 NYStklltdllnycKIKPFMNQIECHPY--------FQNDKL------IKFCIENNIHVTAYRPLGGsygdGNLTFLNDS 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499626852 217 EVKDIWDEAETkrTPAEWALRWVWNH-PEVTVVLSGMNEESHIEENLKIASEAypnsLTDTEMQLVNRV 284
Cdd:cd19128 215 ELKALATKYNT--TPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLA----LTKEDMDAINTL 277
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
22-117 |
3.58e-07 |
|
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: 51.34 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 22 RLPVIEDGTI--DEERA-TRQ-VRYAIDHGVNYIDTAWPYhmgESEPFLG----RALTDGY--REKIKLATKLpsWLVEN 91
Cdd:cd19119 11 SIPALGLGTAspHEDRAeVKEaVEAAIKEGYRHIDTAYAY---ETEDFVGeaikRAIDDGSikREELFITTKV--WPTFY 85
|
90 100
....*....|....*....|....*.
gi 499626852 92 REdMDRFLNTQLERLNTDHIDYYLLH 117
Cdd:cd19119 86 DE-VERSLDESLKALGLDYVDLLLVH 110
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-112 |
6.46e-07 |
|
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: 50.52 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 2 LYRKIPKNGDKLSILGFGCMrlpVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTDG--YREKIK 79
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTW---VTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKgwRRSSYV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLpSW--LVENREDMDRF-----LNTQLERLNTDHID 112
Cdd:cd19141 78 ITTKI-FWggKAETERGLSRKhiiegLKASLERLQLEYVD 116
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-279 |
8.05e-07 |
|
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: 50.04 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 16 LGFGCMRLPviEDGTIDeeratrQVRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDG--YREKIKLATKLpsWlVEN-- 91
Cdd:cd19139 4 FGLGTFRLK--DDVVID------SVRTALELGYRHIDTAQIY---DNEAAVGQAIAESgvPRDELFITTKI--W-IDNls 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 92 REDMDRFLNTQLERLNTDHIDYYLLHslagevW----DKLEPLGVIDFLNKAKDDGRITNAGFS-FHGP-IEDFKRIVDA 165
Cdd:cd19139 70 KDKLLPSLEESLEKLRTDYVDLTLIH------WpspnDEVPVEEYIGALAEAKEQGLTRHIGVSnFTIAlLDEAIAVVGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 166 YPWTFCQIQYN-FMDERNQAgteglKYAASKGLGVIVMEPLLGGN-LASPVpaeVKDIwdEAETKRTPAEWALRWVWnHP 243
Cdd:cd19139 144 GAIATNQIELSpYLQNRKLV-----AHCKQHGIHVTSYMTLAYGKvLDDPV---LAAI--AERHGATPAQIALAWAM-AR 212
|
250 260 270
....*....|....*....|....*....|....*.
gi 499626852 244 EVTVVLSGMNEEsHIEENLKiaseAYPNSLTDTEMQ 279
Cdd:cd19139 213 GYAVIPSSTKRE-HLRSNLL----ALDLTLDADDMA 243
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-112 |
1.61e-06 |
|
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: 49.60 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMrlpVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRAL-TDGYREKIK 79
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTW---VTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILkSKGWRRSSY 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLPSW--LVENREDMDRF-----LNTQLERLNTDHID 112
Cdd:cd19160 80 VVTTKIYWggQAETERGLSRKhiiegLRGSLDRLQLEYVD 119
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
40-289 |
4.28e-06 |
|
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: 48.11 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 40 VRYAIDHGVNYIDTAWPYhmgESEPFLGRALT----DGY--REKIKLATKLpsWLVE-NREDMDRFLNTQLERLNTDHID 112
Cdd:cd19125 30 VKTAIKEGYRHIDCAAIY---GNEKEIGKALKklfeDGVvkREDLFITSKL--WCTDhAPEDVPPALEKTLKDLQLDYLD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 113 YYLLHslagevW--------DKLEPLGVIDF--------LNKAKDDGRITNAGFSFHGpIEDFKRIVDA--YPWTFCQIQ 174
Cdd:cd19125 105 LYLIH------WpvrlkkgaHMPEPEEVLPPdipstwkaMEKLVDSGKVRAIGVSNFS-VKKLEDLLAVarVPPAVNQVE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 175 ynfMDERNQAgTEGLKYAASKGLGVIVMEPLLGGN--------LASPVPAEVkdiwdeAET-KRTPAEWALRwvWNHPEV 245
Cdd:cd19125 178 ---CHPGWQQ-DKLHEFCKSKGIHLSAYSPLGSPGttwvkknvLKDPIVTKV------AEKlGKTPAQVALR--WGLQRG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499626852 246 TVVLSGMNEESHIEENLKIaseaYPNSLTDTEMQLVNRVEQKYR 289
Cdd:cd19125 246 TSVLPKSTNEERIKENIDV----FDWSIPEEDFAKFSSIEQQRR 285
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
296-368 |
5.65e-06 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 43.45 E-value: 5.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499626852 296 CTGCRYCMP-CPSGVNipecfeiyNNLHMFGNVEGARFKYAVRMSGVFTNTEPggfASQCTECGQCMEKCPQNL 368
Cdd:pfam13183 2 CIRCGACLAaCPVYLV--------TGGRFPGDPRGGAAALLGRLEALEGLAEG---LWLCTLCGACTEVCPVGI 64
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-112 |
8.57e-06 |
|
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: 47.34 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMrlpVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRAL-TDGYREKIK 79
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkKKGWRRSSL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLPSW--LVENREDMDRF-----LNTQLERLNTDHID 112
Cdd:cd19159 78 VITTKLYWggKAETERGLSRKhiiegLKGSLQRLQLEYVD 117
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-112 |
1.44e-05 |
|
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: 46.62 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 1 MLYRKIPKNGDKLSILGFGCMrlpVIEDGTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRAL-TDGYREKIK 79
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkKKGWRRSSL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499626852 80 LATKLPSW--LVENREDMDRF-----LNTQLERLNTDHID 112
Cdd:cd19158 78 VITTKIFWggKAETERGLSRKhiiegLKASLERLQLEYVD 117
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
40-117 |
3.42e-05 |
|
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: 45.21 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 40 VRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY-----REKIKLATKLpsWLVENREdMDRFLNTQLERLNTDHIDYY 114
Cdd:cd19121 31 VAHALKIGYRHIDGALCY---QNEDEVGEGIKEAIaggvkREDLFVTTKL--WSTYHRR-VELCLDRSLKSLGLDYVDLY 104
|
...
gi 499626852 115 LLH 117
Cdd:cd19121 105 LVH 107
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-165 |
4.62e-05 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 44.86 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 10 GDKLSILGFGCMRlpviedgtIDEERATRQVRYAIDHGVNYIDTAWPYHmGESEPFLG--RALTDGY--REKIKLATKLp 85
Cdd:cd19114 1 GDKMPLVGFGTAK--------IKANETEEVIYNAIKVGYRLIDGALLYG-NEAEVGRGirKAIQEGLvkREDLFIVTKL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 86 sWLVENREDMDRFL-NTQLERLNTDHIDYYLLHSLAGEVWdkLEPLGVIDFLNKAKDDGRITNAGFSFHGPIEDFKRIVD 164
Cdd:cd19114 71 -WNNFHGKDHVREAfDRQLKDYGLDYIDLYLIHFPIPAAY--VDPAENYPFLWKDKELKKFPLEQSPMQECWREMEKLVD 147
|
.
gi 499626852 165 A 165
Cdd:cd19114 148 A 148
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
9-117 |
1.88e-04 |
|
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: 42.99 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLPviedgTIDEERATRQVRYAIDHGVNYIDTAWPYhmgESEPFLGRAL----TDGY--REKIKLAT 82
Cdd:cd19108 7 DGHFIPVLGFGTYAPE-----EVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIrskiADGTvkREDIFYTS 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 499626852 83 KLpsWLVENREDMDRF-LNTQLERLNTDHIDYYLLH 117
Cdd:cd19108 79 KL--WCTFHRPELVRPaLEKSLKKLQLDYVDLYLIH 112
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-129 |
1.94e-04 |
|
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: 42.99 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMrlpvIEDGTIDEERATrqVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDGY-------REKIKLA 81
Cdd:cd19122 5 NGVKIPAVGFGTF----ANEGAKGETYAA--VTKALDVGYRHLDCAWFYL---NEDEVGDAVRDFLkenpsvkREDLFIC 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499626852 82 TKLPSWLVEnREDMDRFLNTQLERLNTDHIDYYLLH-SLAGEVWDKLEP 129
Cdd:cd19122 76 TKVWNHLHE-PEDVKWSIDNSLKNLKLDYIDLFLVHwPIAAEKNDQRSP 123
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
351-391 |
2.02e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 43.60 E-value: 2.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 499626852 351 ASQCTECGQCMEKCPQNLKIPDLLKAVEEDlegpDLEQRVA 391
Cdd:PRK13984 184 AARCVECGICTDTCPAHMDIPQYIKAIYKD----DLEEGLR 220
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
29-151 |
2.44e-04 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 42.80 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 29 GTIDEERATRQVRYAIDHGVNYIDTAWPYHMGESEPFLGRALTD-GYREKIKLATKLP-------------SWLVENRED 94
Cdd:cd19146 30 GECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASrGNRDEMVLATKYTtgyrrggpikiksNYQGNHAKS 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 499626852 95 MDRFLNTQLERLNTDHIDYYLLHslageVWDKLEPL-GVIDFLNKAKDDGRITNAGFS 151
Cdd:cd19146 110 LRLSVEASLKKLQTSYIDILYVH-----WWDYTTSIpELMQSLNHLVAAGKVLYLGVS 162
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
351-383 |
3.96e-04 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 42.78 E-value: 3.96e-04
10 20 30
....*....|....*....|....*....|....
gi 499626852 351 ASQCTECGQCMEKCPQNLKIPDLLKAVEE-DLEG 383
Cdd:cd01916 364 AAKCTDCGWCTRACPNSLRIKEAMEAAKEgDFSG 397
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-117 |
4.36e-04 |
|
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: 42.05 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 9 NGDKLSILGFGCMRLpviedgtiDEERATRQVRYAIDHGVNYIDTAWPY----HMGESepfLGRALTDGY--REKIKLAT 82
Cdd:cd19113 7 SGYKMPSVGFGCWKL--------DNATAADQIYQAIKAGYRLFDGAEDYgnekEVGEG---VNRAIDEGLvkREELFLTS 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 499626852 83 KLpsW-LVENREDMDRFLNTQLERLNTDHIDYYLLH 117
Cdd:cd19113 76 KL--WnNFHDPKNVETALNKTLSDLKLDYVDLFLIH 109
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
22-286 |
7.60e-04 |
|
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: 41.10 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 22 RLPVIEDGTI----DEERATRQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDGY-------REKIKLATKLpsWLVE 90
Cdd:cd19124 4 TMPVIGMGTAsdppSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEALrlglvksRDELFVTSKL--WCSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 91 -NREDMDRFLNTQLERLNTDHIDYYLLH----SLAGEVWDKLEPLGVIDF--------------LNKAKDDGrITNAGFS 151
Cdd:cd19124 79 aHPDLVLPALKKSLRNLQLEYVDLYLIHwpvsLKPGKFSFPIEEEDFLPFdikgvweameecqrLGLTKAIG-VSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 152 FHGPIEDFKRIvdayPWTFCQIQYNFMDERNQAgtegLKYAASKGLGVIVMEPLLGGN--------LASPVpaeVKDIwd 223
Cdd:cd19124 158 KLQELLSFATI----PPAVNQVEMNPAWQQKKL----REFCKANGIHVTAYSPLGAPGtkwgsnavMESDV---LKEI-- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499626852 224 eAETK-RTPAEWALRWVWNHpEVTVVLSGMNEEsHIEENLKIaseaYPNSLTDTEMQLVNRVEQ 286
Cdd:cd19124 225 -AAAKgKTVAQVSLRWVYEQ-GVSLVVKSFNKE-RMKQNLDI----FDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
23-289 |
2.06e-03 |
|
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: 39.78 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 23 LPVIEDGTIDEERAT------RQVRYAIDHGVNYIDTAWPYHmgeSEPFLGRALTDGY------REKIKLATKLpsWLVE 90
Cdd:cd19109 4 IPIIGLGTYSEPKTTpkgacaEAVKVAIDTGYRHIDGAYIYQ---NEHEVGQAIREKIaegkvkREDIFYCGKL--WNTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 91 NREDMDR-FLNTQLERLNTDHIDYYLLH-SLA---GEV-----------WDKLEPLGVIDFLNKAKDDGRITNAGFS--- 151
Cdd:cd19109 79 HPPELVRpTLERTLKVLQLDYVDLYIIEmPMAfkpGDEiyprdengkwlYHKTNLCATWEALEACKDAGLVKSIGVSnfn 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 152 -------FHGPIEDFKRI---VDAYPWtFCQIQYnfmdernqagtegLKYAASKGLGVIVMEPL------LGGNLASPVP 215
Cdd:cd19109 159 rrqleliLNKPGLKHKPVsnqVECHPY-FTQPKL-------------LEFCQQHDIVIVAYSPLgtcrdpIWVNVSSPPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 216 AEvkdiwDE------AETKRTPAEWALRWVWNHpEVTVVLSGMNEEsHIEENLKIaseaYPNSLTDTEMQLVNRVEQKYR 289
Cdd:cd19109 225 LE-----DPllnsigKKYNKTAAQVVLRFNIQR-GVVVIPKSFNPE-RIKENFQI----FDFSLTEEEMKDIEALNKNVR 293
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
296-365 |
2.24e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 36.07 E-value: 2.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499626852 296 CTGCRYCM-PCPSgvnipecfeiynNLHMFGNVEGARFKYAVRmsgvftntepgGFASQCTECGQCMEKCP 365
Cdd:pfam13237 9 CIGCGRCTaACPA------------GLTRVGAIVERLEGEAVR-----------IGVWKCIGCGACVEACP 56
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
22-305 |
2.43e-03 |
|
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: 39.68 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 22 RLPVIEDGTIDEERATRQ--VRYAIDHGVNYIDTAWPYhmgESEPFLGRALTDGY-------REKIKLATKLpsWLVENR 92
Cdd:cd19106 6 KMPLIGLGTWKSKPGQVKaaVKYALDAGYRHIDCAAVY---GNEQEVGEALKEKVgpgkavpREDLFVTSKL--WNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 93 -EDMDRFLNTQLERLNTDHIDYYLLHS-LAGEVWDKL---EPLGVIDF-----------LNKAKDDGRITNAGFS-FH-- 153
Cdd:cd19106 81 pEDVEPALRKTLKDLQLDYLDLYLIHWpYAFERGDNPfpkNPDGTIRYdsthyketwkaMEKLVDKGLVKAIGLSnFNsr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 154 --GPIEDFKRI------VDAYPWtFCQIQY-NFMDERNqagtegLKYAASKGLG------VIVMEPLLggnLASPVPAEV 218
Cdd:cd19106 161 qiDDILSVARIkpavlqVECHPY-LAQNELiAHCKARG------LVVTAYSPLGspdrpwAKPDEPVL---LEEPKVKAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 219 KDIWdeaetKRTPAEWALRWVWNHPEVTVVLSgmNEESHIEENLKIaseaYPNSLTDTEMQLVNRVEqkyrqlvkigcTG 298
Cdd:cd19106 231 AKKY-----NKSPAQILLRWQVQRGVVVIPKS--VTPSRIKQNIQV----FDFTLSPEEMKQLDALN-----------RN 288
|
....*..
gi 499626852 299 CRYCMPC 305
Cdd:cd19106 289 WRYIVPM 295
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
353-375 |
4.06e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 35.22 E-value: 4.06e-03
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
296-367 |
5.12e-03 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 34.81 E-value: 5.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499626852 296 CTGCRYCMP-CPSGVnipecfeiynnLHMFGNVEGARFKYAVRMSgvftntepggfaSQCTECGQCMEKCPQN 367
Cdd:pfam12838 1 CIGCGACVAaCPVGA-----------ITLDEVGEKKGTKTVVIDP------------ERCVGCGACVAVCPTG 50
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
285-381 |
6.08e-03 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 38.93 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499626852 285 EQKYRQLVKiGCTGCRYCM-PCPSGVNIPECFEIYNNlhmfGNVEGarfkyavrmsgvFTNTEpggfaSQCTECGQCMEK 363
Cdd:cd01916 357 DEEFQELAA-KCTDCGWCTrACPNSLRIKEAMEAAKE----GDFSG------------LADLF-----DQCVGCGRCEQE 414
|
90
....*....|....*...
gi 499626852 364 CPQNLKIPDLLKAVEEDL 381
Cdd:cd01916 415 CPKEIPIINMIEKAARER 432
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
351-383 |
6.51e-03 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 36.36 E-value: 6.51e-03
10 20 30
....*....|....*....|....*....|....*.
gi 499626852 351 ASQCTECG--QCMEKCPQNLKIPDLLKAV-EEDLEG 383
Cdd:pfam14691 21 ASRCLQCKdpPCVKGCPVHIDIPEFIKLIaEGNFEG 56
|
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