|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
11-275 |
0e+00 |
|
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: 508.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 11 GPREVELSNGVKIPTLGLGTSHSGGYSQEAVVYALKVCNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDY 90
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASI 170
Cdd:cd19135 81 GYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 171 APQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIE 250
Cdd:cd19135 161 VPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEE 240
|
250 260
....*....|....*....|....*
gi 1009575138 251 RVKENCKIFDFHLQENEMSILNDLH 275
Cdd:cd19135 241 RIKENCQVFDFSLSEEDMATLDSLH 265
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
19-279 |
2.49e-118 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 340.49 E-value: 2.49e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSHSGGYS-QEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTTRK 97
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEaAAAVRTALEA-GYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 98 AFYGSLKRLGVDYLDLYMMHWPlcvssCPNKkqtLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQVNQV 177
Cdd:COG0656 80 AFEESLERLGLDYLDLYLIHWP-----GPGP---YVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 178 EFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCK 257
Cdd:COG0656 152 ELHPYLQQRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLD 231
|
250 260
....*....|....*....|..
gi 1009575138 258 IFDFHLQENEMSILNDLHDGRR 279
Cdd:COG0656 232 AFDFELSDEDMAAIDALDRGER 253
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
23-272 |
5.93e-114 |
|
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: 329.06 E-value: 5.93e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 23 IPTLGLGTSHSGGYS-QEAVVYALKvCNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTTRKAFYG 101
Cdd:cd19071 1 MPLIGLGTYKLKPEEtAEAVLAALE-AGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 102 SLKRLGVDYLDLYMMHWPLCVSSCPNKKqTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQVNQVEFNP 181
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVPGKEGGSKE-ARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 182 FQNPSELKEFCVENKIQVEGYCPLGKG--KLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIF 259
Cdd:cd19071 159 YLQQKELVEFCKEHGIVVQAYSPLGRGrrPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVF 238
|
250
....*....|...
gi 1009575138 260 DFHLQENEMSILN 272
Cdd:cd19071 239 DFELSEEDMAAID 251
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
15-279 |
2.06e-101 |
|
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: 297.77 E-value: 2.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGT--SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGA 92
Cdd:cd19157 2 VTLNNGVKMPWLGLGVfkVEEGSEVVNAVKTALKN-GYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 93 STTRKAFYGSLKRLGVDYLDLYMMHWPlcvsscpnKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAP 172
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWP--------VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 173 QVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERV 252
Cdd:cd19157 153 MVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRI 232
|
250 260
....*....|....*....|....*..
gi 1009575138 253 KENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19157 233 IENADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
14-269 |
3.88e-94 |
|
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: 278.87 E-value: 3.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 14 EVELSNGVKIPTLGLGT-SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGA 92
Cdd:cd19131 1 TITLNDGNTIPQLGLGVwQVSNDEAASAVREALEV-GYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 93 STTRKAFYGSLKRLGVDYLDLYMMHWPLcvsscPNKKQTLEeTWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAP 172
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPV-----PAQDKYVE-TWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 173 QVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERV 252
Cdd:cd19131 154 VVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRI 233
|
250
....*....|....*..
gi 1009575138 253 KENCKIFDFHLQENEMS 269
Cdd:cd19131 234 AENFDVFDFELDADDMQ 250
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
15-279 |
3.66e-92 |
|
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: 274.40 E-value: 3.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGT--SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGA 92
Cdd:cd19156 1 VKLANGVEMPRLGLGVwrVQDGAEAENAVKWAIEA-GYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 93 STTRKAFYGSLKRLGVDYLDLYMMHWPLcvsscpnkKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAP 172
Cdd:cd19156 80 ESTLAAFEESLEKLGLDYVDLYLIHWPV--------KGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 173 QVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERV 252
Cdd:cd19156 152 MVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERI 231
|
250 260
....*....|....*....|....*..
gi 1009575138 253 KENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19156 232 QENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
15-274 |
5.28e-92 |
|
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: 273.54 E-value: 5.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGT--SHSGGYSQEAVVYALKvCNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGA 92
Cdd:cd19126 1 VTLNNGTRMPWLGLGVfqTPDGDETERAVQTALE-NGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 93 STTRKAFYGSLKRLGVDYLDLYMMHWPLcvsscpnkKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAP 172
Cdd:cd19126 80 RRTEDAFQESLDRLGLDYVDLYLIHWPG--------KDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 173 QVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERV 252
Cdd:cd19126 152 AVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRI 231
|
250 260
....*....|....*....|..
gi 1009575138 253 KENCKIFDFHLQENEMSILNDL 274
Cdd:cd19126 232 KENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
23-274 |
2.05e-91 |
|
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: 272.20 E-value: 2.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 23 IPTLGLGTSHSGGYSQ-EAVVY-ALKvCNYRLIDTAKRYGCEE----FLQAAIHLSGVPREDIFLTTKLWCTDYGASTTR 96
Cdd:cd19136 1 MPILGLGTFRLRGEEEvRQAVDaALK-AGYRLIDTASVYRNEAdigkALRDLLPKYGLSREDIFITSKLAPKDQGYEKAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 97 KAFYGSLKRLGVDYLDLYMMHWP---LCVSSCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQ 173
Cdd:cd19136 80 AACLGSLERLGTDYLDLYLIHWPgvqGLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 174 VNQVEFNP--FQNpsELKEFCVENKIQVEGYCPLGKG--KLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQI 249
Cdd:cd19136 160 VNQVEFHPhlVQK--ELLKFCKDHGIHLQAYSSLGSGdlRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNP 237
|
250 260
....*....|....*....|....*
gi 1009575138 250 ERVKENCKIFDFHLQENEMSILNDL 274
Cdd:cd19136 238 ERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
15-268 |
1.85e-89 |
|
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: 267.13 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSGGYS--QEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGA 92
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEecERAVLEAIKA-GYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 93 STTRKAFYGSLKRLGVDYLDLYMMHWPLcvsscpnkkQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAP 172
Cdd:cd19133 80 EKAKKAFERSLKRLGLDYLDLYLIHQPF---------GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 173 QVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGK--LLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIE 250
Cdd:cd19133 151 AVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPE 230
|
250
....*....|....*...
gi 1009575138 251 RVKENCKIFDFHLQENEM 268
Cdd:cd19133 231 RIAENFDIFDFELSDEDM 248
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
15-279 |
7.61e-84 |
|
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: 254.13 E-value: 7.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSGGYSQ--EAVVYALKVcNYRLIDTAKRYGCEEF----LQAAIHLSGVPREDIFLTTKLWCT 88
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLKDDEGvrQAVKHAIEA-GYRHIDTAYLYGNEAEvgeaIREKIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 89 DYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPNKKQTLE---------ETWRELELLYDEGLSRCIGVSNYGIE 159
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 160 DLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKL---------LGEKAVLQVARRCGRTPAQI 230
Cdd:cd19116 162 QINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgqtnppprLDDPTLVAIAKKYGKTTAQI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1009575138 231 LIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQR 290
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
16-279 |
2.39e-83 |
|
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: 252.65 E-value: 2.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 16 ELSNGVKIPTLGLGTSHSG-GYSQEAVVYALKVcNYRLIDTAKRYGCEE----FLQAAIHLSGVPREDIFLTTKLWCTDY 90
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADpGVVGNAVKTAIKE-GYRHIDCAAIYGNEKeigkALKKLFEDGVVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPlcVSScpnKKQT------------LEETWRELELLYDEGLSRCIGVSNYGI 158
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWP--VRL---KKGAhmpepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 159 EDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG-------KGKLLGEKAVLQVARRCGRTPAQIL 231
Cdd:cd19125 158 KKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGspgttwvKKNVLKDPIVTKVAEKLGKTPAQVA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1009575138 232 IRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19125 238 LRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRR 285
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
15-274 |
9.41e-83 |
|
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: 250.40 E-value: 9.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSGGYSQEAVVYALKVCNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGAST 94
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 95 TRKAFYGSLKRLGVDYLDLYMMHWPLcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQV 174
Cdd:cd19127 81 ALRGFDASLRRLGLDYVDLYLLHWPV-----PNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 175 NQVEFNPFQNPSELKEFCVENKIQVEGYCPLG------------KGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIA 242
Cdd:cd19127 156 NQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygasgptgPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSA 235
|
250 260 270
....*....|....*....|....*....|..
gi 1009575138 243 IPKSTQIERVKENCKIFDFHLQENEMSILNDL 274
Cdd:cd19127 236 IPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
15-279 |
3.50e-80 |
|
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: 243.99 E-value: 3.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSH-SGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGAS 93
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGElSDDEAERSVSAALEA-GYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 94 TTRKAFYGSLKRLGVDYLDLYMMHWPLCVSScpnkkqTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQ 173
Cdd:cd19134 82 ASQAACRASLERLGLDYVDLYLIHWPAGREG------KYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 174 VNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVK 253
Cdd:cd19134 156 VNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIA 235
|
250 260
....*....|....*....|....*.
gi 1009575138 254 ENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19134 236 SNLDVFDFELTADHMDALDGLDDGTR 261
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
18-274 |
4.56e-78 |
|
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: 237.93 E-value: 4.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 18 SNGVKIPTLGLGT-SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTTR 96
Cdd:cd19140 3 VNGVRIPALGLGTyPLTGEECTRAVEHALEL-GYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 97 KAFYGSLKRLGVDYLDLYMMHWPlcvsscpNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQVNQ 176
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWP-------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 177 VEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNE-VIAIPKSTQIERVKEN 255
Cdd:cd19140 155 VEYHPYLDQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQEgVAAIPKATNPERLEEN 234
|
250
....*....|....*....
gi 1009575138 256 CKIFDFHLQENEMSILNDL 274
Cdd:cd19140 235 LDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
20-268 |
7.74e-78 |
|
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: 237.90 E-value: 7.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGT------SHSGGYSQ---EAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCtdy 90
Cdd:cd19120 1 GSKIPAIAFGTgtawykSGDDDIQRdlvDSVKLALKA-GFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPLcvsSCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASI 170
Cdd:cd19120 77 GIKDPREALRKSLAKLGVDYVDLYLIHSPF---FAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 171 APQVNQVEFNPFQNP--SELKEFCVENKIQVEGYCPL-----GKGKLLgEKAVLQVARRCGRTPAQILIRWSIQNEVIAI 243
Cdd:cd19120 154 KPAVNQIEFHPYLYPqqPALLEYCREHGIVVSAYSPLspltrDAGGPL-DPVLEKIAEKYGVTPAQVLLRWALQKGIVVV 232
|
250 260
....*....|....*....|....*
gi 1009575138 244 PKSTQIERVKENCKIFDFHLQENEM 268
Cdd:cd19120 233 TTSSKEERMKEYLEAFDFELTEEEV 257
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
23-272 |
2.58e-77 |
|
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: 235.63 E-value: 2.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 23 IPTLGLGTSH-SGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTTRKAFYG 101
Cdd:cd19073 1 IPALGLGTWQlRGDDCANAVKEALEL-GYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 102 SLKRLGVDYLDLYMMHWPlcvsscpNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQVNQVEFNP 181
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWP-------NPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 182 FQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDF 261
Cdd:cd19073 153 FLYQAELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDW 232
|
250
....*....|.
gi 1009575138 262 HLQENEMSILN 272
Cdd:cd19073 233 ELTSEDVAKID 243
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
15-280 |
5.33e-77 |
|
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: 236.92 E-value: 5.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSGGYS-QEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIH---LSGV-PREDIFLTTKLWCTD 89
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSKGAEgITAVRTALKA-GYRLIDTAFLYQNEEAIGEALAellEEGVvKREDLFITTKLWTHE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 90 YGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPNKKQT------------LEETWRELELLYDEGLSRCIGVSNYG 157
Cdd:cd19154 83 HAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTmengmsihdavdVEDVWRGMEKVYDEGLTKAIGVSNFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 158 IEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGK---------------GKLLGEKAVLQVARR 222
Cdd:cd19154 163 NDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspaPNLLQDPIVKAIAEK 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1009575138 223 CGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRRS 280
Cdd:cd19154 243 HGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
13-281 |
1.87e-76 |
|
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: 235.38 E-value: 1.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 13 REVELSNGVKIPTLGLGTSHSG-GYSQEAVVYALKVcNYRLIDTAKRYGCE----EFLQAAIHLSGVPREDIFLTTKLWC 87
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKpGEVGQAVKQALEA-GYRHIDCAAIYGNEaeigAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 TDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCV-----------SSCPNKKQTLEETWRELELLYDEGLSRCIGVSNY 156
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALkkgvgfpesgeDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 157 GIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKG------------KLLGEKAVLQVARRCG 224
Cdd:cd19123 161 SVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdrpaamkaegepVLLEDPVINKIAEKHG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1009575138 225 RTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRRSV 281
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
17-274 |
7.07e-76 |
|
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: 232.55 E-value: 7.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 17 LSNGVKIPTLGLGT-SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTT 95
Cdd:cd19132 1 LNDGTQIPAIGFGTyPLKGDEGVEAVVAALQA-GYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 96 RKAFYGSLKRLGVDYLDLYMMHWplcvsscPNKKQTLE-ETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQV 174
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHW-------PNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 175 NQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKG-KLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVK 253
Cdd:cd19132 153 NQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGsGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQR 232
|
250 260
....*....|....*....|.
gi 1009575138 254 ENCKIFDFHLQENEMSILNDL 274
Cdd:cd19132 233 ENLAIFDFELSDEDMAAIAAL 253
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
17-279 |
1.80e-74 |
|
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: 230.73 E-value: 1.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 17 LSNGVKIPTLGLGTSHSG-GYSQEAVVYALKvCNYRLIDTAKRYGCE----EFLQAAI-HLSGVPREDIFLTTKLWCTDY 90
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKpGQVKAAVKYALD-AGYRHIDCAAVYGNEqevgEALKEKVgPGKAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPNK------------KQTLEETWRELELLYDEGLSRCIGVSNYGI 158
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 159 EDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG----------KGKLLGEKAVLQVARRCGRTPA 228
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGspdrpwakpdEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1009575138 229 QILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWR 290
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
17-276 |
2.45e-74 |
|
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: 229.69 E-value: 2.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 17 LSNGVKIPTLGLGTSHSG-GYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYgaSTT 95
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKpNEVAKAVEAALKA-GYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWH--RRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 96 RKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPNKKQTLEE--------------TWRELELLYDEGLSRCIGVSNYGIEDL 161
Cdd:cd19117 85 EEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDdgtkdhepdwdfikTWELMQKLPATGKVKAIGVSNFSIKNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 162 ESLLDTAS--IAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGK--GKLLGEKAVLQVARRCGRTPAQILIRWSIQ 237
Cdd:cd19117 165 EKLLASPSakIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGStnAPLLKEPVIIKIAKKHGKTPAQVIISWGLQ 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 1009575138 238 NEVIAIPKSTQIERVKENCKIFDfhLQENEMSILNDLHD 276
Cdd:cd19117 245 RGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHK 281
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
20-272 |
2.30e-72 |
|
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: 223.65 E-value: 2.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYS----------QEAVVYALKVcNYRLIDTAKRYG---CEEFLQAAIhlSGVPREDIFLTTKLW 86
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdysddkkaIEALRYAIEL-GINLIDTAEMYGgghAEELVGKAI--KGFDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 CTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSScpnkkqtLEETWRELELLYDEGLSRCIGVSNYGIEDLE---S 163
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIP-------IEETLRAMEELVEEGKIRYIGVSNFSLEELEeaqS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 164 LLDTASIApqVNQVEFNPFqNPSELKE---FCVENKIQVEGYCPLGKGKLLGEKA---VLQVARRCGRTPAQILIRWSIQ 237
Cdd:cd19072 151 YLKKGPIV--ANQVEYNLF-DREEESGllpYCQKNGIAIIAYSPLEKGKLSNAKGsplLDEIAKKYGKTPAQIALNWLIS 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1009575138 238 NE-VIAIPKSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19072 228 KPnVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
19-269 |
5.14e-72 |
|
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: 223.68 E-value: 5.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSHSGGYSQ---EAVVYALKVcNYRLIDTAKRYGCE----EFLQAAIHLSGVP-REDIFLTTKLWCTDY 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPEdikAAVLEAIEV-GYRHFDTAAAYGTEealgEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPlcVSSCPNKKQT-----------LEETWRELELLYDEGLSRCIGVSNYGIE 159
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWP--VSLKPGKFSFpieeedflpfdIKGVWEAMEECQRLGLTKAIGVSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 160 DLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG-KGKLLGEKAVL------QVARRCGRTPAQILI 232
Cdd:cd19124 158 KLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGaPGTKWGSNAVMesdvlkEIAAAKGKTVAQVSL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1009575138 233 RWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMS 269
Cdd:cd19124 238 RWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLE 274
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
15-279 |
6.17e-72 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 223.03 E-value: 6.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGT-SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGAS 93
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVwQASNEEVITAIHKALEV-GYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKRP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 94 ttRKAFYGSLKRLGVDYLDLYMMHWPlcvssCPNKKQTLEeTWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQ 173
Cdd:PRK11565 86 --REALEESLKKLQLDYVDLYLMHWP-----VPAIDHYVE-AWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 174 VNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGkllGE-----KAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQ 248
Cdd:PRK11565 158 INQIELHPLMQQRQLHAWNATHKIQTESWSPLAQG---GKgvfdqKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVT 234
|
250 260 270
....*....|....*....|....*....|.
gi 1009575138 249 IERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:PRK11565 235 PSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
17-274 |
3.44e-69 |
|
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: 215.54 E-value: 3.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 17 LSNGVKIPTLGLGTSH-SGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTT 95
Cdd:cd19130 4 LNDGNSIPQLGYGVFKvPPADTQRAVATALEV-GYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 96 RKAFYGSLKRLGVDYLDLYMMHWPLcvsscPNKKQTLEeTWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIAPQVN 175
Cdd:cd19130 83 AAAFAESLAKLGLDQVDLYLVHWPT-----PAAGNYVH-TWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 176 QVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKEN 255
Cdd:cd19130 157 QIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDN 236
|
250
....*....|....*....
gi 1009575138 256 CKIFDFHLQENEMSILNDL 274
Cdd:cd19130 237 LDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
12-274 |
1.52e-67 |
|
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: 212.01 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 12 PREVELSNGVKIPTLGLGTSHS-GGYSQEAVVYALKVcNYRLIDTAKRYGCE----EFLQAAIHlSGVPREDIFLTTKLW 86
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAkAGEVKAAVAHALKI-GYRHIDGALCYQNEdevgEGIKEAIA-GGVKREDLFVTTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 ctdygASTTRKAFYG---SLKRLGVDYLDLYMMHWPLCVS---------SCPNKKQTLE------ETWRELELLYDEGLS 148
Cdd:cd19121 79 -----STYHRRVELCldrSLKSLGLDYVDLYLVHWPVLLNpngnhdlfpTLPDGSRDLDwdwnhvDTWKQMEKVLKTGKT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 149 RCIGVSNYGIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGK--GKLLGEKAVLQVARRCGRT 226
Cdd:cd19121 154 KAIGVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGStgSPLISDEPVVEIAKKHNVG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1009575138 227 PAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFhlQENEMSILNDL 274
Cdd:cd19121 234 PGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
20-279 |
5.84e-62 |
|
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: 198.11 E-value: 5.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYS-QEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHL---SG-VPREDIFLTTKLWCTDYGAST 94
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEvRAAVDYALFV-GYRHIDTALSYQNEKAIGEALKWwlkNGkLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 95 TRKAFYGSLKRLGVDYLDLYMMHWPLCVSS------CPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTA 168
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVNkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 169 SIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG------------KGKLLGEKAVLQVARRCGRTPAQILIRWSI 236
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGspgranqslwpdQPDLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1009575138 237 QNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
18-273 |
2.87e-60 |
|
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: 193.83 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 18 SNGVKIPTLGLGTS-HSGGYSQEAVVYALKVcNYRLIDTAKRYGCE----EFLQAAIHLSGVPREDIFLTTKLWCTDYGA 92
Cdd:cd19129 1 NGSGAIPALGFGTLiPDPSATRNAVKAALEA-GFRHFDCAERYRNEaevgEAMQEVFKAGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 93 STTRKAFYGSLKRLGVDYLDLYMMHWPLCVSscPNKKQ---------------TLEETWRELELLYDEGLSRCIGVSNYG 157
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFAFQ--PGDEQdprdangnviyddgvTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 158 IEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKG---KLLGEKAVLQVARRCGRTPAQILIRW 234
Cdd:cd19129 158 LEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmepKLLEDPVITAIARRVNKTPAQVLLAW 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1009575138 235 SIQNEVIAIPKSTQIERVKENckiFDFH-LQENEMSILND 273
Cdd:cd19129 238 AIQRGTALLTTSKTPSRIREN---FDIStLPEDAMREINE 274
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
17-274 |
7.07e-60 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 192.63 E-value: 7.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 17 LSNGVKIPTLGLGTSHSG-GYSQEAVVYALKvCNYRLIDTAKRYGCEEFLQAAI-----HLSGVPREDIFLTTKLWCTDY 90
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEpGEVGAAVKIALK-AGYRHLDLAKVYQNQHEVGQALkellkEEPGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCP-----------------NKKQTLEETWRELELLYDEGLSRCIGV 153
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGdlnpltavptnggevdlDLSVSLVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 154 SNYGIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG-----KGKLLGEKAVLQVARRCGRTPA 228
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGnnlagLPLLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1009575138 229 QILIRWSIQNEVIAIPKSTQIERVKENCKifDFHLQENEMSILNDL 274
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
20-271 |
1.54e-59 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 192.25 E-value: 1.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSG-GYSQEAVVYALKVcNYRLIDTAKRYGCE----EFLQAAIHLSGVPREDIFLTTKLWCTDYGAST 94
Cdd:cd19107 1 GAKMPILGLGTWKSPpGQVTEAVKVAIDA-GYRHIDCAYVYQNEnevgEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 95 TRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPN------------KKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLE 162
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKElfpldesgnvipSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 163 SLLDTASI--APQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGK----------GKLLGEKAVLQVARRCGRTPAQI 230
Cdd:cd19107 160 RILNKPGLkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwakpedPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1009575138 231 LIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSIL 271
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
23-268 |
3.26e-59 |
|
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: 189.49 E-value: 3.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 23 IPTLGLGTshsGGYSQEAVVYALKVC---NYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTTRKAF 99
Cdd:cd19139 1 IPAFGLGT---FRLKDDVVIDSVRTAlelGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 100 YGSLKRLGVDYLDLYMMHWPlcvssCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDT---ASIApqVNQ 176
Cdd:cd19139 78 EESLEKLRTDYVDLTLIHWP-----SPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVvgaGAIA--TNQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 177 VEFNPF-QNpSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKEN 255
Cdd:cd19139 151 IELSPYlQN-RKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSN 229
|
250
....*....|...
gi 1009575138 256 CKIFDFHLQENEM 268
Cdd:cd19139 230 LLALDLTLDADDM 242
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
14-280 |
6.27e-59 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 190.77 E-value: 6.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 14 EVELSNGVKIPTLGLGT-SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCE----EFLQAAIHLSGVPREDIFLTTKLWCT 88
Cdd:cd19112 2 TITLNSGHKMPVIGLGVwRMEPGEIKELILNAIKI-GYRHFDCAADYKNEkevgEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 89 DYGasTTRKAFYGSLKRLGVDYLDLYMMHWPLCV---------SSCPNKKQ-------TLEETWRELELLYDEGLSRCIG 152
Cdd:cd19112 81 DHG--HVIEACKDSLKKLQLDYLDLYLVHFPVATkhtgvgttgSALGEDGVldidvtiSLETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 153 VSNYGIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKG----------KLLGEKAVLQVARR 222
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsvSPLDDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1009575138 223 CGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRRS 280
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
20-272 |
2.16e-58 |
|
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: 188.16 E-value: 2.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGG-----YSQ-EAVVYALKVC---NYRLIDTAKRYG---CEEFLQAAIhlSGVPREDIFLTTKLWC 87
Cdd:cd19137 1 GEKIPALGLGTWGIGGfltpdYSRdEEMVELLKTAielGYTHIDTAEMYGgghTEELVGKAI--KDFPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 TDYGASTTRKAFYGSLKRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDT 167
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHW-------PNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 168 ASIAPQVNQVEFNPFQNPSE---LKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNE-VIAI 243
Cdd:cd19137 152 SQTPIVCNQVKYNLEDRDPErdgLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPnVVAI 231
|
250 260
....*....|....*....|....*....
gi 1009575138 244 PKSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19137 232 PKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
22-279 |
1.45e-57 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 187.09 E-value: 1.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 22 KIPTLGLGT-SHSGGYSQEAVVYALKVcNYRLIDTAKRYGCEE----FLQAAIHLSGVPREDIFLTTKLWCTDYGASTTR 96
Cdd:cd19110 3 DIPAVGLGTwKASPGEVTEAVKVAIDA-GYRHFDCAYLYHNESevgaGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 97 KAFYGSLKRLGVDYLDLYMMHWPLCVSScPNKKQTLEE-------------TWRELELLYDEGLSRCIGVSNYGIEDLES 163
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKP-GEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 164 LLDTAS--IAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG---KGKLLGEKAVLQ-VARRCGRTPAQILIRWSIQ 237
Cdd:cd19110 161 LLNKPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGgscEGVDLIDDPVIQrIAKKHGKSPAQILIRFQIQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1009575138 238 NEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19110 241 RNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLR 282
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
26-274 |
4.90e-57 |
|
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: 185.59 E-value: 4.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 26 LGLGTSHSGG--------YSQEAVVYALKvCNYRLIDTAKRYG---CEEFLQAAIHLSGVPREDIFLTTKL------WCT 88
Cdd:pfam00248 1 IGLGTWQLGGgwgpiskeEALEALRAALE-AGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 89 DYGASTTRKAFYGSLKRLGVDYLDLYMMHWPlcvsscpNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTA 168
Cdd:pfam00248 80 GGSKENIRKSLEESLKRLGTDYIDLYYLHWP-------DPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 169 SIAPQVNQVEFNPF--QNPSELKEFCVENKIQVEGYCPLGKGKLLGEK---------------------------AVLQV 219
Cdd:pfam00248 153 KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYtrdpdkgpgerrrllkkgtplnlealeALEEI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1009575138 220 ARRCGRTPAQILIRWSIQNE--VIAIPKSTQIERVKENCKIFDFHLQENEMSILNDL 274
Cdd:pfam00248 233 AKEHGVSPAQVALRWALSKPgvTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
24-274 |
8.11e-57 |
|
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: 184.65 E-value: 8.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 24 PTLGLGTSHSGGY-SQEAVVYALKVcNYRLIDTAKRYGCEEFL----QAAIHLSGVPREDIFLTTKLWCTDYGASTTRKA 98
Cdd:cd19128 2 PRLGFGTYKITESeSKEAVKNAIKA-GYRHIDCAYYYGNEAFIgiafSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 99 FYGSLKRLGVDYLDLYMMHWPLCVSscPNK--------------KQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESL 164
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAFD--MDTdgdprddnqiqslsKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 165 LDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGK----GKL--LGEKAVLQVARRCGRTPAQILIRWSIQ- 237
Cdd:cd19128 159 LNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGsygdGNLtfLNDSELKALATKYNTTPPQVIIAWHLQk 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 1009575138 238 --NEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDL 274
Cdd:cd19128 239 wpKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
15-279 |
1.16e-55 |
|
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: 182.34 E-value: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSGGYSQEAVVYALKVCNYRLIDTAKRYGCE----EFLQAAIHLSGVPREDIFLTTKLWCTDY 90
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEaaigNVLKKWIDSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPLCV------SSCPNKKQTLE--------ETWRELELLYDEGLSRCIGVSNY 156
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSlskeddSGKLDPTGEHKqdyttdllDIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 157 GIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG-----------------KGKLLGEKAVLQV 219
Cdd:cd19155 164 NREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGspgaahfspgtgspsgsSPDLLQDPVVKAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 220 ARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
13-272 |
1.28e-55 |
|
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: 180.91 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 13 REVELSNGVKIPTLGLGTSHSG--GYSQEAVVYALKV---CNYRLIDTAKRYG---CEEFLQAAIhlSGvPREDIFLTTK 84
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGedPAKRAQEIEALRAgidLGMTLIDTAEMYGdggSEELVGEAI--RG-RRDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 LWCTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPlcvSSCPnkkqtLEETWRELELLYDEGLSRCIGVSNYGIEDLESL 164
Cdd:cd19138 78 VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR---GGVP-----LAETVAAMEELKKEGKIRAWGVSNFDTDDMEEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 165 LDTA-SIAPQVNQVEFNPFQNPSE--LKEFCVENKIQVEGYCPLGKGKLLGE-----KAVLQVARRCGRTPAQILIRWSI 236
Cdd:cd19138 150 WAVPgGGNCAANQVLYNLGSRGIEydLLPWCREHGVPVMAYSPLAQGGLLRRgllenPTLKEIAARHGATPAQVALAWVL 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 1009575138 237 -QNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19138 230 rDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
15-275 |
6.74e-55 |
|
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: 180.12 E-value: 6.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSG----GYSQEAVVYALKVcNYRLIDTAKRYGCEE----FLQAAIHLSGVPREDIFLTTKLW 86
Cdd:cd19108 3 VKLNDGHFIPVLGFGTYAPEevpkSKALEATKLAIDA-GFRHIDSAYLYQNEEevgqAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 CTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPlcVSSCP---------NKKQTLE-----ETWRELELLYDEGLSRCIG 152
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFP--VALKPgeelfpkdeNGKLIFDtvdlcATWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 153 VSNYGIEDLESLLDTASI--APQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGK-----------LLGEKAVLQV 219
Cdd:cd19108 160 VSNFNRRQLEMILNKPGLkyKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRdkewvdqnspvLLEDPVLCAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1009575138 220 ARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLH 275
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLN 295
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
17-261 |
1.15e-54 |
|
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: 179.35 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 17 LSNGVKIPTLGLGTSHSGGYSQE---AVVYALKVcNYRLIDTAKRYGCEEFLQAAIH-----LSGVPREDIFLTTKLWCT 88
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGAKGEtyaAVTKALDV-GYRHLDCAWFYLNEDEVGDAVRdflkeNPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 89 DYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCV---SSCPNK---------KQTL----EETWRELELLYDEGLSRCIG 152
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAeknDQRSPKlgpdgkyviLKDLtenpEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 153 VSNYGIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGK-------GKLLGEKAVL-QVARRCG 224
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvpstGERVSENPTLnEVAEKGG 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 1009575138 225 RTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDF 261
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIEL 278
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
15-276 |
8.28e-54 |
|
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: 177.30 E-value: 8.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTS---HSGGYSQEAVVYALKVcNYRLIDTAKRYGCEEF----LQAAIHLSGVPREDIFLTTKLWC 87
Cdd:cd19119 4 FKLNTGASIPALGLGTAsphEDRAEVKEAVEAAIKE-GYRHIDTAYAYETEDFvgeaIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 TDYgaSTTRKAFYGSLKRLGVDYLDLYMMHWPLCV---SSCPNKKQTLE---------------ETWRELELLYDEGLSR 149
Cdd:cd19119 83 TFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFekdSDDSGKPFTPVnddgktryaasgdhiTTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 150 CIGVSNYGIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGK--LLGEKAVLQVARRCGRTP 227
Cdd:cd19119 161 AIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGapNLKNPLVKKIAEKYNVST 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1009575138 228 AQILIRWSIQNEVIAIPKSTQIERVKENCKIfdFHLQENEMSILNDLHD 276
Cdd:cd19119 241 GDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
20-279 |
2.19e-53 |
|
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: 176.59 E-value: 2.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYSQEAVVY-ALKVcNYRLIDTAKRYGCE----EFLQAAIHLSGVPREDIFLTTKLWCTDYGAST 94
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYnAIKV-GYRLIDGALLYGNEaevgRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 95 TRKAFYGSLKRLGVDYLDLYMMHWPLC------------------VSSCPNKKQTLEETWRELELLYDEGLSRCIGVSNY 156
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPIPaayvdpaenypflwkdkeLKKFPLEQSPMQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 157 GIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKG-------------KLLGEKAVLQVARRC 223
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkhftNLLEHPVVKKLADKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1009575138 224 GRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19114 240 KRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
22-282 |
7.51e-53 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 174.06 E-value: 7.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 22 KIPTLGLGTSH-SGGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLSGVPREDIFLTTKLWCTDYGASTTRKAFY 100
Cdd:PRK11172 2 SIPAFGLGTFRlKDQVVIDSVKTALEL-GYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 101 GSLKRLGVDYLDLYMMHWPlcvssCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDT---ASIApqVNQV 177
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWP-----SPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAvgaENIA--TNQI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 178 EFNPF-QNpSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENC 256
Cdd:PRK11172 154 ELSPYlQN-RKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNL 232
|
250 260
....*....|....*....|....*.
gi 1009575138 257 KIFDFHLQENEMSILNDLHDGRRSVD 282
Cdd:PRK11172 233 LAQDLQLDAEDMAAIAALDRNGRLVS 258
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
20-283 |
6.28e-52 |
|
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: 172.68 E-value: 6.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHS-----GGYSQEAVVYALKVcNYRLIDTAKRYGCEEFLQAAIHLS----GVPREDIFLTTKLWCTDY 90
Cdd:cd19109 1 GNSIPIIGLGTYSEpkttpKGACAEAVKVAIDT-GYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVS------------SCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGI 158
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiyprdengKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 159 EDLESLLDTASIA--PQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGK-----------LLGEKAVLQVARRCGR 225
Cdd:cd19109 160 RQLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1009575138 226 TPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRRSVDI 283
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVEL 297
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
15-279 |
1.19e-48 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 164.52 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSGGYSQEAVVY-ALKVcNYRLIDTAKRYG----CEEFLQAAIHLSGVPREDIFLTTKLWCTD 89
Cdd:cd19115 5 VKLNSGYDMPLVGFGLWKVNNDTCADQVYnAIKA-GYRLFDGACDYGneveAGQGVARAIKEGIVKREDLFIVSKLWNTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 90 YGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSC-PN----------------KKQTLEETWRELELLYDEGLSRCIG 152
Cdd:cd19115 84 HDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVdPAvryppgwfydgkkvefSNAPIQETWTAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 153 VSNYGIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGK--------------GKLLGEKAVLQ 218
Cdd:cd19115 164 VSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPqsfleldlpgakdtPPLFEHDVIKS 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1009575138 219 VARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19115 244 IAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
15-279 |
1.66e-47 |
|
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: 161.46 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 15 VELSNGVKIPTLGLGTSHSGGYSQEAVVY-ALKVcNYRLIDTAKRYGCE----EFLQAAIHLSGVPREDIFLTTKLWCTD 89
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYqAIKA-GYRLFDGAEDYGNEkevgEGVNRAIDEGLVKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 90 YGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPNKKQ------------------TLEETWRELELLYDEGLSRCI 151
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVPIEEKyppgfycgdgdnfvyedvPILDTWKALEKLVDAGKIKSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 152 GVSNYGIEDLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLG----------KGK----LLGEKAVL 217
Cdd:cd19113 162 GVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvelnqgRALntptLFEHDTIK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009575138 218 QVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHDGRR 279
Cdd:cd19113 242 SIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
20-272 |
7.42e-46 |
|
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: 156.53 E-value: 7.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGY---------SQEAVVYALKvCNYRLIDTAKRYGC---EEFLQAAIhlsGVPREDIFLTTK--- 84
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTwwgevddqeSIEAIKAAID-LGINFFDTAPVYGFghsEEILGKAL---KGRRDDVVIATKcgl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 LWCTDYG------ASTTRKAFYGSLKRLGVDYLDLYMMHWPlcvssCPNKKqtLEETWRELELLYDEGLSRCIGVSNYGI 158
Cdd:cd19084 77 RWDGGKGvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWP-----DPNTP--IEETAEALEKLKKEGKIRYIGVSNFSV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 159 EDLESLLDTASIApqVNQVEFNPF--QNPSELKEFCVENKIQVEGYCPLGKGKLLGE----------------------- 213
Cdd:cd19084 150 EQLEEARKYGPIV--SLQPPYSMLerEIEEELLPYCRENGIGVLPYGPLAQGLLTGKykkeptfppddrrsrfpffrgen 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009575138 214 --------KAVLQVARRCGRTPAQILIRWSIQNE--VIAIPKSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19084 228 feknleivDKLKEIAEKYGKSLAQLAIAWTLAQPgvTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
20-276 |
4.08e-42 |
|
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: 147.63 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGT-SHSGGY-------SQEAVVYALK--VcnyRLIDTAKRYGC---EEFLQAAihLSGVPREDIFLTTKL- 85
Cdd:COG0667 10 GLKVSRLGLGTmTFGGPWggvdeaeAIAILDAALDagI---NFFDTADVYGPgrsEELLGEA--LKGRPRDDVVIATKVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 -------WCTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPlcvsscpNKKQTLEETWRELELLYDEGLSRCIGVSNYGI 158
Cdd:COG0667 85 rrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP-------DPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 159 EDLESLLDTASIAPQV--NQVEFNPF-QNP-SELKEFCVENKIQVEGYCPLGKGKLLGE--------------------- 213
Cdd:COG0667 158 EQLRRALAIAEGLPPIvaVQNEYSLLdRSAeEELLPAARELGVGVLAYSPLAGGLLTGKyrrgatfpegdraatnfvqgy 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1009575138 214 ---------KAVLQVARRCGRTPAQILIRWSIQNE--VIAIPKSTQIERVKENCKIFDFHLQENEMSILNDLHD 276
Cdd:COG0667 238 lternlalvDALRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALA 311
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
22-272 |
4.34e-42 |
|
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: 146.60 E-value: 4.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 22 KIPTLGLGT--------SHSGGYSQEAVVYALKVC---NYRLIDTAKRYG---CEEFLQAAIHLSGvPREDIFLTTKLWC 87
Cdd:cd19093 1 EVSPLGLGTwqwgdrlwWGYGEYGDEDLQAAFDAAleaGVNLFDTAEVYGtgrSERLLGRFLKELG-DRDEVVIATKFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 T--DYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSSCpnkkqtLEETWRELELLYDEGLSRCIGVSNYGIEDLE--- 162
Cdd:cd19093 80 LpwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQ------IEALMDGLADAVEEGLVRAVGVSNYSADQLRrah 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 163 SLLDTASIAPQVNQVEFN-----PFQNpsELKEFCVENKIQVEGYCPLGKGKLLGE------------------------ 213
Cdd:cd19093 154 KALKERGVPLASNQVEYSllyrdPEQN--GLLPACDELGITLIAYSPLAQGLLTGKyspenpppggrrrlfgrknlekvq 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009575138 214 ---KAVLQVARRCGRTPAQILIRWSIQNEVIAIPKSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19093 232 pllDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
24-255 |
2.91e-39 |
|
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: 137.65 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 24 PTLGLGTSHSGG-YSQEAVVYALKV---CNYRLIDTAKRYG---CEEFLQAAIHLSGVpREDIFLTTKLWCTDYGASTT- 95
Cdd:cd06660 1 SRLGLGTMTFGGdGDEEEAFALLDAaleAGGNFFDTADVYGdgrSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 96 -------RKAFYGSLKRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTA 168
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHR-------DDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 169 S----IAPQVNQVEFNPFQNP---SELKEFCVENKIQVEGYCPLGKGkllgekavlqvarrcgrtPAQILIRWSIQNE-- 239
Cdd:cd06660 153 KahglPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPfv 214
|
250
....*....|....*.
gi 1009575138 240 VIAIPKSTQIERVKEN 255
Cdd:cd06660 215 TVPIVGARSPEQLEEN 230
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
23-273 |
3.16e-38 |
|
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: 136.56 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 23 IPTLGLGTSHSGGY------SQEAVVYALKVC---NYRLIDTAKRYG---CEEFLQAAihLSGVpREDIFLTTKLWCTDY 90
Cdd:cd19085 1 VSRLGLGCWQFGGGywwgdqDDEESIATIHAAldaGINFFDTAEAYGdghSEEVLGKA--LKGR-RDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTTRKAFYGSLKRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASI 170
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHW-------PSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 171 ApqVNQVEFNPFQNPSE--LKEFCVENKIQVEGYCPLGKGKLLG-------------------------EKAVLQV---- 219
Cdd:cd19085 151 D--SNQLPYNLLWRAIEyeILPFCREHGIGVLAYSPLAQGLLTGkfssaedfppgdartrlfrhfepgaEEETFEAlekl 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1009575138 220 ---ARRCGRTPAQILIRWSIQNEVI--AIPKSTQIERVKENCKIFDFHLQENEMSILND 273
Cdd:cd19085 229 keiADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-274 |
7.55e-31 |
|
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: 117.39 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 23 IPTLGLGT-SHSGGY------------SQEAVVYALKVcNYRLIDTAKRYG---CEEFLQAAihLSGVpREDIFLTTK-- 84
Cdd:cd19102 1 LTTIGLGTwAIGGGGwgggwgpqddrdSIAAIRAALDL-GINWIDTAAVYGlghSEEVVGRA--LKGL-RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 -LW------CTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPlcvssCPNkkQTLEETWRELELLYDEGLSRCIGVSNYG 157
Cdd:cd19102 77 lLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP-----DPD--EPIEEAWGALAELKEEGKVRAIGVSNFS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 158 IEDLESLLDTASIApqvnqvefnPFQNP---------SELKEFCVENKIQVEGYCPLGKGKLLGE--------------- 213
Cdd:cd19102 150 VDQMKRCQAIHPIA---------SLQPPysllrrgieAEILPFCAEHGIGVIVYSPMQSGLLTGKmtpervaslpaddwr 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 214 ------------------KAVLQVARRCGRTPAQILIRWSIQNEVI--AIPKSTQIERVKENCKIFDFHLQENEMSILND 273
Cdd:cd19102 221 rrspffqepnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEIEA 300
|
.
gi 1009575138 274 L 274
Cdd:cd19102 301 L 301
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-257 |
4.45e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 108.34 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYSQEAVV----YALKV-CNYrlIDTAKRYG-CEEFLQAAihLSGvPREDIFLTTKLWCTDYGas 93
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAaiirRALDLgINY--FDTAPSYGdSEEKIGKA--LKG-RRDKVFLATKTGARDYE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 94 TTRKAFYGSLKRLGVDYLDLYMMHwplCVSSCPNKKQTLEE--TWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIa 171
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLH---AVDTEEDLDQVFGPggALEALLEAKEEGKIRFIGISGHSPEVLLRALETGEF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 172 pQVNQVEFNPF--QNPSELKEF---CVENKIQVEGYCPLGKGKLLGEKAVlqvarrcgrTPAQiLIRWSIQNEVI--AIP 244
Cdd:cd19100 157 -DVVLFPINPAgdHIDSFREELlplAREKGVGVIAMKVLAGGRLLSGDPL---------DPEQ-ALRYALSLPPVdvVIV 225
|
250
....*....|...
gi 1009575138 245 KSTQIERVKENCK 257
Cdd:cd19100 226 GMDSPEELDENLA 238
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
25-257 |
9.76e-28 |
|
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: 107.56 E-value: 9.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 25 TLGLGTSHSGGYSQEAVVYALKV-----CNYrlIDTAKRYG---CEEFLQAAihLSGvPREDIFLTTKL---------WC 87
Cdd:cd19086 10 TWGLGGDWWGDVDDAEAIRALRAaldlgINF--FDTADVYGdghSERLLGKA--LKG-RRDKVVIATKFgnrfdggpeRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 TDYGASTTRKAFYGSLKRLGVDYLDLYMMHwplcvsSCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDT 167
Cdd:cd19086 85 QDFSPEYIREAVEASLKRLGTDYIDLYQLH------NPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 168 ASIApqVNQVEFNPF-QNPS-ELKEFCVENKIQVEGYCPLGKGkLLGEKavlqvarrcgrtPAQILIRWSIQNEVI--AI 243
Cdd:cd19086 159 GGID--VVQVIYNLLdQRPEeELFPLAEEHGVGVIARVPLASG-LLTGK------------LAQAALRFILSHPAVstVI 223
|
250
....*....|....
gi 1009575138 244 PKSTQIERVKENCK 257
Cdd:cd19086 224 PGARSPEQVEENAA 237
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-263 |
1.14e-27 |
|
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: 108.41 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 18 SNGVKIPTLGLGTSHSG--GYSQEAVVYALKVC---NYRLIDTAKRYG---CEEFLQAAIHLSGVPREDIFLTTK----L 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLAdwGESAEELLSLIEAAlelGITTFDHADIYGggkCEELFGEALALNPGLREKIEIQTKcgirL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 WCTDYGASTTR---------KAFYGSLKRLGVDYLDLYMMHWPlcvsscpnkkQTL---EETWRELELLYDEGLSRCIGV 153
Cdd:cd19092 81 GDDPRPGRIKHydtskehilASVEGSLKRLGTDYLDLLLLHRP----------DPLmdpEEVAEAFDELVKSGKVRYFGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 154 SNYGIEDLESLldtASIAPQ---VNQVEFNPFQNP---SELKEFCVENKIQVEGYCPLGKGKLLGE---------KAVLQ 218
Cdd:cd19092 151 SNFTPSQIELL---QSYLDQplvTNQIELSLLHTEaidDGTLDYCQLLDITPMAWSPLGGGRLFGGfderfqrlrAALEE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1009575138 219 VARRCGRTPAQILIRWSIQNEVIAIP--KSTQIERVKENCKIFDFHL 263
Cdd:cd19092 228 LAEEYGVTIEAIALAWLLRHPARIQPilGTTNPERIRSAVKALDIEL 274
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
20-266 |
1.34e-27 |
|
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: 108.45 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGT--SHSGGYSQEAVVYALKVCnY----RLIDTAKRYG---CEEFLQAAihLSGVPREDIFLTTKL----- 85
Cdd:cd19074 1 GLKVSELSLGTwlTFGGQVDDEDAKACVRKA-YdlgiNFFDTADVYAagqAEEVLGKA--LKGWPRESYVISTKVfwptg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 -WCTDYGASttRK----AFYGSLKRLGVDYLDLYMMHWPlcVSSCPnkkqtLEETWRELELLYDEGLSRCIGVSNYGIED 160
Cdd:cd19074 78 pGPNDRGLS--RKhifeSIHASLKRLQLDYVDIYYCHRY--DPETP-----LEETVRAMDDLIRQGKILYWGTSEWSAEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 161 LESLLDTAS----IAPQVNQVEFNPFQNPS--ELKEFCVENKIQVEGYCPLGKGKLLGE--------------------- 213
Cdd:cd19074 149 IAEAHDLARqfglIPPVVEQPQYNMLWREIeeEVIPLCEKNGIGLVVWSPLAQGLLTGKyrdgipppsrsratdednrdk 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1009575138 214 -------------KAVLQVARRCGRTPAQILIRWSIQNEVI--AIPKSTQIERVKENCKIFDFHLQEN 266
Cdd:cd19074 229 krrlltdenlekvKKLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
19-276 |
1.54e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 106.83 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSHSGGYSQEAVV----YALK--VcNYrlIDTAKRYG-CEEFLQAAihLSGvPREDIFLTTKL--WCTD 89
Cdd:COG1453 9 TGLEVSVLGFGGMRLPRKDEEEAEalirRAIDngI-NY--IDTARGYGdSEEFLGKA--LKG-PRDKVILATKLppWVRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 90 ygASTTRKAFYGSLKRLGVDYLDLYMMHwplcvssCPNKKQTLEETWRELELL------YDEGLSRCIGVSNYG-IEDLE 162
Cdd:COG1453 83 --PEDMRKDLEESLKRLQTDYIDLYLIH-------GLNTEEDLEKVLKPGGALealekaKAEGKIRHIGFSTHGsLEVIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 163 SLLDTasiapqvNQVEF-----NPF--QNPSELK--EFCVENKIQV---EgycPLGKGKLLGEKAVLQVARRCGRTPAQI 230
Cdd:COG1453 154 EAIDT-------GDFDFvqlqyNYLdqDNQAGEEalEAAAEKGIGViimK---PLKGGRLANPPEKLVELLCPPLSPAEW 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1009575138 231 LIRWSIQNEVIAIPKS--TQIERVKENCKIFD-FH-LQENEMSILNDLHD 276
Cdd:COG1453 224 ALRFLLSHPEVTTVLSgmSTPEQLDENLKTADnLEpLTEEELAILERLAE 273
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
51-263 |
1.17e-25 |
|
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: 102.30 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 51 RLIDTAKRYG---CEEFLQAAIHlsgvPR-EDIFLTTKL---------WCTDYGASTTRKAFYGSLKRLGVDYLDLYMMH 117
Cdd:cd19088 39 NFIDTADSYGpdvNERLIAEALH----PYpDDVVIATKGglvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 118 WPlcvsscpNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTASIApqVNQVEFNPF-QNPSELKEFCVENK 196
Cdd:cd19088 115 RI-------DPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIV--SVQNRYNLAnRDDEGVLDYCEAAG 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 197 IQVEGYCPLGKGKLLGEKAVLQ-VARRCGRTPAQILIRWSIQ--NEVIAIPKSTQIERVKENCKIFDFHL 263
Cdd:cd19088 186 IAFIPWFPLGGGDLAQPGGLLAeVAARLGATPAQVALAWLLArsPVMLPIPGTSSVEHLEENLAAAGLRL 255
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-255 |
6.86e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 100.35 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYSQEAVVYALK--VcNYrlIDTAKRYG---CEEFLQAAihLSGVPREDIFLTTKLWCTDYG--A 92
Cdd:cd19105 10 GLKVSRLGFGGGGLPRESPELLRRALDlgI-NY--FDTAEGYGngnSEEIIGEA--LKGLRRDKVFLATKASPRLDKkdK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 93 STTRKAFYGSLKRLGVDYLDLYMMHwplcvsSCPNKKQTL--EETWRELELLYDEGLSRCIGVS--NYGIEDLESLLDTA 168
Cdd:cd19105 85 AELLKSVEESLKRLQTDYIDIYQLH------GVDTPEERLlnEELLEALEKLKKEGKVRFIGFSthDNMAEVLQAAIESG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 169 SIapQVNQVEFNPFQNPSELKEF---CVENKIQVEGYCPLGKGKLlgEKAVLQVARRCGRTPAQILIRWSIQNEVI--AI 243
Cdd:cd19105 159 WF--DVIMVAYNFLNQPAELEEAlaaAAEKGIGVVAMKTLAGGYL--QPALLSVLKAKGFSLPQAALKWVLSNPRVdtVV 234
|
250
....*....|..
gi 1009575138 244 PKSTQIERVKEN 255
Cdd:cd19105 235 PGMRNFAELEEN 246
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
24-257 |
9.80e-25 |
|
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: 100.00 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 24 PTLGLGTSHSGG----YSQEAV------VYALKVcnyRLIDTAKRYG-CEEFLqaAIHLSGVPREDIFLTTKLWCT---- 88
Cdd:cd19095 1 SVLGLGTSGIGRvwgvPSEAEAarllntALDLGI---NLIDTAPAYGrSEERL--GRALAGLRRDDLFIATKVGTHgegg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 89 ----DYGASTTRKAFYGSLKRLGVDYLDLYMMHwplcvsSCPNKKQTlEETWRELELLYDEGLSRCIGVSNYGiEDLESL 164
Cdd:cd19095 76 rdrkDFSPAAIRASIERSLRRLGTDYIDLLQLH------GPSDDELT-GEVLETLEDLKAAGKVRYIGVSGDG-EELEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 165 LDTASIapQVNQVEFNPF-QNPSELKEFCVENKIQVEGYCPLGKGKLL----GEKAVLQVARRC-------GRTPAQILI 232
Cdd:cd19095 148 IASGVF--DVVQLPYNVLdREEEELLPLAAEAGLGVIVNRPLANGRLRrrvrRRPLYADYARRPefaaeigGATWAQAAL 225
|
250 260
....*....|....*....|....*..
gi 1009575138 233 RWSIQNEVI--AIPKSTQIERVKENCK 257
Cdd:cd19095 226 RFVLSHPGVssAIVGTTNPEHLEENLA 252
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
18-268 |
3.65e-23 |
|
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: 96.52 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 18 SNGVKIPTLGLG-TSHSGGY-------SQEAVVYALKvCNYRLIDTAKRYGC---EEFLQAAIHlsgVPREDIFLTTK-- 84
Cdd:cd19076 7 TQGLEVSALGLGcMGMSAFYgpadeeeSIATLHRALE-LGVTFLDTADMYGPgtnEELLGKALK---DRRDEVVIATKfg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 -LWCTDYGASTT-------RKAFYGSLKRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNY 156
Cdd:cd19076 83 iVRDPGSGFRGVdgrpeyvRAACEASLKRLGTDVIDLYYQHR-------VDPNVPIEETVGAMAELVEEGKVRYIGLSEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 157 GIEDLESlldTASIAP-QVNQVEFNPF-QNP-SELKEFCVENKIQVEGYCPLGKGKLLGE-------------------- 213
Cdd:cd19076 156 SADTIRR---AHAVHPiTAVQSEYSLWtRDIeDEVLPTCRELGIGFVAYSPLGRGFLTGAikspedlpeddfrrnnprfq 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1009575138 214 -----------KAVLQVARRCGRTPAQILIRWSIQ--NEVIAIPKSTQIERVKENCKIFDFHLQENEM 268
Cdd:cd19076 233 genfdknlklvEKLEAIAAEKGCTPAQLALAWVLAqgDDIVPIPGTKRIKYLEENVGALDVVLTPEEL 300
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
20-274 |
3.69e-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: 96.72 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYS---------QEAVVYALKVCNYRLIDTAKRYG---CEEFLQAAIhlSGVPREDIFLTTKlWC 87
Cdd:cd19083 8 DIDVNPIGLGTNAVGGHNlypnldeeeGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVL--KEYNRNEVVIATK-GA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 TDYGASTT---------RKAFYGSLKRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYGI 158
Cdd:cd19083 85 HKFGGDGSvlnnspeflRSAVEKSLKRLNTDYIDLYYIHF-------PDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 159 EDLESlldtASIAPQVN--QVEFNPFQ--NPSELKEFCVENKIQVEGYCPLGKGKLLG---------------EKAVLQ- 218
Cdd:cd19083 158 EQLKE----ANKDGYVDvlQGEYNLLQreAEEDILPYCVENNISFIPYFPLASGLLAGkytkdtkfpdndlrnDKPLFKg 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009575138 219 ---------------VARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKENCKIFDFHLQENEMSILNDL 274
Cdd:cd19083 234 erfsenldkvdklksIADEKGVTVAHLALAWYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
27-212 |
9.36e-23 |
|
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: 95.45 E-value: 9.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 27 GLGTSHSGGY---------SQEAVVYALKvCNYRLIDTAKRYG---CEEFLQAAIHLSGvPREDIFLTTKL---W----- 86
Cdd:cd19148 8 ALGTWAIGGWmwggtdekeAIETIHKALD-LGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVgleWdegge 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 -CTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPlcvsscpNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLL 165
Cdd:cd19148 86 vVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWP-------DPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1009575138 166 DTASIApqVNQVEFNPFQNPSE--LKEFCVENKIQVEGYCPLGKGKLLG 212
Cdd:cd19148 159 KVAPLH--TVQPPYNLFEREIEkdVLPYARKHNIVTLAYGALCRGLLSG 205
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
20-244 |
3.93e-22 |
|
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: 93.79 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYSQEAVVYAL-KVC-----NyrLIDTAKRYG---CEEFLQAAIHLSgvpREDIFLTTKL----- 85
Cdd:cd19087 10 GLKVSRLCLGTMNFGGRTDEETSFAImDRAldagiN--FFDTADVYGggrSEEIIGRWIAGR---RDDIVLATKVfgpmg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 -WCTDYGAST--TRKAFYGSLKRLGVDYLDLYMMHwplcvssCPNKKQTLEETWRELELLYDEGLSRCIGVSNY------ 156
Cdd:cd19087 85 dDPNDRGLSRrhIRRAVEASLRRLQTDYIDLYQMH-------HFDRDTPLEETLRALDDLVRQGKIRYIGVSNFaawqia 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 157 ---GIEDLESLLDTASIAPQVN----QVEfnpfqnpSELKEFCVENKIQVEGYCPLGKGkLLGEK--------------- 214
Cdd:cd19087 158 kaqGIAARRGLLRFVSEQPMYNllkrQAE-------LEILPAARAYGLGVIPYSPLAGG-LLTGKygkgkrpesgrlver 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1009575138 215 -----------------AVLQVARRCGRTPAQILIRWSIQNEVIAIP 244
Cdd:cd19087 230 aryqarygleeyrdiaeRFEALAAEAGLTPASLALAWVLSHPAVTSP 276
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
19-267 |
4.29e-22 |
|
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: 94.05 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGT----SHSGGYSQEAVVYAL--KVCNYR--LIDTAKRYG-CEEFLQAAIHLSGVPREDIFLTTKL---- 85
Cdd:cd19144 9 NGPSVPALGFGAmglsAFYGPPKPDEERFAVldAAFELGctFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFgiek 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 ------WCTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWplcVSScpnkKQTLEETWRELELLYDEGLSRCIGVSNYGIe 159
Cdd:cd19144 89 nvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHR---VDG----KTPIEKTVAAMAELVQEGKIKHIGLSECSA- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 160 dlESLLDTASIAP-QVNQVEFNPF-----QNPSELKEFCVENKIQVEGYCPLGKGKLLGE-------------------- 213
Cdd:cd19144 161 --ETLRRAHAVHPiAAVQIEYSPFsldieRPEIGVLDTCRELGVAIVAYSPLGRGFLTGAirspddfeegdfrrmaprfq 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1009575138 214 ----KAVLQ-------VARRCGRTPAQILIRWSI--QNEVIAIPKSTQIERVKENCKIFDFHLQENE 267
Cdd:cd19144 239 aenfPKNLElvdkikaIAKKKNVTAGQLTLAWLLaqGDDIIPIPGTTKLKRLEENLGALKVKLTEEE 305
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
20-267 |
4.20e-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: 91.18 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGYS-------QEAV--VYALKVCNYRLIDTAKRYG---CEEFLQAAIhlSGVpREDIFLTTK--- 84
Cdd:cd19149 8 GIEASVIGLGTWAIGGGPwwggsddNESIrtIHAALDLGINLIDTAPAYGfghSEEIVGKAI--KGR-RDKVVLATKcgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 LWCTDYG----------------ASTTRKAFYGSLKRLGVDYLDLYMMHWPlcVSSCPnkkqtLEETWRELELLYDEGLS 148
Cdd:cd19149 85 RWDREGGsfffvrdgvtvyknlsPESIREEVEQSLKRLGTDYIDLYQTHWQ--DVETP-----IEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 149 RCIGVSNYGIEDLESLLDTASIApqVNQVEF---NPFQNpSELKEFCVENKIQVEGYCPLGKGKLLG-----EKAVLQVA 220
Cdd:cd19149 158 RAIGASNVSVEQIKEYVKAGQLD--IIQEKYsmlDRGIE-KELLPYCKKNNIAFQAYSPLEQGLLTGkitpdREFDAGDA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009575138 221 RR-----------------------CGR---TPAQILIRWSIQ--NEVIAIPKSTQIERVKENCKIFDFHLQENE 267
Cdd:cd19149 235 RSgipwfspenrekvlallekwkplCEKygcTLAQLVIAWTLAqpGITSALCGARKPEQAEENAKAGDIRLSAED 309
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
26-260 |
6.14e-21 |
|
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: 89.54 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 26 LGLGT-----SHSGGYSQEAVV----YALKV-CNYrlIDTAKRYG---CEEFLQAAihLSGVPREDIFLTTKL-WCTDYG 91
Cdd:cd19096 3 LGFGTmrlpeSDDDSIDEEKAIemirYAIDAgINY--FDTAYGYGggkSEEILGEA--LKEGPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 92 ASTTRKAFYGSLKRLGVDYLDLYMMHWpLCVSSCPNKKQTLeETWRELELLYDEGLSRCIGVSNYG-IEDLESLLDTASI 170
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHG-LNSPEWLEKARKG-GLLEFLEKAKKEGLIRHIGFSFHDsPELLKEILDSYDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 171 ApqVNQVEFNPF----QNPSELKEFCVENKIQVEGYCPLGKGKLL-GEKAVLQVARRCGRTPAQILIRWSIQNEVIAIPK 245
Cdd:cd19096 157 D--FVQLQYNYLdqenQAGRPGIEYAAKKGMGVIIMEPLKGGGLAnNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVL 234
|
250
....*....|....*..
gi 1009575138 246 S--TQIERVKENCKIFD 260
Cdd:cd19096 235 SgmSTPEQLDENIAAAD 251
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
51-272 |
1.92e-20 |
|
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: 89.18 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 51 RLIDTAKRYGC---EEFLQAAIHlSGVPREDIFLTTKLwctdYGAS--------TTRKAFY----GSLKRLGVDYLDLYM 115
Cdd:cd19079 50 NFFDTANVYSGgasEEILGRALK-EFAPRDEVVIATKV----YFPMgdgpngrgLSRKHIMaevdASLKRLGTDYIDLYQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 116 MHW-----PlcvsscpnkkqtLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTAsiapqvNQVEFNPF---QNP-- 185
Cdd:cd19079 125 IHRwdyetP------------IEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLA------EKNGWTKFvsmQNHyn 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 186 ----SELKE---FCVENKIQVEGYCPLGKGKLLGE------------------------------KAVLQVARRCGRTPA 228
Cdd:cd19079 187 llyrEEEREmipLCEEEGIGVIPWSPLARGRLARPwgdtterrrsttdtaklkydyfteadkeivDRVEEVAKERGVSMA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1009575138 229 QILIRWSIQNEVIAIP--KSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19079 267 QVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
19-272 |
4.27e-20 |
|
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: 88.43 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSHSGGYSQEAVVYALKVC----NYRLIDTAKRYGC----------EEFLQAAIHLSGvPREDIFLTTK 84
Cdd:cd19081 5 TGLSVSPLCLGTMVFGWTADEETSFALLDAfvdaGGNFIDTADVYSAwvpgnaggesETIIGRWLKSRG-KRDRVVIATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 L----WCTDYGAS--TTRKAFYGSLKRLGVDYLDLYMMHWPlcvsscpnKKQT-LEETWRELELLYDEGLSRCIGVSNYG 157
Cdd:cd19081 84 VgfpmGPNGPGLSrkHIRRAVEASLRRLQTDYIDLYQAHWD--------DPATpLEETLGALNDLIRQGKVRYIGASNYS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 158 IEDLESLLDTA---------SIAPQVNQVEFNPFQnpSELKEFCVENKIQVEGYCPLGKGKLLGE--------------- 213
Cdd:cd19081 156 AWRLQEALELSrqhglpryvSLQPEYNLVDRESFE--GELLPLCREEGIGVIPYSPLAGGFLTGKyrseadlpgstrrge 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009575138 214 --------------KAVLQVARRCGRTPAQILIRWSIQNEVIAIP--KSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19081 234 aakrylnerglrilDALDEVAAEHGATPAQVALAWLLARPGVTAPiaGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
20-255 |
3.29e-19 |
|
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: 85.68 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGY--------SQEAVVYALKV-CNYrlIDTAKRYGC---EEFLQAAihLSGVPREDIFLTTK--- 84
Cdd:cd19163 10 GLKVSKLGFGASPLGGVfgpvdeeeAIRTVHEALDSgINY--IDTAPWYGQgrsETVLGKA--LKGIPRDSYYLATKvgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 ---LWCT--DYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIE 159
Cdd:cd19163 86 yglDPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFA---PSLDQILNETLPALQKLKEEGKVRFIGITGYPLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 160 DLESLLDTASIAPQVNQVEFNPFQNPSELKE---FCVENKIQVEGYCPLGKGkLLGEK----------AVLQVARRC--- 223
Cdd:cd19163 163 VLKEVLERSPVKIDTVLSYCHYTLNDTSLLEllpFFKEKGVGVINASPLSMG-LLTERgppdwhpaspEIKEACAKAaay 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1009575138 224 ----GRTPAQILIRWSIQNEVIA--IPKSTQIERVKEN 255
Cdd:cd19163 242 cksrGVDISKLALQFALSNPDIAttLVGTASPENLRKN 279
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
20-274 |
1.83e-18 |
|
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: 83.82 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGT----------SHSGGYSQEAVVYALKVC-----NyrLIDTAKRYG---CEEFLQAAIhlsGVPREDIFL 81
Cdd:cd19091 10 GLKVSELALGTmtfgggggffGAWGGVDQEEADRLVDIAldagiN--FFDTADVYSegeSEEILGKAL---KGRRDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 82 TTKLW------CTDYGASTTR--KAFYGSLKRLGVDYLDLYMMHWPlcvsscpnKKQT-LEETWRELELLYDEGLSRCIG 152
Cdd:cd19091 85 ATKVRgrmgegPNDVGLSRHHiiRAVEASLKRLGTDYIDLYQLHGF--------DALTpLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 153 VSNY---------GIEDLESLldTASIAPQVN------QVEFnpfqnpsELKEFCVENKIQVEGYCPLGKGKLLG----- 212
Cdd:cd19091 157 VSNFsawqimkalGISERRGL--ARFVALQAYysllgrDLEH-------ELMPLALDQGVGLLVWSPLAGGLLSGkyrrg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 213 ---------------------EK------AVLQVARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKENCKIFDFHL 263
Cdd:cd19091 228 qpapegsrlrrtgfdfppvdrERgydvvdALREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAGLSL 307
|
330
....*....|.
gi 1009575138 264 QENEMSILNDL 274
Cdd:cd19091 308 TPEEIARLDKV 318
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-257 |
3.52e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 83.14 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 25 TLGLGTsHSGGYS-------QEAVVYALKV-CNyrLIDTAKRYGC---E----EFLQAAIHLSGVPREDIFLTTK----- 84
Cdd:cd19099 5 SLGLGT-YRGDSDdetdeeyREALKAALDSgIN--VIDTAINYRGgrsErligKALRELIEKGGIKRDEVVIVTKagyip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 ----------LWCTDYGASTT------------------RKAFYGSLKRLGVDYLDLYMMHWP---LCVSSCPNKKQTLE 133
Cdd:cd19099 82 gdgdeplrplKYLEEKLGRGLidvadsaglrhcispaylEDQIERSLKRLGLDTIDLYLLHNPeeqLLELGEEEFYDRLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 134 ETWRELELLYDEGLSRCIGVS----------NYGIEDLESLLDTASIAPQVN------QVEFNP-----FQNPSELK--- 189
Cdd:cd19099 162 EAFEALEEAVAEGKIRYYGIStwdgfrappaLPGHLSLEKLVAAAEEVGGDNhhfkviQLPLNLlepeaLTEKNTVKgea 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009575138 190 ----EFCVENKIQVEGYCPLGKGKLLGEKA-VLQVARRCGRTPAQILIRWSI-QNEVI-AIPKSTQIERVKENCK 257
Cdd:cd19099 242 lsllEAAKELGLGVIASRPLNQGQLLGELRlADLLALPGGATLAQRALQFARsTPGVDsALVGMRRPEHVDENLA 316
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
19-268 |
1.51e-17 |
|
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: 81.13 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSH-SGGYSQ-------EAVVYALKvCNYRLIDTAKRYGCEEFLqAAIHL-----SGVP--REDIFLTT 83
Cdd:cd19077 1 NGKLVGPIGLGLMGlTWRPNPtpdeeafETMKAALD-AGSNLWNGGEFYGPPDPH-ANLKLlarffRKYPeyADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 84 KlWCTDYGASTT-------RKAFYGSLKRLG-VDYLDLYmmhwplcvsSCP--NKKQTLEETWRELELLYDEGLSRCIGV 153
Cdd:cd19077 79 K-GGLDPDTLRPdgspeavRKSIENILRALGgTKKIDIF---------EPArvDPNVPIEETIKALKELVKEGKIRGIGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 154 SNYGIEDLESLLDTASIApqVNQVEFNPF-----QNpsELKEFCVENKIQVEGYCPLGKGKLLGE--------------- 213
Cdd:cd19077 149 SEVSAETIRRAHAVHPIA--AVEVEYSLFsreieEN--GVLETCAELGIPIIAYSPLGRGLLTGRiksladipegdfrrh 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1009575138 214 ----------------KAVLQVARRCGRTPAQILIRWSI---QNEVIAIPKSTQIERVKENCKIFDFHLQENEM 268
Cdd:cd19077 225 ldrfngenfeknlklvDALQELAEKKGCTPAQLALAWILaqsGPKIIPIPGSTTLERVEENLKAANVELTDEEL 298
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
26-255 |
2.50e-17 |
|
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: 80.29 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 26 LGLGTSHSGGYSQEAVVYALkvcnY--------RLIDTAKRYG-------CEEFLQAAIHLSGVpREDIFLTTKLWCTDY 90
Cdd:cd19082 3 IVLGTADFGTRIDEEEAFAL----LdafvelggNFIDTARVYGdwvergaSERVIGEWLKSRGN-RDKVVIATKGGHPDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 91 GASTT--------RKAFYGSLKRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLE 162
Cdd:cd19082 78 EDMSRsrlspediRADLEESLERLGTDYIDLYFLHR-------DDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 163 SLLDTASI----APQVNQVEFN---PFQNP----------SELKEFCVENKIQVEGYCPLGKG---KLLGEKA------- 215
Cdd:cd19082 151 EANAYAKAhglpGFAASSPQWSlarPNEPPwpgptlvamdEEMRAWHEENQLPVFAYSSQARGffsKRAAGGAeddselr 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1009575138 216 --------------VLQVARRCGRTPAQILIRWSIQNE--VIAIPKSTQIERVKEN 255
Cdd:cd19082 231 rvyyseenferlerAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQLRDS 286
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
25-265 |
7.44e-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: 79.53 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 25 TLGLGTSHSGGYSQEAVV-----YALKVcNYRLIDTAKRY---------G-CEEFLQAAIHLSGvPREDIFLTTKL---- 85
Cdd:cd19094 3 EICLGTMTWGEQNTEAEAheqldYAFDE-GVNFIDTAEMYpvppspetqGrTEEIIGSWLKKKG-NRDKVVLATKVagpg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 ----WCTDYGASTTRK----AFYGSLKRLGVDYLDLYMMHWP--------LCVSSCPNKKQT---LEETWRELELLYDEG 146
Cdd:cd19094 81 egitWPRGGGTRLDREnireAVEGSLKRLGTDYIDLYQLHWPdrytplfgGGYYTEPSEEEDsvsFEEQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 147 LSRCIGVSN---YGIEDLESLLDTASIAPQVN-QVEFNPF-QNPSE-LKEFCVENKIQVEGYCPLGKGKLLG-------- 212
Cdd:cd19094 161 KIRHIGLSNetpWGVMKFLELAEQLGLPRIVSiQNPYSLLnRNFEEgLAEACHRENVGLLAYSPLAGGVLTGkyldgaar 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009575138 213 ---------------------EKAVLQ---VARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKENCKIFDFHLQE 265
Cdd:cd19094 241 peggrlnlfpgymaryrspqaLEAVAEyvkLARKHGLSPAQLALAWVRSRPFVTstIIGATTLEQLKENIDAFDVPLSD 319
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
24-257 |
9.52e-17 |
|
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: 78.36 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 24 PTLGLGTSHSGG--------YSQEAVVYALKVcNYRLIDTAKRYG-CEEFLQAAihLSGVPREDIFLTTKLWC-----TD 89
Cdd:cd19090 1 SALGLGTAGLGGvfggvdddEAVATIRAALDL-GINYIDTAPAYGdSEERLGLA--LAELPREPLVLSTKVGRlpedtAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 90 YGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVssCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTAS 169
Cdd:cd19090 78 YSADRVRRSVEESLERLGRDRIDLLMIHDPERV--PWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 170 IAPQVNQVEFNP--FQNPSELKEFCVENKIQVEGYCPLGKGKLLGE--------------------KAVLQVARRCGRTP 227
Cdd:cd19090 156 FDVVLTANRYTLldQSAADELLPAAARHGVGVINASPLGMGLLAGRppervrytyrwlspelldraKRLYELCDEHGVPL 235
|
250 260 270
....*....|....*....|....*....|..
gi 1009575138 228 AQILIRWSIQNEVIA--IPKSTQIERVKENCK 257
Cdd:cd19090 236 PALALRFLLRDPRIStvLVGASSPEELEQNVA 267
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-276 |
1.46e-16 |
|
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: 78.14 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 52 LIDTAKRYG---CEEFLQAAihLSGVPREDIFLTTKL--WCTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVsscp 126
Cdd:cd19103 48 LWDTAAVYGmgaSEKILGEF--LKRYPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPADV---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 127 nkkqtleETW-RELELLYDEGLSRCIGVSNYGIEDL---ESLLDTASIAPQVNQVEFNPFQNPSE---LKEFCVENKIQV 199
Cdd:cd19103 122 -------ERWtPELIPLLKSGKVKHVGVSNHNLAEIkraNEILAKAGVSLSAVQNHYSLLYRSSEeagILDYCKENGITF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 200 EGYCPLGKGKLLGE------------------------KAVLQVARRCGR----TPAQILIRWSIQNEVIAIPKSTQIER 251
Cdd:cd19103 195 FAYMVLEQGALSGKydtkhplpegsgraetynpllpqlEELTAVMAEIGAkhgaSIAQVAIAWAIAKGTTPIIGVTKPHH 274
|
250 260
....*....|....*....|....*
gi 1009575138 252 VKENCKIFDFHLQENEMSILNDLHD 276
Cdd:cd19103 275 VEDAARAASITLTDDEIKELEQLAD 299
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
18-269 |
2.46e-16 |
|
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: 77.86 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 18 SNGVKIPTLGLG-TSHSGGYS-----QE--AVVYALKVCNYRLIDTAKRYGC---EEFLQAAihLSGVPREDIFLTTKLW 86
Cdd:cd19145 7 SQGLEVSAQGLGcMGLSGDYGapkpeEEgiALIHHAFNSGVTFLDTSDIYGPntnEVLLGKA--LKDGPREKVQLATKFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 CTDYGAST---------TRKAFYGSLKRLGVDYLDLYMMHwpLCVSSCPnkkqtLEETWRELELLYDEGLSRCIGVSnyg 157
Cdd:cd19145 85 IHEIGGSGvevrgdpayVRAACEASLKRLDVDYIDLYYQH--RIDTTVP-----IEITMGELKKLVEEGKIKYIGLS--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 158 iedlESLLDTASIAPQVN-----QVEFNPFQNPSE--LKEFCVENKIQVEGYCPLGKG---------------------- 208
Cdd:cd19145 155 ----EASADTIRRAHAVHpitavQLEWSLWTRDIEeeIIPTCRELGIGIVPYSPLGRGffagkakleellensdvrkshp 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009575138 209 ----------KLLGEKaVLQVARRCGRTPAQILIRWSIQ--NEVIAIPKSTQIERVKENCKIFDFHLQENEMS 269
Cdd:cd19145 231 rfqgenleknKVLYER-VEALAKKKGCTPAQLALAWVLHqgEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLK 302
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
25-225 |
4.17e-15 |
|
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: 74.13 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 25 TLGLGTSHSGGYSQEAVVYALKVCNYRLIDTAKRYG---CEEFLQAAihlsGVPREDIFLTTK---LWCTDYGASTTRKA 98
Cdd:cd19075 9 TFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPdgtSEELLGEL----GLGERGFKIDTKanpGVGGGLSPENVRKQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 99 FYGSLKRLGVDYLDLYMMHwplcvssCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTAS----IAPQV 174
Cdd:cd19075 85 LETSLKRLKVDKVDVFYLH-------APDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1009575138 175 NQVEFNPF--QNPSELKEFCVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGR 225
Cdd:cd19075 158 YQGMYNAItrQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGR 210
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-182 |
4.27e-15 |
|
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: 73.72 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 26 LGLGT----------SHSGGYSQEAVV----YALKvCNYRLIDTAKRYG-CEEFLQAAIHlsgvPREDIFLTTKL----W 86
Cdd:cd19097 3 LALGTaqfgldygiaNKSGKPSEKEAKkileYALK-AGINTLDTAPAYGdSEKVLGKFLK----RLDKFKIITKLpplkE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 CTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVsscpnkKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLD 166
Cdd:cd19097 78 DKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDL------LKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE 151
|
170
....*....|....*.
gi 1009575138 167 taSIAPQVNQVEFNPF 182
Cdd:cd19097 152 --SFKIDIIQLPFNIL 165
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
50-273 |
3.73e-14 |
|
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: 71.50 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 50 YRLIDTAKRYG---CEEFLQAAIHlsgVPREDIFLTTKLWCTDYGAS-----------TTRKAFYGSLKRLGVDYLDLYM 115
Cdd:cd19078 39 ITFFDTAEVYGpytNEELVGEALK---PFRDQVVIATKFGFKIDGGKpgplgldsrpeHIRKAVEGSLKRLQTDYIDLYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 116 MHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSnygiedlESLLDTASIAPQVN-----QVEFNPF-QNP-SEL 188
Cdd:cd19078 116 QHR-------VDPNVPIEEVAGTMKELIKEGKIRHWGLS-------EAGVETIRRAHAVCpvtavQSEYSMMwREPeKEV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 189 KEFCVENKIQVEGYCPLGKGKLLG---------------------EKAVLQ----------VARRCGRTPAQILIRWSIQ 237
Cdd:cd19078 182 LPTLEELGIGFVPFSPLGKGFLTGkidentkfdegddraslprftPEALEAnqalvdllkeFAEEKGATPAQIALAWLLA 261
|
250 260 270
....*....|....*....|....*....|....*...
gi 1009575138 238 NE--VIAIPKSTQIERVKENCKIFDFHLQENEMSILND 273
Cdd:cd19078 262 KKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-272 |
5.93e-14 |
|
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: 70.70 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 32 HSGGYSQEAVVYALK---VCNYRLIDTAKRYGCEE-----FLQAAIHLSGVPREDIFLTtKlWCTDYGA-----STTRKA 98
Cdd:cd19101 16 HGGIRDEDAAVRAMAayvDAGLTTFDCADIYGPAEeligeFRKRLRRERDAADDVQIHT-K-WVPDPGEltmtrAYVEAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 99 FYGSLKRLGVDYLDLYMMHWplcvsSCPNKKQTLeETWRELELLYDEGLSRCIGVSNYGIEDLESLLDtASIAPQVNQVE 178
Cdd:cd19101 94 IDRSLKRLGVDRLDLVQFHW-----WDYSDPGYL-DAAKHLAELQEEGKIRHLGLTNFDTERLREILD-AGVPIVSNQVQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 179 FNPF-QNP-SELKEFCVENKIQVEGYCPLGKGkLLGEK-------------------------------------AVLQ- 218
Cdd:cd19101 167 YSLLdRRPeNGMAALCEDHGIKLLAYGTLAGG-LLSEKylgvpeptgpaletrslqkyklmidewggwdlfqellRTLKa 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1009575138 219 VARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19101 246 IADKHGVSIANVAVRWVLDQPGVAgvIVGARNSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
12-164 |
6.69e-14 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 70.77 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 12 PREVELSNgVKIPTLGLGTS-HSGGYSQ--------EAVVYALKVcNYRLIDTAKRYG-CEEFLQAAIH--LSGVPREDI 79
Cdd:cd19164 3 PKPVALSL-AGLPPLIFGAAtFSYQYTTdpesippvDIVRRALEL-GIRAFDTSPYYGpSEIILGRALKalRDEFPRDTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 80 FLTTK-----LWCTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSScpnkkqtlEETW---RELELLYDEGLSRCI 151
Cdd:cd19164 81 FIITKvgrygPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVAD--------EEVLealKELFKLKDEGKIRNV 152
|
170
....*....|...
gi 1009575138 152 GVSNYGIEDLESL 164
Cdd:cd19164 153 GISGYPLPVLLRL 165
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-242 |
5.18e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 68.45 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGY----SQE----AVVYALKV-CNYrlIDTAKRYG---CEEFLQAAihLSGVPrEDIFLTTK--L 85
Cdd:cd19104 9 GLKVSELTFGGGGIGGLmgrtTREeqiaAVRRALDLgINF--FDTAPSYGdgkSEENLGRA--LKGLP-AGPYITTKvrL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 WCTDYG--ASTTRKAFYGSLKRLGVDYLDLYMMH--------WPLCVSSCPNKKQTLEETWRELELLYDEGLSRCIGVSN 155
Cdd:cd19104 84 DPDDLGdiGGQIERSVEKSLKRLKRDSVDLLQLHnrigderdKPVGGTLSTTDVLGLGGVADAFERLRSEGKIRFIGITG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 156 YGIED-LESLLDTAsiAPQVNQVEFN--------------PFQNPSELKEFCVENKIQVEGYCPLGKGKLLGE------- 213
Cdd:cd19104 164 LGNPPaIRELLDSG--KFDAVQVYYNllnpsaaearprgwSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTTSldrgrea 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1009575138 214 ---------------KAVLQVARRCGRTPAQILIRWSIQNEVIA 242
Cdd:cd19104 242 pptsdsdvaidfrraAAFRALAREWGETLAQLAHRFALSNPGVS 285
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-257 |
7.00e-13 |
|
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: 67.67 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHS-GGYSQEAVVYALKVCNYRL----IDTAKRYG-----CEEFLQAAIHLSGVP-REDIFLTTK---- 84
Cdd:cd19089 8 GLHLPAISLGLWHNfGDYTSPEEARELLRTAFDLgithFDLANNYGpppgsAEENFGRILKRDLRPyRDELVISTKagyg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 LWCTDYGASTTRKafY------GSLKRLGVDYLDLYMMHWPlcVSSCPnkkqtLEETWRELELLYDEGLSRCIGVSNYGI 158
Cdd:cd19089 88 MWPGPYGDGGSRK--YllasldQSLKRMGLDYVDIFYHHRY--DPDTP-----LEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 159 EDLE---SLLDTASIAPQVNQVEFNPFQNPSE--LKEFCVENKIQVEGYCPLGKGKL--------------------LGE 213
Cdd:cd19089 159 AKARraiALLRELGVPLIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFSPLAQGLLtdkylngippdsrraaeskfLTE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1009575138 214 KAVL-----------QVARRCGRTPAQILIRWSIQNEVI--AIPKSTQIERVKENCK 257
Cdd:cd19089 239 EALTpekleqlrklnKIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDNVA 295
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
19-172 |
8.45e-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: 67.56 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSHSGGYSQ----EAVVYALKVcNYRLIDTAKRYG---CEEFLQAAIHLSGVPREDIFLTTKL-----W 86
Cdd:cd19153 13 SPVGLGTAALGGVYGDGLEQdeavAIVAEAFAA-GINHFDTSPYYGaesSEAVLGKALAALQVPRSSYTVATKVgryrdS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 CTDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLCVSscpnKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLESLLD 166
Cdd:cd19153 92 EFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFVD----YDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATR 167
|
....*.
gi 1009575138 167 TASIAP 172
Cdd:cd19153 168 RCSPGS 173
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
53-272 |
4.72e-12 |
|
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: 65.32 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 53 IDTAKRYGCE-------EFLQAAihlsgvpREDIFLTTKL-WCTDYGASTT----RK----AFYGSLKRLGVDYLDLYMM 116
Cdd:cd19080 48 IDTANNYTNGtserllgEFIAGN-------RDRIVLATKYtMNRRPGDPNAggnhRKnlrrSVEASLRRLQTDYIDLLYV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 117 HWPLCVSScpnkkqtLEETWRELELLYDEGLSRCIGVSnygiedlesllDT-ASIAPQVN--------------QVEFNP 181
Cdd:cd19080 121 HAWDFTTP-------VEEVMRALDDLVRAGKVLYVGIS-----------DTpAWVVARANtlaelrgwspfvalQIEYSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 182 FQNPSElKEF---CVENKIQVEGYCPLGKGKLLGE------------------------------KAVLQVARRCGRTPA 228
Cdd:cd19080 183 LERTPE-RELlpmARALGLGVTPWSPLGGGLLTGKyqrgeegrageakgvtvgfgklternwaivDVVAAVAEELGRSAA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1009575138 229 QILIRWSIQNEVIAIP--KSTQIERVKENCKIFDFHLQENEMSILN 272
Cdd:cd19080 262 QVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
54-261 |
6.38e-12 |
|
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: 64.92 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 54 DTAKRYG---CEEFLQAAIHLSGVPREDIFLTTKL-W------CTDYGASttRK----AFYGSLKRLGVDYLDLYMMHWP 119
Cdd:cd19143 49 DNAEVYAngqSEEIMGQAIKELGWPRSDYVVSTKIfWggggppPNDRGLS--RKhiveGTKASLKRLQLDYVDLVFCHRP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 120 lcvsscpnKKQT-LEETWRELELLYDEGLSRCIGVSNYGIEDLESLLDTAS----IAPQVNQVEFNPFQNPSELKEFCV- 193
Cdd:cd19143 127 --------DPATpIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQYNLFHRERVEVEYAPl 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 194 ------------------------------------ENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQ 237
Cdd:cd19143 199 yekyglgtttwsplasglltgkynngipegsrlalpGYEWLKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLK 278
|
250 260
....*....|....*....|....*.
gi 1009575138 238 NEVI--AIPKSTQIERVKENCKIFDF 261
Cdd:cd19143 279 NPNVstVITGATKVEQLEENLKALEV 304
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
24-172 |
8.03e-12 |
|
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: 64.30 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 24 PTLGLGTSHSGG---YSQEAVVYALKVC---NYRLIDTAKRYG---CEEFLQAAIHlsGVPREDIFLTTKL--------- 85
Cdd:cd19162 1 PRLGLGAASLGNlarAGEDEAAATLDAAwdaGIRYFDTAPLYGlglSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 ---------WctDYGASTTRKAFYGSLKRLGVDYLDLYMMHWPLcvsscPNKKQTLEETWRELELLYDEGLSRCIGVsny 156
Cdd:cd19162 79 grpagadrrF--DFSADGIRRSIEASLERLGLDRLDLVFLHDPD-----RHLLQALTDAFPALEELRAEGVVGAIGV--- 148
|
170
....*....|....*.
gi 1009575138 157 GIEDLESLLDTASIAP 172
Cdd:cd19162 149 GVTDWAALLRAARRAD 164
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
21-275 |
1.67e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 64.10 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 21 VKIPTLGLGTSHSGGYSQEAVVYA---LKVCN-YRLIDTAKRYGC----------EEFLQAAIHLSGvPREDIFLTTKLW 86
Cdd:PRK10625 11 LEVSTLGLGTMTFGEQNSEADAHAqldYAVAQgINLIDVAEMYPVpprpetqgltETYIGNWLAKRG-SREKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 87 CTDYGASTT------------RKAFYGSLKRLGVDYLDLYMMHWPLCVSSCPNKKQ----------TLEETWRELELLYD 144
Cdd:PRK10625 90 GPSRNNDKGirpnqaldrkniREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGyswtdsapavSLLETLDALAEQQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 145 EGLSRCIGVSN---YGIEDLESLLDTASIaPQVNQVEfNPFQ--NPS---ELKEFCVENKIQVEGYCPLGKGKLLG---- 212
Cdd:PRK10625 170 AGKIRYIGVSNetaFGVMRYLHLAEKHDL-PRIVTIQ-NPYSllNRSfevGLAEVSQYEGVELLAYSCLAFGTLTGkyln 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 213 -----------------------EKAV---LQVARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKENCKIFDFHLQ 264
Cdd:PRK10625 248 gakpagarntlfsrftrysgeqtQKAVaayVDIAKRHGLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNIESLHLTLS 327
|
330
....*....|.
gi 1009575138 265 ENEMSILNDLH 275
Cdd:PRK10625 328 EEVLAEIEAVH 338
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
24-261 |
1.98e-11 |
|
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: 63.40 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 24 PTLGLGTSHSGG-Y-------SQEAVVYALKVCnYRLIDTAKRYGC---EEFLQAAihLSGVPREDIFLTTKL------- 85
Cdd:cd19152 1 PKLGFGTAPLGNlYeavsdeeAKATLVAAWDLG-IRYFDTAPWYGAglsEERLGAA--LRELGREDYVISTKVgrllvpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 86 -----------WCT-------DYGASTTRKAFYGSLKRLGVDYLDLYMMHWP----LCVSSCPNKKQTLEETWRELELLY 143
Cdd:cd19152 78 qeveptfepgfWNPlpfdavfDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPdedlAGAESDEHFAQAIKGAFRALEELR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 144 DEGLSRCIGVsnyGIEDLESLLDTAS--------IAPQVNQVEFnpfqnpSELKEF---CVENKIQVEGYCPLGKGKLLG 212
Cdd:cd19152 158 EEGVIKAIGL---GVNDWEVILRILEeadldwvmLAGRYTLLDH------SAARELlpeCEKRGVKVVNAGPFNSGFLAG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 213 E-------------------KAVLQVARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKENCKIFDF 261
Cdd:cd19152 229 GdnfdyyeygpappeliarrDRIEALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVALLAT 298
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
76-255 |
3.09e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 62.73 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 76 REDIFLTTKL---------WCTDY---GASTTRKAFYGSLKRLGVDYLDLYMMHwplcvssCPNKKQTLEETWRELELLY 143
Cdd:cd19752 66 RDDVVIATKVgagprdpdgGPESPeglSAETIEQEIDKSLRRLGTDYIDLYYAH-------VDDRDTPLEETLEAFNELV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 144 DEGLSRCIGVSNYGIEDLE---------------------SLLDTASIAPQVNQVEFNPfqnpsELKEFCVENK-IQVEG 201
Cdd:cd19752 139 KAGKVRAIGASNFAAWRLErarqiarqqgwaefsaiqqrhSYLRPRPGADFGVQRIVTD-----ELLDYASSRPdLTLLA 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009575138 202 YCPLGKG------KLLGEK----------AVL-QVARRCGRTPAQILIRWSIQNEVIAIP--KSTQIERVKEN 255
Cdd:cd19752 214 YSPLLSGaytrpdRPLPEQydgpdsdarlAVLeEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEEN 286
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
19-257 |
6.89e-10 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 59.23 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSHSGGY-----SQEAVV---YALKVCNYrliDTAKRYG-----CEEFLQAAIHLSGVP-REDIFLTTK 84
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGHvnaleSQRAILrkaFDLGITHF---DLANNYGpppgsAEENFGRLLREDFAAyRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 ----LWCTDYGASTTRKAFYGSL----KRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNY 156
Cdd:PRK09912 98 agydMWPGPYGSGGSRKYLLASLdqslKRMGLEYVDIFYSHR-------VDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 157 GIE---DLESLLDTASIAPQVNQVEFNPFQ---NPSELKEFCVENKIQVEGYCPLGKGKLLGE----------------- 213
Cdd:PRK09912 171 SPErtqKMVELLREWKIPLLIHQPSYNLLNrwvDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdsrmhregnk 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009575138 214 -----------------KAVLQVARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKENCK 257
Cdd:PRK09912 251 vrgltpkmlteanlnslRLLNEMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVQ 313
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
20-265 |
8.75e-09 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 55.49 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGG------YSQEAVVYA--LKVCNYrliDTAKRYG-----CEEFLQAAIHLSGVP-REDIFLTTK- 84
Cdd:cd19151 9 GLKLPAISLGLWHNFGdvdryeNSRAMLRRAfdLGITHF---DLANNYGpppgsAEENFGRILKEDLKPyRDELIISTKa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 ---LWCTDYGASTTRKAFYGSL----KRLGVDYLDLYMMHWPlcvsscpNKKQTLEETWRELELLYDEGLSRCIGVSNYG 157
Cdd:cd19151 86 gytMWPGPYGDWGSKKYLIASLdqslKRMGLDYVDIFYHHRP-------DPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 158 IEDLE---SLLDTASIAPQVNQVEFNPFQNPSE--LKEFCVENKIQVEGYCPLGKGKL--------------------LG 212
Cdd:cd19151 159 PEEAReaaAILKDLGTPCLIHQPKYSMFNRWVEegLLDVLEEEGIGCIAFSPLAQGLLtdrylngipedsraakgssfLK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009575138 213 EKAVL-----------QVARRCGRTPAQILIRWSIQNE-----VIAIPKSTQIERVKENCKIFDFHLQE 265
Cdd:cd19151 239 PEQITeeklakvrrlnEIAQARGQKLAQMALAWVLRNKrvtsvLIGASKPSQIEDAVGALDNREFSEEE 307
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
19-255 |
7.13e-08 |
|
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: 53.12 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGTSHS-GGYSQEAVVYALKVCNYR----LIDTAKRYGC---EEFLQAAIHLSGVPREDIFLTTKLWC--- 87
Cdd:cd19159 9 SGLRVSCLGLGTWVTfGGQISDEVAERLMTIAYEsgvnLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLYWggk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 --TDYGASTTR--KAFYGSLKRLGVDYLDLYMmhwplcvSSCPNKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDles 163
Cdd:cd19159 89 aeTERGLSRKHiiEGLKGSLQRLQLEYVDVVF-------ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 164 LLDTASIAPQVN-------QVEFNPFQNPS---ELKEFCVENKIQVEGYCPLG--------------------------K 207
Cdd:cd19159 159 IMEAYSVARQFNmippvceQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1009575138 208 GKLLGE---------KAVLQVARRCGRTPAQILIRWSIQNEVIA--IPKSTQIERVKEN 255
Cdd:cd19159 239 ERIVSEegrkqqnklKDLSPIAERLGCTLPQLAVAWCLRNEGVSsvLLGSSTPEQLIEN 297
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
53-274 |
5.23e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 49.97 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 53 IDTAKRYG---CEEFLQAAIHlsgvP-REDIFLTTKL---------WCTDYGASTTRKAFYGSLKRLGVDYLD---LYMM 116
Cdd:PRK10376 57 IDTSDFYGphvTNQLIREALH----PyPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLGLDVLDvvnLRLM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 117 ---HWPlcvsscpnKKQTLEETWRELELLYDEGLSRCIGVSNYGIEDLEsllDTASIAPQVN-QVEFN-PFQNPSELKEF 191
Cdd:PRK10376 133 gdgHGP--------AEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVA---EARKIAEIVCvQNHYNlAHRADDALIDA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 192 CVENKIQVEGYCPLGKGKLLGEKAVLQVARRCGRTPAQILIRWSIQN--EVIAIPKSTQIERVKENCKIFDFHLQENEMS 269
Cdd:PRK10376 202 LARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLA 281
|
....*
gi 1009575138 270 ILNDL 274
Cdd:PRK10376 282 ELDGI 286
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
20-260 |
1.23e-06 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 48.99 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 20 GVKIPTLGLGTSHSGGY-----SQEAVV---YALKVCNYrliDTAKRYG-----CEEFLQAAIHLSGVP-REDIFLTTK- 84
Cdd:cd19150 9 GLKLPALSLGLWHNFGDdtpleTQRAILrtaFDLGITHF---DLANNYGpppgsAEENFGRILREDFAGyRDELIISTKa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 85 ---LWCTDYGASTTRKAFYGS----LKRLGVDYLDLYMMHWplcvsscPNKKQTLEETWRELELLYDEGLSRCIGVSNYG 157
Cdd:cd19150 86 gydMWPGPYGEWGSRKYLLASldqsLKRMGLDYVDIFYSHR-------FDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 158 IE------DLESLLDTASIAPQVNQVEFNPFQNPSELKEFCVENKIQVEGYCPLGKGKLLGE------------------ 213
Cdd:cd19150 159 PErtreaaAILRELGTPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKylngipegsraskersls 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1009575138 214 ------------KAVLQVARRCGRTPAQILIRWSIQNEVI--AIPKSTQIERVKENCKIFD 260
Cdd:cd19150 239 pkmlteanlnsiRALNEIAQKRGQSLAQMALAWVLRDGRVtsALIGASRPEQLEENVGALD 299
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
18-166 |
1.74e-05 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 45.54 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 18 SNGVKIPTLGLGTSHSG---GYSQEAVVYALKVCNYRL----IDTAKRYG---CEEFLQAAIHLSGVPREDIFLTTKlwC 87
Cdd:PLN02587 6 STGLKVSSVGFGASPLGsvfGPVSEEDAIASVREAFRLginfFDTSPYYGgtlSEKVLGKALKALGIPREKYVVSTK--C 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 TDYG------ASTTRKAFYGSLKRLGVDYLDLYMMHwPLCVSSCpnkKQTLEETWRELELLYDEGLSRCIGVSNYGIEDL 161
Cdd:PLN02587 84 GRYGegfdfsAERVTKSVDESLARLQLDYVDILHCH-DIEFGSL---DQIVNETIPALQKLKESGKVRFIGITGLPLAIF 159
|
....*
gi 1009575138 162 ESLLD 166
Cdd:PLN02587 160 TYVLD 164
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
19-239 |
4.99e-05 |
|
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: 44.38 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGT--SHSGGYSQEA----VVYALKV-CNYrlIDTAKRY---GCEEFLQAAIHLSGVPREDIFLTTKL-WC 87
Cdd:cd19142 9 SGLRVSNVGLGTwsTFSTAISEEQaeeiVTLAYENgINY--FDTSDAFtsgQAETELGRILKKKGWKRSSYIVSTKIyWS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 T-DYGASTTRK----AFYGSLKRLGVDYLDLYMMHwpLCVSSCPnkkqtLEETWRELELLYDEGLSRCIGVSNYG-IEDL 161
Cdd:cd19142 87 YgSEERGLSRKhiieSVRASLRRLQLDYIDIVIIH--KADPMCP-----MEEVVRAMSYLIDNGLIMYWGTSRWSpVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 162 ESLldtaSIAPQVN-------QVEFNPF-QNPSELKEFCVENKIQV-------------------------------EGY 202
Cdd:cd19142 160 EAF----SIARQFNcptpiceQSEYHMFcREKMELYMPELYNKVGVglitwsplslgldpgiseetrrlvtklsfksSKY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1009575138 203 CPLGKGKLLGE---------KAVLQVARRCGRTPAQILIRWSIQNE 239
Cdd:cd19142 236 KVGSDGNGIHEetrrashklRELSLIAERLGCDLTQLLIAWSLKNE 281
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
19-239 |
5.44e-05 |
|
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: 44.21 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 19 NGVKIPTLGLGT-----SHSGGYSQEAVVYALKVCNYRLIDTAKRYG---CEEFLQAAIHLSGVPREDIFLTTKLWC--- 87
Cdd:cd19160 11 SGLRVSCLGLGTwvtfgSQISDETAEDLLTVAYEHGVNLFDTAEVYAagkAERTLGNILKSKGWRRSSYVVTTKIYWggq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 88 --TDYGASTTR--KAFYGSLKRLGVDYLDLYMMHwpLCVSSCPnkkqtLEETWRELELLYDEGLSRCIGVSNYGIEDles 163
Cdd:cd19160 91 aeTERGLSRKHiiEGLRGSLDRLQLEYVDIVFAN--RSDPNSP-----MEEIVRAMTYVINQGMAMYWGTSRWSAME--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009575138 164 LLDTASIAPQVN-------QVEFNPFQN---PSELKEfcVENKIQVEG--YCPLGKGKLLGE------------------ 213
Cdd:cd19160 161 IMEAYSVARQFNlippvceQAEYHLFQRekvEMQLPE--LYHKIGVGSvtWSPLACGLITGKydgrvpdtcraavkgyqw 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1009575138 214 -----------------KAVLQVARRCGRTPAQILIRWSIQNE 239
Cdd:cd19160 239 lkekvqseegkkqqakvKELHPIADRLGCTVAQLAIAWCLRSE 281
|
|
| |
