|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-259 |
4.57e-157 |
|
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: 437.78 E-value: 4.57e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 5 TKLNNGVVMPQLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYE 84
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 85 RAKQGIDASLQRLGVDYLDLYLLHQPYGDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPW 164
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHPF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 165 YQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFD 244
Cdd:cd19133 161 NQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFD 240
|
250
....*....|....*
gi 489741763 245 FELTAAEMSAMAELD 259
Cdd:cd19133 241 FELSDEDMEAIAALD 255
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-267 |
1.58e-147 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 413.68 E-value: 1.58e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERAKQ 88
Cdd:COG0656 1 NGVEIPALGLGTWQLPG-EEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 89 GIDASLQRLGVDYLDLYLLHQPY-GDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQ 167
Cdd:COG0656 80 AFEESLERLGLDYLDLYLIHWPGpGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 168 ADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFEL 247
Cdd:COG0656 160 RELLAFCREHGIVVEAYSPLGRGK--LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFEL 237
|
250 260
....*....|....*....|
gi 489741763 248 TAAEMSAMAELDQGVSQFFD 267
Cdd:COG0656 238 SDEDMAAIDALDRGERLGPD 257
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-256 |
3.86e-126 |
|
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: 359.10 E-value: 3.86e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERAKQGIDA 92
Cdd:cd19071 1 MPLIGLGTYKLKP-EETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 93 SLQRLGVDYLDLYLLHQPY--------GDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPW 164
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVpgkeggskEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 165 YQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFD 244
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|..
gi 489741763 245 FELTAAEMSAMA 256
Cdd:cd19071 240 FELSEEDMAAID 251
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-259 |
8.49e-114 |
|
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: 328.60 E-value: 8.49e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 5 TKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYE 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPP-EETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 85 RAKQGIDASLQRLGVDYLDLYLLHQP----YGDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIE 160
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPvpndFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 161 VNPWYQQADEVRFNQGEHVRVEAWAPF-----------EEGKHaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPK 229
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgpTGPGD-VLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPK 238
|
250 260 270
....*....|....*....|....*....|
gi 489741763 230 SVHPERMAENIAVFDFELTAAEMSAMAELD 259
Cdd:cd19127 239 SVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
4-259 |
5.68e-112 |
|
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: 323.56 E-value: 5.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 4 TTKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTY 83
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSN-DEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 84 ERAKQGIDASLQRLGVDYLDLYLLHQP---YGDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIE 160
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPvpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 161 VNPWYQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENI 240
Cdd:cd19131 160 LHPRFQQRELRAFHAKHGIQTESWSPLGQGG--LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENF 237
|
250
....*....|....*....
gi 489741763 241 AVFDFELTAAEMSAMAELD 259
Cdd:cd19131 238 DVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-262 |
4.24e-108 |
|
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: 314.33 E-value: 4.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 4 TTKLNNGVVMPQLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTY 83
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 84 ERAKQGIDASLQRLGVDYLDLYLLHQPYGDV-MGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVN 162
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGKyKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 163 PWYQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAV 242
Cdd:cd19157 161 PRLTQKELRDYCKKQGIQLEAWSPLMQGQ--LLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADV 238
|
250 260
....*....|....*....|
gi 489741763 243 FDFELTAAEMSAMAELDQGV 262
Cdd:cd19157 239 FDFELSQEDMDKIDALNENL 258
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-259 |
5.92e-104 |
|
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: 303.20 E-value: 5.92e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 6 KLNNGVVMPQLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYER 85
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 86 AKQGIDASLQRLGVDYLDLYLLHQPYGD-VMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPW 164
Cdd:cd19126 82 TEDAFQESLDRLGLDYVDLYLIHWPGKDkFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 165 YQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFD 244
Cdd:cd19126 162 LTQKELRGYCKSKGIVVEAWSPLGQGG--LLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFD 239
|
250
....*....|....*
gi 489741763 245 FELTAAEMSAMAELD 259
Cdd:cd19126 240 FELSEDDMTAIDALN 254
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
6-271 |
2.87e-101 |
|
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: 296.74 E-value: 2.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 6 KLNNGVVMPQLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYER 85
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 86 AKQGIDASLQRLGVDYLDLYLLHQPYGD-VMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPW 164
Cdd:cd19156 82 TLAAFEESLEKLGLDYVDLYLIHWPVKGkFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 165 YQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFD 244
Cdd:cd19156 162 LTQEPLRKFCKEKNIAVEAWSPLGQGK--LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFD 239
|
250 260 270
....*....|....*....|....*....|
gi 489741763 245 FELTAAEMSAMAELDQgvsqffDHR---DP 271
Cdd:cd19156 240 FELTAEEIRQIDGLNT------DHRygpDP 263
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-258 |
1.04e-99 |
|
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: 292.61 E-value: 1.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ----KSGLRRDELFVTSKLWVSEFTYERAKQ 88
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRdllpKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 89 GIDASLQRLGVDYLDLYLLHQPYGDVM------------GAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAV 156
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLkpsdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 157 NQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERM 236
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 489741763 237 AENIAVFDFELTAAEMSAMAEL 258
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
7-260 |
9.11e-99 |
|
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: 289.94 E-value: 9.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 7 LNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERA 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKG-DEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 87 KQGIDASLQRLGVDYLDLYLLHQP---YGDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNP 163
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHWPnpsRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 164 WYQQADEVRFNQGEHVRVEAWAPFEEGKhAIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVF 243
Cdd:cd19132 160 YFPQAEQRAYHREHGIVTQSWSPLGRGS-GLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIF 238
|
250
....*....|....*..
gi 489741763 244 DFELTAAEMSAMAELDQ 260
Cdd:cd19132 239 DFELSDEDMAAIAALDR 255
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-261 |
4.27e-94 |
|
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: 279.55 E-value: 4.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKLNNGVVMPQLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQK----SGLRRDELFVTSKLWV 78
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREkiaeGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 79 SEFTYERAKQGIDASLQRLGVDYLDLYLLHQPYG------------------DVMGAWRALEEAYHAGKIRAIGVSNFYA 140
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAfkenndsesngdgslsdiDYLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 141 DQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFeeGKHA---------IFSNPSIQTIAQAHGKTT 211
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPF--GRLVprgqtnpppRLDDPTLVAIAKKYGKTT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489741763 212 GQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQG 261
Cdd:cd19116 239 AQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTN 288
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-253 |
3.16e-92 |
|
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: 273.82 E-value: 3.16e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 1 MVPTTKLNNGVVMPQLGFGVFQVPdlNECEAAVTAALK-AGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVS 79
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGTSHSG--GYSHEAVVYALKeCGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 80 EFTYERAKQGIDASLQRLGVDYLDLYLLHQPYGDVMG---------AWRALEEAYHAGKIRAIGVSNFYADQLKNLELTM 150
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketraeTWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 151 SVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKS 230
Cdd:cd19135 159 SVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK--ALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKS 236
|
250 260
....*....|....*....|...
gi 489741763 231 VHPERMAENIAVFDFELTAAEMS 253
Cdd:cd19135 237 TKEERIKENCQVFDFSLSEEDMA 259
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
3-261 |
9.47e-92 |
|
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: 272.50 E-value: 9.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFT 82
Cdd:cd19134 1 PTVTLNDDNTMPVIGLGVGELSD-DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLHQPYGDV---MGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQI 159
Cdd:cd19134 80 FTASQAACRASLERLGLDYVDLYLIHWPAGREgkyVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 160 EVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAEN 239
Cdd:cd19134 160 ELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR--LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASN 237
|
250 260
....*....|....*....|..
gi 489741763 240 IAVFDFELTAAEMSAMAELDQG 261
Cdd:cd19134 238 LDVFDFELTADHMDALDGLDDG 259
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-261 |
2.44e-91 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 271.95 E-value: 2.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEft 82
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLHQPY---GDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQI 159
Cdd:PRK11565 82 HKRPREALEESLKKLQLDYVDLYLMHWPVpaiDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 160 EVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAEN 239
Cdd:PRK11565 162 ELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAEN 241
|
250 260
....*....|....*....|..
gi 489741763 240 IAVFDFELTAAEMSAMAELDQG 261
Cdd:PRK11565 242 FDVFDFRLDKDELGEIAKLDQG 263
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-259 |
1.16e-88 |
|
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: 264.47 E-value: 1.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 7 LNNGVVMPQLGFGVFQVPDLnECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERA 86
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPA-DTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 87 KQGIDASLQRLGVDYLDLYLLHQPY---GDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNP 163
Cdd:cd19130 83 AAAFAESLAKLGLDQVDLYLVHWPTpaaGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 164 WYQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVF 243
Cdd:cd19130 163 AYQQRTIRDWAQAHDVKIEAWSPLGQGK--LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVF 240
|
250
....*....|....*.
gi 489741763 244 DFELTAAEMSAMAELD 259
Cdd:cd19130 241 DFDLTDTEIAAIDALD 256
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-260 |
6.29e-84 |
|
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: 253.42 E-value: 6.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 6 KLNNGVVMPQLGFGVFQVpDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSG----LRRDELFVTSKLWVSEF 81
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQA-DPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 82 TYERAKQGIDASLQRLGVDYLDLYLLHQPY----GDVM------------GAWRALEEAYHAGKIRAIGVSNFYADQLKN 145
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVrlkkGAHMpepeevlppdipSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 146 LELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF-----EEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLL 220
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgtTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489741763 221 QRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQ 260
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQ 282
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-265 |
2.31e-82 |
|
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: 250.02 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 2 VPTTKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQK---SG-LRRDELFVTSKLW 77
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKG-AEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGvVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 78 VSEFTYERAKQGIDASLQRLGVDYLDLYLLHQPYG---------------------DVMGAWRALEEAYHAGKIRAIGVS 136
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAfkddegesgtmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 137 NFYADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF-------------EEGKHAIFSNPSIQTI 203
Cdd:cd19154 160 NFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgranftkstgVSPAPNLLQDPIVKAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489741763 204 AQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGVSQF 265
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-258 |
6.48e-82 |
|
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: 247.17 E-value: 6.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERAKQ 88
Cdd:cd19140 4 NGVRIPALGLGTYPLTG-EECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 89 GIDASLQRLGVDYLDLYLLHQPYGDVMGAW--RALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQ 166
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWPNKDVPLAEtlGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 167 QADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQR-GITVIPKSVHPERMAENIAVFDF 245
Cdd:cd19140 163 QRKLLDAAREHGIALTAYSPLARGE--VLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDF 240
|
250
....*....|...
gi 489741763 246 ELTAAEMSAMAEL 258
Cdd:cd19140 241 TLSDEEMARIAAL 253
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-255 |
3.79e-81 |
|
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: 244.87 E-value: 3.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERAKQGIDA 92
Cdd:cd19073 1 IPALGLGTWQLRG-DDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 93 SLQRLGVDYLDLYLLHQP-----YGDVMGawrALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQ 167
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWPnptvpLEETLG---ALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 168 ADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFEL 247
Cdd:cd19073 157 AELLEYCRENDIVITAYSPLARGE--VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWEL 234
|
....*...
gi 489741763 248 TAAEMSAM 255
Cdd:cd19073 235 TSEDVAKI 242
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-260 |
4.00e-80 |
|
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: 243.71 E-value: 4.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVF-QVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ---KSGL--RRDELFVTSKLWVSEFT 82
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGLvkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLHQPYG------------------DVMGAWRALEEAYHAGKIRAIGVSNFYADQLK 144
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSlkpgkfsfpieeedflpfDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 145 NLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEE-----GKHAIFSNPSIQTIAQAHGKTTGQVILRWL 219
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGApgtkwGSNAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489741763 220 LQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQ 260
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-257 |
9.53e-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: 237.13 E-value: 9.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFGV----FQVPDLN---ECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEft 82
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 yERAKQGIDASLQRLGVDYLDLYLLHQPY------GDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAV 156
Cdd:cd19120 79 -KDPREALRKSLAKLGVDYVDLYLIHSPFfakeggPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 157 NQIEVNP--WYQQADEVRFNQGEHVRVEAWAPF-----EEGKHAifsNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPK 229
Cdd:cd19120 158 NQIEFHPylYPQQPALLEYCREHGIVVSAYSPLspltrDAGGPL---DPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTT 234
|
250 260
....*....|....*....|....*...
gi 489741763 230 SVHPERMAENIAVFDFELTAAEMSAMAE 257
Cdd:cd19120 235 SSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
4-258 |
2.01e-76 |
|
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: 234.31 E-value: 2.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 4 TTKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEftY 83
Cdd:cd19117 5 TFKLNTGAEIPAVGLGTWQSKP-NEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTW--H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 84 ERAKQGIDASLQRLGVDYLDLYLLHQPYG-----------------------DVMGAWRALEEAYHAGKIRAIGVSNFYA 140
Cdd:cd19117 82 RRVEEALDQSLKKLGLDYVDLYLMHWPVPldpdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 141 DQLKNLELTMS--VQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSNPSIQTIAQAHGKTTGQVILRW 218
Cdd:cd19117 162 KNLEKLLASPSakIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTPAQVIISW 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489741763 219 LLQRGITVIPKSVHPERMAENIAVfdFELTAAEMSAMAEL 258
Cdd:cd19117 242 GLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-261 |
2.73e-76 |
|
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: 234.59 E-value: 2.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 7 LNNGVVMPQLGFGVFQvPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKS-----GLRRDELFVTSKLWVSEF 81
Cdd:cd19106 1 LHTGQKMPLIGLGTWK-SKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 82 TYERAKQGIDASLQRLGVDYLDLYLLHQPYG---------------------DVMGAWRALEEAYHAGKIRAIGVSNFYA 140
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAfergdnpfpknpdgtirydstHYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 141 DQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF--------EEGKHAIFSNPSIQTIAQAHGKTTG 212
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwaKPDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489741763 213 QVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQG 261
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRN 288
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-262 |
3.93e-76 |
|
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: 234.62 E-value: 3.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 1 MVPTTKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVG----RAIQKSGLRRDELFVTSKL 76
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNN-DTCADQVYNAIKAGYRLFDGACDYGNEVEAGqgvaRAIKEGIVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 77 WVSEFTYERAKQGIDASLQRLGVDYLDLYLLHQP----YGD----------------------VMGAWRALEEAYHAGKI 130
Cdd:cd19115 80 WNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPialkYVDpavryppgwfydgkkvefsnapIQETWTAMEKLVDKGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 131 RAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFE-------EGKHA-----IFSNP 198
Cdd:cd19115 160 RSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsflelDLPGAkdtppLFEHD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489741763 199 SIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGV 262
Cdd:cd19115 240 VIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGL 303
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
4-261 |
6.61e-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: 233.46 E-value: 6.61e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 4 TTKLNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAI----QKSGLRRDELFVTSKLWVS 79
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKP-GEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 80 EFTYERAKQGIDASLQRLGVDYLDLYLLHQP----------------YGD----VMGAWRALEEAYHAGKIRAIGVSNFY 139
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedlLSLspipLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 140 ADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF----------EEGKHAIFSNPSIQTIAQAHGK 209
Cdd:cd19123 162 VKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLgsgdrpaamkAEGEPVLLEDPVINKIAEKHGA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489741763 210 TTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQG 261
Cdd:cd19123 242 SPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRH 293
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-265 |
2.28e-75 |
|
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: 231.62 E-value: 2.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ---KSG-LRRDELFVTSKLWVSEFTYER 85
Cdd:cd19111 1 GFPMPVIGLGTYQSPP-EEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 86 AKQGIDASLQRLGVDYLDLYLLHQPYG---------------DVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTM 150
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGfvnkkdkgerelassDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 151 SVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF----------EEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLL 220
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgspgranqslWPDQPDLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489741763 221 QRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGVSQF 265
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYF 284
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-265 |
6.78e-74 |
|
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: 228.56 E-value: 6.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 7 LNNGVVMPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQK---SG-LRRDELFVTSKLWVSEFT 82
Cdd:cd19155 6 FNNGEKMPVVGLGTWQSSP-EEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGGNR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLHQPYG-----------------------DVMGAWRALEEAYHAGKIRAIGVSNFY 139
Cdd:cd19155 85 REKVEKFLLKSLEKLQLDYVDLYLIHFPVGslskeddsgkldptgehkqdyttDLLDIWKAMEAQVDQGLTRSIGLSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 140 ADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF-EEGKHA--------------IFSNPSIQTIA 204
Cdd:cd19155 165 REQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgSPGAAHfspgtgspsgsspdLLQDPVVKAIA 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489741763 205 QAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGVSQF 265
Cdd:cd19155 245 ERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
3-262 |
1.08e-72 |
|
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: 225.79 E-value: 1.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKLNNGVVMPQLGFGVFQVPDLNeCEAAVTAALKAGYRLIDTATAYQNETAVG----RAIQKSGLRRDELFVTSKLWV 78
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNAT-AADQIYQAIKAGYRLFDGAEDYGNEKEVGegvnRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 79 SEFTYERAKQGIDASLQRLGVDYLDLYLLHQP-------------------------YGDV--MGAWRALEEAYHAGKIR 131
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVpiLDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 132 AIGVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF--------EEGK----HAIFSNPS 199
Cdd:cd19113 160 SIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFgpqsfvelNQGRalntPTLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489741763 200 IQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGV 262
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGL 302
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-258 |
5.83e-72 |
|
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: 223.06 E-value: 5.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 7 LNNGVVMPQLGFGVFQV-PDlnECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKS-----GLRRDELFVTSKLWVSE 80
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAePG--EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 81 FTYERAKQGIDASLQRLGVDYLDLYLLH-----QPYGD---------------------VMGAWRALEEAYHAGKIRAIG 134
Cdd:cd19118 79 HRPEYVEPALDDTLKELGLDYLDLYLIHwpvafKPTGDlnpltavptnggevdldlsvsLVDTWKAMVELKKTGKVKSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 135 VSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF---EEGKHAIFSNPSIQTIAQAHGKTT 211
Cdd:cd19118 159 VSNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLPLLVQHPEVKAIAAKLGKTP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489741763 212 GQVILRWLLQRGITVIPKSVHPERMAENIAvfDFELTAAEMSAMAEL 258
Cdd:cd19118 239 AQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-258 |
2.52e-67 |
|
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: 209.90 E-value: 2.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERAKQGIDA 92
Cdd:cd19139 1 IPAFGLGTFRLKD-DVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 93 SLQRLGVDYLDLYLLH--QPYGDV-----MGawrALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQP-AVNQIEVNPW 164
Cdd:cd19139 80 SLEKLRTDYVDLTLIHwpSPNDEVpveeyIG---ALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAiATNQIELSPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 165 YQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFD 244
Cdd:cd19139 157 LQNRKLVAHCKQHGIHVTSYMTLAYGK--VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALD 234
|
250
....*....|....
gi 489741763 245 FELTAAEMSAMAEL 258
Cdd:cd19139 235 LTLDADDMAAIAAL 248
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
3-263 |
8.87e-67 |
|
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: 210.42 E-value: 8.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKLNNGVVMPQLGFGVFQVpDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ---KSGL-RRDELFVTSKLWV 78
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAeafKTGLvKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 79 SEftYERAKQGIDASLQRLGVDYLDLYLLHQP--------------YGD-----------VMGAWRALEEAYHAGKIRAI 133
Cdd:cd19112 80 SD--HGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsaLGEdgvldidvtisLETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 134 GVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF------EE--GKHAIFSNPSIQTIAQ 205
Cdd:cd19112 158 GISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLggaaanAEwfGSVSPLDDPVLKDLAK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489741763 206 AHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGVS 263
Cdd:cd19112 238 KYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
10-270 |
3.49e-66 |
|
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: 208.81 E-value: 3.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFGVFQVPdLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQK----SGLRRDELFVTSKLWVSEFTYER 85
Cdd:cd19107 1 GAKMPILGLGTWKSP-PGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEkikeQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 86 AKQGIDASLQRLGVDYLDLYLLHQPYG---------------------DVMGAWRALEEAYHAGKIRAIGVSNFYADQLK 144
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkelfpldesgnvipsdtTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 145 NL--ELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF--------EEGKHAIFSNPSIQTIAQAHGKTTGQV 214
Cdd:cd19107 160 RIlnKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwaKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489741763 215 ILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQ-----GVSQFFDHRD 270
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRnwracALLSCSSHKD 300
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
6-258 |
4.05e-66 |
|
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: 207.77 E-value: 4.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 6 KLNNGVVMPQLGFGVFQvPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKS---GLRRDELFVTSKLWVSEFT 82
Cdd:cd19121 5 KLNTGASIPAVGLGTWQ-AKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTYHR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 yeRAKQGIDASLQRLGVDYLDLYLLH-----QPYG-------------------DVMGAWRALEEAYHAGKIRAIGVSNF 138
Cdd:cd19121 84 --RVELCLDRSLKSLGLDYVDLYLVHwpvllNPNGnhdlfptlpdgsrdldwdwNHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 139 YADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSNPSIQTIAQAHGKTTGQVILRW 218
Cdd:cd19121 162 SIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGPGTVLISY 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489741763 219 LLQRGITVIPKSVHPERMAENIAVFDFelTAAEMSAMAEL 258
Cdd:cd19121 242 QVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-261 |
8.20e-64 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 201.41 E-value: 8.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKSGLRRDELFVTSKLWVSEFTYERAKQGIDA 92
Cdd:PRK11172 3 IPAFGLGTFRLKD-QVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 93 SLQRLGVDYLDLYLLHQPYGD-------VMGawrALEEAYHAGKIRAIGVSNFYADQLKN-LELTMSVQPAVNQIEVNPW 164
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWPSPNdevsveeFMQ---ALLEAKKQGLTREIGISNFTIALMKQaIAAVGAENIATNQIELSPY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 165 YQQADEVRFNQGEHVRVEAWAPFEEGKhaIFSNPSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFD 244
Cdd:PRK11172 159 LQNRKVVAFAKEHGIHVTSYMTLAYGK--VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQD 236
|
250
....*....|....*..
gi 489741763 245 FELTAAEMSAMAELDQG 261
Cdd:PRK11172 237 LQLDAEDMAAIAALDRN 253
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-259 |
8.28e-62 |
|
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: 197.40 E-value: 8.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLGFGVFQVpDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKS---GL-RRDELFVTSKLWVSEFTYERAKQ 88
Cdd:cd19114 4 MPLVGFGTAKI-KANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAiqeGLvKREDLFIVTKLWNNFHGKDHVRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 89 GIDASLQRLGVDYLDLYLLHQP----YGD-----------------------VMGAWRALEEAYHAGKIRAIGVSNFYAD 141
Cdd:cd19114 83 AFDRQLKDYGLDYIDLYLIHFPipaaYVDpaenypflwkdkelkkfpleqspMQECWREMEKLVDAGLVRNIGIANFNVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 142 QLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF---------EEGKH--AIFSNPSIQTIAQAHGKT 210
Cdd:cd19114 163 LILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFgnavytkvtKHLKHftNLLEHPVVKKLADKHKRD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489741763 211 TGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELD 259
Cdd:cd19114 243 TGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELE 291
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
13-275 |
2.32e-61 |
|
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: 196.33 E-value: 2.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ---KSG-LRRDELFVTSKLWVSEFTYERAKQ 88
Cdd:cd19110 4 IPAVGLGTWKASP-GEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekiKEGvVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 89 GIDASLQRLGVDYLDLYLLHQPYG---------------------DVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNL- 146
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGfkpgepdlpldrsgmvipsdtDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 147 -ELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPF---EEGKHAIfSNPSIQTIAQAHGKTTGQVILRWLLQR 222
Cdd:cd19110 163 nKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLggsCEGVDLI-DDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489741763 223 GITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQG--VSQF---FDHRD-PVTIE 275
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNlrLATFpitENHKDyPFHIE 300
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-262 |
1.50e-59 |
|
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: 191.52 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFGVFqVPDLNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ---KSG-LRRDELFVTSKLWVSEFTY 83
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQevfKAGkIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 84 ERAKQGIDASLQRLGVDYLDLYLLHQPY--------------GDV--------MGAWRALEEAYHAGKIRAIGVSNFYAD 141
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFafqpgdeqdprdanGNViyddgvtlLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 142 QLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEG-KHAIFSNPSIQTIAQAHGKTTGQVILRWLL 220
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489741763 221 QRGITVIPKSVHPERMAENiavfdFELTAAEMSAMAELDQGV 262
Cdd:cd19129 240 QRGTALLTTSKTPSRIREN-----FDISTLPEDAMREINEGI 276
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-240 |
3.36e-59 |
|
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: 190.40 E-value: 3.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 6 KLNNGVVMPQLGFGVFQ-VPDLNECEAAVTAALKAGYRLIDTATAYQNETAVG----RAIQKSGLRRDELFVTSKLWVSe 80
Cdd:cd19119 5 KLNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGeaikRAIDDGSIKREELFITTKVWPT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 81 fTYERAKQGIDASLQRLGVDYLDLYLLHQPY---------------------------GDVMGAWRALEEAYHAGKIRAI 133
Cdd:cd19119 84 -FYDEVERSLDESLKALGLDYVDLLLVHWPVcfekdsddsgkpftpvnddgktryaasGDHITTYKQLEKIYLDGRAKAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 134 GVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSNPSIQTIAQAHGKTTGQ 213
Cdd:cd19119 163 GVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKYNVSTGD 242
|
250 260
....*....|....*....|....*..
gi 489741763 214 VILRWLLQRGITVIPKSVHPERMAENI 240
Cdd:cd19119 243 ILISYHVRQGVIVLPKSLKPVRIVSNG 269
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-253 |
1.31e-56 |
|
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: 182.81 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 13 MPQLG-----FGVFQVPDLNECEAAVTA---ALKAGYRLIDTATAYQN---ETAVGRAIqkSGLRRDELFVTSKLWVSEF 81
Cdd:cd19072 4 VPVLGlgtwgIGGGMSKDYSDDKKAIEAlryAIELGINLIDTAEMYGGghaEELVGKAI--KGFDREDLFITTKVSPDHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 82 TYERAKQGIDASLQRLGVDYLDLYLLHQP--YGDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKN-LELTMSVQPAVNQ 158
Cdd:cd19072 82 KYDDVIKAAKESLKRLGTDYIDLYLIHWPnpSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEaQSYLKKGPIVANQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 159 IEVN-----------PWYQQadevrfnqgEHVRVEAWAPFEEGKHAI-FSNPSIQTIAQAHGKTTGQVILRWLLQR-GIT 225
Cdd:cd19072 162 VEYNlfdreeesgllPYCQK---------NGIAIIAYSPLEKGKLSNaKGSPLLDEIAKKYGKTPAQIALNWLISKpNVI 232
|
250 260
....*....|....*....|....*...
gi 489741763 226 VIPKSVHPERMAENIAVFDFELTAAEMS 253
Cdd:cd19072 233 AIPKASNIEHLEENAGALGWELSEEDLQ 260
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-258 |
2.32e-56 |
|
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: 182.72 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQK----SGLRRDELFVTSKLWVSEFTYERAKQG 89
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 90 IDASLQRLGVDYLDLYLLHQPYGDVMGA---------------------WRALEEAYHAGKIRAIGVSNFYADQLKNLEL 148
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAFDMDTdgdprddnqiqslskkpledtWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 149 TMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAP----FEEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQR-- 222
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPlggsYGDGNLTFLNDSELKALATKYNTTPPQVIIAWHLQKwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 489741763 223 -GITVIPKSVHPERMAENIAVFDFELTAAEMSAMAEL 258
Cdd:cd19128 241 kNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-260 |
3.06e-56 |
|
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: 183.20 E-value: 3.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKLNNGVVMPQLGFGVF---QVPDlNECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ---KSG-LRRDELFVTSK 75
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYapeEVPK-SKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRskiADGtVKREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 LWVSEFTYERAKQGIDASLQRLGVDYLDLYLLHQPYG---------------------DVMGAWRALEEAYHAGKIRAIG 134
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeelfpkdengklifdtvDLCATWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 135 VSNFYADQlknLELTMS-----VQPAVNQIEVNPWYQQADEVRFNQ------------GEHvRVEAWApfEEGKHAIFSN 197
Cdd:cd19108 160 VSNFNRRQ---LEMILNkpglkYKPVCNQVECHPYLNQSKLLDFCKskdivlvaysalGSQ-RDKEWV--DQNSPVLLED 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489741763 198 PSIQTIAQAHGKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQ 260
Cdd:cd19108 234 PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNR 296
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
3-259 |
4.20e-56 |
|
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: 181.68 E-value: 4.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKLNNGVVMPQLGFGVFQV----PDLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKsglRRDELFVTSK 75
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG---RRDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 LWVSEFTYERAKQGIDASLQRLGVDYLDLYLLH----QPYGDVMgawRALEEAYHAGKIRAIGVSNFYADQLKNL-ELTM 150
Cdd:cd19138 78 VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHwrggVPLAETV---AAMEELKKEGKIRAWGVSNFDTDDMEELwAVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 151 SVQPAVNQIEVN-----------PWYQQadevrfnqgEHVRVEAWAPFEEG---KHAIFSNPSIQTIAQAHGKTTGQVIL 216
Cdd:cd19138 155 GGNCAANQVLYNlgsrgieydllPWCRE---------HGVPVMAYSPLAQGgllRRGLLENPTLKEIAARHGATPAQVAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489741763 217 RWLLQRGITV-IPKSVHPERMAENIAVFDFELTAAEmsaMAELD 259
Cdd:cd19138 226 AWVLRDGNVIaIPKSGSPEHARENAAAADLELTEED---LAELD 266
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
15-259 |
9.71e-55 |
|
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: 179.04 E-value: 9.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 15 QLGFGVFQVPDlNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGLRRDELFVTSKL------WVSEFTYER 85
Cdd:pfam00248 7 QLGGGWGPISK-EEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSGGSKEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 86 AKQGIDASLQRLGVDYLDLYLLHQPYGDV--MGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNP 163
Cdd:pfam00248 86 IRKSLEESLKRLGTDYIDLYYLHWPDPDTpiEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 164 WYQQADE--VRFNQGEHVRVEAWAP------------------FEEGKHAIFSNPSIQT-------IAQAHGKTTGQVIL 216
Cdd:pfam00248 166 LRRRQEEelLEYCKKNGIPLIAYSPlggglltgkytrdpdkgpGERRRLLKKGTPLNLEalealeeIAKEHGVSPAQVAL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489741763 217 RWLLQ--RGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELD 259
Cdd:pfam00248 246 RWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
10-262 |
2.42e-53 |
|
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: 175.76 E-value: 2.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFGVFQVPDLN---ECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQKS----GLRRDELFVTSKLWVSEFT 82
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLHQPYG---------------------DVMGAWRALEEAYHAGKIRAIGVSNFYAD 141
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAfkpgdeiyprdengkwlyhktNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 142 QLknlELTMS-----VQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSN---------PSIQTIAQAH 207
Cdd:cd19109 161 QL---ELILNkpglkHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNvsspplledPLLNSIGKKY 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489741763 208 GKTTGQVILRWLLQRGITVIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGV 262
Cdd:cd19109 238 NKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNV 292
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
6-255 |
6.69e-53 |
|
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: 174.35 E-value: 6.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 6 KLNNGVVMPQLGFGVFQVPDLN-ECEAAVTAALKAGYRLIDTATAYQNETAVGRAIQ-----KSGLRRDELFVTSKLWVS 79
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAKgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRdflkeNPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 80 EFTYERAKQGIDASLQRLGVDYLDLYLLHQPY-----GDVM--------------------GAWRALEEAYHAGKIRAIG 134
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaeknDQRSpklgpdgkyvilkdltenpePTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 135 VSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQADEVRFNQGEHVRVEAWAPFEEGKHA------IFSNPSIQTIAQAHG 208
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVpstgerVSENPTLNEVAEKGG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489741763 209 KTTGQVILRWLLQRGITVIPKSVHPERMAENIAVfdFELTAAEMSAM 255
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAI 286
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
8-258 |
1.60e-48 |
|
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: 163.43 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFG------VFQVPDLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQksGLRRDELFVTSKL-- 76
Cdd:COG0667 8 RSGLKVSRLGLGtmtfggPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVVIATKVgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 77 ------WVSEFTYERAKQGIDASLQRLGVDYLDLYLLHQPYGDVM--GAWRALEEAYHAGKIRAIGVSNFYADQLKN-LE 147
Cdd:COG0667 86 rmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPieETLGALDELVREGKIRYIGVSNYSAEQLRRaLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 148 LTMSVQP-AVNQIEVNPWYQQADE--VRFNQGEHVRVEAWAPFEEG-----------------KHAIFSNPS-------- 199
Cdd:COG0667 166 IAEGLPPiVAVQNEYSLLDRSAEEelLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdrAATNFVQGYlternlal 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489741763 200 ---IQTIAQAHGKTTGQVILRWLLQRG--ITVIPKSVHPERMAENIAVFDFELTAAEMSAMAEL 258
Cdd:COG0667 246 vdaLRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-252 |
1.55e-43 |
|
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: 149.26 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFGV-----FQVPDLNECEAAV---TAALKAGYRLIDTATAY---QNETAVGRAIQKsgLRRDELFVTSKLWV 78
Cdd:cd19137 1 GEKIPALGLGTwgiggFLTPDYSRDEEMVellKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 79 SEFTYERAKQGIDASLQRLGVDYLDLYLLHQPYGDV--MGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAV 156
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIplEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 157 NQIE---VNPWYQQADEVRFNQGEHVRVEAWAPFEEGkhAIFSNPSIQTIAQAHGKTTGQVILRWLLQR-GITVIPKSVH 232
Cdd:cd19137 159 NQVKynlEDRDPERDGLLEYCQKNGITVVAYSPLRRG--LEKTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGR 236
|
250 260
....*....|....*....|
gi 489741763 233 PERMAENIAVFDFELTAAEM 252
Cdd:cd19137 237 VEHLKENLKATEIKLSEEEM 256
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
15-255 |
1.20e-42 |
|
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: 147.67 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 15 QLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKsglRRDELFVTSK--LWVSEF-------T 82
Cdd:cd19084 13 AIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG---RRDDVVIATKcgLRWDGGkgvtkdlS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLHQPYGDV-MG-AWRALEEAYHAGKIRAIGVSNFYADQLKnlELTMSVQPAVNQIE 160
Cdd:cd19084 90 PESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTpIEeTAEALEKLKKEGKIRYIGVSNFSVEQLE--EARKYGPIVSLQPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 161 VNPWYQQADE--VRFNQGEHVRVEAWAP---------------FEEG----KHAIFSNP----------SIQTIAQAHGK 209
Cdd:cd19084 168 YSMLEREIEEelLPYCRENGIGVLPYGPlaqglltgkykkeptFPPDdrrsRFPFFRGEnfeknleivdKLKEIAEKYGK 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489741763 210 TTGQVILRWLLQR-GITVI---PKSvhPERMAENIAVFDFELTAAEMSAM 255
Cdd:cd19084 248 SLAQLAIAWTLAQpGVTSAivgAKN--PEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
28-260 |
1.62e-41 |
|
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: 144.65 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 28 ECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKsglRRDELFVTSKLWVSEFTYERAKQGIDASLQRLGVDYLDL 104
Cdd:cd19085 24 ESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNLTPEDVRKSCERSLKRLGTDYIDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 105 YLLHQPYGDV-----MGawrALEEAYHAGKIRAIGVSNFyadQLKNLELTMSVQP-AVNQIEVNP-WYQQADEV------ 171
Cdd:cd19085 101 YQIHWPSSDVpleetME---ALEKLKEEGKIRAIGVSNF---GPAQLEEALDAGRiDSNQLPYNLlWRAIEYEIlpfcre 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 172 ------------------RFNQGEHV-----RVEAWAPFEEGKHAIFSN--PSIQTIAQAHGKTTGQVILRWLLQR-GIT 225
Cdd:cd19085 175 hgigvlaysplaqglltgKFSSAEDFppgdaRTRLFRHFEPGAEEETFEalEKLKEIADELGVTMAQLALAWVLQQpGVT 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 489741763 226 -VIPKSVHPERMAENIAVFDFELTAaemSAMAELDQ 260
Cdd:cd19085 255 sVIVGARNPEQLEENAAAVDLELSP---SVLERLDE 287
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
28-259 |
6.83e-41 |
|
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: 143.14 E-value: 6.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 28 ECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGLRrDELFVTSKLWV--SEFTYERAKQGIDASLQRLGVDYL 102
Cdd:cd19093 27 DLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGDR-DEVVIATKFAPlpWRLTRRSVVKALKASLERLGLDSI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 103 DLYLLHQP---YGDVMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTMS---VQPAVNQIEVNPWYQQADE---VRF 173
Cdd:cd19093 106 DLYQLHWPgpwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKergVPLASNQVEYSLLYRDPEQnglLPA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 174 NQGEHVRVEAWAPF--------------EEGKHAIFSNPS-----------IQTIAQAHGKTTGQVILRWLLQRGITVIP 228
Cdd:cd19093 186 CDELGITLIAYSPLaqglltgkyspenpPPGGRRRLFGRKnlekvqplldaLEEIAEKYGKTPAQVALNWLIAKGVVPIP 265
|
250 260 270
....*....|....*....|....*....|.
gi 489741763 229 KSVHPERMAENIAVFDFELTAAEmsaMAELD 259
Cdd:cd19093 266 GAKNAEQAEENAGALGWRLSEEE---VAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-241 |
3.87e-36 |
|
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: 128.79 E-value: 3.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFGVFQV---PDLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGlRRDELFVTSKL--------WVS 79
Cdd:cd06660 1 SRLGLGTMTFggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRG-NRDDVVIATKGghppggdpSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 80 EFTYERAKQGIDASLQRLGVDYLDLYLLH-----QPYGDVMgawRALEEAYHAGKIRAIGVSNFYADQLKNL----ELTM 150
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHrddpsTPVEETL---EALNELVREGKIRYIGVSNWSAERLAEAlayaKAHG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 151 SVQPAVNQIEVNPWYQQADE---VRFNQGEHVRVEAWAPfeegkhaifsnpsiqtiaQAHGKTtgQVILRWLLQR--GIT 225
Cdd:cd06660 157 LPGFAAVQPQYSLLDRSPMEeelLDWAEENGLPLLAYSP------------------LARGPA--QLALAWLLSQpfVTV 216
|
250
....*....|....*.
gi 489741763 226 VIPKSVHPERMAENIA 241
Cdd:cd06660 217 PIVGARSPEQLEENLA 232
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
30-251 |
1.61e-35 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 129.12 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 30 EAAVTAALKAGYRLIDTA---TAYQNETAVGRAIQKSGLRRDELFVTSK---LWVSE----------FTYERAKQGIDAS 93
Cdd:COG4989 34 AALIEAALELGITTFDHAdiyGGYTCEALFGEALKLSPSLREKIELQTKcgiRLPSEardnrvkhydTSKEHIIASVEGS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 94 LQRLGVDYLDLYLLHQPygD-VMGAW---RALEEAYHAGKIRAIGVSNFYADQLKNLELTMSVQPAVNQIEVNPWYQQAd 169
Cdd:COG4989 114 LRRLGTDYLDLLLLHRP--DpLMDPEevaEAFDELKASGKVRHFGVSNFTPSQFELLQSALDQPLVTNQIELSLLHTDA- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 170 evrFNQG-------EHVRVEAWAPFEEGKhaIFSNPS---------IQTIAQAHGKTTGQVILRWLLQR--GITVIPKSV 231
Cdd:COG4989 191 ---FDDGtldycqlNGITPMAWSPLAGGR--LFGGFDeqfprlraaLDELAEKYGVSPEAIALAWLLRHpaGIQPVIGTT 265
|
250 260
....*....|....*....|
gi 489741763 232 HPERMAENIAVFDFELTAAE 251
Cdd:COG4989 266 NPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-251 |
4.73e-35 |
|
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: 127.67 E-value: 4.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFGVFQVPDLN----ECEAAVTAALKAGYRLIDTA---TAYQNETAVGRAIQKSGLRRDELFVTSK----- 75
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGesaeELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALALNPGLREKIEIQTKcgirl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 -----LWVSE---FTYERAKQGIDASLQRLGVDYLDLYLLHQPygDV-MGAW---RALEEAYHAGKIRAIGVSNFYADQL 143
Cdd:cd19092 81 gddprPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRP--DPlMDPEevaEAFDELVKSGKVRYFGVSNFTPSQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 144 KNLELTMSVQPAVNQIEVNPWYQQA------DEVRFNQgehVRVEAWAPFEEGKhaIFSNPS---------IQTIAQAHG 208
Cdd:cd19092 159 ELLQSYLDQPLVTNQIELSLLHTEAiddgtlDYCQLLD---ITPMAWSPLGGGR--LFGGFDerfqrlraaLEELAEEYG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489741763 209 KTTGQVILRWLLQR--GITVIPKSVHPERMAENIAVFDFELTAAE 251
Cdd:cd19092 234 VTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-258 |
1.98e-34 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 126.25 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 25 DLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKsglRRDELFVTSK---LWVSE---FTYERAKQ---GIDA 92
Cdd:cd19102 24 DDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKG---LRDRPIVATKcglLWDEEgriRRSLKPASiraECEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 93 SLQRLGVDYLDLYLLHQPYGD--VMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELT---MSVQPA----VNQIEvnp 163
Cdd:cd19102 101 SLRRLGVDVIDLYQIHWPDPDepIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIhpiASLQPPysllRRGIE--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 164 wyqqADEVRFNQGEHVRVEAWAPFEEG---------------------KHAIFSNPSIQT----------IAQAHGKTTG 212
Cdd:cd19102 178 ----AEILPFCAEHGIGVIVYSPMQSGlltgkmtpervaslpaddwrrRSPFFQEPNLARnlalvdalrpIAERHGRTVA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489741763 213 QVILRWLLQR-GIT-VIPKSVHPERMAENIAVFDFELTAAEMSAMAEL 258
Cdd:cd19102 254 QLAIAWVLRRpEVTsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
3-254 |
1.28e-31 |
|
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: 118.86 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKL-NNGVVMPQLGFGV------FQVPDLNECEAAVTAALKAGYRLIDTATAYQ---NETAVGRAIQKsglRRDELFV 72
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGCmgmsafYGPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 73 TSK--LWVSEFTYER--------AKQGIDASLQRLGVDYLDLYLLHQ-----PYGDVMGawrALEEAYHAGKIRAIGVSN 137
Cdd:cd19076 78 ATKfgIVRDPGSGFRgvdgrpeyVRAACEASLKRLGTDVIDLYYQHRvdpnvPIEETVG---AMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 138 FYADQLKNlelTMSVQP--AVnQIEVNPWYQQA-DEV------------------------------------------R 172
Cdd:cd19076 155 ASADTIRR---AHAVHPitAV-QSEYSLWTRDIeDEVlptcrelgigfvaysplgrgfltgaikspedlpeddfrrnnpR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 173 FnQGEHvrveawapFEEGKHAIFsnpSIQTIAQAHGKTTGQVILRWLLQRG--ITVIPKSVHPERMAENIAVFDFELTAA 250
Cdd:cd19076 231 F-QGEN--------FDKNLKLVE---KLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPE 298
|
....
gi 489741763 251 EMSA 254
Cdd:cd19076 299 ELAE 302
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-242 |
3.10e-31 |
|
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: 116.57 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFGVFQ------VPDLNECEAAVTAALKAGYRLIDTATAYQN-ETAVGRAIqkSGLRRDELFVTSKLW--------V 78
Cdd:cd19095 1 SVLGLGTSGigrvwgVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGthgeggrdR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 79 SEFTYERAKQGIDASLQRLGVDYLDLYLLH-----QPYGDVMgawRALEEAYHAGKIRAIGVSNFYADqlknLELTMSVQ 153
Cdd:cd19095 79 KDFSPAAIRASIERSLRRLGTDYIDLLQLHgpsddELTGEVL---ETLEDLKAAGKVRYIGVSGDGEE----LEAAIASG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 154 P--AVnQIEVNPwYQQADEVRFNQ-GEH-VRVEAWAPFEEGK--HAIFSNPSIQTIAQAH-------GKTTGQVILRWLL 220
Cdd:cd19095 152 VfdVV-QLPYNV-LDREEEELLPLaAEAgLGVIVNRPLANGRlrRRVRRRPLYADYARRPefaaeigGATWAQAALRFVL 229
|
250 260
....*....|....*....|....
gi 489741763 221 -QRGIT-VIPKSVHPERMAENIAV 242
Cdd:cd19095 230 sHPGVSsAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
10-258 |
1.23e-30 |
|
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: 116.36 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFGVFQV------PDLNECE--AAVTAALKAGYRLIDTATAY---QNETAVGRAIQksGLRRDELFVTSK--- 75
Cdd:cd19083 8 DIDVNPIGLGTNAVgghnlyPNLDEEEgkDLVREALDNGVNLLDTAFIYglgRSEELVGEVLK--EYNRNEVVIATKgah 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 LWV---SEFTYERA--KQGIDASLQRLGVDYLDLYLLHQPYGDVM--GAWRALEEAYHAGKIRAIGVSNFYADQLK---- 144
Cdd:cd19083 86 KFGgdgSVLNNSPEflRSAVEKSLKRLNTDYIDLYYIHFPDGETPkaEAVGALQELKDEGKIRAIGVSNFSLEQLKeank 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 145 -----------NL-----ELTMSVQPAVNQIEVNPWYQQA---------------DEVRFNQGEHVRVEAwapFEEGKHA 193
Cdd:cd19083 166 dgyvdvlqgeyNLlqreaEEDILPYCVENNISFIPYFPLAsgllagkytkdtkfpDNDLRNDKPLFKGER---FSENLDK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489741763 194 IfsnPSIQTIAQAHGKTTGQVILRWLLQR-GI-TVIPKSVHPERMAENIAVFDFELTAAEMSAMAEL 258
Cdd:cd19083 243 V---DKLKSIADEKGVTVAHLALAWYLTRpAIdVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-136 |
2.79e-30 |
|
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: 113.73 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFG--VFQVPDLNECEAAVTAALKAGYRLIDTATAYQN-ETAVGRAIQKsglRRDELFVTSKLWvsEFTYERAKQGI 90
Cdd:cd19100 12 SRLGFGggPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTG--ARDYEGAKRDL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489741763 91 DASLQRLGVDYLDLYLLHQP-----YGDVM---GAWRALEEAYHAGKIRAIGVS 136
Cdd:cd19100 87 ERSLKRLGTDYIDLYQLHAVdteedLDQVFgpgGALEALLEAKEEGKIRFIGIS 140
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-248 |
6.10e-30 |
|
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: 113.47 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFGVFQV---------PDLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQ----------KSGLRRDElf 71
Cdd:cd19088 2 SRLGYGAMRLtgpgiwgppADREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHpypddvviatKGGLVRTG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 72 vtSKLWVSEFTYERAKQGIDASLQRLGVDYLDLYLLHQ-----PYGDVMGAWRALEEayhAGKIRAIGVSNFYADQLKN- 145
Cdd:cd19088 80 --PGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRidpkvPFEEQLGALAELQD---EGLIRHIGLSNVTVAQIEEa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 146 LELT--MSVQpavNQIevNPWYQQADEV-RFNQGEHVRVEAWAPFEEGKHAiFSNPSIQTIAQAHGKTTGQVILRWLLQR 222
Cdd:cd19088 155 RAIVriVSVQ---NRY--NLANRDDEGVlDYCEAAGIAFIPWFPLGGGDLA-QPGGLLAEVAARLGATPAQVALAWLLAR 228
|
250 260
....*....|....*....|....*...
gi 489741763 223 G--ITVIPKSVHPERMAENIAVFDFELT 248
Cdd:cd19088 229 SpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
2-258 |
1.51e-29 |
|
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: 114.08 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 2 VPTTKL-NNGVVMPQLGFGVFQV--------PDlNECEAAVTAALKAGYRLIDTATAYQ-NETAVGRAIQKSGLRRDELF 71
Cdd:cd19144 1 IPTRTLgRNGPSVPALGFGAMGLsafygppkPD-EERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 72 VTSK-----------LWVSEfTYERAKQGIDASLQRLGVDYLDLYLLHQ-----PYGDVMGawrALEEAYHAGKIRAIGV 135
Cdd:cd19144 80 LATKfgieknvetgeYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQHRvdgktPIEKTVA---AMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 136 SNFYADQLKNlelTMSVQP--AVnQIEVNPWYQQADEVRFNQGEHVR-----VEAWAP---------------FEEG--- 190
Cdd:cd19144 156 SECSAETLRR---AHAVHPiaAV-QIEYSPFSLDIERPEIGVLDTCRelgvaIVAYSPlgrgfltgairspddFEEGdfr 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 191 -------KHAIFSNPS----IQTIAQAHGKTTGQVILRWLLQRG--ITVIPKSVHPERMAENIAVFDFELTAAEMSAMAE 257
Cdd:cd19144 232 rmaprfqAENFPKNLElvdkIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIRE 311
|
.
gi 489741763 258 L 258
Cdd:cd19144 312 I 312
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-242 |
5.71e-29 |
|
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: 110.26 E-value: 5.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 15 QLGFGVFQVPDLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKsglRRDELFVTSKL---------WVSEFT 82
Cdd:cd19086 12 GLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFgnrfdggpeRPQDFS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLHQPYGDVMG---AWRALEEAYHAGKIRAIGVSnfyADQLKNLELTM------SVQ 153
Cdd:cd19086 89 PEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDndeLFEALEKLKQEGKIRAYGVS---VGDPEEALAALrrggidVVQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 154 PAVNQIEVNPWYQQADEVRfnqgEH-----VRVeawaPFEEGkhaIFSnpsiqtiaqahGKTTgQVILRWLLQR-GI-TV 226
Cdd:cd19086 166 VIYNLLDQRPEEELFPLAE----EHgvgviARV----PLASG---LLT-----------GKLA-QAALRFILSHpAVsTV 222
|
250
....*....|....*.
gi 489741763 227 IPKSVHPERMAENIAV 242
Cdd:cd19086 223 IPGARSPEQVEENAAA 238
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
25-257 |
1.34e-27 |
|
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: 108.51 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 25 DLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKsglRRDELFVTSK---LW---VSEFTYERA--------- 86
Cdd:cd19149 31 DDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG---RRDKVVLATKcglRWdreGGSFFFVRDgvtvyknls 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 87 ----KQGIDASLQRLGVDYLDLYLLH-----QPYGDVMGawrALEEAYHAGKIRAIGVSNFYADQLKnlELTMSVQPAVN 157
Cdd:cd19149 108 pesiREEVEQSLKRLGTDYIDLYQTHwqdveTPIEETME---ALEELKRQGKIRAIGASNVSVEQIK--EYVKAGQLDII 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 158 QIEVNP-WYQQADEVRFNQGEH-VRVEAWAPFEEG-------------------KHAIFSNPS----------IQTIAQA 206
Cdd:cd19149 183 QEKYSMlDRGIEKELLPYCKKNnIAFQAYSPLEQGlltgkitpdrefdagdarsGIPWFSPENrekvlallekWKPLCEK 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489741763 207 HGKTTGQVILRWLLQRG--ITVIPKSVHPERMAENIAVFDFELTAAEMSAMAE 257
Cdd:cd19149 263 YGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
36-255 |
2.06e-27 |
|
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: 108.06 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 36 ALKAGYRLIDTATAYQN---ETAVGRAIqKSGLRRDELFVTSKLW--VSEFTYER---AK---QGIDASLQRLGVDYLDL 104
Cdd:cd19079 44 ALDLGINFFDTANVYSGgasEEILGRAL-KEFAPRDEVVIATKVYfpMGDGPNGRglsRKhimAEVDASLKRLGTDYIDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 105 YLLHQ-----PYGDVMgawRALEEAYHAGKIRAIGVSNFYADQLKNLELTM---------SVQPAVNQI------EVNPw 164
Cdd:cd19079 123 YQIHRwdyetPIEETL---EALHDVVKSGKVRYIGASSMYAWQFAKALHLAekngwtkfvSMQNHYNLLyreeerEMIP- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 165 yqqadevrFNQGEHVRVEAWAP------------------------------FEEGKHAIFSNpsIQTIAQAHGKTTGQV 214
Cdd:cd19079 199 --------LCEEEGIGVIPWSPlargrlarpwgdtterrrsttdtaklkydyFTEADKEIVDR--VEEVAKERGVSMAQV 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489741763 215 ILRWLLQRGITVIP-----KsvhPERMAENIAVFDFELTAAEMSAM 255
Cdd:cd19079 269 ALAWLLSKPGVTAPivgatK---LEHLEDAVAALDIKLSEEEIKYL 311
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
8-258 |
1.24e-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: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFGV--FQVPDLNECEAAVTAALKAGYRLIDTATAY-QNETAVGRAIQKsglRRDELFVTSKLWVSEFTYE 84
Cdd:COG1453 8 KTGLEVSVLGFGGmrLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKG---PRDKVILATKLPPWVRDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 85 RAKQGIDASLQRLGVDYLDLYLLH---------QPYGDvMGAWRALEEAYHAGKIRAIGVSnfYADQLKNLeltmsvQPA 155
Cdd:COG1453 85 DMRKDLEESLKRLQTDYIDLYLIHglnteedleKVLKP-GGALEALEKAKAEGKIRHIGFS--THGSLEVI------KEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 156 VN-------QIEVNPWYQqadevrFNQgehvrvEAWAPFEEGKH---AIFS----------NPSIQTIAQA-HGKTTGQV 214
Cdd:COG1453 156 IDtgdfdfvQLQYNYLDQ------DNQ------AGEEALEAAAEkgiGVIImkplkggrlaNPPEKLVELLcPPLSPAEW 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489741763 215 ILRWLLQR-GITVIpkSVHPERMA---ENIAVFD-FE-LTAAEMSAMAEL 258
Cdd:COG1453 224 ALRFLLSHpEVTTV--LSGMSTPEqldENLKTADnLEpLTEEELAILERL 271
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-136 |
3.50e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 103.43 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 2 VPTTKL-NNGVVMPQLGFGVfqVPDLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQksGLRRDELFVTSK-- 75
Cdd:cd19105 1 MPYRTLgKTGLKVSRLGFGG--GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKas 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489741763 76 LWVSEFTYERAKQGIDASLQRLGVDYLDLYLLH-----QPYGDVMGAWRALEEAYHAGKIRAIGVS 136
Cdd:cd19105 77 PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHgvdtpEERLLNEELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
8-260 |
6.18e-24 |
|
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: 98.84 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFG---------VFQVP---DLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKsglRRDELFV 72
Cdd:cd19091 8 RSGLKVSELALGtmtfgggggFFGAWggvDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKG---RRDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 73 TSK--LWVSEFTYERAK------QGIDASLQRLGVDYLDLYLLHQ--PYGDVMGAWRALEEAYHAGKIRAIGVSNFYADQ 142
Cdd:cd19091 85 ATKvrGRMGEGPNDVGLsrhhiiRAVEASLKRLGTDYIDLYQLHGfdALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 143 LKNLeLTMS-----VQPAVNQI-----------EVNPwyqqadevrFNQGEHVRVEAWAP----FEEGKH---------- 192
Cdd:cd19091 165 IMKA-LGISerrglARFVALQAyysllgrdlehELMP---------LALDQGVGLLVWSPlaggLLSGKYrrgqpapegs 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 193 ----AIFSNPSI------------QTIAQAHGKTTGQVILRWLLQR--GITVIPKSVHPERMAENIAVFDFELTAAEmsa 254
Cdd:cd19091 235 rlrrTGFDFPPVdrergydvvdalREIAKETGATPAQVALAWLLSRptVSSVIIGARNEEQLEDNLGAAGLSLTPEE--- 311
|
....*.
gi 489741763 255 MAELDQ 260
Cdd:cd19091 312 IARLDK 317
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
39-254 |
2.70e-23 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 96.90 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 39 AGYRLIDTATAY----------QNETAVGRAIQKSGlRRDELFVTSKlwVSEFTYERAK--------QGIDASLQRLGVD 100
Cdd:cd19081 38 AGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATK--VGFPMGPNGPglsrkhirRAVEASLRRLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 101 YLDLYLLHQ-----PYGDVMGawrALEEAYHAGKIRAIGVSNFYADQLK---------NLELTMSVQPAVN--------- 157
Cdd:cd19081 115 YIDLYQAHWddpatPLEETLG---ALNDLIRQGKVRYIGASNYSAWRLQealelsrqhGLPRYVSLQPEYNlvdresfeg 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 158 ---------QIEVNPW-----------YQQADEVrfnQGEHVRVEAWAPFE-EGKHAIFSnpSIQTIAQAHGKTTGQVIL 216
Cdd:cd19081 192 ellplcreeGIGVIPYsplaggfltgkYRSEADL---PGSTRRGEAAKRYLnERGLRILD--ALDEVAAEHGATPAQVAL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489741763 217 RWLLQR-GIT-VIPKSVHPERMAENIAVFDFELTAAEMSA 254
Cdd:cd19081 267 AWLLARpGVTaPIAGARTVEQLEDLLAAAGLRLTDEEVAR 306
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-248 |
5.26e-23 |
|
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: 95.74 E-value: 5.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFG----VFQVPDLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQksGLRRDELFVTSKL-W-VSE 80
Cdd:cd19074 1 GLKVSELSLGtwltFGGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALK--GWPRESYVISTKVfWpTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 81 FTYER---AKQ---GIDASLQRLGVDYLDLYLLHQPYGDV--MGAWRALEEAYHAGKIRAIGVSNFYADQLK-------- 144
Cdd:cd19074 79 GPNDRglsRKHifeSIHASLKRLQLDYVDIYYCHRYDPETplEETVRAMDDLIRQGKILYWGTSEWSAEQIAeahdlarq 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 145 -NLELTMSVQPAVN------QIEVNPWYQqadevrfNQGehVRVEAWAPFEEG-------------KHAIFSNP------ 198
Cdd:cd19074 159 fGLIPPVVEQPQYNmlwreiEEEVIPLCE-------KNG--IGLVVWSPLAQGlltgkyrdgipppSRSRATDEdnrdkk 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489741763 199 -------------SIQTIAQAHGKTTGQVILRWLLQR--GITVIPKSVHPERMAENIAVFDFELT 248
Cdd:cd19074 230 rrlltdenlekvkKLKPIADELGLTLAQLALAWCLRNpaVSSAIIGASRPEQLEENVKASGVKLS 294
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
25-259 |
7.11e-23 |
|
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: 95.75 E-value: 7.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 25 DLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKsglRRDELFVTSKlwvseFTYERAK-------------- 87
Cdd:cd19080 29 DREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAG---NRDRIVLATK-----YTMNRRPgdpnaggnhrknlr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 88 QGIDASLQRLGVDYLDLYLLH-----QPYGDVMgawRALEEAYHAGKIRAIGVSNF---YADQLKNL-ELTMSVQPAVNQ 158
Cdd:cd19080 101 RSVEASLRRLQTDYIDLLYVHawdftTPVEEVM---RALDDLVRAGKVLYVGISDTpawVVARANTLaELRGWSPFVALQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 159 IE----------------------VNPW-----------YQQADEVRFNQGEHVRVEAwAPFEEGKHAIFSnpSIQTIAQ 205
Cdd:cd19080 178 IEysllertperellpmaralglgVTPWsplggglltgkYQRGEEGRAGEAKGVTVGF-GKLTERNWAIVD--VVAAVAE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489741763 206 AHGKTTGQVILRWLLQRGITVIP-----KsvhPERMAENIAVFDFELTAAEmsaMAELD 259
Cdd:cd19080 255 ELGRSAAQVALAWVRQKPGVVIPiigarT---LEQLKDNLGALDLTLSPEQ---LARLD 307
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
35-258 |
4.00e-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: 93.41 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 35 AALKAGYRLIDTATAYQN---ETAVGRAIQKsglRRDELFVTSKlwVSEFTYERA----------KQGIDASLQRLGVDY 101
Cdd:cd19087 38 RALDAGINFFDTADVYGGgrsEEIIGRWIAG---RRDDIVLATK--VFGPMGDDPndrglsrrhiRRAVEASLRRLQTDY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 102 LDLYLLHQPYGDVMG--AWRALEEAYHAGKIRAIGVSNFYADQL-KNLELTM--------SVQPAVN----QIEVN---- 162
Cdd:cd19087 113 IDLYQMHHFDRDTPLeeTLRALDDLVRQGKIRYIGVSNFAAWQIaKAQGIAArrgllrfvSEQPMYNllkrQAELEilpa 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 163 ---------PW-----------YQQADEVRFNQGEHVRVEAWAPFEEGKHAIFSnpSIQTIAQAHGKTTGQVILRWLLQR 222
Cdd:cd19087 193 arayglgviPYsplagglltgkYGKGKRPESGRLVERARYQARYGLEEYRDIAE--RFEALAAEAGLTPASLALAWVLSH 270
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489741763 223 -GIT--VI-PKSvhPERMAENIAVFDFELTAAEMSAMAEL 258
Cdd:cd19087 271 pAVTspIIgPRT--LEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-136 |
4.19e-22 |
|
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: 93.00 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFG------VFQVPDLNECEAAVTAALKAGYRLIDTATAYQN-ETAVGRAIQksGLRRDELFVTSKL-----WVSEF 81
Cdd:cd19090 1 SALGLGtaglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489741763 82 TYERAKQGIDASLQRLGVDYLDLYLLHQPY----GDVM---GAWRALEEAYHAGKIRAIGVS 136
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHDPErvpwVDILapgGALEALLELKEEGLIKHIGLG 140
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-136 |
6.14e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 93.15 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 15 QLGFGVFQVPDLNEC----EAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQ----KSGLRRDELFVTSK-------- 75
Cdd:cd19099 5 SLGLGTYRGDSDDETdeeyREALKAALDSGINVIDTAINYRGgrsERLIGKALRelieKGGIKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 -------LWV------SEFTYERAKQG------------IDASLQRLGVDYLDLYLLHQPYGDVM------------GAW 118
Cdd:cd19099 85 deplrplKYLeeklgrGLIDVADSAGLrhcispayledqIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefydrleEAF 164
|
170
....*....|....*...
gi 489741763 119 RALEEAYHAGKIRAIGVS 136
Cdd:cd19099 165 EALEEAVAEGKIRYYGIS 182
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-244 |
8.63e-22 |
|
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: 91.47 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFGVFQVP-------DLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIqkSGLRRDELFVTSKL-WVSEFT 82
Cdd:cd19096 1 SVLGFGTMRLPesdddsiDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEAL--KEGPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 83 YERAKQGIDASLQRLGVDYLDLYLLH---QPYGDVM----GAWRALEEAYHAGKIRAIGVSnfYADQLKNLELTMSVQP- 154
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHglnSPEWLEKarkgGLLEFLEKAKKEGLIRHIGFS--FHDSPELLKEILDSYDf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 155 AVNQIEVNPWYQqadevRFNQGEHVRVEAWA---------PFEEGKHAiFSNPSIQTIAQAHGKTTGQVILRWLL-QRGI 224
Cdd:cd19096 157 DFVQLQYNYLDQ-----ENQAGRPGIEYAAKkgmgviimePLKGGGLA-NNPPEALAILCGAPLSPAEWALRFLLsHPEV 230
|
250 260
....*....|....*....|...
gi 489741763 225 TVIpkSV---HPERMAENIAVFD 244
Cdd:cd19096 231 TTV--LSgmsTPEQLDENIAAAD 251
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-259 |
9.41e-22 |
|
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: 92.30 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 10 GVVMPQLGFGVF-------QVPDLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKsglRRDELFVTSKL--- 76
Cdd:cd19078 1 GLEVSAIGLGCMgmshgygPPPDKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKFgfk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 77 -----WVSEFT---YERAKQGIDASLQRLGVDYLDLYLLHQ-----PYGDVMGawrALEEAYHAGKIRAIGVSNFYADQL 143
Cdd:cd19078 78 idggkPGPLGLdsrPEHIRKAVEGSLKRLQTDYIDLYYQHRvdpnvPIEEVAG---TMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 144 KNlelTMSVQP--AVnQIEVNPWYQQADEVRFNQGEHV-----------------RVEAWAPFEEG----------KHAI 194
Cdd:cd19078 155 RR---AHAVCPvtAV-QSEYSMMWREPEKEVLPTLEELgigfvpfsplgkgfltgKIDENTKFDEGddraslprftPEAL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489741763 195 FSNPS----IQTIAQAHGKTTGQVILRWLLQRG--ITVIPKSVHPERMAENIAVFDFELTAAEmsaMAELD 259
Cdd:cd19078 231 EANQAlvdlLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEE---LREIE 298
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
8-136 |
7.30e-21 |
|
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: 89.92 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFG------VFQVPDLNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQksGLRRDELFVTSK--- 75
Cdd:cd19163 8 KTGLKVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYYLATKvgr 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489741763 76 --LWVSE---FTYERAKQGIDASLQRLGVDYLDLYLLH----QPYGDVM--GAWRALEEAYHAGKIRAIGVS 136
Cdd:cd19163 86 ygLDPDKmfdFSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQIlnETLPALQKLKEEGKVRFIGIT 157
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
35-244 |
3.41e-20 |
|
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: 87.99 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 35 AALKAGYRLIDTATAYQN-------ETAVGRAIQKSGlRRDELFVTSK--------LWVSEFTYERAKQGIDASLQRLGV 99
Cdd:cd19082 25 AFVELGGNFIDTARVYGDwvergasERVIGEWLKSRG-NRDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 100 DYLDLYLLH-----QPYGDVMGawrALEEAYHAGKIRAIGVSNF----------YADQlKNLELTMSVQPAVNQIEVNP- 163
Cdd:cd19082 104 DYIDLYFLHrddpsVPVGEIVD---TLNELVRAGKIRAFGASNWsteriaeanaYAKA-HGLPGFAASSPQWSLARPNEp 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 164 -------------WYQQADEVRFN------QG----EHVRVEAWAPFEEGKHAIFSNPSI------QTIAQAHGKTTGQV 214
Cdd:cd19082 180 pwpgptlvamdeeMRAWHEENQLPvfayssQArgffSKRAAGGAEDDSELRRVYYSEENFerleraKELAEEKGVSPTQI 259
|
250 260 270
....*....|....*....|....*....|..
gi 489741763 215 ILRWLLQRGITVIP--KSVHPERMAENIAVFD 244
Cdd:cd19082 260 ALAYVLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
37-241 |
4.07e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 87.77 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 37 LKAGYRLIDTATAY----------QNETAVGRAIQKSGlRRDELFVTSKL-------WVSEFTYE-----RAKQGIDASL 94
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDRG-NRDDVVIATKVgagprdpDGGPESPEglsaeTIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 95 QRLGVDYLDLYLLH-----QPYGDVMGAWRALEEayhAGKIRAIGVSNFYADQL---------KNLELTMSVQPAVNQIE 160
Cdd:cd19752 106 RRLGTDYIDLYYAHvddrdTPLEETLEAFNELVK---AGKVRAIGASNFAAWRLerarqiarqQGWAEFSAIQQRHSYLR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 161 VNPWYQQADEVRFNQG--EHVRVE------AWAPFEEGKHAIFSNP---------------SIQTIAQAHGKTTGQVILR 217
Cdd:cd19752 183 PRPGADFGVQRIVTDEllDYASSRpdltllAYSPLLSGAYTRPDRPlpeqydgpdsdarlaVLEEVAGELGATPNQVVLA 262
|
250 260
....*....|....*....|....*.
gi 489741763 218 WLLQRGITVIP--KSVHPERMAENIA 241
Cdd:cd19752 263 WLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
31-160 |
5.79e-20 |
|
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: 87.36 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 31 AAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGlRRDELFVTSKL---WVSEFTY------ERAKQGIDASLQRLG 98
Cdd:cd19148 29 ETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGEVvrnsspARIRKEVEDSLRRLQ 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489741763 99 VDYLDLYLLHQPYGDV--MGAWRALEEAYHAGKIRAIGVSNFYADQLKNLELTM---SVQPAVNQIE 160
Cdd:cd19148 108 TDYIDLYQVHWPDPLVpiEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAplhTVQPPYNLFE 174
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-136 |
3.70e-18 |
|
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: 82.41 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFGVFQVPDLN-----ECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQksGLRRDELFVTSKL--------- 76
Cdd:cd19162 1 PRLGLGAASLGNLAragedEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489741763 77 -------WVSEFTYERAKQGIDASLQRLGVDYLDLYLLHQPYGD----VMGAWRALEEAYHAGKIRAIGVS 136
Cdd:cd19162 79 grpagadRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHllqaLTDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-253 |
3.47e-17 |
|
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: 79.78 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 3 PTTKL-NNGVVMPQLGFGV-----FQVPDLNECE--AAVTAALKAGYRLIDTATAY---QNETAVGRAIQksGLRRDELF 71
Cdd:cd19145 1 PRVKLgSQGLEVSAQGLGCmglsgDYGAPKPEEEgiALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 72 VTSKLWVSEF-----------TYERAkqGIDASLQRLGVDYLDLYLLHQ-----PYGDVMGAWRALEEayhAGKIRAIGV 135
Cdd:cd19145 79 LATKFGIHEIggsgvevrgdpAYVRA--ACEASLKRLDVDYIDLYYQHRidttvPIEITMGELKKLVE---EGKIKYIGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 136 SNFYADQLKNlelTMSVQP--AVnQIEVNPWYQQADE--VRFNQGEHVRVEAWAP----FEEGKHAIFSNPS-------- 199
Cdd:cd19145 154 SEASADTIRR---AHAVHPitAV-QLEWSLWTRDIEEeiIPTCRELGIGIVPYSPlgrgFFAGKAKLEELLEnsdvrksh 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489741763 200 -----------------IQTIAQAHGKTTGQVILRWLLQRGITV--IPKSVHPERMAENIAVFDFELTAAEMS 253
Cdd:cd19145 230 prfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGEDVvpIPGTTKIKNLNQNIGALSVKLTKEDLK 302
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-154 |
6.23e-16 |
|
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: 76.16 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 18 FGVFQVPDLNEC--EAAVTAALKAGYRLIDTATAYQN-ETAVGRAIQK--SGLRRDELFVTSK---LWVSEFTY--ERAK 87
Cdd:cd19164 23 FSYQYTTDPESIppVDIVRRALELGIRAFDTSPYYGPsEIILGRALKAlrDEFPRDTYFIITKvgrYGPDDFDYspEWIR 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489741763 88 QGIDASLQRLGVDYLDLYLLHQ----PYGDVMGAWRALEEAYHAGKIRAIGVSNFYAD---QLKNLELTMSVQP 154
Cdd:cd19164 103 ASVERSLRRLHTDYLDLVYLHDvefvADEEVLEALKELFKLKDEGKIRNVGISGYPLPvllRLAELARTTAGRP 176
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-136 |
1.02e-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: 75.26 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 24 PDLNECEAAVTAALKAGYRLIDTATAYQN-ETAVGRAIqksgLRRDELFVTSKL----WVSEFTYERAKQGIDASLQRLG 98
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFL----KRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRLK 98
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489741763 99 VDYLDLYLLHQP-----YGDVMgaWRALEEAYHAGKIRAIGVS 136
Cdd:cd19097 99 VDSLDGLLLHNPddllkHGGKL--VEALLELKKEGLIRKIGVS 139
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-136 |
3.26e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 74.22 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 28 ECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKsglRRDELFVTSKLWVSEFT----YERAKQGIDASLQRLGVD 100
Cdd:cd19104 33 EQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKG---LPAGPYITTKVRLDPDDlgdiGGQIERSVEKSLKRLKRD 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489741763 101 YLDLYLLH-----------QPYG---DVM---GAWRALEEAYHAGKIRAIGVS 136
Cdd:cd19104 110 SVDLLQLHnrigderdkpvGGTLsttDVLglgGVADAFERLRSEGKIRFIGIT 162
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
9-143 |
4.11e-15 |
|
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: 73.72 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFG-VFQV-PDLNECEAAVTAALKAGYRLIDTATAYQNETA---VGRAIQKSGLRRDELFVTSKLW---VSE 80
Cdd:cd19153 13 SPVGLGTAALGgVYGDgLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSeavLGKALAALQVPRSSYTVATKVGryrDSE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 81 FTY--ERAKQGIDASLQRLGVDYLDLYLLH-----QPYGDVMGAWRALEEAYHAGKIRAIGVSNFYADQL 143
Cdd:cd19153 93 FDYsaERVRASVATSLERLHTTYLDVVYLHdiefvDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTL 162
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
36-137 |
2.32e-14 |
|
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: 71.83 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 36 ALKAGYRLIDTATAY----------QNETAVGRAIQKSGlRRDELFVTSKL--------WVSE----FTYERAKQGIDAS 93
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRGggtrLDRENIREAVEGS 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489741763 94 LQRLGVDYLDLYLLHQPYGDV-MGAW-------------------RALEEAYHAGKIRAIGVSN 137
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPDRYTpLFGGgyytepseeedsvsfeeqlEALGELVKAGKIRHIGLSN 169
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-144 |
4.07e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 70.83 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 28 ECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKsgLRRDELFVTSKlwvseFTYERAKQG-------IDASLQRL 97
Cdd:cd19103 33 TLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTK-----FTPQIAGQSadpvadmLEGSLARL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489741763 98 GVDYLDLYLLHQPyGDVMGAWRALEEAYHAGKIRAIGVSNFYADQLK 144
Cdd:cd19103 106 GTDYIDIYWIHNP-ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIK 151
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
25-143 |
9.29e-13 |
|
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: 67.20 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 25 DLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRA-IQKSGLRrdelfVTSK---LWVSEFTYERAKQGIDASLQRL 97
Cdd:cd19075 18 TAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELgLGERGFK-----IDTKanpGVGGGLSPENVRKQLETSLKRL 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489741763 98 GVDYLDLYLLHQP-----YGDVMgawRALEEAYHAGKIRAIGVSNFYADQL 143
Cdd:cd19075 93 KVDKVDVFYLHAPdrstpLEETL---AAIDELYKEGKFKEFGLSNYSAWEV 140
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
8-251 |
2.12e-12 |
|
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: 66.13 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFGVFQ----VPDLNECEAAVTAALKAGYRLIDTATAY-----QNETAVGRaIQKSGLR--RDELFVTSK- 75
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGR-ILKRDLRpyRDELVISTKa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 ---LWVSEF------TYERAkqGIDASLQRLGVDYLDLYLLHQPYGDV-----MGawrALEEAYHAGKIRAIGVSNFYAD 141
Cdd:cd19089 85 gygMWPGPYgdggsrKYLLA--SLDQSLKRMGLDYVDIFYHHRYDPDTpleetMT---ALADAVRSGKALYVGISNYPGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 142 QLKNL-ELTMS--VQPAVNQIEVNPWYQQADEVRFNQGEH--VRVEAWAPFEEG------KHAIFSNPS----------- 199
Cdd:cd19089 160 KARRAiALLRElgVPLIIHQPRYSLLDRWAEDGLLEVLEEagIGFIAFSPLAQGlltdkyLNGIPPDSRraaeskfltee 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489741763 200 ------------IQTIAQAHGKTTGQVILRWLLQR-GITVIPKSVH-PERMAENIAVFD-FELTAAE 251
Cdd:cd19089 240 altpekleqlrkLNKIAAKRGQSLAQLALSWVLRDpRVTSVLIGASsPSQLEDNVAALKnLDFSEEE 306
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
25-110 |
2.52e-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: 66.08 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 25 DLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKSGLRRDELFVTSKL---WVSEFTYER---AK---QGIDA 92
Cdd:cd19143 29 DVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfwgGGGPPPNDRglsRKhivEGTKA 108
|
90
....*....|....*...
gi 489741763 93 SLQRLGVDYLDLYLLHQP 110
Cdd:cd19143 109 SLKRLQLDYVDLVFCHRP 126
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-259 |
2.84e-12 |
|
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: 65.72 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGV-------FQVPDlNECEAAVTAALKAGYRLIDTATAY------QNETAVGRAIQKSGLRRDELFVTSK 75
Cdd:cd19077 1 NGKLVGPIGLGLmgltwrpNPTPD-EEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 L-WVSEF-----TYERAKQGIDASLQRLG-VDYLDLYLL-----HQPYGDVMGAwraLEEAYHAGKIRAIGVSNFYADQL 143
Cdd:cd19077 80 GgLDPDTlrpdgSPEAVRKSIENILRALGgTKKIDIFEParvdpNVPIEETIKA---LKELVKEGKIRGIGLSEVSAETI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 144 KNlelTMSVQP-AVNQIEVNPW---------YQQADEVRfnqgehVRVEAWAPFEEG----------------KHAIFSN 197
Cdd:cd19077 157 RR---AHAVHPiAAVEVEYSLFsreieengvLETCAELG------IPIIAYSPLGRGlltgriksladipegdFRRHLDR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489741763 198 PS-------------IQTIAQAHGKTTGQVILRWLLQRG---ITVIPKSVHPERMAENIAVFDFELTAAEmsaMAELD 259
Cdd:cd19077 228 FNgenfeknlklvdaLQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEE---LKEIN 302
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
15-137 |
3.56e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 65.65 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 15 QLGFGVFQVPDLN---ECEAAVTAALKAGYRLIDTATAYQ----------NETAVGRAIQKSGlRRDELFVTSKlwVS-- 79
Cdd:PRK10625 15 TLGLGTMTFGEQNseaDAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASK--VSgp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 80 ----------EFTYERA--KQGIDASLQRLGVDYLDLYLLHQP------YGDVMGAW-------------RALEEAYHAG 128
Cdd:PRK10625 92 srnndkgirpNQALDRKniREALHDSLKRLQTDYLDLYQVHWPqrptncFGKLGYSWtdsapavslletlDALAEQQRAG 171
|
....*....
gi 489741763 129 KIRAIGVSN 137
Cdd:PRK10625 172 KIRYIGVSN 180
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
9-109 |
1.75e-11 |
|
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: 63.64 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVFQV--PDLNE--CEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKSGLRRDELFVTSKLWVSEF 81
Cdd:cd19142 9 SGLRVSNVGLGTWSTfsTAISEeqAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIYWSYG 88
|
90 100 110
....*....|....*....|....*....|....
gi 489741763 82 TYERA------KQGIDASLQRLGVDYLDLYLLHQ 109
Cdd:cd19142 89 SEERGlsrkhiIESVRASLRRLQLDYIDIVIIHK 122
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
9-263 |
6.54e-11 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 61.93 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVFQ----VPDLNECEAAVTAALKAGYRLIDTATAY-----QNETAVGRAIQKS-GLRRDELFVTSK--- 75
Cdd:PRK09912 21 SGLRLPALSLGLWHnfghVNALESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDfAAYRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 -LWVSEFTYERAKQ----GIDASLQRLGVDYLDLYLLHQ-----PYGDVMGawrALEEAYHAGKIRAIGVSNF------- 138
Cdd:PRK09912 101 dMWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSHRvdentPMEETAS---ALAHAVQSGKALYVGISSYspertqk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 139 YADQLKNLELTMSV-QPAVNQIevNPWYQQADEVRFNQGEHVRVEAWAPFEEG--------------------------K 191
Cdd:PRK09912 178 MVELLREWKIPLLIhQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrglT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 192 HAIFSNPSIQTI------AQAHGKTTGQVILRWLL--QRGITVIPKSVHPERMAENI-AVFDFELTAAEmsaMAELDQGV 262
Cdd:PRK09912 256 PKMLTEANLNSLrllnemAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVqALNNLTFSTEE---LAQIDQHI 332
|
.
gi 489741763 263 S 263
Cdd:PRK09912 333 A 333
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
8-136 |
1.22e-10 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 60.95 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFG------VFQVPDLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKSGLRRDELFVTSKL-- 76
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCgr 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 77 WVS--EFTYERAKQGIDASLQRLGVDYLDLYLLH--------QPYGDVMGAWRALEEayhAGKIRAIGVS 136
Cdd:PLN02587 86 YGEgfDFSAERVTKSVDESLARLQLDYVDILHCHdiefgsldQIVNETIPALQKLKE---SGKVRFIGIT 152
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
53-253 |
1.87e-10 |
|
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: 60.55 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 53 ETAVGRaIQKSGLR--RDELFVTSK----LWVSEFTYERAKQ----GIDASLQRLGVDYLDLYLLHQ-----PYGDVMGa 117
Cdd:cd19150 61 EENFGR-ILREDFAgyRDELIISTKagydMWPGPYGEWGSRKyllaSLDQSLKRMGLDYVDIFYSHRfdpdtPLEETMG- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 118 wrALEEAYHAGKIRAIGVSNF-------YADQLKNLELTMSV-QPAVNQIevNPWYQQADEVRFNQGEHVRVEAWAPFEE 189
Cdd:cd19150 139 --ALDHAVRSGKALYVGISSYspertreAAAILRELGTPLLIhQPSYNML--NRWVEESGLLDTLQELGVGCIAFTPLAQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 190 G----------------------------KHAIFSNPSIQTIAQAHGKTTGQVILRWLLQRG--ITVIPKSVHPERMAEN 239
Cdd:cd19150 215 GlltdkylngipegsraskerslspkmltEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEEN 294
|
250
....*....|....*
gi 489741763 240 IAVFD-FELTAAEMS 253
Cdd:cd19150 295 VGALDnLTFSADELA 309
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-255 |
2.77e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 59.92 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 22 QVPDLNECEAAVTAALKAGYRLIDTATAYQN-ETAVGRAI---QKSGLRRDELFVTSKlWV-----SEFTYERAKQGIDA 92
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRkrlRRERDAADDVQIHTK-WVpdpgeLTMTRAYVEAAIDR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 93 SLQRLGVDYLDLYLLH-QPYGD--VMGAWRALEEAYHAGKIRAIGVSNFYADQLKNLeLTMSVQPAVNQI---------- 159
Cdd:cd19101 97 SLKRLGVDRLDLVQFHwWDYSDpgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREI-LDAGVPIVSNQVqyslldrrpe 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 160 -EVNPWYQQ----------------------ADEVRFNQGEHVR-------VEA---WAPFEEGKHAifsnpsIQTIAQA 206
Cdd:cd19101 176 nGMAALCEDhgikllaygtlaggllsekylgVPEPTGPALETRSlqkyklmIDEwggWDLFQELLRT------LKAIADK 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489741763 207 HGKTTGQVILRWLLQR--------GITVIpksvhpERMAENIAVFDFELTAAEMSAM 255
Cdd:cd19101 250 HGVSIANVAVRWVLDQpgvagvivGARNS------EHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
9-241 |
1.89e-09 |
|
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: 57.36 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVF-----QVPDlNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGLRRDELFVTSKL-WVS 79
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 80 EFTYERAK------QGIDASLQRLGVDYLDLYLLHQPYGD--VMGAWRALEEAYHAGKIRAIGVSNFYADQLKNL----- 146
Cdd:cd19159 88 KAETERGLsrkhiiEGLKGSLQRLQLEYVDVVFANRPDSNtpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAysvar 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 147 ELTMsVQPAVNQIEVNPWYQQADEVRFNQGEH---VRVEAWAPF---------------------------------EEG 190
Cdd:cd19159 168 QFNM-IPPVCEQAEYHLFQREKVEVQLPELYHkigVGAMTWSPLacgiisgkygngvpessraslkcyqwlkerivsEEG 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489741763 191 KHAIFSNPSIQTIAQAHGKTTGQVILRWLLQ-RGI-TVIPKSVHPERMAENIA 241
Cdd:cd19159 247 RKQQNKLKDLSPIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLG 299
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-135 |
4.48e-09 |
|
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: 56.08 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFG------VFQVPDLNECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQksGLRRDELFVTSKL-W------ 77
Cdd:cd19152 1 PKLGFGtaplgnLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR--ELGREDYVISTKVgRllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 78 ------------------VSEFTYERAKQGIDASLQRLGVDYLDLYLLHQP-------------YGDVMGAWRALEEAYH 126
Cdd:cd19152 79 eveptfepgfwnplpfdaVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPdedlagaesdehfAQAIKGAFRALEELRE 158
|
....*....
gi 489741763 127 AGKIRAIGV 135
Cdd:cd19152 159 EGVIKAIGL 167
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-134 |
4.08e-08 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 53.48 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 14 PQLGFGVFQVPDLN------ECEAAVTAALKAGYRLIDTATAYQN---ETAVGRAIQKsgLRRDELFVTSKL-------- 76
Cdd:cd19161 1 SELGLGTAGLGNLYtavsnaDADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkpar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 77 ---------WVSE--------FTYERAKQGIDASLQRLGVDYLDLYLLHQ--PY--GD----------VMGAWRALEEAY 125
Cdd:cd19161 79 egsvpdpngFVDPlpfeivydYSYDGIMRSFEDSLQRLGLNRIDILYVHDigVYthGDrkerhhfaqlMSGGFKALEELK 158
|
....*....
gi 489741763 126 HAGKIRAIG 134
Cdd:cd19161 159 KAGVIKAFG 167
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
8-144 |
4.98e-08 |
|
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: 53.18 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 8 NNGVVMPQLGFGVFQ----VPDLNECEAAVTAALKAGYRLIDTATAY-----QNETAVGRaIQKSGLR--RDELFVTSK- 75
Cdd:cd19151 7 RSGLKLPAISLGLWHnfgdVDRYENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGR-ILKEDLKpyRDELIISTKa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 76 ---LWVSEFTYERAKQ----GIDASLQRLGVDYLDLYLLHQPYGDV-----MGawrALEEAYHAGKIRAIGVSNFYADQL 143
Cdd:cd19151 86 gytMWPGPYGDWGSKKyliaSLDQSLKRMGLDYVDIFYHHRPDPETpleetMG---ALDQIVRQGKALYVGISNYPPEEA 162
|
.
gi 489741763 144 K 144
Cdd:cd19151 163 R 163
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
16-110 |
7.27e-08 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 52.83 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 16 LGFGVF-----QVPDlNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGLRRDELFVTSKL-WVSEFTYERA 86
Cdd:cd19141 15 LGLGTWvtfgsQISD-EVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKKGWRRSSYVITTKIfWGGKAETERG 93
|
90 100 110
....*....|....*....|....*....|
gi 489741763 87 ---KQ---GIDASLQRLGVDYLDLYLLHQP 110
Cdd:cd19141 94 lsrKHiieGLKASLERLQLEYVDIVFANRP 123
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
15-259 |
1.77e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 51.51 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 15 QL-GFGVFQVP-DLNECEAAVTAALKAGYRLIDTATAYQNEtaVGRAIQKSGLR--RDELFVTSKL---------WVSEF 81
Cdd:PRK10376 26 QLaGPGVFGPPkDRDAAIAVLREAVALGVNHIDTSDFYGPH--VTNQLIREALHpyPDDLTIVTKVgarrgedgsWLPAF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 82 TYERAKQGIDASLQRLGVDYLDLYLLhQPYGDVMG-AWRALEEAYHA-------GKIRAIGVSNFYADQL---KNLELTM 150
Cdd:PRK10376 104 SPAELRRAVHDNLRNLGLDVLDVVNL-RLMGDGHGpAEGSIEEPLTVlaelqrqGLVRHIGLSNVTPTQVaeaRKIAEIV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 151 SVQpavNQIEVnpwYQQADEVRFNQGEHVRVeAWAP-FEEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQRG--ITVI 227
Cdd:PRK10376 183 CVQ---NHYNL---AHRADDALIDALARDGI-AYVPfFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLI 255
|
250 260 270
....*....|....*....|....*....|..
gi 489741763 228 PKSVHPERMAENIAVFDFELTAAemsAMAELD 259
Cdd:PRK10376 256 PGTSSVAHLRENLAAAELVLSEE---VLAELD 284
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
9-259 |
2.40e-07 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 51.24 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVF-----QVPDlNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGLRRDELFVTSKL-WVS 79
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITD-EMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 80 EFTYERAK------QGIDASLQRLGVDYLDLYLLHQPYGD--VMGAWRALEEAYHAGKIRAIGVSNFYADQLknleltMS 151
Cdd:cd19158 88 KAETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPDPNtpMEETVRAMTHVINQGMAMYWGTSRWSSMEI------ME 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 152 VQPAVNQIEVNPWYQQADEVRFNQGEHVRVE-------------AWAPF------------------------------- 187
Cdd:cd19158 162 AYSVARQFNLIPPICEQAEYHMFQREKVEVQlpelfhkigvgamTWSPLacgivsgkydsgippysraslkgyqwlkdki 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489741763 188 --EEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQ-RGI-TVIPKSVHPERMAENIAVFDFeLTAAEMSAMAELD 259
Cdd:cd19158 242 lsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNAEQLMENIGAIQV-LPKLSSSIVHEID 316
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
9-104 |
1.34e-06 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 48.83 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 9 NGVVMPQLGFGVF-----QVPDlNECEAAVTAALKAGYRLIDTATAY---QNETAVGRAIQKSGLRRDELFVTSKL-WVS 79
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISD-ETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVVTTKIyWGG 89
|
90 100 110
....*....|....*....|....*....|.
gi 489741763 80 EFTYERAK------QGIDASLQRLGVDYLDL 104
Cdd:cd19160 90 QAETERGLsrkhiiEGLRGSLDRLQLEYVDI 120
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
39-253 |
8.58e-06 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 46.36 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 39 AGYRLIDTATAYQN---ETAVGRAIQKSGLrRDELFVTSKLwvsEFTYERAKQG------------------IDASLQRL 97
Cdd:cd19147 46 AGGNFIDTANNYQDeqsETWIGEWMKSRKN-RDQIVIATKF---TTDYKAYEVGkgkavnycgnhkrslhvsVRDSLRKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 98 GVDYLDLYLLHqpYGDVMGAWRALEEAYH----AGKIRAIGVS----------NFYADQ--------------LKNLELT 149
Cdd:cd19147 122 QTDWIDILYVH--WWDYTTSIEEVMDSLHilvqQGKVLYLGVSdtpawvvsaaNYYATAhgktpfsvyqgrwnVLNRDFE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 150 MSVQPAVNQ--IEVNPW-------YQQAD--EVRFNQGEHVRvEAWAPFEEGKHAIFSNPSIQTIAQAHGKTT-GQVILR 217
Cdd:cd19147 200 RDIIPMARHfgMALAPWdvlgggkFQSKKavEERKKNGEGLR-SFVGGTEQTPEEVKISEALEKVAEEHGTESvTAIALA 278
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489741763 218 WLLQRGITVIP----KSVhpERMAENIAVFDFELTAAEMS 253
Cdd:cd19147 279 YVRSKAPNVFPlvggRKI--EHLKDNIEALSIKLTPEEIE 316
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-269 |
1.39e-04 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 42.72 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 27 NECEAAVTAALKAGYRLIDTATAY-QNETAVGRAIQKSGLRRDELFVTSKlW----------------VSEFTYERAKQG 89
Cdd:cd19098 35 AHTHAVLDAAWAAGVRYFDAARSYgRAEEFLGSWLRSRNIAPDAVFVGSK-WgytytadwqvdaavheVKDHSLARLLKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 90 IDASLQRLGvDYLDLYLLHQPYGD--VMGAWR---ALEEAYHAGkiRAIGVSNFYADQLKNLELTM-----------SVQ 153
Cdd:cd19098 114 WEETRSLLG-KHLDLYQIHSATLEsgVLEDADvlaALAELKAEG--VKIGLSLSGPQQAETLRRALeieidgarlfdSVQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 154 PAVNQIEVNPwyQQADEVRFNQGEHVRV-EAWA-----PFEEGKHAIFSNPSIQTIAQAHGKTTGQVILRWLLQRGIT-- 225
Cdd:cd19098 191 ATWNLLEQSA--GEALEEAHEAGMGVIVkEALAngrltDRNPSPELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVdv 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489741763 226 VIPKSVHPERMAENIAVFDFELTAAEMSAMAELDQGVSQFFDHR 269
Cdd:cd19098 269 VLSGAATPEQLRSNLRALDVSLDLELLAALADLAEPPEDYWATR 312
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
39-252 |
1.60e-04 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 42.41 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 39 AGYRLIDTATAYQNETA---VGRAIQKSGlRRDELFVTSKLWVSEFTYERAK-----QG---------IDASLQRLGVDY 101
Cdd:cd19146 47 QGGNFIDTANNYQGEESerwVGEWMASRG-NRDEMVLATKYTTGYRRGGPIKiksnyQGnhakslrlsVEASLKKLQTSY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 102 LDLYLLH-----QPYGDVMgawRALEEAYHAGKIRAIGVS----------NFYAdqlKNLELTMSV------QPAVNQIE 160
Cdd:cd19146 126 IDILYVHwwdytTSIPELM---QSLNHLVAAGKVLYLGVSdtpawvvskaNAYA---RAHGLTQFVvyqghwSAAFRDFE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741763 161 -------------VNPW-------YQQADEvrFNQGEHVRVEAWAPFEegKHAIFSNpSIQTIAQAHGKTTGQVILRWLL 220
Cdd:cd19146 200 rdilpmceaegmaLAPWgvlgqgqFRTEEE--FKRRGRSGRKGGPQTE--KERKVSE-KLEKVAEEKGTAITSVALAYVM 274
|
250 260 270
....*....|....*....|....*....|....*.
gi 489741763 221 QRGITVIP----KSVhpERMAENIAVFDFELTAAEM 252
Cdd:cd19146 275 HKAPYVFPivggRKV--EHLKGNIEALGISLSDEEI 308
|
|
| |
