|
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 ... |
4-258 |
4.06e-177 |
|
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: 488.24 E-value: 4.06e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYE 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 84 SAKIAFSKSLSKLQLDYLDLYLIHQPYGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHPF 163
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHPF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 164 YQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFD 243
Cdd:cd19133 161 NQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFD 240
|
250
....*....|....*
gi 1070084393 244 FELSLEDIEQISTLD 258
Cdd:cd19133 241 FELSDEDMEAIAALD 255
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-270 |
9.34e-144 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 404.05 E-value: 9.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 8 NGVKMPIIGFGVYQVPDaQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYESAKI 87
Cdd:COG0656 1 NGVEIPALGLGTWQLPG-EEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 88 AFSKSLSKlqldyldlyLIHQPY-GDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQ 166
Cdd:COG0656 80 AFEESLERlgldyldlyLIHWPGpGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 167 KESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFEL 246
Cdd:COG0656 160 RELLAFCREHGIVVEAYSPLGRGK--LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFEL 237
|
250 260
....*....|....*....|....
gi 1070084393 247 SLEDIEQISTLDKGESLFgshRDP 270
Cdd:COG0656 238 SDEDMAAIDALDRGERLG---PDP 258
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
3-270 |
1.18e-120 |
|
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: 345.92 E-value: 1.18e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 3 TVTLNNGVKMPIIGFGVYQVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGY 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 83 ESAKIAFSKSLSKLQLDYLDLYLIHQPYGD-YYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETH 161
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGkYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 162 PFYQQKESAAFMKAQGVQHESWAPFAEGrnNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDI 241
Cdd:cd19157 161 PRLTQKELRDYCKKQGIQLEAWSPLMQG--QLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADV 238
|
250 260
....*....|....*....|....*....
gi 1070084393 242 FDFELSLEDIEQISTLDKGESLFgshRDP 270
Cdd:cd19157 239 FDFELSQEDMDKIDALNENLRVG---PDP 264
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
12-254 |
1.79e-115 |
|
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: 332.14 E-value: 1.79e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 12 MPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYESAKIAFSK 91
Cdd:cd19071 1 MPLIGLGTYKLKPE-ETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 92 SLSKLQLDYLDLYLIHQPY--------GDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHPF 163
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVpgkeggskEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 164 YQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFD 243
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|.
gi 1070084393 244 FELSLEDIEQI 254
Cdd:cd19071 240 FELSEEDMAAI 250
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-258 |
1.21e-113 |
|
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: 327.47 E-value: 1.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYE 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 84 SAKIAFSKSLSKLQLDYLDLYLIHQPYGDYY-GAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHP 162
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHWPGKDKFiDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 163 FYQQKESAAFMKAQGVQHESWAPFaeGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIF 242
Cdd:cd19126 161 YLTQKELRGYCKSKGIVVEAWSPL--GQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIF 238
|
250
....*....|....*.
gi 1070084393 243 DFELSLEDIEQISTLD 258
Cdd:cd19126 239 DFELSEDDMTAIDALN 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
3-258 |
3.35e-111 |
|
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: 321.63 E-value: 3.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 3 TVTLNNGVKMPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGY 82
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSND-EAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 83 ESAKIAFSKSLSKLQLDYLDLYLIHQP---YGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVE 159
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPvpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 160 THPFYQQKESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENF 239
Cdd:cd19131 160 LHPRFQQRELRAFHAKHGIQTESWSPLGQGG--LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENF 237
|
250
....*....|....*....
gi 1070084393 240 DIFDFELSLEDIEQISTLD 258
Cdd:cd19131 238 DVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
4-258 |
3.00e-109 |
|
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: 317.04 E-value: 3.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQVPdAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYE 83
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP-PEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 84 SAKIAFSKSLSKLQLDYLDLYLIHQP----YGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVE 159
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPvpndFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 160 THPFYQQKESAAFMKAQGVQHESWAPF----------AEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKS 229
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgPTGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKS 239
|
250 260
....*....|....*....|....*....
gi 1070084393 230 VRKERIVENFDIFDFELSLEDIEQISTLD 258
Cdd:cd19127 240 VHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-261 |
2.66e-108 |
|
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: 314.46 E-value: 2.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYE 83
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 84 SAKIAFSKSLSKLQLDYLDLYLIHQPYGD-YYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHP 162
Cdd:cd19156 81 STLAAFEESLEKLGLDYVDLYLIHWPVKGkFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 163 FYQQKESAAFMKAQGVQHESWAPFAEGrnNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIF 242
Cdd:cd19156 161 LLTQEPLRKFCKEKNIAVEAWSPLGQG--KLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVF 238
|
250
....*....|....*....
gi 1070084393 243 DFELSLEDIEQISTLDKGE 261
Cdd:cd19156 239 DFELTAEEIRQIDGLNTDH 257
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
12-257 |
3.32e-92 |
|
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: 273.35 E-value: 3.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 12 MPIIGFGVYQVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRS----GVPREELFITTKLWIQDAGYESAKI 87
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 88 AFSKSLSKLQLDYLDLYLIHQPygdyyGA-----------------WRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNE 150
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP-----GVqglkpsdprnaelrresWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 151 IVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSV 230
Cdd:cd19136 156 VPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKST 235
|
250 260
....*....|....*....|....*..
gi 1070084393 231 RKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19136 236 NPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
6-258 |
3.96e-91 |
|
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: 270.68 E-value: 3.96e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 6 LNNGVKMPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYESA 85
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGD-EGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 86 KIAFSKSLSKLQLDYLDLYLIHQP---YGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHP 162
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHWPnpsRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 163 FYQQKESAAFMKAQGVQHESWAPFAEGrNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIF 242
Cdd:cd19132 160 YFPQAEQRAYHREHGIVTQSWSPLGRG-SGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIF 238
|
250
....*....|....*.
gi 1070084393 243 DFELSLEDIEQISTLD 258
Cdd:cd19132 239 DFELSDEDMAAIAALD 254
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-257 |
2.14e-90 |
|
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: 269.19 E-value: 2.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTLNNGVKMPIIGFGVYQVpdAQECENAVYEAL-MAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQD 79
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTSHS--GGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 80 AGYESAKIAFSKSLSKLQLDYLDLYLIHQPYGDYYG---------AWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNE 150
Cdd:cd19135 80 YGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketraeTWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 151 IVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSV 230
Cdd:cd19135 160 VVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK--ALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKST 237
|
250 260
....*....|....*....|....*..
gi 1070084393 231 RKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19135 238 KEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-263 |
1.65e-88 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 264.63 E-value: 1.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTV-TLNNGVKMPIIGFGVYQVPDaQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQD 79
Cdd:PRK11565 3 NPTViKLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 80 agYESAKIAFSKSLSKLQLDYLDLYLIHQPY---GDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVN 156
Cdd:PRK11565 82 --HKRPREALEESLKKLQLDYVDLYLMHWPVpaiDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 157 QVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIV 236
Cdd:PRK11565 160 QIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIA 239
|
250 260
....*....|....*....|....*..
gi 1070084393 237 ENFDIFDFELSLEDIEQISTLDKGESL 263
Cdd:PRK11565 240 ENFDVFDFRLDKDELGEIAKLDQGKRL 266
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-264 |
1.04e-86 |
|
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: 260.68 E-value: 1.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 3 TVTLNNGVKMPIIGFGVYQVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRA----IKRSGVPREELFITTKLWIQ 78
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 79 DAGYESAKIAFSKSLSKLQLDYLDLYLIHQPYG------------------DYYGAWRAMEDLYREGKIRAIGVSNFHpD 140
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAfkenndsesngdgslsdiDYLETWRGMEDLVKLGLTRSIGVSNFN-S 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 141 RLMDLILHN-EIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFaeGRNNM---------FSNEVLTSIAEKHNKSV 210
Cdd:cd19116 161 EQINRLLSNcNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPF--GRLVPrgqtnppprLDDPTLVAIAKKYGKTT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1070084393 211 AQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKGESLF 264
Cdd:cd19116 239 AQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
3-263 |
2.03e-85 |
|
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: 256.32 E-value: 2.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 3 TVTLNNGVKMPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGY 82
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDD-EAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 83 ESAKIAFSKSLSKLQLDYLDLYLIHQPYGD---YYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVE 159
Cdd:cd19134 81 TASQAACRASLERLGLDYVDLYLIHWPAGRegkYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 160 THPFYQQKESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENF 239
Cdd:cd19134 161 LHPLLNQAELRKVNAQHGIVTQAYSPLGVGR--LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNL 238
|
250 260
....*....|....*....|....
gi 1070084393 240 DIFDFELSLEDIEQISTLDKGESL 263
Cdd:cd19134 239 DVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
4-258 |
4.25e-85 |
|
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: 255.22 E-value: 4.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQVPDAQEcENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYE 83
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPPADT-QRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 84 SAKIAFSKSLSKLQLDYLDLYLIHQPY---GDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVET 160
Cdd:cd19130 81 EPAAAFAESLAKLGLDQVDLYLVHWPTpaaGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 161 HPFYQQKESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFD 240
Cdd:cd19130 161 HPAYQQRTIRDWAQAHDVKIEAWSPLGQGK--LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLD 238
|
250
....*....|....*...
gi 1070084393 241 IFDFELSLEDIEQISTLD 258
Cdd:cd19130 239 VFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-264 |
1.88e-81 |
|
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: 247.71 E-value: 1.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKR---SGV-PREELFITTKLWIQD 79
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSKGA-EGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 80 AGYESAKIAFSKSLSKLQLDYLDLYLIHQPYG---------------------DYYGAWRAMEDLYREGKIRAIGVSNFH 138
Cdd:cd19154 83 HAPEDVEEALRESLKKLQLEYVDLYLIHAPAAfkddegesgtmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVSNFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 139 PDRlMDLILHN-EIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAE-GRN------------NMFSNEVLTSIAE 204
Cdd:cd19154 163 NDQ-IQRILDNaRVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpGRAnftkstgvspapNLLQDPIVKAIAE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 205 KHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKGESLF 264
Cdd:cd19154 242 KHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
12-254 |
1.28e-79 |
|
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: 240.64 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 12 MPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYESAKIAFSK 91
Cdd:cd19073 1 IPALGLGTWQLRGD-DCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 92 SLSKLQLDYLDLYLIHQPYGDYYGA--WRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKES 169
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWPNPTVPLEetLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 170 AAFMKAQGVQHESWAPFAEGrnNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLE 249
Cdd:cd19073 160 LEYCRENDIVITAYSPLARG--EVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSE 237
|
....*
gi 1070084393 250 DIEQI 254
Cdd:cd19073 238 DVAKI 242
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
5-257 |
4.27e-78 |
|
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: 238.40 E-value: 4.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 5 TLNNGVKMPIIGFGVYQVpDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSG----VPREELFITTKLWIQDA 80
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQA-DPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 81 GYESAKIAFSKSLSKLQLDYLDLYLIHQPYG----------------DYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMD 144
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpepeevlppDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 145 LILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPF-----AEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLV 219
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgtTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 1070084393 220 QREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
8-257 |
6.47e-78 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 236.77 E-value: 6.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 8 NGVKMPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYESAKI 87
Cdd:cd19140 4 NGVRIPALGLGTYPLTGE-ECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 88 AFSKSLSKLQLDYLDLYLIHQPYGDYYGAW--RAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQVETHPFYQ 165
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWPNKDVPLAEtlGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 166 QKESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQRE-VVTIPKSVRKERIVENFDIFDF 244
Cdd:cd19140 163 QRKLLDAAREHGIALTAYSPLARGE--VLKDPVLQEIGRKHGKTPAQVALRWLLQQEgVAAIPKATNPERLEENLDIFDF 240
|
250
....*....|...
gi 1070084393 245 ELSLEDIEQISTL 257
Cdd:cd19140 241 TLSDEEMARIAAL 253
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-259 |
1.91e-74 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 229.31 E-value: 1.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 2 QTVTLNNGVKMPIIGFGVYQ-VPDaqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLW---- 76
Cdd:cd19117 4 KTFKLNTGAEIPAVGLGTWQsKPN--EVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWctwh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 77 --IQDAGYESAK---------------IAFSKSLSKLQLDYLDLYLIHQPYGDYYGAWRAMEDLYREGKIRAIGVSNFHP 139
Cdd:cd19117 82 rrVEEALDQSLKklgldyvdlylmhwpVPLDPDGNDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 140 DRLMDLI--LHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTSIAEKHNKSVAQVVLRW 217
Cdd:cd19117 162 KNLEKLLasPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTPAQVIISW 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1070084393 218 LVQREVVTIPKSVRKERIVENFDIfdFELSLEDIEQISTLDK 259
Cdd:cd19117 242 GLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
6-264 |
1.07e-73 |
|
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: 228.04 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 6 LNNGVKMPIIGFGVYQVPDAQeCENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRS-----GVPREELFITTKLWIQDA 80
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQ-VKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 81 GYESAKIAFSKSLSKLQLDYLDLYLIHQPYG---------------------DYYGAWRAMEDLYREGKIRAIGVSNFHP 139
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAfergdnpfpknpdgtirydstHYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 140 DRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPF--------AEGRNNMFSNEVLTSIAEKHNKSVA 211
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwaKPDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1070084393 212 QVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKGESLF 264
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-260 |
9.62e-72 |
|
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: 223.07 E-value: 9.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 2 QTVTLNNGVKMPIIGFGVYQVPDAQeCENAVYEALMAGYRLIDTASGYLNE----EAVGRAIKRSGVPREELFITTKLWI 77
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLWKVNNDT-CADQVYNAIKAGYRLFDGACDYGNEveagQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 78 QDAGYESAKIAFSKSLSKLQLDYLDLYLIHQP----YGD----------------------YYGAWRAMEDLYREGKIRA 131
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPialkYVDpavryppgwfydgkkvefsnapIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 132 IGVSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPF------------AEGRNNMFSNEVL 199
Cdd:cd19115 162 IGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFgpqsfleldlpgAKDTPPLFEHDVI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1070084393 200 TSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKG 260
Cdd:cd19115 242 KSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIG 302
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
9-256 |
1.22e-71 |
|
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: 221.34 E-value: 1.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGV----YQVPDA---QECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWiqdAG 81
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiqRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVS---PG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 82 YESAKIAFSKSLSKLQLDYLDLYLIHQPY------GDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAV 155
Cdd:cd19120 78 IKDPREALRKSLAKLGVDYVDLYLIHSPFfakeggPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 156 NQVETHPF--YQQKESAAFMKAQGVQHESW---APFAEGRNNMFsNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSV 230
Cdd:cd19120 158 NQIEFHPYlyPQQPALLEYCREHGIVVSAYsplSPLTRDAGGPL-DPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSS 236
|
250 260
....*....|....*....|....*.
gi 1070084393 231 RKERIVENFDIFDFELSLEDIEQIST 256
Cdd:cd19120 237 KEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
2-260 |
1.26e-71 |
|
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: 222.71 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 2 QTVTLNNGVKMPIIGFGVYQVPDAQeCENAVYEALMAGYRLIDTASGYLNEEAVG----RAIKRSGVPREELFITTKLWI 77
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNAT-AADQIYQAIKAGYRLFDGAEDYGNEKEVGegvnRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 78 QDAGYESAKIAFSKSLSKLQLDYLDLYLIH-------------QPYGDYYGA--------------WRAMEDLYREGKIR 130
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHfpiafkfvpieekYPPGFYCGDgdnfvyedvpildtWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 131 AIGVSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQ---HESWAP--FAEGRNN-------MFSNEV 198
Cdd:cd19113 160 SIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITitaYSSFGPqsFVELNQGralntptLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1070084393 199 LTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKG 260
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIG 301
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
8-257 |
4.02e-71 |
|
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: 220.60 E-value: 4.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 8 NGVKMPIIGFGVY-QVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIK---RSGV--PREELFITTKLWIQDAG 81
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGLvkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 82 YESAKIAFSKSLSKLQLDYLDLYLIHQPYG------------------DYYGAWRAMEDLYREGKIRAIGVSNFHPDRLM 143
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSlkpgkfsfpieeedflpfDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 144 DLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTS-----IAEKHNKSVAQVVLRWL 218
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSNAVMESdvlkeIAAAKGKTVAQVSLRWV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1070084393 219 VQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-264 |
1.31e-70 |
|
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: 220.09 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQVPDaQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKR---SG-VPREELFITTKLWIQD 79
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSP-EEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 80 AGYESAKIAFSKSLSKLQLDYLDLYLIHQPYG-----------------------DYYGAWRAMEDLYREGKIRAIGVSN 136
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGslskeddsgkldptgehkqdyttDLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 137 FHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPF-AEGRNN--------------MFSNEVLTS 201
Cdd:cd19155 163 FNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgSPGAAHfspgtgspsgsspdLLQDPVVKA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070084393 202 IAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKGESLF 264
Cdd:cd19155 243 IAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-264 |
1.96e-69 |
|
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: 216.89 E-value: 1.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTLNNGVKMPIIGFGVYQvPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAI----KRSGVPREELFITTKLW 76
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWK-SKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 77 IQDAGYESAKIAFSKSLSKLQLDYLDLYLIHQPYG------------DYYG--------AWRAMEDLYREGKIRAIGVSN 136
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVAlkkgvgfpesgeDLLSlspipledTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 137 FHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPF----------AEGRNNMFSNEVLTSIAEKH 206
Cdd:cd19123 160 FSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLgsgdrpaamkAEGEPVLLEDPVINKIAEKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1070084393 207 NKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKGESLF 264
Cdd:cd19123 240 GASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
9-264 |
2.34e-68 |
|
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: 213.51 E-value: 2.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIK---RSG-VPREELFITTKLWIQDAGYES 84
Cdd:cd19111 1 GFPMPVIGLGTYQSPPE-EVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 85 AKIAFSKSLSKLQLDYLDLYLIHQPYG---------------DYYGAWRAMEDLYREGKIRAIGVSNFHPdRLMDLILHN 149
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGfvnkkdkgerelassDVTSVWRAMEALVSEGKVKSIGLSNFNP-RQINKILAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 150 EIVPAVN-QVETHPFYQQKESAAFMKAQGVQHESWAPF-AEGRNNMFS---------NEVLTSIAEKHNKSVAQVVLRWL 218
Cdd:cd19111 159 AKVKPSNlQLECHAYLQQRELRKFCNKKNIVVTAYAPLgSPGRANQSLwpdqpdlleDPTVLAIAKELDKTPAQVLLRFV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1070084393 219 VQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDKGESLF 264
Cdd:cd19111 239 LQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYF 284
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
3-259 |
8.08e-68 |
|
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: 213.12 E-value: 8.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 3 TVTLNNGVKMPIIGFGVYQVpDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIK---RSG-VPREELFITTKLWIQ 78
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAeafKTGlVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 79 DAGYesAKIAFSKSLSKLQLDYLDLYLIHQPYGDYY-------------------------GAWRAMEDLYREGKIRAIG 133
Cdd:cd19112 81 DHGH--VIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvgttgsalgedgvldidvtisleTTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 134 VSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNN--MFS------NEVLTSIAEK 205
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANaeWFGsvspldDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1070084393 206 HNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDK 259
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDR 292
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
9-258 |
5.40e-61 |
|
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: 195.47 E-value: 5.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGVYQVpDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRS----GVPREELFITTKLWIQDAGYES 84
Cdd:cd19114 1 GDKMPLVGFGTAKI-KANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAiqegLVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 85 AKIAFSKSLSKLQLDYLDLYLIHQPYGDYY---------------------------GAWRAMEDLYREGKIRAIGVSNF 137
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPIPAAYvdpaenypflwkdkelkkfpleqspmqECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 138 HPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFA---------EGRN--NMFSNEVLTSIAEKH 206
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtkHLKHftNLLEHPVVKKLADKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1070084393 207 NKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLD 258
Cdd:cd19114 240 KRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELE 291
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
12-257 |
7.73e-60 |
|
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: 190.64 E-value: 7.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 12 MPIIGFGVYQVPDaQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAGYESAKIAFSK 91
Cdd:cd19139 1 IPAFGLGTFRLKD-DVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 92 SLSKLQLDYLDLYLIHQP-------YGDYYGawrAMEDLYREGKIRAIGVSNF---HPDRLMDLILHNEIvpAVNQVETH 161
Cdd:cd19139 80 SLEKLRTDYVDLTLIHWPspndevpVEEYIG---ALAEAKEQGLTRHIGVSNFtiaLLDEAIAVVGAGAI--ATNQIELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 162 PFYQQKESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDI 241
Cdd:cd19139 155 PYLQNRKLVAHCKQHGIHVTSYMTLAYGK--VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLA 232
|
250
....*....|....*.
gi 1070084393 242 FDFELSLEDIEQISTL 257
Cdd:cd19139 233 LDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
6-257 |
4.09e-59 |
|
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: 189.93 E-value: 4.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 6 LNNGVKMPIIGFGVYQV-PDaqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRS-----GVPREELFITTKLWIQD 79
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAePG--EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 80 AGYESAKIAFSKSLSKLQLDYLDLYLIHQPYGDYYGA--------------------------WRAMEDLYREGKIRAIG 133
Cdd:cd19118 79 HRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGdlnpltavptnggevdldlsvslvdtWKAMVELKKTGKVKSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 134 VSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPF---AEGRNNMFSNEVLTSIAEKHNKSV 210
Cdd:cd19118 159 VSNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLPLLVQHPEVKAIAAKLGKTP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1070084393 211 AQVVLRWLVQREVVTIPKSVRKERIVENFDifDFELSLEDIEQISTL 257
Cdd:cd19118 239 AQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-259 |
2.90e-58 |
|
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: 187.35 E-value: 2.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTLNNGVKMPIIGFGVYQvPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRS---GVPREELFITTKLWi 77
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQ-AKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 78 qdAGYES-AKIAFSKSLSKLQLDYLDLYLIH-----QPYG-------------------DYYGAWRAMEDLYREGKIRAI 132
Cdd:cd19121 79 --STYHRrVELCLDRSLKSLGLDYVDLYLVHwpvllNPNGnhdlfptlpdgsrdldwdwNHVDTWKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 133 GVSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTSIAEKHNKSVAQ 212
Cdd:cd19121 157 GVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGPGT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1070084393 213 VVLRWLVQREVVTIPKSVRKERIVENFDIFDFelsleDIEQISTLDK 259
Cdd:cd19121 237 VLISYQVARGAVVLPKSVTPDRIKSNLEIIDL-----DDEDMNKLND 278
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
9-254 |
7.11e-56 |
|
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: 182.23 E-value: 7.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGVYQVPDAQECEnAVYEALMAGYRLIDTASGYLNEEAVGRAI----KRSGVPREELFITTKLWIQDAGYES 84
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTE-AVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 85 AKIAFSKSLSKLQLDYLDLYLIHQPYG---------------------DYYGAWRAMEDLYREGKIRAIGVSNFHPDRLm 143
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkelfpldesgnvipsdtTFLDTWEAMEELVDEGLVKAIGVSNFNHLQI- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 144 DLILHN---EIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAE--------GRNNMFSNEVLTSIAEKHNKSVAQ 212
Cdd:cd19107 159 ERILNKpglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwakpEDPSLLEDPKIKEIAAKHNKTTAQ 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1070084393 213 VVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19107 239 VLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
9-255 |
4.09e-54 |
|
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: 176.27 E-value: 4.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGVYQV--------PDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKrsGVPREELFITTKLWI 77
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdySDDKKAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 78 QDAGYESAKIAFSKSLSKLQLDYLDLYLIHQP--YGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRL---MDLILHNEIV 152
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPnpSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELeeaQSYLKKGPIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 153 paVNQVETHPF--YQQKESAAFMKAQGVQHESWAPFAEGR-NNMFSNEVLTSIAEKHNKSVAQVVLRWLVQRE-VVTIPK 228
Cdd:cd19072 159 --ANQVEYNLFdrEEESGLLPYCQKNGIAIIAYSPLEKGKlSNAKGSPLLDEIAKKYGKTPAQIALNWLISKPnVIAIPK 236
|
250 260
....*....|....*....|....*..
gi 1070084393 229 SVRKERIVENFDIFDFELSLEDIEQIS 255
Cdd:cd19072 237 ASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
11-263 |
7.74e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 175.60 E-value: 7.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 11 KMPIIGFGVYQVPDaQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRSGVPREELFITTKLWIqdAGYESAKIAFS 90
Cdd:PRK11172 2 SIPAFGLGTFRLKD-QVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWI--DNLAKDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 91 --KSLSKLQLDYLDLYLIHQPY-GDYYGAWRAMEDLY---REGKIRAIGVSNFHPDRL---MDLILHNEIvpAVNQVETH 161
Cdd:PRK11172 79 lkESLQKLRTDYVDLTLIHWPSpNDEVSVEEFMQALLeakKQGLTREIGISNFTIALMkqaIAAVGAENI--ATNQIELS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 162 PFYQQKESAAFMKAQGVQHESWAPFAEGRnnMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDI 241
Cdd:PRK11172 157 PYLQNRKVVAFAKEHGIHVTSYMTLAYGK--VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLA 234
|
250 260
....*....|....*....|..
gi 1070084393 242 FDFELSLEDIEQISTLDKGESL 263
Cdd:PRK11172 235 QDLQLDAEDMAAIAALDRNGRL 256
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
11-259 |
5.68e-53 |
|
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: 174.76 E-value: 5.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 11 KMPIIGFGVYQVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAI----KRSGVPREELFITTKLWIQDAGYESAK 86
Cdd:cd19110 3 DIPAVGLGTWKASPG-EVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIrekiKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 87 IAFSKSLSKLQLDYLDLYLIHQPYG---------------------DYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDL 145
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGfkpgepdlpldrsgmvipsdtDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 146 ILHN--EIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPF--AEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQR 221
Cdd:cd19110 162 LNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLggSCEGVDLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1070084393 222 EVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDK 259
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDR 279
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
7-241 |
9.86e-53 |
|
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: 173.80 E-value: 9.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 7 NNGVKMPIIGFGVYqVPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKR----SGVPREELFITTKLWIQDAGY 82
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 83 ESAKIAFSKSLSKLQLDYLDLYLIHQPYG----------DYYGA------------WRAMEDLYREGKIRAIGVSNFHPD 140
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFAfqpgdeqdprDANGNviyddgvtlldtWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 141 RLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEG-RNNMFSNEVLTSIAEKHNKSVAQVVLRWLV 219
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260
....*....|....*....|..
gi 1070084393 220 QREVVTIPKSVRKERIVENFDI 241
Cdd:cd19129 240 QRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
13-257 |
4.28e-52 |
|
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: 171.55 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 13 PIIGFGVYQVPDaQECENAVYEALMAGYRLIDTASGYLNEEAVGRAI----KRSGVPREELFITTKLWIQDAGYESAKIA 88
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFseifKDGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 89 FSKSLSKLQLDYLDLYLIHQPY-------GDYYGA--------------WRAMEDLYREGKIRAIGVSNFHPDRLMDLIL 147
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLafdmdtdGDPRDDnqiqslskkpledtWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 148 HNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAP----FAEGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREV 223
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPlggsYGDGNLTFLNDSELKALATKYNTTPPQVIIAWHLQKWP 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1070084393 224 VT---IPKSVRKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19128 241 KNysvIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
2-259 |
9.39e-52 |
|
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: 171.64 E-value: 9.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 2 QTVTLNNGVKMPIIGFGVY---QVPDAqECENAVYEALMAGYRLIDTASGYLNEEAVGRAIkRSG-----VPREELFITT 73
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYapeEVPKS-KALEATKLAIDAGFRHIDSAYLYQNEEEVGQAI-RSKiadgtVKREDIFYTS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 74 KLWIQDAGYESAKIAFSKSLSKLQLDYLDLYLIHQPYG---------------------DYYGAWRAMEDLYREGKIRAI 132
Cdd:cd19108 79 KLWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeelfpkdengklifdtvDLCATWEAMEKCKDAGLAKSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 133 GVSNFHpDRLMDLILHN---EIVPAVNQVETHPFYQQKESAAFMK----------AQGVQ-HESW----APFaegrnnMF 194
Cdd:cd19108 159 GVSNFN-RRQLEMILNKpglKYKPVCNQVECHPYLNQSKLLDFCKskdivlvaysALGSQrDKEWvdqnSPV------LL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1070084393 195 SNEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDK 259
Cdd:cd19108 232 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNR 296
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-257 |
3.27e-51 |
|
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: 169.99 E-value: 3.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 4 VTLNNGVKMPIIGFGVYQ-VPDAQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRS----GVPREELFITTKLWiq 78
Cdd:cd19119 4 FKLNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAiddgSIKREELFITTKVW-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 79 DAGYESAKIAFSKSLSKLQLDYLDLYLIHQPY---------------------------GDYYGAWRAMEDLYREGKIRA 131
Cdd:cd19119 82 PTFYDEVERSLDESLKALGLDYVDLLLVHWPVcfekdsddsgkpftpvnddgktryaasGDHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 132 IGVSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNNMFSNEVLTSIAEKHNKSVA 211
Cdd:cd19119 162 IGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKYNVSTG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1070084393 212 QVVLRWLVQREVVTIPKSVRKERIVENFDIfdFELSLEDIEQISTL 257
Cdd:cd19119 242 DILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
5-259 |
1.85e-50 |
|
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: 167.80 E-value: 1.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 5 TLNNGVKMPIIGFGVYQVPDAQ-ECENAVYEALMAGYRLIDTASGYLNEEAVGRAIK-----RSGVPREELFITTKLWIQ 78
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAKgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRdflkeNPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 79 DAGYESAKIAFSKSLSKLQLDYLDLYLIHQPY---------------GDYY----------GAWRAMEDLYREGKIRAIG 133
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaekndqrspklgpdGKYVilkdltenpePTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 134 VSNFHPDRLMDLILHNEIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFaeGRNNMF--------SNEVLTSIAEK 205
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPL--GSQNQVpstgervsENPTLNEVAEK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1070084393 206 HNKSVAQVVLRWLVQREVVTIPKSVRKERIVENFDIfdFELSLEDIEQISTLDK 259
Cdd:cd19122 240 GGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQVAK 291
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
9-259 |
6.80e-50 |
|
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: 166.90 E-value: 6.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGVYQVPD---AQECENAVYEALMAGYRLIDTASGYLNEEAVGRAIKRS----GVPREELFITTKLWIQDAG 81
Cdd:cd19109 1 GNSIPIIGLGTYSEPKttpKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 82 YESAKIAFSKSLSKLQLDYLDLYLIHQPY----GD------------YY-----GAWRAMEDLYREGKIRAIGVSNFHpD 140
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMafkpGDeiyprdengkwlYHktnlcATWEALEACKDAGLVKSIGVSNFN-R 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 141 RLMDLILHN---EIVPAVNQVETHPFYQQKESAAFMKAQGVQHESWAPFAEGRNNMFSN---------EVLTSIAEKHNK 208
Cdd:cd19109 160 RQLELILNKpglKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNvsspplledPLLNSIGKKYNK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1070084393 209 SVAQVVLRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQISTLDK 259
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNK 290
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
15-254 |
2.19e-46 |
|
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: 157.09 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 15 IGFGVYQ------VPDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSGVPREELFITTKLWIQDAGYESA 85
Cdd:pfam00248 1 IGLGTWQlgggwgPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 86 KI------AFSKSLSKLQLDYLDLYLIHQPYGDYY--GAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAVNQ 157
Cdd:pfam00248 81 GSkenirkSLEESLKRLGTDYIDLYYLHWPDPDTPieETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 158 VETHPFYQQKES--AAFMKAQGVQHESWAPFAEG--------------------RNNMFS-----NEVLTSIAEKHNKSV 210
Cdd:pfam00248 161 VEYNLLRRRQEEelLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrlLKKGTPlnleaLEALEEIAKEHGVSP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1070084393 211 AQVVLRWLVQREVVT--IPKSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:pfam00248 241 AQVALRWALSKPGVTipIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
2-254 |
1.04e-44 |
|
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: 152.02 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 2 QTVTLNNGVKMPIIGFGVYQV----PDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSgvpREELFITTK 74
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMgedpAKRAQEIEALRAGIDLGMTLIDTAEMYgdgGSEELVGEAIRGR---RDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 75 LWIQDAGYESAKIAFSKSLSKLQLDYLDLYLIHqpygdyygaWR----------AMEDLYREGKIRAIGVSNFHPDRLMD 144
Cdd:cd19138 78 VLPSNASRQGTVRACERSLRRLGTDYLDLYLLH---------WRggvplaetvaAMEELKKEGKIRAWGVSNFDTDDMEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 145 LI-LHNEIVPAVNQVETHPFYQQKESAAF--MKAQGVQHESWAPFAEG---RNNMFSNEVLTSIAEKHNKSVAQVVLRWL 218
Cdd:cd19138 149 LWaVPGGGNCAANQVLYNLGSRGIEYDLLpwCREHGVPVMAYSPLAQGgllRRGLLENPTLKEIAARHGATPAQVALAWV 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 1070084393 219 V-QREVVTIPKSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19138 229 LrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
9-254 |
1.71e-35 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 128.07 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGV-----YQVPDAQECENAV---YEALMAGYRLIDTASGYL---NEEAVGRAIKRsgVPREELFITTKLWI 77
Cdd:cd19137 1 GEKIPALGLGTwgiggFLTPDYSRDEEMVellKTAIELGYTHIDTAEMYGgghTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 78 QDAGYESAKIAFSKSLSKLQLDYLDLYLIHQPYGD--YYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVPAV 155
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNipLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 156 NQVETHPF---YQQKESAAFMKAQGVQHESWAPFAegRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQRE-VVTIPKSVR 231
Cdd:cd19137 159 NQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLR--RGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPnVVAIPKAGR 236
|
250 260
....*....|....*....|...
gi 1070084393 232 KERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19137 237 VEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-254 |
1.41e-32 |
|
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: 121.18 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 17 FGVYQVPDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSGvPREELFITTKL----WiqDAGYESAKIAF 89
Cdd:cd19093 17 WWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKFaplpW--RLTRRSVVKAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 90 SKSLSKLQLDYLDLYLIHQPYGDYYGA---WRAMEDLYREGKIRAIGVSNFHPDRLMD----LILHnEIVPAVNQVE--- 159
Cdd:cd19093 94 KASLERLGLDSIDLYQLHWPGPWYSQIealMDGLADAVEEGLVRAVGVSNYSADQLRRahkaLKER-GVPLASNQVEysl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 160 THPFYQQKESAAFMKAQGVQHESWAPFAEG---------------RNNMFSN----------EVLTSIAEKHNKSVAQVV 214
Cdd:cd19093 173 LYRDPEQNGLLPACDELGITLIAYSPLAQGlltgkyspenpppggRRRLFGRknlekvqpllDALEEIAEKYGKTPAQVA 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1070084393 215 LRWLVQREVVTIPKSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19093 253 LNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-254 |
1.20e-31 |
|
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: 119.13 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTL-NNGVKMPIIGFG------VYQVPDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKrsGVPREELF 70
Cdd:COG0667 1 MEYRRLgRSGLKVSRLGLGtmtfggPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 71 ITTKL--------WIQDAGYESAKIAFSKSLSklqldyldlylIHQPYGDYY--GAWRAMEDLYREGKIRAIGVSNFHPD 140
Cdd:COG0667 79 IATKVgrrmgpgpNGRGLSREHIRRAVEASLRrlgtdyidlyqLHRPDPDTPieETLGALDELVREGKIRYIGVSNYSAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 141 RLMDL--ILHNEIVPAVNQVETHPFYQQ--KESAAFMKAQGVQHESWAPFAEG-----------------RNNMFSN--- 196
Cdd:COG0667 159 QLRRAlaIAEGLPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdrAATNFVQgyl 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 197 --------EVLTSIAEKHNKSVAQVVLRWLVQREVVTIP----KSVrkERIVENFDIFDFELSLEDIEQI 254
Cdd:COG0667 239 ternlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSVipgaRSP--EQLEENLAAADLELSAEDLAAL 306
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
9-254 |
9.54e-28 |
|
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: 108.38 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGVYQV-------PDAQECENAVYEALMAGYRLIDTASGYLN---EEAVGRAIKRSgvpREELFITTK---L 75
Cdd:cd19084 1 DLKVSRIGLGTWAIggtwwgeVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKcglR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 76 WIQ------DAGYESAKIAFSKSLSKLQLDYLDLYLIHQPygDYY----GAWRAMEDLYREGKIRAIGVSNFHPDRLMDL 145
Cdd:cd19084 78 WDGgkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHWP--DPNtpieETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 146 ILHNEIVpaVNQVETHPFYQQKESA--AFMKAQGVQHESWAPFAEG-------------------RNNMFSNE------- 197
Cdd:cd19084 156 RKYGPIV--SLQPPYSMLEREIEEEllPYCRENGIGVLPYGPLAQGlltgkykkeptfppddrrsRFPFFRGEnfeknle 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1070084393 198 ---VLTSIAEKHNKSVAQVVLRWLVQREVVTI----PKSVrkERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19084 234 ivdKLKEIAEKYGKSLAQLAIAWTLAQPGVTSaivgAKNP--EQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
24-256 |
4.01e-26 |
|
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: 103.82 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 24 DAQECENAVYEALMAGYRLIDTASGYLN---EEAVGRAIKRsgvPREELFITTKLWIQDAGYESAKIAFSKSLSKLQLDY 100
Cdd:cd19085 21 DDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNLTPEDVRKSCERSLKRLGTDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 101 LDLYLIHQPYGD-----YYGawrAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIVpaVNQVETHPFYQQ--KESAAFM 173
Cdd:cd19085 98 IDLYQIHWPSSDvpleeTME---ALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQLPYNLLWRAieYEILPFC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 174 KAQGVQHESWAPFAEG-----------------RNNMFSN-------------EVLTSIAEKHNKSVAQVVLRWLVQREV 223
Cdd:cd19085 173 REHGIGVLAYSPLAQGlltgkfssaedfppgdaRTRLFRHfepgaeeetfealEKLKEIADELGVTMAQLALAWVLQQPG 252
|
250 260 270
....*....|....*....|....*....|....*...
gi 1070084393 224 VTipkSV-----RKERIVENFDIFDFELSLEDIEQIST 256
Cdd:cd19085 253 VT---SVivgarNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-257 |
5.89e-24 |
|
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: 98.51 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 31 AVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSgvpREELFITTK---LWIQDAGY------ESAKIAFSKSLSKLQL 98
Cdd:cd19102 31 AIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWDEEGRIrrslkpASIRAECEASLRRLGV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 99 DYLDLYLIHQPYGD--YYGAWRAMEDLYREGKIRAIGVSNFHPDRLmdlilhnEIVPAVNQVET-HPFYQ------QKES 169
Cdd:cd19102 108 DVIDLYQIHWPDPDepIEEAWGALAELKEEGKVRAIGVSNFSVDQM-------KRCQAIHPIASlQPPYSllrrgiEAEI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 170 AAFMKAQG-----------------VQHESWAPFAEG----RNNMFSN----------EVLTSIAEKHNKSVAQVVLRWL 218
Cdd:cd19102 181 LPFCAEHGigvivyspmqsglltgkMTPERVASLPADdwrrRSPFFQEpnlarnlalvDALRPIAERHGRTVAQLAIAWV 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1070084393 219 VQREVVT--IPKSVRKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19102 261 LRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-227 |
5.94e-24 |
|
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: 96.82 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 15 IGFGVYQV---PDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSGVpREELFITTKLWIQDAGYESAKI- 87
Cdd:cd06660 3 LGLGTMTFggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRSRl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 88 -------AFSKSLSKlqldyldlylIHQPYGDYY------------GAWRAMEDLYREGKIRAIGVSNFHPDRLMDLI-- 146
Cdd:cd06660 82 spehirrDLEESLRR----------LGTDYIDLYylhrddpstpveETLEALNELVREGKIRYIGVSNWSAERLAEALay 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 147 --LHNEIVPAVNQVETHPFYQQ---KESAAFMKAQGVQHESWAPFAEGrnnmfsnevltsiaekhnksVAQVVLRWLVQR 221
Cdd:cd06660 152 akAHGLPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLARG--------------------PAQLALAWLLSQ 211
|
....*.
gi 1070084393 222 EVVTIP 227
Cdd:cd06660 212 PFVTVP 217
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
15-257 |
1.78e-21 |
|
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: 91.71 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 15 IGFGVYQV------PDAQECE--NAVYEALMAGYRLIDTASGY---LNEEAVGRAIKrsGVPREELFITTKLWIQDAGYE 83
Cdd:cd19083 14 IGLGTNAVgghnlyPNLDEEEgkDLVREALDNGVNLLDTAFIYglgRSEELVGEVLK--EYNRNEVVIATKGAHKFGGDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 84 SA--------KIAFSKSLSKLQLDYLDLYLIHQPYGDY--YGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLIlHNEIVP 153
Cdd:cd19083 92 SVlnnspeflRSAVEKSLKRLNTDYIDLYYIHFPDGETpkAEAVGALQELKDEGKIRAIGVSNFSLEQLKEAN-KDGYVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 154 AVnQVETHPFYQQKESAAF--MKAQGVQHESWAPFAEG-----------------RN------------NMFSNEVLTSI 202
Cdd:cd19083 171 VL-QGEYNLLQREAEEDILpyCVENNISFIPYFPLASGllagkytkdtkfpdndlRNdkplfkgerfseNLDKVDKLKSI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1070084393 203 AEKHNKSVAQVVLRWLVQREVVT--IPKSVRKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19083 250 ADEKGVTVAHLALAWYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-250 |
5.36e-21 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 90.21 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTL-NNGVKMPIIGFGVYQVPDA----QECENAVYEALMAGYRLIDTA---SGYLNEEAVGRAIKRSGVPREELFIT 72
Cdd:COG4989 1 MKRIKLgASGLSVSRIVLGCMRLGEWdlspAEAAALIEAALELGITTFDHAdiyGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 73 TKLWIQ-DAGYESAKIA---FSK---------SLSKLQLDYLDLYLIHQPygDY-YGAW---RAMEDLYREGKIRAIGVS 135
Cdd:COG4989 81 TKCGIRlPSEARDNRVKhydTSKehiiasvegSLRRLGTDYLDLLLLHRP--DPlMDPEevaEAFDELKASGKVRHFGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 136 NFHPDRlMDLI---LHNEIVpaVNQVE-----THPFYQqkESAAFMKAQGVQHESWAPFAEGRnnMFS---------NEV 198
Cdd:COG4989 159 NFTPSQ-FELLqsaLDQPLV--TNQIElsllhTDAFDD--GTLDYCQLNGITPMAWSPLAGGR--LFGgfdeqfprlRAA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1070084393 199 LTSIAEKHNKSVAQVVLRWLVQR--EVVTIPKSVRKERIVENFDIFDFELSLED 250
Cdd:COG4989 232 LDELAEKYGVSPEAIALAWLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-138 |
1.65e-18 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 84.10 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTL-NNGVKMPIIGFGV--YQVPDAQECENAVYEALMAGYRLIDTASGYLN-EEAVGRAIKRsgvPREELFITTKL- 75
Cdd:COG1453 1 MQYRRLgKTGLEVSVLGFGGmrLPRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKLp 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070084393 76 -WIQDAgyESAKIAFSKSLSKLQLDYLDLYLIH---------QPYGDyYGAWRAMEDLYREGKIRAIGVSnFH 138
Cdd:COG1453 78 pWVRDP--EDMRKDLEESLKRLQTDYIDLYLIHglnteedleKVLKP-GGALEALEKAKAEGKIRHIGFS-TH 146
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-257 |
2.55e-18 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 83.05 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTL-NNGVKMPIIGFG-------------VYQVpDAQECENAVYEALMAGYRLIDTASGYLN---EEAVGRAIKRSg 63
Cdd:cd19091 1 MEYRTLgRSGLKVSELALGtmtfgggggffgaWGGV-DQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 64 vpREELFITTKLWIQ------DAGYESAKI--AFSKSLSKLQLDYLDLYLIHQPygDYYG----AWRAMEDLYREGKIRA 131
Cdd:cd19091 79 --RDDVLIATKVRGRmgegpnDVGLSRHHIirAVEASLKRLGTDYIDLYQLHGF--DALTpleeTLRALDDLVRQGKVRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 132 IGVSNFHPDRLMDLI----LHNEIVPAVNQVethpFYQ------QKESAAFMKAQGVQHESWAPFAEGR----------- 190
Cdd:cd19091 155 IGVSNFSAWQIMKALgiseRRGLARFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAGGLlsgkyrrgqpa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 191 ------------NNMFSNE-------VLTSIAEKHNKSVAQVVLRWLVQREVVTipkSV-----RKERIVENFDIFDFEL 246
Cdd:cd19091 231 pegsrlrrtgfdFPPVDRErgydvvdALREIAKETGATPAQVALAWLLSRPTVS---SViigarNEEQLEDNLGAAGLSL 307
|
330
....*....|.
gi 1070084393 247 SLEDIEQISTL 257
Cdd:cd19091 308 TPEEIARLDKV 318
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-254 |
4.28e-18 |
|
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: 82.26 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 2 QTVTL-NNGVKMPIIGFGV------YQVPDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRsgvPREELFI 71
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGCmgmsafYGPADEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 72 TTKLWIQ----------DAGYESAKIAFSKSLSKLQLDYLDLYLIHQ-----PYGDyygAWRAMEDLYREGKIRAIGVSN 136
Cdd:cd19076 78 ATKFGIVrdpgsgfrgvDGRPEYVRAACEASLKRLGTDVIDLYYQHRvdpnvPIEE---TVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 137 FHPDRL-------------MDLIL-----HNEIVPAVNQ-----VETHPFYQQKESAAFMKAQGVQHESW---APFAEGR 190
Cdd:cd19076 155 ASADTIrrahavhpitavqSEYSLwtrdiEDEVLPTCRElgigfVAYSPLGRGFLTGAIKSPEDLPEDDFrrnNPRFQGE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1070084393 191 N---NMFSNEVLTSIAEKHNKSVAQVVLRWLVQR--EVVTIPKSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19076 235 NfdkNLKLVEKLEAIAAEKGCTPAQLALAWVLAQgdDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
24-250 |
5.47e-18 |
|
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: 81.83 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 24 DAQECENAVYEALMAGYRLIDTA---SGYLNEEAVGRAIKRSGVPREELFITTKLWIQDAG---------YESAK--IAF 89
Cdd:cd19092 22 SAEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALALNPGLREKIEIQTKCGIRLGDdprpgrikhYDTSKehILA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 90 S--KSLSKLQLDYLDLYLIHQPygDY-YGAW---RAMEDLYREGKIRAIGVSNFHPDRlMDLI---LHNEIVpaVNQVE- 159
Cdd:cd19092 102 SveGSLKRLGTDYLDLLLLHRP--DPlMDPEevaEAFDELVKSGKVRYFGVSNFTPSQ-IELLqsyLDQPLV--TNQIEl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 160 ----THPFYQqkESAAFMKAQGVQHESWAPFAEGRnnMFS---------NEVLTSIAEKHNKSVAQVVLRWLVQR--EVV 224
Cdd:cd19092 177 sllhTEAIDD--GTLDYCQLLDITPMAWSPLGGGR--LFGgfderfqrlRAALEELAEEYGVTIEAIALAWLLRHpaRIQ 252
|
250 260
....*....|....*....|....*.
gi 1070084393 225 TIPKSVRKERIVENFDIFDFELSLED 250
Cdd:cd19092 253 PILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-135 |
1.19e-17 |
|
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: 79.94 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTL-NNGVKMPIIGFGVYqvPDAQECENAVYEALMAGYRLIDTASGYLN---EEAVGRAIKrsGVPREELFITTKLW 76
Cdd:cd19105 1 MPYRTLgKTGLKVSRLGFGGG--GLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKAS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1070084393 77 IQDAGYESAKI--AFSKSLSKLQLDYLDLYLIHQ-PYGDYY----GAWRAMEDLYREGKIRAIGVS 135
Cdd:cd19105 77 PRLDKKDKAELlkSVEESLKRLQTDYIDIYQLHGvDTPEERllneELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
7-255 |
1.28e-17 |
|
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: 81.16 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 7 NNGVKMPIIGFGVYQV--------PDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSgvpREELFITTK- 74
Cdd:cd19149 6 KSGIEASVIGLGTWAIgggpwwggSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGR---RDKVVLATKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 75 -LWIQDAGYESAKIAFSKSLSKLQLDYLDLYLIHQP-------YGDYY------------GAWRAMEDLYREGKIRAIGV 134
Cdd:cd19149 83 gLRWDREGGSFFFVRDGVTVYKNLSPESIREEVEQSlkrlgtdYIDLYqthwqdvetpieETMEALEELKRQGKIRAIGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 135 SNFHPDRLMDLILHNEIvpAVNQ---------VETHPF-YQQKESAAFMK----AQGV--------------QHESWAPF 186
Cdd:cd19149 163 SNVSVEQIKEYVKAGQL--DIIQekysmldrgIEKELLpYCKKNNIAFQAysplEQGLltgkitpdrefdagDARSGIPW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1070084393 187 -----AEGRNNMFsnEVLTSIAEKHNKSVAQVVLRW-LVQREVVTIPKSVRK-ERIVENFDIFDFELSLEDIEQIS 255
Cdd:cd19149 241 fspenREKVLALL--EKWKPLCEKYGCTLAQLVIAWtLAQPGITSALCGARKpEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-254 |
3.40e-17 |
|
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: 79.79 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTL-NNGVKMPIIGFGV------YQVPDAQECENAVYEALM-AGYRLIDTASGYL-NEEAVGRAIKRSGVPREELFI 71
Cdd:cd19144 1 IPTRTLgRNGPSVPALGFGAmglsafYGPPKPDEERFAVLDAAFeLGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 72 TTKLWIQ----------DAGYESAKIAFSKSLSKlqldyldlylIHQPYGDYYGAWR------------AMEDLYREGKI 129
Cdd:cd19144 81 ATKFGIEknvetgeysvDGSPEYVKKACETSLKR----------LGVDYIDLYYQHRvdgktpiektvaAMAELVQEGKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 130 RAIGVSN-----------FHPdrlmdlilhneiVPAVnQVETHPFYQQKESA--AFMKA---QGVQHESWAP-------- 185
Cdd:cd19144 151 KHIGLSEcsaetlrrahaVHP------------IAAV-QIEYSPFSLDIERPeiGVLDTcreLGVAIVAYSPlgrgfltg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 186 -------FAEG----RNNMFSNE----------VLTSIAEKHNKSVAQVVLRWLVQR--EVVTIPKSVRKERIVENFDIF 242
Cdd:cd19144 218 airspddFEEGdfrrMAPRFQAEnfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|..
gi 1070084393 243 DFELSLEDIEQI 254
Cdd:cd19144 298 KVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-161 |
1.52e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 76.75 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFG--VYQVPDAQECENAVYEALMAGYRLIDTASGYLN-EEAVGRAIKRsgvPREELFITTKLWIQDagYESA 85
Cdd:cd19100 8 GLKVSRLGFGggPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARD--YEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 86 KIAFSKSLSKLQLDYLDLYLIH---------QPYGDyYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNE---IVP 153
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHavdteedldQVFGP-GGALEALLEAKEEGKIRFIGISGHSPEVLLRALETGEfdvVLF 161
|
....*...
gi 1070084393 154 AVNQVETH 161
Cdd:cd19100 162 PINPAGDH 169
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
12-247 |
7.12e-16 |
|
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: 75.33 E-value: 7.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 12 MPIIGFGVYQVP-DAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSGvprEELFITTKL---------WIQ 78
Cdd:cd19088 9 MRLTGPGIWGPPaDREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvrtgpgwWGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 79 DAGYESAKIAFSKSLSKLQLDYLDLYLIHQ-----PYGDYYGAWRAMEDlyrEGKIRAIGVSNFHPDRLMDLILHNEIVp 153
Cdd:cd19088 86 DGSPEYLRQAVEASLRRLGLDRIDLYQLHRidpkvPFEEQLGALAELQD---EGLIRHIGLSNVTVAQIEEARAIVRIV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 154 AVnQVETHPFYQQKES-AAFMKAQGVQHESWAPFAeGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQRE--VVTIPKSV 230
Cdd:cd19088 162 SV-QNRYNLANRDDEGvLDYCEAAGIAFIPWFPLG-GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTS 239
|
250
....*....|....*..
gi 1070084393 231 RKERIVENFDIFDFELS 247
Cdd:cd19088 240 SVEHLEENLAAAGLRLS 256
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
24-254 |
1.68e-15 |
|
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: 74.93 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 24 DAQECENAVYEALMAGYRLIDTASGYLN---EEAVGRAIKRSGvPREELFITTKLwiqdaGYESAKIAFSKSLSKLQldy 100
Cdd:cd19079 33 DEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATKV-----YFPMGDGPNGRGLSRKH--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 101 ldlylIHQP-----------YGDYYGA--W----------RAMEDLYREGKIRAIGVSNFHPDRLMDL----ILHNEIVP 153
Cdd:cd19079 104 -----IMAEvdaslkrlgtdYIDLYQIhrWdyetpieetlEALHDVVKSGKVRYIGASSMYAWQFAKAlhlaEKNGWTKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 154 AVNQvethPFY------QQKESAAFMKAQGVQHESWAPFAEGR---------------------NNMFSNEV-------L 199
Cdd:cd19079 179 VSMQ----NHYnllyreEEREMIPLCEEEGIGVIPWSPLARGRlarpwgdtterrrsttdtaklKYDYFTEAdkeivdrV 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1070084393 200 TSIAEKHNKSVAQVVLRWLVQREVVTIP--KSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19079 255 EEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
15-256 |
1.32e-14 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 72.27 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 15 IGFGVY-------QVPDAQECENAVYEALMAGYRLIDTAS---GYLNEEAVGRAIKRsgvPREELFITTKLWIQ------ 78
Cdd:cd19078 7 IGLGCMgmshgygPPPDKEEMIELIRKAVELGITFFDTAEvygPYTNEELVGEALKP---FRDQVVIATKFGFKidggkp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 79 -----DAGYESAKIAFSKSLSKLQLDYLDLYLIHQ-----PYGDYYGAwraMEDLYREGKIRAIGVSNFHPDRLMDliLH 148
Cdd:cd19078 84 gplglDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRvdpnvPIEEVAGT---MKELIKEGKIRHWGLSEAGVETIRR--AH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 149 nEIVP--AVnQVETHPFYQQKESAAF--MKAQGVQHESWAPFAEG-----------------RNNM--FSNE-------- 197
Cdd:cd19078 159 -AVCPvtAV-QSEYSMMWREPEKEVLptLEELGIGFVPFSPLGKGfltgkidentkfdegddRASLprFTPEaleanqal 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070084393 198 --VLTSIAEKHNKSVAQVVLRWLVQRE--VVTIPKSVRKERIVENFDIFDFELSLEDIEQIST 256
Cdd:cd19078 237 vdLLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
23-254 |
2.28e-14 |
|
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: 71.57 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 23 PDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSGvPREELFITTKL---WIQDAGYE----SAKIA--FS 90
Cdd:cd19148 22 TDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGEVVrnssPARIRkeVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 91 KSLSKLQLDYLDLYLIHQP--YGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRlMDLIlhNEIVP-AVNQVETHPFYQQK 167
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPdpLVPIEETAEALKELLDEGKIRAIGVSNFSPEQ-METF--RKVAPlHTVQPPYNLFEREI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 168 ESA--AFMKAQGVQHESWAPFAEG-------RNNMFSN----------------------EVLTSIA-EKHNKSVAQVVL 215
Cdd:cd19148 178 EKDvlPYARKHNIVTLAYGALCRGllsgkmtKDTKFEGddlrrtdpkfqeprfsqylaavEELDKLAqERYGKSVIHLAV 257
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1070084393 216 RWLVQREVVTIP--KSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19148 258 RWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEI 298
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-238 |
5.14e-14 |
|
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: 69.81 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 15 IGFGVYQV-------PDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRsgvPREELFITTKLWIQDAGYES 84
Cdd:cd19086 6 IGFGTWGLggdwwgdVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKG---RRDKVVIATKFGNRFDGGPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 85 AKIAFSK---------SLSKLQLDYLDLYLIHQPYGDYYG---AWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIv 152
Cdd:cd19086 83 RPQDFSPeyireaveaSLKRLGTDYIDLYQLHNPPDEVLDndeLFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 153 pAVNQVETHPFYQQKESAAFMKAqgvQHESWA-----PFAEGrnnmfsneVLTSiaekhnkSVAQVVLRWLVQREVVT-- 225
Cdd:cd19086 162 -DVVQVIYNLLDQRPEEELFPLA---EEHGVGviarvPLASG--------LLTG-------KLAQAALRFILSHPAVStv 222
|
250
....*....|...
gi 1070084393 226 IPKSVRKERIVEN 238
Cdd:cd19086 223 IPGARSPEQVEEN 235
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
38-254 |
5.86e-14 |
|
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: 70.71 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 38 AGYRLIDTASGY----------LNEEAVGRAIKRSGvPREELFITTKL----WIQDAGYESAKIAFS--KSLSKLQLDYL 101
Cdd:cd19081 38 AGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgfpmGPNGPGLSRKHIRRAveASLRRLQTDYI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 102 DLYLIHQ-----PYGDYYGAwraMEDLYREGKIRAIGVSNFHPDRLMdlilhnEIV---------------PAVNQVETH 161
Cdd:cd19081 117 DLYQAHWddpatPLEETLGA---LNDLIRQGKVRYIGASNYSAWRLQ------EALelsrqhglpryvslqPEYNLVDRE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 162 PFyqQKESAAFMKAQGVQHESWAPFAEG--------------------RNNMFSNE-------VLTSIAEKHNKSVAQVV 214
Cdd:cd19081 188 SF--EGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeAAKRYLNErglrildALDEVAAEHGATPAQVA 265
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1070084393 215 LRWLVQREVVTIP-KSVRK-ERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19081 266 LAWLLARPGVTAPiAGARTvEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
13-140 |
7.78e-14 |
|
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: 69.57 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 13 PIIGFGVYQ------VPDAQECENAVYEALMAGYRLIDTASGY-LNEEAVGRAIkrSGVPREELFITTKLWIQDAGYESA 85
Cdd:cd19095 1 SVLGLGTSGigrvwgVPSEAEAARLLNTALDLGINLIDTAPAYgRSEERLGRAL--AGLRRDDLFIATKVGTHGEGGRDR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1070084393 86 KiAFSK---------SLSKLQLDYLDLYLIHQPYGDYY--GAWRAMEDLYREGKIRAIGVSNFHPD 140
Cdd:cd19095 79 K-DFSPaairasierSLRRLGTDYIDLLQLHGPSDDELtgEVLETLEDLKAAGKVRYIGVSGDGEE 143
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
9-247 |
8.08e-13 |
|
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: 67.23 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 9 GVKMPIIGFGVY-----QVPD--AQECENAVYEAlmaGYRLIDTASGYLN---EEAVGRAIKrsGVPREELFITTKL--- 75
Cdd:cd19074 1 GLKVSELSLGTWltfggQVDDedAKACVRKAYDL---GINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfwp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 76 ---WIQDAGYeSAK-I--AFSKSLSKLQLDYLDLYLIHQPYGD--YYGAWRAMEDLYREGKIRAIGVSNFHPDRLM---D 144
Cdd:cd19074 76 tgpGPNDRGL-SRKhIfeSIHASLKRLQLDYVDIYYCHRYDPEtpLEETVRAMDDLIRQGKILYWGTSEWSAEQIAeahD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 145 LIL-HNEIVPAVNQVETHPFYQQKESA--AFMKAQGVQHESWAPFAEG-------------------------------- 189
Cdd:cd19074 155 LARqFGLIPPVVEQPQYNMLWREIEEEviPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrrllt 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 190 RNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVT--IPKSVRKERIVENFDIFDFELS 247
Cdd:cd19074 235 DENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLS 294
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-257 |
3.88e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 65.05 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 31 AVYEALMA-GYRLIDTASGY---LNEEAVGRAIKRsgVPREELFITTKLWIQDAGYESAKIA--FSKSLSKLQLDYLDLY 104
Cdd:cd19103 36 AVFDKAMAaGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKFTPQIAGQSADPVAdmLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 105 LIHQPyGDYYGAWRAMEDLYREGKIRAIGVSNFHpdrLMDLILHNEIVPA----VNQVETH--PFYQQKESA---AFMKA 175
Cdd:cd19103 114 WIHNP-ADVERWTPELIPLLKSGKVKHVGVSNHN---LAEIKRANEILAKagvsLSAVQNHysLLYRSSEEAgilDYCKE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 176 QGVQHESWA---------------PFAEG--RNNMFS---------NEVLTSIAEKHNKSVAQVVLRWLVQREVVTIPKS 229
Cdd:cd19103 190 NGITFFAYMvleqgalsgkydtkhPLPEGsgRAETYNpllpqleelTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGV 269
|
250 260
....*....|....*....|....*...
gi 1070084393 230 VRKERIVENFDIFDFELSLEDIEQISTL 257
Cdd:cd19103 270 TKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
13-226 |
7.70e-12 |
|
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: 63.73 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 13 PIIGFGVYQVP-------DAQECENAVYEALMAGYRLIDTASGYLN---EEAVGRAIKRsgVPREELFITTKL-WIQDAG 81
Cdd:cd19096 1 SVLGFGTMRLPesdddsiDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 82 YESAKIAFSKSLSKLQLDYLDLYLIH-------QPYGDYYGAWRAMEDLYREGKIRAIGVSnFH--PDRLMDLILHNEIv 152
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHglnspewLEKARKGGLLEFLEKAKKEGLIRHIGFS-FHdsPELLKEILDSYDF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 153 pAVNQVETHPFYQ--QKESAAFMKAQG-----VQHEswaPFAEGR--NNmfsNEVLTSIAEKHNKSVAQVVLRWLV-QRE 222
Cdd:cd19096 157 -DFVQLQYNYLDQenQAGRPGIEYAAKkgmgvIIME---PLKGGGlaNN---PPEALAILCGAPLSPAEWALRFLLsHPE 229
|
....
gi 1070084393 223 VVTI 226
Cdd:cd19096 230 VTTV 233
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
34-137 |
1.95e-11 |
|
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: 63.36 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 34 EALMAGYRLIDTASGY---LNEEAVGRAIKRSgvpREELFITTKL------WIQDAGYESAKI--AFSKSLSKLQLDYLD 102
Cdd:cd19087 38 RALDAGINFFDTADVYgggRSEEIIGRWIAGR---RDDIVLATKVfgpmgdDPNDRGLSRRHIrrAVEASLRRLQTDYID 114
|
90 100 110
....*....|....*....|....*....|....*....
gi 1070084393 103 LYLIHQPygDYYGA----WRAMEDLYREGKIRAIGVSNF 137
Cdd:cd19087 115 LYQMHHF--DRDTPleetLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
18-146 |
9.31e-11 |
|
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: 61.01 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 18 GVYQVPDAQ-ECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSGVPREELFITTKLW-IQDAGYESAK--IAFS 90
Cdd:cd19153 24 GVYGDGLEQdEAVAIVAEAFAAGINHFDTSPYYgaeSSEAVLGKALAALQVPRSSYTVATKVGrYRDSEFDYSAerVRAS 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070084393 91 --KSLSKLQLDYLDLYLIHQ-PYGDYYG----AWRAMEDLYREGKIRAIGVSNFHPDRLMDLI 146
Cdd:cd19153 104 vaTSLERLHTTYLDVVYLHDiEFVDYDTlvdeALPALRTLKDEGVIKRIGIAGYPLDTLTRAT 166
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
110-254 |
2.70e-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: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 110 YGD--YYGAWRAMEDLYREGKIRAIGVSNFHPDRLmDLILHNEIVPAVNQVE-----THPfyqQKESAAFMKAQGVQH-- 180
Cdd:cd19101 116 YSDpgYLDAAKHLAELQEEGKIRHLGLTNFDTERL-REILDAGVPIVSNQVQyslldRRP---ENGMAALCEDHGIKLla 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 181 ----------ESWAPFAEGRNNMFSN-----------------------EVLTSIAEKHNKSVAQVVLRWLVQREVV--T 225
Cdd:cd19101 192 ygtlaggllsEKYLGVPEPTGPALETrslqkyklmidewggwdlfqellRTLKAIADKHGVSIANVAVRWVLDQPGVagV 271
|
170 180
....*....|....*....|....*....
gi 1070084393 226 IPKSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19101 272 IVGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-135 |
2.89e-10 |
|
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: 59.49 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 1 MQTVTL-NNGVKMPIIGFG------VYQVPDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKrsGVPREELF 70
Cdd:cd19163 1 MKYRKLgKTGLKVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1070084393 71 ITTK------LWIQDAGYESAKIAFS--KSLSKLQLDYLDLYLIHQP-YGDYYG-----AWRAMEDLYREGKIRAIGVS 135
Cdd:cd19163 79 LATKvgryglDPDKMFDFSAERITKSveESLKRLGLDYIDIIQVHDIeFAPSLDqilneTLPALQKLKEEGKVRFIGIT 157
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
38-258 |
5.82e-10 |
|
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: 58.77 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 38 AGYRLIDTASGYLN---EEAVGRAIKRSgvpREELFITTKLWIQD------AGYESAK---IAFSKSLSKlqldyldlyl 105
Cdd:cd19080 43 AGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYTMNRrpgdpnAGGNHRKnlrRSVEASLRR---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 106 IHQPYGD--YYGAW----------RAMEDLYREGKIRAIGVSNFhpdrlmdlilhneivPA--VNQVET-------HPF- 163
Cdd:cd19080 110 LQTDYIDllYVHAWdfttpveevmRALDDLVRAGKVLYVGISDT---------------PAwvVARANTlaelrgwSPFv 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 164 -YQQKESAAF---------M-KAQGVQHESWAPFA------------EGRNNMFSN----------------EVLTSIAE 204
Cdd:cd19080 175 aLQIEYSLLErtperellpMaRALGLGVTPWSPLGgglltgkyqrgeEGRAGEAKGvtvgfgklternwaivDVVAAVAE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1070084393 205 KHNKSVAQVVLRWLVQREVVTIP--KSVRKERIVENFDIFDFELSledIEQISTLD 258
Cdd:cd19080 255 ELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLS---PEQLARLD 307
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
13-151 |
1.23e-09 |
|
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: 57.56 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 13 PIIGFGVYQ-------VPDAQECEnAVYEALMAGYRLIDTASGYLN-EEAVGRAIKrsGVPREELFITTKL-----WIQD 79
Cdd:cd19090 1 SALGLGTAGlggvfggVDDDEAVA-TIRAALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKVgrlpeDTAD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1070084393 80 AGYESAKIAFSKSLSKLQLDYLDLYLIHQPYGDYY-------GAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEI 151
Cdd:cd19090 78 YSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWvdilapgGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGDF 156
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
7-238 |
1.43e-09 |
|
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: 57.65 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 7 NNGVKMPIIGFGVYQ----VPDAQECENAVYEALMAGYRLIDTASGYLN-----EEAVGRAIKRSGVP-REELFITTKlw 76
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPyRDELVISTK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 77 iqdAGYE----------SAKIAFS---KSLSKLQLdyldlylihqPYGDYYGAWR------------AMEDLYREGKIRA 131
Cdd:cd19089 84 ---AGYGmwpgpygdggSRKYLLAsldQSLKRMGL----------DYVDIFYHHRydpdtpleetmtALADAVRSGKALY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 132 IGVSNFHPDRLMDLI-LHNEI-VP-AVNQVETHPFYQQKESAAF--MKAQGVQHESWAPFAEG----------------- 189
Cdd:cd19089 151 VGISNYPGAKARRAIaLLRELgVPlIIHQPRYSLLDRWAEDGLLevLEEAGIGFIAFSPLAQGlltdkylngippdsrra 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1070084393 190 RNNMFSNEV------------LTSIAEKHNKSVAQVVLRWLVQREVVTipkSV-----RKERIVEN 238
Cdd:cd19089 231 AESKFLTEEaltpekleqlrkLNKIAAKRGQSLAQLALSWVLRDPRVT---SVligasSPSQLEDN 293
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-254 |
1.98e-08 |
|
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: 54.49 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 35 ALMAGYRLIDTASGY----------LNEEAVGRAIKRSGvPREELFITTKL--------WIQDAG----YESAKIAFSKS 92
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRGGGtrldRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 93 LSKLQLDYLDLYLIHQP--Y-----GDYYGAW-------------RAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEIV 152
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPdrYtplfgGGYYTEPseeedsvsfeeqlEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 153 ----PAVNQVETHPFYQQKESA----------AFMK----AQGV---QHESWAPFAE-GRNNMFSN-------------- 196
Cdd:cd19094 186 glprIVSIQNPYSLLNRNFEEGlaeachrenvGLLAysplAGGVltgKYLDGAARPEgGRLNLFPGymaryrspqaleav 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1070084393 197 EVLTSIAEKHNKSVAQVVLRWLVQREVV--TIPKSVRKERIVENFDIFDFELS---LEDIEQI 254
Cdd:cd19094 266 AEYVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSdelLAEIDAV 328
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
13-247 |
4.11e-08 |
|
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: 53.38 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 13 PIIGFG-------VYQVPDAQEcENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRsgVPREELFITTKL-WI---- 77
Cdd:cd19152 1 PKLGFGtaplgnlYEAVSDEEA-KATLVAAWDLGIRYFDTAPWYgagLSEERLGAALRE--LGREDYVISTKVgRLlvpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 78 --------------------QDAGYESAKIAFSKSLSKLQLDYLDLYLIHQPYGDYY-------------GAWRAMEDLY 124
Cdd:cd19152 78 qeveptfepgfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaikGAFRALEELR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 125 REGKIRAIGV-SNFhPDRLMDLILH---NEIVPA-----VNQVETHPFYQQkesaafMKAQGVQHESWAPF-----AEGR 190
Cdd:cd19152 158 EEGVIKAIGLgVND-WEVILRILEEadlDWVMLAgrytlLDHSAARELLPE------CEKRGVKVVNAGPFnsgflAGGD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1070084393 191 NNMFSN------EVL------TSIAEKHNKSVAQVVLRWLVQREVVT--IPKSVRKERIVENFDIFDFELS 247
Cdd:cd19152 231 NFDYYEygpappELIarrdriEALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVALLATEIP 301
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
8-254 |
6.24e-08 |
|
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: 52.63 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 8 NGVKMPIIGFGV-------YQVPDAQ--ECENAvyeALMAGYRLIDTASGY------LNEEAVGRAIKRSGVPREELFIT 72
Cdd:cd19077 1 NGKLVGPIGLGLmgltwrpNPTPDEEafETMKA---ALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 73 TK--LWIQDAGYESAKIAFSKSLSKLQLDYLDLYLIhqpygDYYGAWR------------AMEDLYREGKIRAIGVSN-- 136
Cdd:cd19077 78 VKggLDPDTLRPDGSPEAVRKSIENILRALGGTKKI-----DIFEPARvdpnvpieetikALKELVKEGKIRGIGLSEvs 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 137 ---------FHPdrlmdlilhneivPAVNQVETHPFYQQKESAAFMKAQgvqHE------SWAPFAEG------------ 189
Cdd:cd19077 153 aetirrahaVHP-------------IAAVEVEYSLFSREIEENGVLETC---AElgipiiAYSPLGRGlltgriksladi 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 190 -----RNNM--FSNEV----------LTSIAEKHNKSVAQVVLRWLVQR---EVVTIPKSVRKERIVENFDIFDFELSLE 249
Cdd:cd19077 217 pegdfRRHLdrFNGENfeknlklvdaLQELAEKKGCTPAQLALAWILAQsgpKIIPIPGSTTLERVEENLKAANVELTDE 296
|
....*
gi 1070084393 250 DIEQI 254
Cdd:cd19077 297 ELKEI 301
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-149 |
6.71e-08 |
|
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: 52.65 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 24 DAQECENAVYEALMAGYRLIDTASGYLN---EEAVGRAIKrsGVPrEELFITTKLWIQDAGYESAKIAFSKSLSKLQLDY 100
Cdd:cd19104 30 TREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALK--GLP-AGPYITTKVRLDPDDLGDIGGQIERSVEKSLKRL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1070084393 101 LD----LYLIHQPYGD-----------------YYGAWRAMEDLYREGKIRAIGVSNF-HPDRLMDLILHN 149
Cdd:cd19104 107 KRdsvdLLQLHNRIGDerdkpvggtlsttdvlgLGGVADAFERLRSEGKIRFIGITGLgNPPAIRELLDSG 177
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-82 |
1.07e-07 |
|
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: 51.94 E-value: 1.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1070084393 15 IGFGVYQVP----DAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRS----GVPREELFITTKlwiqdAGY 82
Cdd:cd19099 6 LGLGTYRGDsddeTDEEYREALKAALDSGINVIDTAINYrggRSERLIGKALRELiekgGIKRDEVVIVTK-----AGY 79
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-151 |
1.18e-07 |
|
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: 51.76 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 35 ALMAGYRLIDTASGYLN-EEAVGRAIKRSgvprEELFITTKL----WIQDAGYESAKIAFSKSLSKLQLDYLDLYLIHQP 109
Cdd:cd19097 35 ALKAGINTLDTAPAYGDsEKVLGKFLKRL----DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNP 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1070084393 110 ---YGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILHNEI 151
Cdd:cd19097 111 ddlLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKI 155
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
36-227 |
2.21e-07 |
|
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: 51.01 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 36 LMAGYRLIDTASGY-------LNEEAVGRAIKRSGVpREELFITTK-----LWIQDAGYESAK-IA--FSKSLSKlqldy 100
Cdd:cd19082 27 VELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-RDKVVIATKgghpdLEDMSRSRLSPEdIRadLEESLER----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 101 ldlylIHQPYGDYYGAWR------------AMEDLYREGKIRAIGVSNFHPDRLMDLIL----HNEIVPAVNQVE----- 159
Cdd:cd19082 101 -----LGTDYIDLYFLHRddpsvpvgeivdTLNELVRAGKIRAFGASNWSTERIAEANAyakaHGLPGFAASSPQwslar 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 160 -THPF-------YQQKESAAFMKAQGVQHESWAPFAEG---------------RNNMFSNEV-------LTSIAEKHNKS 209
Cdd:cd19082 176 pNEPPwpgptlvAMDEEMRAWHEENQLPVFAYSSQARGffskraaggaeddseLRRVYYSEEnferlerAKELAEEKGVS 255
|
250
....*....|....*...
gi 1070084393 210 VAQVVLRWLVQREVVTIP 227
Cdd:cd19082 256 PTQIALAYVLNQPFPTVP 273
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
16-145 |
8.51e-07 |
|
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: 49.20 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 16 GFGVYQVPDAQECENAVYEALMAGYRLIDTASGYLNEEAV-GRAIK--RSGVPREELFITTK---LWIQDAGYESAKIAF 89
Cdd:cd19164 24 SYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRALKalRDEFPRDTYFIITKvgrYGPDDFDYSPEWIRA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1070084393 90 S--KSLSKLQLDYLDLYLIHQ----PYGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDL 145
Cdd:cd19164 104 SveRSLRRLHTDYLDLVYLHDvefvADEEVLEALKELFKLKDEGKIRNVGISGYPLPVLLRL 165
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
8-189 |
1.34e-06 |
|
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: 49.00 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 8 NGVKMPIIGFGVYQ-----VPDAQeCENAVYEALMAGYRLIDTASGYLNEEA---VGRAIKRSGVPREELFITTKL-W-- 76
Cdd:cd19142 9 SGLRVSNVGLGTWStfstaISEEQ-AEEIVTLAYENGINYFDTSDAFTSGQAeteLGRILKKKGWKRSSYIVSTKIyWsy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 77 -IQDAGYESAKI--AFSKSLSKLQLDYLDLYLIHQ--PYGDYYGAWRAMEDLYREGKIRAIGVSNFHPDRLMDLILH--- 148
Cdd:cd19142 88 gSEERGLSRKHIieSVRASLRRLQLDYIDIVIIHKadPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIarq 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1070084393 149 -NEIVPAVNQVETHPFYQQK---ESAAFMKAQGVQHESWAPFAEG 189
Cdd:cd19142 168 fNCPTPICEQSEYHMFCREKmelYMPELYNKVGVGLITWSPLSLG 212
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
13-135 |
1.91e-06 |
|
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: 48.12 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 13 PIIGFGVYQV-----PDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSgvPREELFITTK----LWIQDA 80
Cdd:cd19162 1 PRLGLGAASLgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH--PRAEYVVSTKvgrlLEPGAA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1070084393 81 GYESAKIA---FSK---------SLSKLQLDYLDLYLIHQPYGDYY----GAWRAMEDLYREGKIRAIGVS 135
Cdd:cd19162 79 GRPAGADRrfdFSAdgirrsieaSLERLGLDRLDLVFLHDPDRHLLqaltDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
7-254 |
3.46e-06 |
|
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: 47.59 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 7 NNGVKMPIIGFGVY-------QVPDAQECENAVYEAlmaGYRLIDTASGYLN---EEAVGRAIKRSGVPREELFITTKLW 76
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnqvDVDEAKECMKAAYDA---GVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 77 IQDAGyesaKIAFSKSLSKLQLDYLDLYLIHQ---PYGDYYGAWR------------AMEDLYREGKIRAIGVSNFHPDR 141
Cdd:cd19143 85 WGGGG----PPPNDRGLSRKHIVEGTKASLKRlqlDYVDLVFCHRpdpatpieetvrAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 142 LMDLIL----HNEIVPAVNQVETHPFYQQK---ESAAFMKAQGVQHESWAPFAEG--------------RNNMFSNEV-- 198
Cdd:cd19143 161 IEEAHEiadrLGLIPPVMEQPQYNLFHRERvevEYAPLYEKYGLGTTTWSPLASGlltgkynngipegsRLALPGYEWlk 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1070084393 199 ----------------LTSIAEKHNKSVAQVVLRWLVQREVV--TIPKSVRKERIVENFDIFDFELSL-----EDIEQI 254
Cdd:cd19143 241 drkeelgqekiekvrkLKPIAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEENLKALEVLPKLtpevmEKIEAI 319
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
32-254 |
1.35e-05 |
|
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: 45.89 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 32 VYEALMAGYRLIDTASGY---LNEEAVGRAIKrsGVPREELFITTKLWIQDAGYESAKI---------AFSKSLSKLQLD 99
Cdd:cd19145 39 IHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQLATKFGIHEIGGSGVEVrgdpayvraACEASLKRLDVD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 100 YLDLYLIHQ-----PYGDYYGawrAMEDLYREGKIRAIGVSNFHPD------------------RLMDLILHNEIVPAVN 156
Cdd:cd19145 117 YIDLYYQHRidttvPIEITMG---ELKKLVEEGKIKYIGLSEASADtirrahavhpitavqlewSLWTRDIEEEIIPTCR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 157 Q-----VETHPFyqqkeSAAFMKAQGVQHESWA--------PFAEGRN---NMFSNEVLTSIAEKHNKSVAQVVLRWLVQ 220
Cdd:cd19145 194 ElgigiVPYSPL-----GRGFFAGKAKLEELLEnsdvrkshPRFQGENlekNKVLYERVEALAKKKGCTPAQLALAWVLH 268
|
250 260 270
....*....|....*....|....*....|....*.
gi 1070084393 221 R--EVVTIPKSVRKERIVENFDIFDFELSLEDIEQI 254
Cdd:cd19145 269 QgeDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-227 |
3.10e-05 |
|
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: 44.63 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 38 AGYRLIDTASGYL----------NEEAVGRAIKRSGVpREELFITTKLwiqDAGYESAKIAFS--KSLSKLQldyldlyl 105
Cdd:cd19752 29 AGGNFLDTANNYAfwteggvggeSERLIGRWLKDRGN-RDDVVIATKV---GAGPRDPDGGPEspEGLSAET-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 106 IHQP-----------YGD-YYG-----------AWRAMEDLYREGKIRAIGVSNFHPDRLMDL--ILHNEIVP---AVNQ 157
Cdd:cd19752 97 IEQEidkslrrlgtdYIDlYYAhvddrdtpleeTLEAFNELVKAGKVRAIGASNFAAWRLERArqIARQQGWAefsAIQQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 158 veTHPFYQQKESAAFMKAQGVQHE--------------------------SWAPFAE---GRNNMFSNEVLTSIAEKHNK 208
Cdd:cd19752 177 --RHSYLRPRPGADFGVQRIVTDElldyassrpdltllayspllsgaytrPDRPLPEqydGPDSDARLAVLEEVAGELGA 254
|
250
....*....|....*....
gi 1070084393 209 SVAQVVLRWLVQREVVTIP 227
Cdd:cd19752 255 TPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
8-239 |
7.96e-05 |
|
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: 43.49 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 8 NGVKMPIIGFGVYqVPDAQECENAVYEALM-----AGYRLIDTASGYLNEEA---VGRAIKRSGVPREELFITTKLwiqd 79
Cdd:cd19159 9 SGLRVSCLGLGTW-VTFGGQISDEVAERLMtiayeSGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 80 agYESAKIAFSKSLSKLQLDYLDLYLIHQ---PYGDYYGAWR-----AMEDLYR-------EGKIRAIGVSNFHPDRLMD 144
Cdd:cd19159 84 --YWGGKAETERGLSRKHIIEGLKGSLQRlqlEYVDVVFANRpdsntPMEEIVRamthvinQGMAMYWGTSRWSAMEIME 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 145 LI----LHNEIVPAVNQVETHPFYQQKESAAFMKAQ---GVQHESWAPFA------------------------------ 187
Cdd:cd19159 162 AYsvarQFNMIPPVCEQAEYHLFQREKVEVQLPELYhkiGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlkeri 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1070084393 188 ---EGRNNMFSNEVLTSIAEKHNKSVAQVVLRWLVQREVVT--IPKSVRKERIVENF 239
Cdd:cd19159 242 vseEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSsvLLGSSTPEQLIENL 298
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
22-219 |
1.72e-04 |
|
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: 42.16 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 22 VPDAQECENAVYEAlmaGYRLIDTASGYLN---EEAVGRAikrsGVPREELFITTK---LWIQDAGYESAKIAFSKSLSK 95
Cdd:cd19075 19 AEAAAELLDAFLER---GHTEIDTARVYPDgtsEELLGEL----GLGERGFKIDTKanpGVGGGLSPENVRKQLETSLKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 96 LQLDYLDLYLIHQP-----YGDYYgawRAMEDLYREGKIRAIGVSNFHPDRLMDLIL----HNEIVPAVNQ--------- 157
Cdd:cd19075 92 LKVDKVDVFYLHAPdrstpLEETL---AAIDELYKEGKFKEFGLSNYSAWEVAEIVEickeNGWVLPTVYQgmynaitrq 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 158 VET--------H--PFY----------QQKESAAFMKAQGVQHESWAPFAEGRNNMFSN-------EVLTSIAEKHNKSV 210
Cdd:cd19075 169 VETelfpclrkLgiRFYaysplaggflTGKYKYSEDKAGGGRFDPNNALGKLYRDRYWKpsyfealEKVEEAAEKEGISL 248
|
....*....
gi 1070084393 211 AQVVLRWLV 219
Cdd:cd19075 249 AEAALRWLY 257
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
35-256 |
2.75e-04 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 41.76 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 35 ALMAGYRLIDTASGY----------LNEEAVGRAIKRSGvPREELFITTKLWIQDAGYESA------------KIAFSKS 92
Cdd:PRK10625 39 AVAQGINLIDVAEMYpvpprpetqgLTETYIGNWLAKRG-SREKLIIASKVSGPSRNNDKGirpnqaldrkniREALHDS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 93 LSKLQLDYLDLYLIHQP------YGDYYGAW-------------RAMEDLYREGKIRAIGVSNFHP---DRLMDLILHNE 150
Cdd:PRK10625 118 LKRLQTDYLDLYQVHWPqrptncFGKLGYSWtdsapavslletlDALAEQQRAGKIRYIGVSNETAfgvMRYLHLAEKHD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 151 IvPAVNQVEtHPFYQQKESAAFMKAQGVQHE-----SWAPFAEG---------------RNNMFSNEVLTS--------- 201
Cdd:PRK10625 198 L-PRIVTIQ-NPYSLLNRSFEVGLAEVSQYEgvellAYSCLAFGtltgkylngakpagaRNTLFSRFTRYSgeqtqkava 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1070084393 202 ----IAEKHNKSVAQVVLRWLVQREVV--TIPKSVRKERIVENFDIFDFELS------LEDIEQIST 256
Cdd:PRK10625 276 ayvdIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLSeevlaeIEAVHQVYT 342
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
7-74 |
3.66e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 41.30 E-value: 3.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1070084393 7 NNGVKMPIIGFG------VYQVPDAQECENAVYEALMAGYRLIDTASGY---LNEEAVGRAIKRSGVPREELFITTK 74
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFGPVSEEDAIASVREAFRLGINFFDTSPYYggtLSEKVLGKALKALGIPREKYVVSTK 82
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| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-225 |
3.17e-03 |
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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: 38.54 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 7 NNGVKMPIIGFGVYQ----VPDAQECENAVYEALMAGYRLIDTASGY-----LNEEAVGRAIKRSGVP-REELFITTKlw 76
Cdd:cd19151 7 RSGLKLPAISLGLWHnfgdVDRYENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTK-- 84
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 77 iqdAGYE----------SAK--IA-FSKSLSKLQLDYLDLYLIHQPYGD--YYGAWRAMEDLYREGKIRAIGVSNFHPD- 140
Cdd:cd19151 85 ---AGYTmwpgpygdwgSKKylIAsLDQSLKRMGLDYVDIFYHHRPDPEtpLEETMGALDQIVRQGKALYVGISNYPPEe 161
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070084393 141 -RLMDLILHNEIVPA-VNQVETHPFYQQKESAAF--MKAQGVQHESWAPFAEG-----------------RNNMFSNE-- 197
Cdd:cd19151 162 aREAAAILKDLGTPClIHQPKYSMFNRWVEEGLLdvLEEEGIGCIAFSPLAQGlltdrylngipedsraaKGSSFLKPeq 241
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250 260 270
....*....|....*....|....*....|....*...
gi 1070084393 198 ----------VLTSIAEKHNKSVAQVVLRWLVQREVVT 225
Cdd:cd19151 242 iteeklakvrRLNEIAQARGQKLAQMALAWVLRNKRVT 279
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