|
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 |
1.08e-178 |
|
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: 492.09 E-value: 1.08e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 4 VKLNNGIEMPLLGFGVFQMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYE 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 84 GAKAQFERSLNRLQLDYVDLYLIHQPYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNPF 163
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHPF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 164 NQQLHAVPWNQSRGIQPEAWAPFAEGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLD 243
Cdd:cd19133 161 NQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFD 240
|
250
....*....|....*
gi 1798692641 244 FELSSADMLQIAALD 258
Cdd:cd19133 241 FELSDEDMEAIAALD 255
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-271 |
1.09e-145 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 409.06 E-value: 1.09e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGAKA 87
Cdd:COG0656 1 NGVEIPALGLGTWQLPGE-EAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 88 QFERSLNRLQLDYVDLYLIHQPY-GDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQ 166
Cdd:COG0656 80 AFEESLERLGLDYLDLYLIHWPGpGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 167 LHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFEL 246
Cdd:COG0656 160 RELLAFCREHGIVVEAYSPLGRGK--LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFEL 237
|
250 260
....*....|....*....|....*
gi 1798692641 247 SSADMLQIAALDTATSAFFshrDPA 271
Cdd:COG0656 238 SDEDMAAIDALDRGERLGP---DPD 259
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
12-255 |
7.07e-124 |
|
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: 353.32 E-value: 7.07e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 12 MPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGAKAQFER 91
Cdd:cd19071 1 MPLIGLGTYKLKPE-ETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 92 SLNRLQLDYVDLYLIHQPYGDVHG--------AWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNPF 163
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVPGKEGgskearleTWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 164 NQQLHAVPWNQSRGIQPEAWAPFAEGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLD 243
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|..
gi 1798692641 244 FELSSADMLQIA 255
Cdd:cd19071 240 FELSEEDMAAID 251
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-258 |
1.27e-111 |
|
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: 322.46 E-value: 1.27e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 4 VKLNNGIEMPLLGFGVFQMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYE 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 84 GAKAQFERSLNRLQLDYVDLYLIHQPYGD-VHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNP 162
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHWPGKDkFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 163 FNQQLHAVPWNQSRGIQPEAWAPFAEGknGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVL 242
Cdd:cd19126 161 YLTQKELRGYCKSKGIVVEAWSPLGQG--GLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIF 238
|
250
....*....|....*.
gi 1798692641 243 DFELSSADMLQIAALD 258
Cdd:cd19126 239 DFELSEDDMTAIDALN 254
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
4-258 |
1.37e-108 |
|
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: 315.50 E-value: 1.37e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 4 VKLNNGIEMPLLGFGVFQMSdAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYE 83
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP-PEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 84 GAKAQFERSLNRLQLDYVDLYLIHQP----YGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIE 159
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPvpndFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 160 VNPFNQQLHAVPWNQSRGIQPEAWAPF----------AEGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKS 229
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgPTGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKS 239
|
250 260
....*....|....*....|....*....
gi 1798692641 230 VRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19127 240 VHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
3-259 |
1.85e-108 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 315.10 E-value: 1.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKLNNGIEMPLLGFGVFQMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSY 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 83 EGAKAQFERSLNRLQLDYVDLYLIHQPYGDV-HGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVN 161
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGKyKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 162 PFNQQLHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINV 241
Cdd:cd19157 161 PRLTQKELRDYCKKQGIQLEAWSPLMQGQ--LLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADV 238
|
250
....*....|....*...
gi 1798692641 242 LDFELSSADMLQIAALDT 259
Cdd:cd19157 239 FDFELSQEDMDKIDALNE 256
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
3-258 |
4.06e-106 |
|
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: 308.53 E-value: 4.06e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKLNNGIEMPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSY 82
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSND-EAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 83 EGAKAQFERSLNRLQLDYVDLYLIHQP---YGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIE 159
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPvpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 160 VNPFNQQLHAVPWNQSRGIQPEAWAPFAEGknGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENI 239
Cdd:cd19131 160 LHPRFQQRELRAFHAKHGIQTESWSPLGQG--GLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENF 237
|
250
....*....|....*....
gi 1798692641 240 NVLDFELSSADMLQIAALD 258
Cdd:cd19131 238 DVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
6-259 |
2.41e-101 |
|
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: 296.49 E-value: 2.41e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 6 LNNGIEMPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGA 85
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGD-EGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 86 KAQFERSLNRLQLDYVDLYLIHQP------YGDvhgAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIE 159
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHWPnpsrdlYVE---AWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 160 VNPFNQQLHAVPWNQSRGIQPEAWAPFAEGkNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENI 239
Cdd:cd19132 157 LHPYFPQAEQRAYHREHGIVTQSWSPLGRG-SGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENL 235
|
250 260
....*....|....*....|
gi 1798692641 240 NVLDFELSSADMLQIAALDT 259
Cdd:cd19132 236 AIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-259 |
1.76e-100 |
|
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: 294.81 E-value: 1.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 4 VKLNNGIEMPLLGFGVFQMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYE 83
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 84 GAKAQFERSLNRLQLDYVDLYLIHQPYGDVH-GAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNP 162
Cdd:cd19156 81 STLAAFEESLEKLGLDYVDLYLIHWPVKGKFkDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 163 FNQQLHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVL 242
Cdd:cd19156 161 LLTQEPLRKFCKEKNIAVEAWSPLGQGK--LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVF 238
|
250
....*....|....*..
gi 1798692641 243 DFELSSADMLQIAALDT 259
Cdd:cd19156 239 DFELTAEEIRQIDGLNT 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-258 |
1.50e-96 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 285.04 E-value: 1.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTV-KLNNGIEMPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQD 79
Cdd:PRK11565 3 NPTViKLQDGNVMPQLGLGVWQASNE-EVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 tsYEGAKAQFERSLNRLQLDYVDLYLIHQP------YGDvhgAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAP 153
Cdd:PRK11565 82 --HKRPREALEESLKKLQLDYVDLYLMHWPvpaidhYVE---AWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 154 AVNQIEVNPFNQQ--LHAvpWNQSRGIQPEAWAPFAEGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVR 231
Cdd:PRK11565 157 VINQIELHPLMQQrqLHA--WNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVT 234
|
250 260
....*....|....*....|....*..
gi 1798692641 232 KERMAENINVLDFELSSADMLQIAALD 258
Cdd:PRK11565 235 PSRIAENFDVFDFRLDKDELGEIAKLD 261
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-259 |
1.85e-93 |
|
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: 277.63 E-value: 1.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKLNNGIEMPLLGFGVFQMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQ----QTGIARNELFVTTKLWLQ 78
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIRekiaEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 79 DTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYG------------------DVHGAWRAMEELQQAGKIRAIGVSNFHPD 140
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAfkenndsesngdgslsdiDYLETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 141 RLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPF-------AEGKNGLFQHPVLTAIGQKYGKSVGQV 213
Cdd:cd19116 162 QINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvprgQTNPPPRLDDPTLVAIAKKYGKTTAQI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1798692641 214 VLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALDT 259
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNT 287
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
12-257 |
1.45e-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: 274.51 E-value: 1.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 12 MPLLGFGVFQMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQ----TGIARNELFVTTKLWLQDTSYEGAKA 87
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDllpkYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 88 QFERSLNRLQLDYVDLYLIH-------QPYGDVH-----GAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAV 155
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHwpgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 156 NQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERM 235
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 1798692641 236 AENINVLDFELSSADMLQIAAL 257
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-257 |
1.60e-88 |
|
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: 264.19 E-value: 1.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKLNNGIEMPLLGFGVFQMsdAAECERAVIDAI-DTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQD 79
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTSHS--GGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 TSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVHG---------AWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNK 150
Cdd:cd19135 80 YGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketraeTWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 151 VAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSV 230
Cdd:cd19135 160 VVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK--ALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKST 237
|
250 260
....*....|....*....|....*..
gi 1798692641 231 RKERMAENINVLDFELSSADMLQIAAL 257
Cdd:cd19135 238 KEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
6-258 |
8.11e-86 |
|
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: 257.15 E-value: 8.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 6 LNNGIEMPLLGFGVFQMSDAAEcERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGA 85
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADT-QRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 86 KAQFERSLNRLQLDYVDLYLIHQPY---GDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNP 162
Cdd:cd19130 83 AAAFAESLAKLGLDQVDLYLVHWPTpaaGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 163 FNQQLHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVL 242
Cdd:cd19130 163 AYQQRTIRDWAQAHDVKIEAWSPLGQGK--LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVF 240
|
250
....*....|....*.
gi 1798692641 243 DFELSSADMLQIAALD 258
Cdd:cd19130 241 DFDLTDTEIAAIDALD 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
3-261 |
2.29e-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: 2.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKLNNGIEMPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSY 82
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDD-EAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 83 EGAKAQFERSLNRLQLDYVDLYLIHQPYGDVH---GAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIE 159
Cdd:cd19134 81 TASQAACRASLERLGLDYVDLYLIHWPAGREGkyvDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 160 VNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENI 239
Cdd:cd19134 161 LHPLLNQAELRKVNAQHGIVTQAYSPLGVGR--LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNL 238
|
250 260
....*....|....*....|..
gi 1798692641 240 NVLDFELSSADMLQIAALDTAT 261
Cdd:cd19134 239 DVFDFELTADHMDALDGLDDGT 260
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
5-251 |
8.01e-83 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 250.73 E-value: 8.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 5 KLNNGIEMPLLGFGVFQmSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQ---QTGIA-RNELFVTTKLWLQDT 80
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQ-ADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKklfEDGVVkREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 81 SYEGAKAQFERSLNRLQLDYVDLYLIHQPYG----------------DVHGAWRAMEELQQAGKIRAIGVSNFHPDRLAD 144
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpepeevlppDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 145 LIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPF-----AEGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIF 219
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgtTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270
....*....|....*....|....*....|..
gi 1798692641 220 QRGIVSLAKSVRKERMAENINVLDFELSSADM 251
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDF 274
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
8-257 |
9.53e-83 |
|
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: 249.10 E-value: 9.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGAKA 87
Cdd:cd19140 4 NGVRIPALGLGTYPLTGE-ECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 88 QFERSLNRLQLDYVDLYLIHQPYGDVHGAW--RAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQ 165
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWPNKDVPLAEtlGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 166 QLHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQR-GIVSLAKSVRKERMAENINVLDF 244
Cdd:cd19140 163 QRKLLDAAREHGIALTAYSPLARGE--VLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDF 240
|
250
....*....|...
gi 1798692641 245 ELSSADMLQIAAL 257
Cdd:cd19140 241 TLSDEEMARIAAL 253
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
12-254 |
1.13e-82 |
|
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: 248.72 E-value: 1.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 12 MPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGAKAQFER 91
Cdd:cd19073 1 IPALGLGTWQLRGD-DCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 92 SLNRLQLDYVDLYLIHQPYGDVHGA--WRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHA 169
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWPNPTVPLEetLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 170 VPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSA 249
Cdd:cd19073 160 LEYCRENDIVITAYSPLARGE--VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSE 237
|
....*
gi 1798692641 250 DMLQI 254
Cdd:cd19073 238 DVAKI 242
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-264 |
8.41e-82 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 248.48 E-value: 8.41e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 4 VKLNNGIEMPLLGFGVFQMSdAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQ---TGI-ARNELFVTTKLWLQD 79
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 TSYEGAKAQFERSLNRLQLDYVDLYLIHQPYG---------------------DVHGAWRAMEELQQAGKIRAIGVSNFH 138
Cdd:cd19154 83 HAPEDVEEALRESLKKLQLEYVDLYLIHAPAAfkddegesgtmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVSNFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 139 PDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPF--------------AEGKNgLFQHPVLTAIGQ 204
Cdd:cd19154 163 NDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgranftkstgvSPAPN-LLQDPIVKAIAE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 205 KYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALDTATSAF 264
Cdd:cd19154 242 KHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
6-259 |
5.60e-81 |
|
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: 246.53 E-value: 5.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 6 LNNGIEMPLLGFGVFQmSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQT-----GIARNELFVTTKLWLQDT 80
Cdd:cd19106 1 LHTGQKMPLIGLGTWK-SKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 81 SYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVHG---------------------AWRAMEELQQAGKIRAIGVSNFHP 139
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGdnpfpknpdgtirydsthykeTWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 140 DRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPF--------AEGKNGLFQHPVLTAIGQKYGKSVG 211
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwaKPDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1798692641 212 QVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALDT 259
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNR 287
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
9-256 |
9.28e-80 |
|
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: 242.14 E-value: 9.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGV---FQMSDAAECERAVID----AIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTS 81
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQRDLVDsvklALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 82 YEGAkaqFERSLNRLQLDYVDLYLIHQPY------GDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAV 155
Cdd:cd19120 81 PREA---LRKSLAKLGVDYVDLYLIHSPFfakeggPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 156 NQIEVNPF--NQQLHAVPWNQSRGIQPEAW---APFAEGKNGLFQhPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSV 230
Cdd:cd19120 158 NQIEFHPYlyPQQPALLEYCREHGIVVSAYsplSPLTRDAGGPLD-PVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSS 236
|
250 260
....*....|....*....|....*.
gi 1798692641 231 RKERMAENINVLDFELSSADMLQIAA 256
Cdd:cd19120 237 KEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-258 |
3.04e-78 |
|
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: 239.24 E-value: 3.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKLNNGIEMPLLGFGVFQmSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNAL----QQTGIARNELFVTTKLW 76
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWK-SKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 77 LQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVHGA--------------------WRAMEELQQAGKIRAIGVSN 136
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGVgfpesgedllslspipledtWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 137 FHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPF----------AEGKNGLFQHPVLTAIGQKY 206
Cdd:cd19123 160 FSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLgsgdrpaamkAEGEPVLLEDPVINKIAEKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1798692641 207 GKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19123 240 GASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALD 291
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
3-258 |
4.23e-78 |
|
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: 239.31 E-value: 4.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKLNNGIEMPLLGFGVFQMsDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQ---TG-IARNELFVTTKLWlq 78
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEafkTGlVKREDLFITTKLW-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 79 DTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVH-------------------------GAWRAMEELQQAGKIRAIG 133
Cdd:cd19112 79 NSDHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvgttgsalgedgvldidvtisleTTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 134 VSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKNGL--------FQHPVLTAIGQK 205
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAewfgsvspLDDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1798692641 206 YGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLD 291
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-257 |
6.86e-78 |
|
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: 237.78 E-value: 6.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 2 QTVKLNNGIEMPLLGFGVFQmSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWlqDTS 81
Cdd:cd19117 4 KTFKLNTGAEIPAVGLGTWQ-SKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLW--CTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 82 YEGAKAQFERSLNRLQLDYVDLYLIHQPYG-----------------------DVHGAWRAMEELQQAGKIRAIGVSNFH 138
Cdd:cd19117 81 HRRVEEALDQSLKKLGLDYVDLYLMHWPVPldpdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIGVSNFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 139 PDRLADLIA--FNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKNGLFQHPVLTAIGQKYGKSVGQVVLR 216
Cdd:cd19117 161 IKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTPAQVIIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1798692641 217 WIFQRGIVSLAKSVRKERMAENINVldFELSSADMLQIAAL 257
Cdd:cd19117 241 WGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
8-257 |
1.22e-77 |
|
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: 237.17 E-value: 1.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGVF-QMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQ---TG--IARNELFVTTKLWLQDTS 81
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGlvKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 82 YEGAKAQFERSLNRLQLDYVDLYLIHQPYG------------------DVHGAWRAMEELQQAGKIRAIGVSNFHPDRLA 143
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSlkpgkfsfpieeedflpfDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 144 DLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAE-----GKNGLFQHPVLTAIGQKYGKSVGQVVLRWI 218
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGApgtkwGSNAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1798692641 219 FQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAAL 257
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
2-258 |
1.06e-72 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 225.40 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 2 QTVKLNNGIEMPLLGFGVFQMsDAAECERAVIDAIDTGYRLIDTAASYQNETQVGN----ALQQTGIARNELFVTTKLWL 77
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKL-DNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEgvnrAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 78 QDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP-------------------------YGDVH--GAWRAMEELQQAGKIR 130
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPilDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 131 AIGVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFA-----EGKNG-------LFQHPV 198
Cdd:cd19113 160 SIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvELNQGralntptLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 199 LTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLD 299
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|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
9-264 |
9.78e-70 |
|
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: 216.98 E-value: 9.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVFQMSdAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQ---QTG-IARNELFVTTKLWLQDTSYEG 84
Cdd:cd19111 1 GFPMPVIGLGTYQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 85 AKAQFERSLNRLQLDYVDLYLIHQPYG---------------DVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFN 149
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGfvnkkdkgerelassDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 150 KVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAE----------GKNGLFQHPVLTAIGQKYGKSVGQVVLRWIF 219
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpgranqslwpDQPDLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1798692641 220 QRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALDTATSAF 264
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYF 284
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|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-258 |
6.81e-69 |
|
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: 215.75 E-value: 6.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 2 QTVKLNNGIEMPLLGFGVFQMsDAAECERAVIDAIDTGYRLIDTAASYQNETQVGN----ALQQTGIARNELFVTTKLWL 77
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLWKV-NNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQgvarAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 78 QDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP----YGD----------------------VHGAWRAMEELQQAGKIRA 131
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPialkYVDpavryppgwfydgkkvefsnapIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 132 IGVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPF------------AEGKNGLFQHPVL 199
Cdd:cd19115 162 IGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFgpqsfleldlpgAKDTPPLFEHDVI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1798692641 200 TAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19115 242 KSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALD 300
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-258 |
1.18e-66 |
|
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: 210.07 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 4 VKLNNGIEMPLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQ---QTG-IARNELFVTTKLWLQD 79
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPE-EIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwiDSGkVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 TSYEGAKAQFERSLNRLQLDYVDLYLIHQPYG-----------------------DVHGAWRAMEELQQAGKIRAIGVSN 136
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGslskeddsgkldptgehkqdyttDLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 137 FHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAP--------FAEGKNG-------LFQHPVLTA 201
Cdd:cd19155 163 FNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPlgspgaahFSPGTGSpsgsspdLLQDPVVKA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1798692641 202 IGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19155 243 IAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLD 299
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
9-259 |
1.18e-65 |
|
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: 207.41 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVFQMsDAAECERAVIDAIDTGYRLIDTAASYQNETQVG----NALQQTGIARNELFVTTKLWLQDTSYEG 84
Cdd:cd19114 1 GDKMPLVGFGTAKI-KANETEEVIYNAIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 85 AKAQFERSLNRLQLDYVDLYLIHQP----YGD-----------------------VHGAWRAMEELQQAGKIRAIGVSNF 137
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPipaaYVDpaenypflwkdkelkkfpleqspMQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 138 HPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFA---------EGKN--GLFQHPVLTAIGQKY 206
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtkHLKHftNLLEHPVVKKLADKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1798692641 207 GKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALDT 259
Cdd:cd19114 240 KRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEA 292
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
6-257 |
1.19e-65 |
|
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: 206.49 E-value: 1.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 6 LNNGIEMPLLGFGVFQmSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQ-----QTGIARNELFVTTKLWLQDT 80
Cdd:cd19118 1 LNTGNKIPAIGLGTWQ-AEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKellkeEPGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 81 SYEGAKAQFERSLNRLQLDYVDLYLIH-----QPYGDVHG---------------------AWRAMEELQQAGKIRAIGV 134
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHwpvafKPTGDLNPltavptnggevdldlsvslvdTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 135 SNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPF---AEGKNGLFQHPVLTAIGQKYGKSVG 211
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLPLLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1798692641 212 QVVLRWIFQRGIVSLAKSVRKERMAENINvlDFELSSADMLQIAAL 257
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
12-257 |
8.69e-65 |
|
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: 203.35 E-value: 8.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 12 MPLLGFGVFQMSDAAeCERAVIDAIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGAKAQFER 91
Cdd:cd19139 1 IPAFGLGTFRLKDDV-VIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 92 SLNRLQLDYVDLYLIH--QPYG--DVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIA-FNKVAPAVNQIEVNPFNQQ 166
Cdd:cd19139 80 SLEKLRTDYVDLTLIHwpSPNDevPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAvVGAGAIATNQIELSPYLQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 167 LHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFEL 246
Cdd:cd19139 160 RKLVAHCKQHGIHVTSYMTLAYGK--VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTL 237
|
250
....*....|.
gi 1798692641 247 SSADMLQIAAL 257
Cdd:cd19139 238 DADDMAAIAAL 248
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
2-258 |
4.66e-64 |
|
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: 203.23 E-value: 4.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 2 QTVKLNNGIEMPLLGFGVFQMSD--AAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQqTGIA-----RNELFVTTK 74
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIR-SKIAdgtvkREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 LWLQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYG----------DVHG-----------AWRAMEELQQAGKIRAIG 133
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeelfpkDENGklifdtvdlcaTWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 134 VSNFHpDRLADLIaFNK----VAPAVNQIEVNPFNQQLHAVPWNQSRGI-----------QPEAW----APFaegkngLF 194
Cdd:cd19108 160 VSNFN-RRQLEMI-LNKpglkYKPVCNQVECHPYLNQSKLLDFCKSKDIvlvaysalgsqRDKEWvdqnSPV------LL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1798692641 195 QHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19108 232 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLN 295
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
9-254 |
1.06e-63 |
|
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: 202.26 E-value: 1.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVFQmSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQT----GIARNELFVTTKLWlqDTSYEG 84
Cdd:cd19107 1 GAKMPILGLGTWK-SPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKikeqVVKREDLFIVSKLW--CTFHEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 85 A--KAQFERSLNRLQLDYVDLYLIHQPYGDVHG---------------------AWRAMEELQQAGKIRAIGVSNFHPDR 141
Cdd:cd19107 78 GlvKGACQKTLSDLKLDYLDLYLIHWPTGFKPGkelfpldesgnvipsdttfldTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 142 LADLIafNKVA----PAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAE--------GKNGLFQHPVLTAIGQKYGKS 209
Cdd:cd19107 158 IERIL--NKPGlkykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwakpEDPSLLEDPKIKEIAAKHNKT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1798692641 210 VGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQI 254
Cdd:cd19107 236 TAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-245 |
9.18e-62 |
|
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: 196.60 E-value: 9.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKLNNGIEMPLLGFGVFQmSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQT---GIARNELFVTTKLWl 77
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQ-AKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 78 qDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP-------------------------YGDVHGaWRAMEELQQAGKIRAI 132
Cdd:cd19121 79 -STYHRRVELCLDRSLKSLGLDYVDLYLVHWPvllnpngnhdlfptlpdgsrdldwdWNHVDT-WKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 133 GVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKNGLFQHPVLTAIGQKYGKSVGQ 212
Cdd:cd19121 157 GVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGPGT 236
|
250 260 270
....*....|....*....|....*....|...
gi 1798692641 213 VVLRWIFQRGIVSLAKSVRKERMAENINVLDFE 245
Cdd:cd19121 237 VLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD 269
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-258 |
1.94e-60 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 192.55 E-value: 1.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 12 MPLLGFGVFQMSDaaeceRAVID----AIDTGYRLIDTAASYQNETQVGNALQQTGIARNELFVTTKLWLQDTSYEGAKA 87
Cdd:PRK11172 3 IPAFGLGTFRLKD-----QVVIDsvktALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 88 QFERSLNRLQLDYVDLYLIHQPY-GDVHGAWRAMEELQQA---GKIRAIGVSNFHPDRLADLI-AFNKVAPAVNQIEVNP 162
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPSpNDEVSVEEFMQALLEAkkqGLTREIGISNFTIALMKQAIaAVGAENIATNQIELSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 163 FNQQLHAVPWNQSRGIQPEAWAPFAEGKngLFQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVL 242
Cdd:PRK11172 158 YLQNRKVVAFAKEHGIHVTSYMTLAYGK--VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQ 235
|
250
....*....|....*.
gi 1798692641 243 DFELSSADMLQIAALD 258
Cdd:PRK11172 236 DLQLDAEDMAAIAALD 251
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
9-254 |
3.42e-60 |
|
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: 192.06 E-value: 3.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFG----VFQMSDAAECERAVID----AIDTGYRLIDTAASYQN---ETQVGNALQqtGIARNELFVTTKLWL 77
Cdd:cd19072 1 GEEVPVLGLGtwgiGGGMSKDYSDDKKAIEalryAIELGINLIDTAEMYGGghaEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 78 QDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP--YGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAP-A 154
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPnpSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPiV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 155 VNQIEVNPFNQ--QLHAVPWNQSRGIQPEAWAPFAEGK-NGLFQHPVLTAIGQKYGKSVGQVVLRWIFQR-GIVSLAKSV 230
Cdd:cd19072 159 ANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEKGKlSNAKGSPLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKAS 238
|
250 260
....*....|....*....|....
gi 1798692641 231 RKERMAENINVLDFELSSADMLQI 254
Cdd:cd19072 239 NIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
7-241 |
2.89e-59 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 190.75 E-value: 2.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 7 NNGIEMPLLGFGVFqMSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQT----GIARNELFVTTKLWLQDTSY 82
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVfkagKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 83 EGAKAQFERSLNRLQLDYVDLYLIHQPYG----------DVHGA------------WRAMEELQQAGKIRAIGVSNFHPD 140
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFAfqpgdeqdprDANGNviyddgvtlldtWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 141 RLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEG-KNGLFQHPVLTAIGQKYGKSVGQVVLRWIF 219
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260
....*....|....*....|..
gi 1798692641 220 QRGIVSLAKSVRKERMAENINV 241
Cdd:cd19129 240 QRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
2-258 |
7.04e-58 |
|
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: 185.92 E-value: 7.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 2 QTVKLNNGIEMPLLGFGVFQM----SDAAECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQqtGIaRNELFVTTK 74
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIR--GR-RDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 LWLQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPyGDVHGA--WRAMEELQQAGKIRAIGVSNFHPDRLADLIAF-NKV 151
Cdd:cd19138 78 VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR-GGVPLAetVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVpGGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 152 APAVNQIEVNPFNQ--QLHAVPWNQSRGIQPEAWAPFAEG---KNGLFQHPVLTAIGQKYGKSVGQVVLRW-IFQRGIVS 225
Cdd:cd19138 157 NCAANQVLYNLGSRgiEYDLLPWCREHGVPVMAYSPLAQGgllRRGLLENPTLKEIAARHGATPAQVALAWvLRDGNVIA 236
|
250 260 270
....*....|....*....|....*....|...
gi 1798692641 226 LAKSVRKERMAENINVLDFELSSADmlqIAALD 258
Cdd:cd19138 237 IPKSGSPEHARENAAAADLELTEED---LAELD 266
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
5-250 |
1.06e-56 |
|
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: 183.98 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 5 KLNNGIEMPLLGFGVFQmSDAAECE--RAVIDAIDTGYRLIDTAASYQNETQVGNALQ-----QTGIARNELFVTTKLWL 77
Cdd:cd19122 2 TLNNGVKIPAVGFGTFA-NEGAKGEtyAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRdflkeNPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 78 QDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYG-------------------------DVHGAWRAMEELQQAGKIRAI 132
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAaekndqrspklgpdgkyvilkdlteNPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 133 GVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKN------GLFQHPVLTAIGQKY 206
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQvpstgeRVSENPTLNEVAEKG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1798692641 207 GKSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLdfELSSAD 250
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSI--ELSDED 282
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
9-258 |
2.78e-56 |
|
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: 183.46 E-value: 2.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVFQ---MSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQT----GIARNELFVTTKLWLQDTS 81
Cdd:cd19109 1 GNSIPIIGLGTYSepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 82 YEGAKAQFERSLNRLQLDYVDLYLIHQPYG---------------------DVHGAWRAMEELQQAGKIRAIGVSNFHPD 140
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAfkpgdeiyprdengkwlyhktNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 141 RLaDLIaFNKVA----PAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKNG---------LFQHPVLTAIGQKYG 207
Cdd:cd19109 161 QL-ELI-LNKPGlkhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPiwvnvssppLLEDPLLNSIGKKYN 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1798692641 208 KSVGQVVLRWIFQRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19109 239 KTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALN 289
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
13-257 |
1.42e-55 |
|
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: 180.41 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 13 PLLGFGVFQMSDAaECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQ----TGIARNELFVTTKLWLQDTSYEGAKAQ 88
Cdd:cd19128 2 PRLGFGTYKITES-ESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 89 FERSLNRLQLDYVDLYLIHQPYGDVHGA---------------------WRAMEELQQAGKIRAIGVSNFHPDRLADLIA 147
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAFDMDTdgdprddnqiqslskkpledtWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 148 FNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAP----FAEGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQR-- 221
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPlggsYGDGNLTFLNDSELKALATKYNTTPPQVIIAWHLQKwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1798692641 222 GIVS-LAKSVRKERMAENINVLDFELSSADMLQIAAL 257
Cdd:cd19128 241 KNYSvIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
11-258 |
1.66e-55 |
|
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: 181.31 E-value: 1.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 11 EMPLLGFGVFQMSdAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQ---QTGIARNE-LFVTTKLWLQDTSYEGAK 86
Cdd:cd19110 3 DIPAVGLGTWKAS-PGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekiKEGVVRREdLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 87 AQFERSLNRLQLDYVDLYLIHQPYG---------------------DVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADL 145
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGfkpgepdlpldrsgmvipsdtDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 146 IafNK----VAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKNG--LFQHPVLTAIGQKYGKSVGQVVLRWIF 219
Cdd:cd19110 162 L--NKpglrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGvdLIDDPVIQRIAKKHGKSPAQILIRFQI 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1798692641 220 QRGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:cd19110 240 QRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLD 278
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
15-258 |
4.29e-52 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 172.11 E-value: 4.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQM------SDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIARNELFVTTKL------WLQD 79
Cdd:pfam00248 1 IGLGTWQLgggwgpISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 TSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVH--GAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAVNQ 157
Cdd:pfam00248 81 GSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPieETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 158 IEVNPFN--QQLHAVPWNQSRGIQPEAWAPFAEG-----------------------KNGLFQH--PVLTAIGQKYGKSV 210
Cdd:pfam00248 161 VEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkGTPLNLEalEALEEIAKEHGVSP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1798692641 211 GQVVLRWIFQ--RGIVSLAKSVRKERMAENINVLDFELSSADMLQIAALD 258
Cdd:pfam00248 241 AQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-239 |
5.71e-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: 169.22 E-value: 5.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 4 VKLNNGIEMPLLGFGVFQ-MSDAAECERAVIDAIDTGYRLIDTAASYQNETQVGNALQQ---TG-IARNELFVTTKLWlq 78
Cdd:cd19119 4 FKLNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRaidDGsIKREELFITTKVW-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 79 DTSYEGAKAQFERSLNRLQLDYVDLYLIHQPY---------------------------GDVHGAWRAMEELQQAGKIRA 131
Cdd:cd19119 82 PTFYDEVERSLDESLKALGLDYVDLLLVHWPVcfekdsddsgkpftpvnddgktryaasGDHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 132 IGVSNFHPDRLADLIAFNKVAPAVNQIEVNPFNQQLHAVPWNQSRGIQPEAWAPFAEGKNGLFQHPVLTAIGQKYGKSVG 211
Cdd:cd19119 162 IGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKYNVSTG 241
|
250 260
....*....|....*....|....*...
gi 1798692641 212 QVVLRWIFQRGIVSLAKSVRKERMAENI 239
Cdd:cd19119 242 DILISYHVRQGVIVLPKSLKPVRIVSNG 269
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-257 |
1.42e-50 |
|
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: 168.82 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKL-NNGIEMPLLGFGVFQMS------DAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQqtGIARNELF 70
Cdd:COG0667 1 MEYRRLgRSGLKVSRLGLGTMTFGgpwggvDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 71 VTTKL--------WLQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHPD 140
Cdd:COG0667 79 IATKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTpiEETLGALDELVREGKIRYIGVSNYSAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 141 RLADL--IAFNKVAPAVNQIEVNPFNQQLHA--VPWNQSRGIQPEAWAPFAEG-----------------KNGLFQHPV- 198
Cdd:COG0667 159 QLRRAlaIAEGLPPIVAVQNEYSLLDRSAEEelLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdrAATNFVQGYl 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1798692641 199 ----------LTAIGQKYGKSVGQVVLRWIFQRGIVSL----AKSVrkERMAENINVLDFELSSADMLQIAAL 257
Cdd:COG0667 239 ternlalvdaLRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARSP--EQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
9-254 |
9.49e-44 |
|
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: 150.37 E-value: 9.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVFQMS-------DAAECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQQTgiaRNELFVTTKLWLQ 78
Cdd:cd19084 1 DLKVSRIGLGTWAIGgtwwgevDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKCGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 79 ---------DTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIA 147
Cdd:cd19084 78 wdggkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTpiEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 148 FNKVapAVNQIEVNPFNQQL--HAVPWNQSRGIQPEAWAPFAEG-------------------KNGLFQHP--------- 197
Cdd:cd19084 158 YGPI--VSLQPPYSMLEREIeeELLPYCRENGIGVLPYGPLAQGlltgkykkeptfppddrrsRFPFFRGEnfeknleiv 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1798692641 198 -VLTAIGQKYGKSVGQVVLRWIFQRGIVSL----AKSVrkERMAENINVLDFELSSADMLQI 254
Cdd:cd19084 236 dKLKEIAEKYGKSLAQLAIAWTLAQPGVTSaivgAKNP--EQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
15-261 |
1.40e-42 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 147.35 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQMSDAA--------ECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQQTgiaRNELFVTTKLWLQDTSYE 83
Cdd:cd19085 4 LGLGCWQFGGGYwwgdqddeESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR---RDDVVIATKVSPDNLTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 84 GAKAQFERSLNRLQLDYVDLYLIHQPYGDVHGA--WRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVapAVNQIEVN 161
Cdd:cd19085 81 DVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEetMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI--DSNQLPYN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 162 PFNQQLHA--VPWNQSRGIQPEAWAPFAEG-----------------KNGLFQH-------------PVLTAIGQKYGKS 209
Cdd:cd19085 159 LLWRAIEYeiLPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdaRTRLFRHfepgaeeetfealEKLKEIADELGVT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1798692641 210 VGQVVLRWIFQR-GIVS-LAKSVRKERMAENINVLDFELSSADMlqiAALDTAT 261
Cdd:cd19085 239 MAQLALAWVLQQpGVTSvIVGARNPEQLEENAAAVDLELSPSVL---ERLDEIS 289
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
9-251 |
3.34e-41 |
|
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: 143.09 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVFQM--------SDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQtgIARNELFVTTKLWL 77
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 78 QDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAPAV 155
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIplEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 156 NQIEVNPFNQQLH---AVPWNQSRGIQPEAWAPFAEGknGLFQHPVLTAIGQKYGKSVGQVVLRWIFQR-GIVSLAKSVR 231
Cdd:cd19137 159 NQVKYNLEDRDPErdgLLEYCQKNGITVVAYSPLRRG--LEKTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGR 236
|
250 260
....*....|....*....|
gi 1798692641 232 KERMAENINVLDFELSSADM 251
Cdd:cd19137 237 VEHLKENLKATEIKLSEEEM 256
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
11-258 |
3.07e-40 |
|
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: 141.21 E-value: 3.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 11 EMPLLGFGVFQMSD----------AAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGiARNELFVTTKL-- 75
Cdd:cd19093 1 EVSPLGLGTWQWGDrlwwgygeygDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKFap 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 76 ----WLQDTSYEGAKAqferSLNRLQLDYVDLYLIHQP---YGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRL---ADL 145
Cdd:cd19093 80 lpwrLTRRSVVKALKA----SLERLGLDSIDLYQLHWPgpwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLrraHKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 146 IAFNKVAPAVNQIEVN-----PFNQQLhaVPWNQSRGIQPEAWAPFA--------------EGKNGLFQHP--------- 197
Cdd:cd19093 156 LKERGVPLASNQVEYSllyrdPEQNGL--LPACDELGITLIAYSPLAqglltgkyspenppPGGRRRLFGRknlekvqpl 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1798692641 198 --VLTAIGQKYGKSVGQVVLRWIFQRGIVSL--AKSVrkERMAENINVLDFELSSADMlqiAALD 258
Cdd:cd19093 234 ldALEEIAEKYGKTPAQVALNWLIAKGVVPIpgAKNA--EQAEENAGALGWRLSEEEV---AELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-239 |
3.33e-39 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 136.88 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQMS---DAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIaRNELFVTTKL---WLQDTSYEGA 85
Cdd:cd06660 3 LGLGTMTFGgdgDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGghpPGGDPSRSRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 86 -----KAQFERSLNRLQLDYVDLYLIHQPygD----VHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIA----FNKVA 152
Cdd:cd06660 82 spehiRRDLEESLRRLGTDYIDLYYLHRD--DpstpVEETLEALNELVREGKIRYIGVSNWSAERLAEALAyakaHGLPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 153 PAVNQIEVNPFNQQLH---AVPWNQSRGIQPEAWAPFAEGknglfqhpvltaigqkygksVGQVVLRWIFQRGIVS--LA 227
Cdd:cd06660 160 FAAVQPQYSLLDRSPMeeeLLDWAEENGLPLLAYSPLARG--------------------PAQLALAWLLSQPFVTvpIV 219
|
250
....*....|..
gi 1798692641 228 KSVRKERMAENI 239
Cdd:cd06660 220 GARSPEQLEENL 231
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-169 |
3.75e-36 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 132.25 E-value: 3.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKL-NNGIEMPLLGFGV--FQMSDAAECERaVID-AIDTGYRLIDTAASY-QNETQVGNALQQTgiaRNELFVTTKL 75
Cdd:COG1453 1 MQYRRLgKTGLEVSVLGFGGmrLPRKDEEEAEA-LIRrAIDNGINYIDTARGYgDSEEFLGKALKGP---RDKVILATKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 76 --WLQDtsYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVH--------GAWRAMEELQQAGKIRAIGVSnFHpDRLADL 145
Cdd:COG1453 77 ppWVRD--PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDlekvlkpgGALEALEKAKAEGKIRHIGFS-TH-GSLEVI 152
|
170 180 190
....*....|....*....|....*....|.
gi 1798692641 146 IAfnkvapAVN-------QIEVNPFNQQLHA 169
Cdd:COG1453 153 KE------AIDtgdfdfvQLQYNYLDQDNQA 177
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-146 |
5.51e-35 |
|
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: 126.06 E-value: 5.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFG--VFQMSDAAECERAVIDAIDTGYRLIDTAASYQN-ETQVGNALQQtgiARNELFVTTKLWlqDTSYEGA 85
Cdd:cd19100 8 GLKVSRLGFGggPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTG--ARDYEGA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 86 KAQFERSLNRLQLDYVDLYLIH---------QPYGDvHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLI 146
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHavdteedldQVFGP-GGALEALLEAKEEGKIRFIGISGHSPEVLLRAL 151
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
7-247 |
9.22e-34 |
|
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: 124.21 E-value: 9.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 7 NNGIEMPLLGFGVFQMSD----AAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIARNELFVTTK----- 74
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADwgesAEELLSLIEAALELGITTFDHADIYgggKCEELFGEALALNPGLREKIEIQTKcgirl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 ------LWLQ--DTSYEGAKAQFERSLNRLQLDYVDLYLIHQP-----YGDVHgawRAMEELQQAGKIRAIGVSNFHPDR 141
Cdd:cd19092 81 gddprpGRIKhyDTSKEHILASVEGSLKRLGTDYLDLLLLHRPdplmdPEEVA---EAFDELVKSGKVRYFGVSNFTPSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 142 LADLIAFNKVAPAVNQIEVNPfnqqLHAVPWN-------QSRGIQPEAWAPFAEGKngLFQ---------HPVLTAIGQK 205
Cdd:cd19092 158 IELLQSYLDQPLVTNQIELSL----LHTEAIDdgtldycQLLDITPMAWSPLGGGR--LFGgfderfqrlRAALEELAEE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1798692641 206 YGKSVGQVVLRWIFQR--GIVSLAKSVRKERMAENINVLDFELS 247
Cdd:cd19092 232 YGVTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-135 |
1.17e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 117.69 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKL-NNGIEMPLLGFGVfqMSDAAECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQqtGIARNELFVTTKLW 76
Cdd:cd19105 1 MPYRTLgKTGLKVSRLGFGG--GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKAS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1798692641 77 LQD--TSYEGAKAQFERSLNRLQLDYVDLYLIHQP----YGDVHGAW-RAMEELQQAGKIRAIGVS 135
Cdd:cd19105 77 PRLdkKDKAELLKSVEESLKRLQTDYIDIYQLHGVdtpeERLLNEELlEALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-241 |
5.69e-31 |
|
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: 115.65 E-value: 5.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQMS-------DAAECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQQTgiaRNELFVTTKL--------- 75
Cdd:cd19086 6 IGFGTWGLGgdwwgdvDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR---RDKVVIATKFgnrfdggpe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 76 WLQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP---YGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVA 152
Cdd:cd19086 83 RPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPpdeVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 153 pAVnQIEVNPFNQQ--LHAVPWNQSRGIQPEAWAPFAEGknglfqhpVLTaigqkyGKsVGQVVLRWIFQRGIVSL---- 226
Cdd:cd19086 163 -VV-QVIYNLLDQRpeEELFPLAEEHGVGVIARVPLASG--------LLT------GK-LAQAALRFILSHPAVSTvipg 225
|
250
....*....|....*
gi 1798692641 227 AKSVrkERMAENINV 241
Cdd:cd19086 226 ARSP--EQVEENAAA 238
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
3-261 |
1.62e-30 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 115.98 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKL-NNGIEMPLLGFG--------VFQMSDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQqtGIARNELF 70
Cdd:cd19083 1 KVKLgKSDIDVNPIGLGtnavgghnLYPNLDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 71 VTTKLWLQ--------DTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHPD 140
Cdd:cd19083 79 IATKGAHKfggdgsvlNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETpkAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 141 RLAdliAFNKvAPAVN--QIEVNPFNQQL--HAVPWNQSRGIQPEAWAPFAEG-------------------KNGLFQHP 197
Cdd:cd19083 159 QLK---EANK-DGYVDvlQGEYNLLQREAeeDILPYCVENNISFIPYFPLASGllagkytkdtkfpdndlrnDKPLFKGE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1798692641 198 V----------LTAIGQKYGKSVGQVVLRWIFQRGIVS--LAKSVRKERMAENINVLDFELSSADmlqIAALDTAT 261
Cdd:cd19083 235 RfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEE---IAFIDALF 307
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-241 |
1.87e-30 |
|
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: 114.64 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQ------MSDAAECERAVIDAIDTGYRLIDTAASYQN-ETQVGNALQqtGIARNELFVTTKLW--------LQD 79
Cdd:cd19095 3 LGLGTSGigrvwgVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA--GLRRDDLFIATKVGthgeggrdRKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 TSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHPDrLADLIAFNKVapAVNQ 157
Cdd:cd19095 81 FSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDEltGEVLETLEDLKAAGKVRYIGVSGDGEE-LEAAIASGVF--DVVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 158 IEVNPFNQQL-HAVPWNQSRGIQPEAWAPFAEGKNG--LFQHPVLTAIGQKY-------GKSVGQVVLRWIFQRGIVS-- 225
Cdd:cd19095 158 LPYNVLDREEeELLPLAAEAGLGVIVNRPLANGRLRrrVRRRPLYADYARRPefaaeigGATWAQAALRFVLSHPGVSsa 237
|
250
....*....|....*.
gi 1798692641 226 LAKSVRKERMAENINV 241
Cdd:cd19095 238 IVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-254 |
5.83e-30 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 114.62 E-value: 5.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 2 QTVKL-NNGIEMPLLGFGVFQMSDA-----AECERAVID-AIDTGYRLIDTAASYQ---NETQVGNALQQtgiARNELFV 71
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGCMGMSAFygpadEEESIATLHrALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 72 TTKLWLQ----------DTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHP 139
Cdd:cd19076 78 ATKFGIVrdpgsgfrgvDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVpiEETVGAMAELVEEGKVRYIGLSEASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 140 DrlaDLIAFNKVAP--AVnQIEVNPF--NQQLHAVPWNQSRGIQPEAWAPFAEG------------KNGLF--QHP---- 197
Cdd:cd19076 158 D---TIRRAHAVHPitAV-QSEYSLWtrDIEDEVLPTCRELGIGFVAYSPLGRGfltgaikspedlPEDDFrrNNPrfqg 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 198 -----------VLTAIGQKYGKSVGQVVLRWIFQRG--IVSLAKSVRKERMAENINVLDFELSSADMLQI 254
Cdd:cd19076 234 enfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
23-254 |
1.46e-29 |
|
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: 113.56 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 23 SDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIaRNELFVTTKLWLQ---------DTSYEGAKAQFE 90
Cdd:cd19148 22 TDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYGK-RDRVVIATKVGLEwdeggevvrNSSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 91 RSLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHPDRLAdliAFNKVAP-AVNQIEVNPFNQQL 167
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPDPLVpiEETAEALKELLDEGKIRAIGVSNFSPEQME---TFRKVAPlHTVQPPYNLFEREI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 168 HA--VPWNQSRGIQPEAWAPFAEG-------------KNGL------FQHP----VLTAIGQ-------KYGKSVGQVVL 215
Cdd:cd19148 178 EKdvLPYARKHNIVTLAYGALCRGllsgkmtkdtkfeGDDLrrtdpkFQEPrfsqYLAAVEEldklaqeRYGKSVIHLAV 257
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1798692641 216 RWIFQRGIVSLAK-SVRKERMAENIN-VLDFELSSADMLQI 254
Cdd:cd19148 258 RWLLDQPGVSIALwGARKPEQLDAVDeVFGWSLNDEDMKEI 298
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-257 |
4.48e-29 |
|
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: 112.00 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 24 DAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTgiaRNELFVTTK---LW------LQDTSYEGAKAQFER 91
Cdd:cd19102 24 DDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWdeegriRRSLKPASIRAECEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 92 SLNRLQLDYVDLYLIHQPYGD--VHGAWRAMEELQQAGKIRAIGVSNFHPDRLAdliAFNKVAP-AVNQI---------- 158
Cdd:cd19102 101 SLRRLGVDVIDLYQIHWPDPDepIEEAWGALAELKEEGKVRAIGVSNFSVDQMK---RCQAIHPiASLQPpysllrrgie 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 159 -EVNPF------------------------NQQLHAVPWNQSRGIQPEawapFAEGKNGLFQHPV--LTAIGQKYGKSVG 211
Cdd:cd19102 178 aEILPFcaehgigvivyspmqsglltgkmtPERVASLPADDWRRRSPF----FQEPNLARNLALVdaLRPIAERHGRTVA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1798692641 212 QVVLRWIFQR-GIVS-LAKSVRKERMAENINVLDFELSSADMLQIAAL 257
Cdd:cd19102 254 QLAIAWVLRRpEVTSaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-261 |
2.45e-26 |
|
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: 105.00 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKL-NNGIEMPLLGFGVFQM------------SDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQtgi 64
Cdd:cd19091 1 MEYRTLgRSGLKVSELALGTMTFgggggffgawggVDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 65 ARNELFVTTKLWLQ--------DTSYEGAKAQFERSLNRLQLDYVDLYLIHQ--PYGDVHGAWRAMEELQQAGKIRAIGV 134
Cdd:cd19091 78 RRDDVLIATKVRGRmgegpndvGLSRHHIIRAVEASLKRLGTDYIDLYQLHGfdALTPLEETLRALDDLVRQGKVRYIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 135 SNFHPDRLADLIAF----NKVAPAVNQI-----------EVNPFN--QQLHAVPWNQ----------SRGIQPEAWAPFA 187
Cdd:cd19091 158 SNFSAWQIMKALGIserrGLARFVALQAyysllgrdlehELMPLAldQGVGLLVWSPlaggllsgkyRRGQPAPEGSRLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 188 EGknGLFQHPV-----------LTAIGQKYGKSVGQVVLRWIFQR-GIVSLAKSVRK-ERMAENINVLDFELSSAdmlQI 254
Cdd:cd19091 238 RT--GFDFPPVdrergydvvdaLREIAKETGATPAQVALAWLLSRpTVSSVIIGARNeEQLEDNLGAAGLSLTPE---EI 312
|
....*..
gi 1798692641 255 AALDTAT 261
Cdd:cd19091 313 ARLDKVS 319
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
13-169 |
6.47e-26 |
|
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: 102.64 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 13 PLLGFGV--FQMS-----DAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQqtGIARNELFVTTKL-WLQDTS 81
Cdd:cd19096 1 SVLGFGTmrLPESdddsiDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALK--EGPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 82 YEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVH-------GAWRAMEELQQAGKIRAIGVSnFH--PDRLADLIAFNKVa 152
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWlekarkgGLLEFLEKAKKEGLIRHIGFS-FHdsPELLKEILDSYDF- 156
|
170
....*....|....*..
gi 1798692641 153 pAVNQIEVNPFNQQLHA 169
Cdd:cd19096 157 -DFVQLQYNYLDQENQA 172
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
15-151 |
3.07e-25 |
|
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: 101.09 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQMSDAAECER-----AVID-AIDTGYRLIDTAASYQN-ETQVGNALQqtGIARNELFVTTKL-----WLQDTSY 82
Cdd:cd19090 3 LGLGTAGLGGVFGGVDddeavATIRaALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKVgrlpeDTADYSA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1798692641 83 EGAKAQFERSLNRLQLDYVDLYLIHQPYGDVH-------GAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKV 151
Cdd:cd19090 81 DRVRRSVEESLERLGRDRIDLLMIHDPERVPWvdilapgGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGDF 156
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-256 |
4.38e-25 |
|
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: 101.58 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKL-NNGIEMPLLGFGVFQM--------SDAAECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQQTgiaRNELF 70
Cdd:cd19149 1 YRKLgKSGIEASVIGLGTWAIgggpwwggSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 71 VTTKLWL-------------------QDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGD--VHGAWRAMEELQQAGKI 129
Cdd:cd19149 78 LATKCGLrwdreggsfffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVEtpIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 130 RAIGVSNFHPDRLADLIAFNKVapAVNQIEVNPFNQQLHA--VPWNQSRGIQPEAWAPFAEG------------------ 189
Cdd:cd19149 158 RAIGASNVSVEQIKEYVKAGQL--DIIQEKYSMLDRGIEKelLPYCKKNNIAFQAYSPLEQGlltgkitpdrefdagdar 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 190 -KNGLFQ----HPVLTAIGQ------KYGKSVGQVVLRWIF-QRGIVSLAKSVRK-ERMAENINVLDFELSSADMLQIAA 256
Cdd:cd19149 236 sGIPWFSpenrEKVLALLEKwkplceKYGCTLAQLVIAWTLaQPGITSALCGARKpEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
12-247 |
5.07e-24 |
|
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: 97.67 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 12 MPLLGFGVFQM-SDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQtgiARNELFVTTKL---------WLQ 78
Cdd:cd19088 9 MRLTGPGIWGPpADREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHP---YPDDVVIATKGglvrtgpgwWGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 79 DTSYEGAKAQFERSLNRLQLDYVDLYLIHQ--PYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVApAVn 156
Cdd:cd19088 86 DGSPEYLRQAVEASLRRLGLDRIDLYQLHRidPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIV-SV- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 157 QIEVNPFNQQ-LHAVPWNQSRGIQPEAWAPFAeGKNGLFQHPVLTAIGQKYGKSVGQVVLRWIFQRG--IVSLAKSVRKE 233
Cdd:cd19088 164 QNRYNLANRDdEGVLDYCEAAGIAFIPWFPLG-GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVE 242
|
250
....*....|....
gi 1798692641 234 RMAENINVLDFELS 247
Cdd:cd19088 243 HLEENLAAAGLRLS 256
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
31-258 |
6.42e-24 |
|
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: 98.44 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 31 AVIDA-IDTGYRLIDTAASY----------QNETQVGNALQQTGiARNELFVTTKL-WLQDTSYEGA-----KAQFERSL 93
Cdd:cd19081 30 ALLDAfVDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgFPMGPNGPGLsrkhiRRAVEASL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 94 NRLQLDYVDLYLIHQPYGDVHGA--WRAMEELQQAGKIRAIGVSNFHPDRLAD---------LIAFNKVAPAVNQIEVNP 162
Cdd:cd19081 109 RRLQTDYIDLYQAHWDDPATPLEetLGALNDLIRQGKVRYIGASNYSAWRLQEalelsrqhgLPRYVSLQPEYNLVDRES 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 163 FNQQLhaVPWNQSRGIQPEAWAPFAEG---------------------------KNGLFQHPVLTAIGQKYGKSVGQVVL 215
Cdd:cd19081 189 FEGEL--LPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakrylnERGLRILDALDEVAAEHGATPAQVAL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1798692641 216 RWIFQR-GIVSLAKSVRK-ERMAENINVLDFELSSAdmlQIAALD 258
Cdd:cd19081 267 AWLLARpGVTAPIAGARTvEQLEDLLAAAGLRLTDE---EVARLD 308
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-254 |
1.35e-23 |
|
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: 97.90 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKL-NNGIEMPLLGFGVFQMS-----DAAECER-AVID-AIDTGYRLIDTAASYQ-NETQVGNALQQTGIARNELFV 71
Cdd:cd19144 1 IPTRTLgRNGPSVPALGFGAMGLSafygpPKPDEERfAVLDaAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 72 TTK-----------LWLqDTSYEGAKAQFERSLNRLQLDYVDLYLIHQ--PYGDVHGAWRAMEELQQAGKIRAIGVSNFH 138
Cdd:cd19144 81 ATKfgieknvetgeYSV-DGSPEYVKKACETSLKRLGVDYIDLYYQHRvdGKTPIEKTVAAMAELVQEGKIKHIGLSECS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 139 PDRLADLIAFNKVApAVnQIEVNPFNQQLHAVPWN-----QSRGIQPEAWAP---------------FAEG----KNGLF 194
Cdd:cd19144 160 AETLRRAHAVHPIA-AV-QIEYSPFSLDIERPEIGvldtcRELGVAIVAYSPlgrgfltgairspddFEEGdfrrMAPRF 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1798692641 195 QHP----------VLTAIGQKYGKSVGQVVLRWIFQRG--IVSLAKSVRKERMAENINVLDFELSSADMLQI 254
Cdd:cd19144 238 QAEnfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
23-248 |
1.77e-23 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 96.89 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 23 SDAAECERAvidAIDTGYRLIDTAASY---QNETQVGNALQqtGIARNELFVTTKL-W-LQDTSYE---GAK---AQFER 91
Cdd:cd19074 22 EDAKACVRK---AYDLGINFFDTADVYaagQAEEVLGKALK--GWPRESYVISTKVfWpTGPGPNDrglSRKhifESIHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 92 SLNRLQLDYVDLYLIHQPYGDV--HGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIA----FNKVAPAVNQIEVNPFNQ 165
Cdd:cd19074 97 SLKRLQLDYVDIYYCHRYDPETplEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDlarqFGLIPPVVEQPQYNMLWR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 166 QLHA--VPWNQSRGIQPEAWAPFAEG--------------------------KNGLFQHPV------LTAIGQKYGKSVG 211
Cdd:cd19074 177 EIEEevIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkKRRLLTDENlekvkkLKPIADELGLTLA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1798692641 212 QVVLRWIFQRGIVSlakSV-----RKERMAENINVLDFELSS 248
Cdd:cd19074 257 QLALAWCLRNPAVS---SAiigasRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
31-243 |
1.13e-22 |
|
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: 94.54 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 31 AVIDA-IDTGYRLIDTAASYQN-------ETQVGNALQQTGIaRNELFVTTK-----LWLQDTSYEGAK---AQFERSLN 94
Cdd:cd19082 21 ALLDAfVELGGNFIDTARVYGDwvergasERVIGEWLKSRGN-RDKVVIATKgghpdLEDMSRSRLSPEdirADLEESLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 95 RLQLDYVDLYLIH-----QPYGDVHGAwraMEELQQAGKIRAIGVSNFHPDRLADLIAF----NKVAPAVNQI-----EV 160
Cdd:cd19082 100 RLGTDYIDLYFLHrddpsVPVGEIVDT---LNELVRAGKIRAFGASNWSTERIAEANAYakahGLPGFAASSPqwslaRP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 161 NPFN-------------------QQLHAVPWN-QSRG-----IQPEAWAPFAEGKngLFQHPV-------LTAIGQKYGK 208
Cdd:cd19082 177 NEPPwpgptlvamdeemrawheeNQLPVFAYSsQARGffskrAAGGAEDDSELRR--VYYSEEnferlerAKELAEEKGV 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 1798692641 209 SVGQVVLRWIFQRG--IVSLAKSVRKERMAENINVLD 243
Cdd:cd19082 255 SPTQIALAYVLNQPfpTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-173 |
6.08e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 93.15 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQMS----DAAECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQQ----TGIARNELFVTTK--------- 74
Cdd:cd19099 6 LGLGTYRGDsddeTDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALREliekGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 ------LWLQ-------DTSYEGA-----------KAQFERSLNRLQLDYVDLYLIHQP------------YGDVHGAWR 118
Cdd:cd19099 86 eplrplKYLEeklgrglIDVADSAglrhcispaylEDQIERSLKRLGLDTIDLYLLHNPeeqllelgeeefYDRLEEAFE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1798692641 119 AMEELQQAGKIRAIGVSNFHPDRLA-------DLIAFNKVAPAVN---------QIEVNPFNQQLHAVPWN 173
Cdd:cd19099 166 ALEEAVAEGKIRYYGISTWDGFRAPpalpghlSLEKLVAAAEEVGgdnhhfkviQLPLNLLEPEALTEKNT 236
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-247 |
4.79e-21 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 90.30 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 1 MQTVKL-NNGIEMPLLGFG------VFQMSDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQqtGIARNELF 70
Cdd:cd19163 1 MKYRKLgKTGLKVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 71 VTTK------LWLQ--DTSYEGAKAQFERSLNRLQLDYVDLYLIH----QPYGD--VHGAWRAMEELQQAGKIRAIGVSN 136
Cdd:cd19163 79 LATKvgryglDPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDqiLNETLPALQKLKEEGKVRFIGITG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 137 FhpdrlaDLIAFNKVAPAV-NQIEV-------NPFNQQL-HAVPWNQSRGIQPEAWAPFAEG---KNGLFQ-HPVLTAIG 203
Cdd:cd19163 159 Y------PLDVLKEVLERSpVKIDTvlsychyTLNDTSLlELLPFFKEKGVGVINASPLSMGlltERGPPDwHPASPEIK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1798692641 204 ----------QKYGKSVGQVVLRWIFQ--RGIVSLAKSVRKERMAENINVLDFELS 247
Cdd:cd19163 233 eacakaaaycKSRGVDISKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLD 288
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-165 |
1.99e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 88.86 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFG------VFQMSDAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTgiaRNELFVTTKLWLQD 79
Cdd:cd19104 9 GLKVSELTFGgggiggLMGRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL---PAGPYITTKVRLDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 TSYEGAKAQFER----SLNRLQLDYVDLYLIHQ-------PYGDVH----------GAWRAMEELQQAGKIRAIGVSNF- 137
Cdd:cd19104 86 DDLGDIGGQIERsvekSLKRLKRDSVDLLQLHNrigderdKPVGGTlsttdvlglgGVADAFERLRSEGKIRFIGITGLg 165
|
170 180
....*....|....*....|....*...
gi 1798692641 138 HPDRLADLIAFNKvaPAVNQIEVNPFNQ 165
Cdd:cd19104 166 NPPAIRELLDSGK--FDAVQVYYNLLNP 191
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-172 |
2.19e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 87.97 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 35 AIDTGYRLIDTAASYQN-ETQVGNALQQTGiarnELFVTTKL----WLQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP 109
Cdd:cd19097 35 ALKAGINTLDTAPAYGDsEKVLGKFLKRLD----KFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNP 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1798692641 110 ---YGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKvaPAVNQIEVNPFNQQLHAVPW 172
Cdd:cd19097 111 ddlLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFK--IDIIQLPFNILDQRFLKSGL 174
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
17-137 |
3.32e-20 |
|
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: 88.01 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 17 FGvfqmSDAAECE-RAVID-AIDTGYRLIDTAASYQN---ETQVGNALQQTgiaRNELFVTTK--------LWLQDTSYE 83
Cdd:cd19087 23 FG----GRTDEETsFAIMDrALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKvfgpmgddPNDRGLSRR 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1798692641 84 GAKAQFERSLNRLQLDYVDLYLIHQPYGDVHG--AWRAMEELQQAGKIRAIGVSNF 137
Cdd:cd19087 96 HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLeeTLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
9-254 |
4.71e-20 |
|
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: 87.67 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVFQMS-------DAAECERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTgiaRNELFVTTKLWLQ 78
Cdd:cd19078 1 GLEVSAIGLGCMGMShgygpppDKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF---RDQVVIATKFGFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 79 -----------DTSYEGAKAQFERSLNRLQLDYVDLYLIHQ-----PYGDVHGawrAMEELQQAGKIRAIGVSNFHPD-- 140
Cdd:cd19078 78 idggkpgplglDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRvdpnvPIEEVAG---TMKELIKEGKIRHWGLSEAGVEti 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 141 RLAdliafNKVAP--AVNQI----------EVNPFNQQLhavpwnqsrGIQPEAWAPFAEG-------KNGLFQH----- 196
Cdd:cd19078 155 RRA-----HAVCPvtAVQSEysmmwrepekEVLPTLEEL---------GIGFVPFSPLGKGfltgkidENTKFDEgddra 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1798692641 197 --P---------------VLTAIGQKYGKSVGQVVLRWIFQRG--IVSLAKSVRKERMAENINVLDFELSSADMLQI 254
Cdd:cd19078 221 slPrftpealeanqalvdLLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
35-251 |
1.79e-18 |
|
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: 83.40 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 35 AIDTGYRLIDTAASYQN---ETQVGNALQqTGIARNELFVTTKLWLQ---DTSYEGAK-----AQFERSLNRLQLDYVDL 103
Cdd:cd19079 44 ALDLGINFFDTANVYSGgasEEILGRALK-EFAPRDEVVIATKVYFPmgdGPNGRGLSrkhimAEVDASLKRLGTDYIDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 104 YLIHQpygdvhgaW----------RAMEELQQAGKIRAIGVSNFHP------DRLADLIAFNKVAPAVNQI--------- 158
Cdd:cd19079 123 YQIHR--------WdyetpieetlEALHDVVKSGKVRYIGASSMYAwqfakaLHLAEKNGWTKFVSMQNHYnllyreeer 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 159 EVNPFNQQ--LHAVPWNQ-SRGIQPEAWAPFAEGKNGLFQHPVLT----------------AIGQKYGKSVGQVVLRWIF 219
Cdd:cd19079 195 EMIPLCEEegIGVIPWSPlARGRLARPWGDTTERRRSTTDTAKLKydyfteadkeivdrveEVAKERGVSMAQVALAWLL 274
|
250 260 270
....*....|....*....|....*....|....*..
gi 1798692641 220 QRG-----IVSLAKsvrKERMAENINVLDFELSSADM 251
Cdd:cd19079 275 SKPgvtapIVGATK---LEHLEDAVAALDIKLSEEEI 308
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
22-258 |
4.61e-18 |
|
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: 82.27 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 22 MSDAAECeRAVIDA-IDTGYRLIDTAASYQN---ETQVGNALQQTgiaRNELFVTTKLWL----QDTSYEG--AKA---Q 88
Cdd:cd19080 27 GADREEA-RAMFDAyVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYTMnrrpGDPNAGGnhRKNlrrS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 89 FERSLNRLQLDYVDLYLIHQPYG--DVHGAWRAMEELQQAGKIRAIGVSNFHPDRL--ADLIA-FNKVAPAVN-QIEVNP 162
Cdd:cd19080 103 VEASLRRLQTDYIDLLYVHAWDFttPVEEVMRALDDLVRAGKVLYVGISDTPAWVVarANTLAeLRGWSPFVAlQIEYSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 163 FNQQLHA--VPWNQSRGIQPEAWAPFAEGK-------------------NGLFQH---------PVLTAIGQKYGKSVGQ 212
Cdd:cd19080 183 LERTPERelLPMARALGLGVTPWSPLGGGLltgkyqrgeegrageakgvTVGFGKlternwaivDVVAAVAEELGRSAAQ 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1798692641 213 VVLRWIFQR-GIVSLAKSVRK-ERMAENINVLDFELSSAdmlQIAALD 258
Cdd:cd19080 263 VALAWVRQKpGVVIPIIGARTlEQLKDNLGALDLTLSPE---QLARLD 307
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-243 |
2.84e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 79.68 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 27 ECERAVIDA-IDTGYRLIDTAASY----------QNETQVGNALQQTGiARNELFVTTKL-------WLQDTSYEGA--- 85
Cdd:cd19752 17 ETSFAILDRyVAAGGNFLDTANNYafwteggvggESERLIGRWLKDRG-NRDDVVIATKVgagprdpDGGPESPEGLsae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 86 --KAQFERSLNRLQLDYVDLYLIH--QPYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLAD---------LIAFNKV- 151
Cdd:cd19752 96 tiEQEIDKSLRRLGTDYIDLYYAHvdDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERarqiarqqgWAEFSAIq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 152 -----------APAVNQIEVNP-------FNQQLHAVPWN-QSRGIQPEAWAPFAEGknglFQHP-------VLTAIGQK 205
Cdd:cd19752 176 qrhsylrprpgADFGVQRIVTDelldyasSRPDLTLLAYSpLLSGAYTRPDRPLPEQ----YDGPdsdarlaVLEEVAGE 251
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1798692641 206 YGKSVGQVVLRWIFQR--GIVSLAKSVRKERMAENINVLD 243
Cdd:cd19752 252 LGATPNQVVLAWLLHRtpAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
13-135 |
3.29e-17 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 79.71 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 13 PLLGFGVFQMSDAAECER----AVID-AIDTGYRLIDTAASY---QNETQVGNALQqtGIARNELFVTTKL--------- 75
Cdd:cd19162 1 PRLGLGAASLGNLARAGEdeaaATLDaAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1798692641 76 -------WLQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQPYGDVH----GAWRAMEELQQAGKIRAIGVS 135
Cdd:cd19162 79 grpagadRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLqaltDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
8-189 |
5.84e-17 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 79.43 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFG---VFQMSDAAECERAVID-AIDTGYRLIDTAASYQN---ETQVGNALQQTGIARNELFVTTKLWLQDT 80
Cdd:cd19142 9 SGLRVSNVGLGtwsTFSTAISEEQAEEIVTlAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIYWSYG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 81 SYEGAKAQ------FERSLNRLQLDYVDLYLIHQ--PYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLI----AF 148
Cdd:cd19142 89 SEERGLSRkhiiesVRASLRRLQLDYIDIVIIHKadPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFsiarQF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1798692641 149 NKVAPAVNQIEVNPFNQ---QLHAVPWNQSRGIQPEAWAPFAEG 189
Cdd:cd19142 169 NCPTPICEQSEYHMFCRekmELYMPELYNKVGVGLITWSPLSLG 212
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-257 |
2.78e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 76.99 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 30 RAVID-AIDTGYRLIDTAASY---QNETQVGNALQQtgIARNELFVTTKLWLQ--DTSYEGAKAQFERSLNRLQLDYVDL 103
Cdd:cd19103 35 KAVFDkAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKFTPQiaGQSADPVADMLEGSLARLGTDYIDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 104 YLIHQPyGDVHGAWRAMEELQQAGKIRAIGVSNFHPD--RLADLIafnkVAPAVNQIE--------VNPFNQQLHAVPWN 173
Cdd:cd19103 113 YWIHNP-ADVERWTPELIPLLKSGKVKHVGVSNHNLAeiKRANEI----LAKAGVSLSavqnhyslLYRSSEEAGILDYC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 174 QSRGIQPEAWA---------------PFAEGK------NGLFQH-----PVLTAIGQKYGKSVGQVVLRWIFQRGIVSLA 227
Cdd:cd19103 188 KENGITFFAYMvleqgalsgkydtkhPLPEGSgraetyNPLLPQleeltAVMAEIGAKHGASIAQVAIAWAIAKGTTPII 267
|
250 260 270
....*....|....*....|....*....|
gi 1798692641 228 KSVRKERMAENINVLDFELSSADMLQIAAL 257
Cdd:cd19103 268 GVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-166 |
1.24e-15 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 75.29 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 16 GFGVFQMSDAAECERAVIDAI-DTGYRLIDTAASYQN---ETQVGnalqQTGIARNELFVTTKL--WLQDT-SYEGAKAQ 88
Cdd:cd19075 9 TFGSQGRFTTAEAAAELLDAFlERGHTEIDTARVYPDgtsEELLG----ELGLGERGFKIDTKAnpGVGGGlSPENVRKQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 89 FERSLNRLQLDYVDLYLIHQPygD----VHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNK----VAPAVNQIEV 160
Cdd:cd19075 85 LETSLKRLKVDKVDVFYLHAP--DrstpLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVYQGMY 162
|
....*.
gi 1798692641 161 NPFNQQ 166
Cdd:cd19075 163 NAITRQ 168
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-254 |
2.91e-15 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 74.39 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 3 TVKL-NNGIEMPLLGFGVFQMS---DAAECERAVID----AIDTGYRLIDTAASY---QNETQVGNALQqtGIARNELFV 71
Cdd:cd19145 2 RVKLgSQGLEVSAQGLGCMGLSgdyGAPKPEEEGIAlihhAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 72 TTKLWLQDTSYEG---------AKAQFERSLNRLQLDYVDLYLIHQ-----PYGDVHGawrAMEELQQAGKIRAIGVSNF 137
Cdd:cd19145 80 ATKFGIHEIGGSGvevrgdpayVRAACEASLKRLDVDYIDLYYQHRidttvPIEITMG---ELKKLVEEGKIKYIGLSEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 138 HPD--RLAdliafNKVAP--AVnQIEVNPFNQQLHA--VPWNQSRGIQPEAWAPFAEG------------KNGLF--QHP 197
Cdd:cd19145 157 SADtiRRA-----HAVHPitAV-QLEWSLWTRDIEEeiIPTCRELGIGIVPYSPLGRGffagkakleellENSDVrkSHP 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1798692641 198 ---------------VLTAIGQKYGKSVGQVVLRWIFQRG--IVSLAKSVRKERMAENINVLDFELSSADMLQI 254
Cdd:cd19145 231 rfqgenleknkvlyeRVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
15-153 |
1.77e-14 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 71.80 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 15 LGFGVFQMSDAAECERAVIDAIDT-------GYRLIDTAASYQN---ETQVGNALQQTGIARNELFVTTKL-----WLQD 79
Cdd:cd19153 15 VGLGTAALGGVYGDGLEQDEAVAIvaeafaaGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVgryrdSEFD 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1798692641 80 TSYEGAKAQFERSLNRLQLDYVDLYLIH-----QPYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADLIAFNKVAP 153
Cdd:cd19153 95 YSAERVRASVATSLERLHTTYLDVVYLHdiefvDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS 173
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-256 |
2.76e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 71.47 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 11 EMPLLGFGVFQMSDA-------AECERAVIDAIDTGYRLIDTAASYQN-ETQVG---NALQQTGIARNELFVTTKL---- 75
Cdd:cd19101 1 TISRVINGMWQLSGGhggirdeDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGefrKRLRRERDAADDVQIHTKWvpdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 76 WLQDTSYEGAKAQFERSLNRLQLDYVDLYLIH-QPYGD---VHGAwRAMEELQQAGKIRAIGVSNFHPDRLADLIAfNKV 151
Cdd:cd19101 81 GELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHwWDYSDpgyLDAA-KHLAELQEEGKIRHLGLTNFDTERLREILD-AGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 152 APAVNQIEVNPFNQ--QLHAVPWNQSRGIQ-------------------PEAWAPFAE--------------GKNGLFQH 196
Cdd:cd19101 159 PIVSNQVQYSLLDRrpENGMAALCEDHGIKllaygtlaggllsekylgvPEPTGPALEtrslqkyklmidewGGWDLFQE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1798692641 197 --PVLTAIGQKYGKSVGQVVLRWIFQR-GIVSLAKSVR-KERMAENINVLDFELSSADMLQIAA 256
Cdd:cd19101 239 llRTLKAIADKHGVSIANVAVRWVLDQpGVAGVIVGARnSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
7-243 |
9.30e-14 |
|
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: 69.98 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 7 NNGIEMPLLGFGVFQ----MSDAAECERAVIDAIDTGYRLIDTAASY-----QNETQVGNALQQTGIA-RNELFVTTKlw 76
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRPyRDELVISTK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 77 lqdTSYE---------GAK----AQFERSLNRLQLDYVDLYLIHQPYGDVhgawrAMEELQQA-------GKIRAIGVSN 136
Cdd:cd19089 84 ---AGYGmwpgpygdgGSRkyllASLDQSLKRMGLDYVDIFYHHRYDPDT-----PLEETMTAladavrsGKALYVGISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 137 FHPDRLADLIAF---NKVAPAVNQIEVNPFNQqlhavpWN--------QSRGIQPEAWAPFAEG---------------- 189
Cdd:cd19089 156 YPGAKARRAIALlreLGVPLIIHQPRYSLLDR------WAedgllevlEEAGIGFIAFSPLAQGlltdkylngippdsrr 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1798692641 190 -KNGLFQHPV------------LTAIGQKYGKSVGQVVLRWIFQR-GIVSLAKSV-RKERMAENINVLD 243
Cdd:cd19089 230 aAESKFLTEEaltpekleqlrkLNKIAAKRGQSLAQLALSWVLRDpRVTSVLIGAsSPSQLEDNVAALK 298
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
13-134 |
1.16e-13 |
|
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: 69.56 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 13 PLLGFG------VFQMSDAAECERAVIDAIDTGYRLIDTAASYQN---ETQVGNALQqtGIARNELFVTTKL-WL----- 77
Cdd:cd19152 1 PKLGFGtaplgnLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR--ELGREDYVISTKVgRLlvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 78 -------------------QDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP----YGDVH---------GAWRAMEELQQ 125
Cdd:cd19152 79 eveptfepgfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPdedlAGAESdehfaqaikGAFRALEELRE 158
|
....*....
gi 1798692641 126 AGKIRAIGV 134
Cdd:cd19152 159 EGVIKAIGL 167
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
8-254 |
2.98e-13 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 68.86 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGV---FQMSDAAECERAVI-DAIDTGYRLIDTAASY-----QNETQVGNALQQTGIA-RNELFVTTK--- 74
Cdd:PRK09912 21 SGLRLPALSLGLwhnFGHVNALESQRAILrKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 -LWLQDTSYEGAK----AQFERSLNRLQLDYVDLYLIHQ-----PYGDVHGawrAMEELQQAGKIRAIGVSNFHPDR--- 141
Cdd:PRK09912 101 dMWPGPYGSGGSRkyllASLDQSLKRMGLEYVDIFYSHRvdentPMEETAS---ALAHAVQSGKALYVGISSYSPERtqk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 142 LADLIAFNKVAPAVNQIEVNPFNQ---QLHAVPWNQSRGIQPEAWAPFAEG------KNGL---------------FQHP 197
Cdd:PRK09912 178 MVELLREWKIPLLIHQPSYNLLNRwvdKSGLLDTLQNNGVGCIAFTPLAQGlltgkyLNGIpqdsrmhregnkvrgLTPK 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1798692641 198 VLTA-----------IGQKYGKSVGQVVLRWIFQRGIVS--LAKSVRKERMAENINVL-DFELSSADMLQI 254
Cdd:PRK09912 258 MLTEanlnslrllneMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVQALnNLTFSTEELAQI 328
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-136 |
4.97e-13 |
|
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: 67.98 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 35 AIDTGYRLIDTAASY----QNETQ------VGNALQQTGiARNELFVTTKL--------WLQDT----SYEGAKAQFERS 92
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppSPETQgrteeiIGSWLKKKG-NRDKVVLATKVagpgegitWPRGGgtrlDRENIREAVEGS 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1798692641 93 LNRLQLDYVDLYLIHQP-----------YGDVHGAW---------RAMEELQQAGKIRAIGVSN 136
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPdrytplfgggyYTEPSEEEdsvsfeeqlEALGELVKAGKIRHIGLSN 169
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
29-145 |
6.11e-13 |
|
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: 67.69 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 29 ERAVIDAIDTGYRLIDTAASYQN-ETQVGNALQ--QTGIARNELFVTTK-----LWLQDTSYEGAKAQFERSLNRLQLDY 100
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGPsEIILGRALKalRDEFPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTDY 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1798692641 101 VDLYLIHQ----PYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLADL 145
Cdd:cd19164 117 LDLVYLHDvefvADEEVLEALKELFKLKDEGKIRNVGISGYPLPVLLRL 165
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
7-135 |
5.00e-12 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 65.18 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 7 NNGIEMPLLGFG------VF---QMSDAAECERaviDAIDTGYRLIDTAASYQN---ETQVGNALQQTGIARNELFVTTK 74
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFgpvSEEDAIASVR---EAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 LWLQ----DTSYEGAKAQFERSLNRLQLDYVDLYLIHQ-PYGD----VHGAWRAMEELQQAGKIRAIGVS 135
Cdd:PLN02587 83 CGRYgegfDFSAERVTKSVDESLARLQLDYVDILHCHDiEFGSldqiVNETIPALQKLKESGKVRFIGIT 152
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
10-136 |
1.21e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 64.10 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 10 IEMPLLGFGVF----QMSDAAEceRAVID-AIDTGYRLIDTAASY----QNETQ------VGNALQQTGiARNELFVTTK 74
Cdd:PRK10625 11 LEVSTLGLGTMtfgeQNSEADA--HAQLDyAVAQGINLIDVAEMYpvppRPETQgltetyIGNWLAKRG-SREKLIIASK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 LW------------LQDTSYEGAKAQFERSLNRLQLDYVDLYLIHQP------YGDVHGAW-------------RAMEEL 123
Cdd:PRK10625 88 VSgpsrnndkgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncFGKLGYSWtdsapavslletlDALAEQ 167
|
170
....*....|...
gi 1798692641 124 QQAGKIRAIGVSN 136
Cdd:PRK10625 168 QRAGKIRYIGVSN 180
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
8-189 |
3.35e-11 |
|
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: 62.75 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGVF-----QMSDAAeCERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIARNELFVTTKLwlqd 79
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEV-AERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 tsYEGAKAQFER-------------SLNRLQLDYVDLYLIHQPYGD--VHGAWRAMEELQQAGKIRAIGVSNFHPDRLAD 144
Cdd:cd19159 84 --YWGGKAETERglsrkhiieglkgSLQRLQLEYVDVVFANRPDSNtpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1798692641 145 LIA----FNKVAPAVNQIEVNPFNQQLHAVPWNQ---SRGIQPEAWAPFAEG 189
Cdd:cd19159 162 AYSvarqFNMIPPVCEQAEYHLFQREKVEVQLPElyhKIGVGAMTWSPLACG 213
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
8-254 |
1.37e-10 |
|
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: 60.72 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGVFQMS---------DAAECERAVIDAidtGYRLIDTAASY------QNETQVGNALQQTGIARNELFVT 72
Cdd:cd19077 1 NGKLVGPIGLGLMGLTwrpnptpdeEAFETMKAALDA---GSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 73 TK-----LWLQ-DTSYEGAKAQFERSLNRL-QLDYVDLYlihqpygdvhGAWR------------AMEELQQAGKIRAIG 133
Cdd:cd19077 78 VKggldpDTLRpDGSPEAVRKSIENILRALgGTKKIDIF----------EPARvdpnvpieetikALKELVKEGKIRGIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 134 VSnfHPDrlADLIA-FNKVAP-AVNQIEVNPFNQQ-LHA--VPWNQSRGIQPEAWAPFAEG------------KNGLF-Q 195
Cdd:cd19077 148 LS--EVS--AETIRrAHAVHPiAAVEVEYSLFSREiEENgvLETCAELGIPIIAYSPLGRGlltgriksladiPEGDFrR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1798692641 196 HP----------------VLTAIGQKYGKSVGQVVLRWIFQRG---IVSLAKSVRKERMAENINVLDFELSSADMLQI 254
Cdd:cd19077 224 HLdrfngenfeknlklvdALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
25-210 |
1.78e-10 |
|
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: 60.30 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 25 AAECERAvidAIDTGYRLIDTAASYQN---ETQVGNALQQTGIARNELFVTTKL-W------LQDTS------YEGAKAq 88
Cdd:cd19143 33 AKECMKA---AYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWggggppPNDRGlsrkhiVEGTKA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 89 ferSLNRLQLDYVDLYLIHQPygDVHG----AWRAMEELQQAGKIRAIGVSNF------HPDRLADliAFNKVAPAVNQI 158
Cdd:cd19143 109 ---SLKRLQLDYVDLVFCHRP--DPATpieeTVRAMNDLIDQGKAFYWGTSEWsaqqieEAHEIAD--RLGLIPPVMEQP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1798692641 159 EVNPFNQQLHAV---PWNQSRGIQPEAWAPFAEGknglfqhpVLTAigqKYGKSV 210
Cdd:cd19143 182 QYNLFHRERVEVeyaPLYEKYGLGTTTWSPLASG--------LLTG---KYNNGI 225
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
9-189 |
2.39e-10 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 60.15 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGVF-----QMSDAAeCERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIARNELFVTTKLwlqdt 80
Cdd:cd19141 9 GLRVSCLGLGTWvtfgsQISDEV-AEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKKGWRRSSYVITTKI----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 81 sYEGAKAQFER-------------SLNRLQLDYVDLYLIHQPygDVHgawRAMEELQQA-------GKIRAIGVSNFHPD 140
Cdd:cd19141 83 -FWGGKAETERglsrkhiieglkaSLERLQLEYVDIVFANRP--DPN---TPMEEIVRAfthvinqGMAMYWGTSRWSAM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1798692641 141 RLADLIA----FNKVAPAVNQIEVNPFNQ---QLHAVPWNQSRGIQPEAWAPFAEG 189
Cdd:cd19141 157 EIMEAYSvarqFNLIPPIVEQAEYHLFQRekvEMQLPELFHKIGVGAMTWSPLACG 212
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
30-133 |
4.15e-10 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 59.26 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 30 RAVID-AIDTGYRLIDTAASYQN---ETQVGNALQQTGiaRNELFVTTKL-----------------WLQ--------DT 80
Cdd:cd19161 23 DATLDaAWDSGIRYFDTAPMYGHglaEHRLGDFLREKP--RDEFVLSTKVgrllkparegsvpdpngFVDplpfeivyDY 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1798692641 81 SYEGAKAQFERSLNRLQLDYVDLYLIHQ--PY--GDVH----------GAWRAMEELQQAGKIRAIG 133
Cdd:cd19161 101 SYDGIMRSFEDSLQRLGLNRIDILYVHDigVYthGDRKerhhfaqlmsGGFKALEELKKAGVIKAFG 167
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-251 |
6.01e-10 |
|
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: 58.95 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 7 NNGIEMPLLGFGV---FQMSDAAECERAVI-DAIDTGYRLIDTAASY-----QNETQVGNALQQTGIA-RNELFVTTK-- 74
Cdd:cd19151 7 RSGLKLPAISLGLwhnFGDVDRYENSRAMLrRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 --LWlqDTSYE--GAK----AQFERSLNRLQLDYVDLYLIHQPYGD--VHGAWRAMEELQQAGKIRAIGVSNFHPDRLAD 144
Cdd:cd19151 87 ytMW--PGPYGdwGSKkyliASLDQSLKRMGLDYVDIFYHHRPDPEtpLEETMGALDQIVRQGKALYVGISNYPPEEARE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 145 LIAFNK---VAPAVNQIEVNPFNQqlhavpWN--------QSRGIQPEAWAPFAEG-----------------KNGLFQH 196
Cdd:cd19151 165 AAAILKdlgTPCLIHQPKYSMFNR------WVeeglldvlEEEGIGCIAFSPLAQGlltdrylngipedsraaKGSSFLK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 197 P------------VLTAIGQKYGKSVGQVVLRWIFQRGIVS--LAKSVRKERMAENINVLD-FELSSADM 251
Cdd:cd19151 239 PeqiteeklakvrRLNEIAQARGQKLAQMALAWVLRNKRVTsvLIGASKPSQIEDAVGALDnREFSEEEL 308
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
8-189 |
1.98e-09 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 57.30 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGVF-----QMSDAAeCERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIARNELFVTTKLwlqd 79
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDET-AEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVVTTKI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 tsYEGAKAQFER-------------SLNRLQLDYVDLYLIHQ--PYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDRLAD 144
Cdd:cd19160 86 --YWGGQAETERglsrkhiieglrgSLDRLQLEYVDIVFANRsdPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIME 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1798692641 145 LIA----FNKVAPAVNQIEVNPFNQ-----QL----HAVpwnqsrGIQPEAWAPFAEG 189
Cdd:cd19160 164 AYSvarqFNLIPPVCEQAEYHLFQRekvemQLpelyHKI------GVGSVTWSPLACG 215
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-243 |
2.14e-09 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 57.08 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 9 GIEMPLLGFGV---FQMSDAAECERAVI-DAIDTGYRLIDTAASY-----QNETQVGNALQQTGIA-RNELFVTTK---- 74
Cdd:cd19150 9 GLKLPALSLGLwhnFGDDTPLETQRAILrTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKagyd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 75 LWLQDTSYEGAK----AQFERSLNRLQLDYVDLYLIHQ--PYGDVHGAWRAMEELQQAGKIRAIGVSNFHPDR---LADL 145
Cdd:cd19150 89 MWPGPYGEWGSRkyllASLDQSLKRMGLDYVDIFYSHRfdPDTPLEETMGALDHAVRSGKALYVGISSYSPERtreAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 146 IAFNKVAPAVNQIEVNPFN--------------------------------QQLHAVPWNqSRGIQPEAWAPFAEGKNGL 193
Cdd:cd19150 169 LRELGTPLLIHQPSYNMLNrwveesglldtlqelgvgciaftplaqglltdKYLNGIPEG-SRASKERSLSPKMLTEANL 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1798692641 194 FQHPVLTAIGQKYGKSVGQVVLRWIFQRGIVS--LAKSVRKERMAENINVLD 243
Cdd:cd19150 248 NSIRALNEIAQKRGQSLAQMALAWVLRDGRVTsaLIGASRPEQLEENVGALD 299
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
8-189 |
8.59e-09 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 55.48 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 8 NGIEMPLLGFGVF-----QMSDAAeCERAVIDAIDTGYRLIDTAASY---QNETQVGNALQQTGIARNELFVTTKLwlqd 79
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEM-AEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKI---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 tsYEGAKAQFER-------------SLNRLQLDYVDLYLIHQPYGD--VHGAWRAMEELQQAGKIRAIGVSNFHPDRLAD 144
Cdd:cd19158 84 --FWGGKAETERglsrkhiieglkaSLERLQLEYVDVVFANRPDPNtpMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1798692641 145 LIA----FNKVAPAVNQIEVNPFNQQLHAVPWNQ---SRGIQPEAWAPFAEG 189
Cdd:cd19158 162 AYSvarqFNLIPPICEQAEYHMFQREKVEVQLPElfhKIGVGAMTWSPLACG 213
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
12-261 |
6.46e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 46.50 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 12 MPLLGFGVF---QMSDAAeceRAVI-DAIDTGYRLIDTAASYQneTQVGNALQQTGIA--RNELFVTTKL---------W 76
Cdd:PRK10376 25 MQLAGPGVFgppKDRDAA---IAVLrEAVALGVNHIDTSDFYG--PHVTNQLIREALHpyPDDLTIVTKVgarrgedgsW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 77 LQDTSYEGAKAQFERSLNRLQ---LDYVDLYLIhqpyGDVHG--------AWRAMEELQQAGKIRAIGVSNFHPDRLADL 145
Cdd:PRK10376 100 LPAFSPAELRRAVHDNLRNLGldvLDVVNLRLM----GDGHGpaegsieePLTVLAELQRQGLVRHIGLSNVTPTQVAEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 146 iafNKVAPAV---NQIEV-----NPFNQQLHAvpwnqsRGIqpeAWAPFAE--GKNGLfQHPVLTAIGQKYGKSVGQVVL 215
Cdd:PRK10376 176 ---RKIAEIVcvqNHYNLahradDALIDALAR------DGI---AYVPFFPlgGFTPL-QSSTLSDVAASLGATPMQVAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1798692641 216 RWIFQRG----IVSLAKSVRKERmaENINVLDFELSSADMLQIAALDTAT 261
Cdd:PRK10376 243 AWLLQRSpnilLIPGTSSVAHLR--ENLAAAELVLSEEVLAELDGIAREA 290
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
37-136 |
7.46e-06 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 46.74 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 37 DTGYRLIDTAASYQN---ETQVGNALQQTGIaRNELFVTTKLWLQDTSYE---GAKAQF------------ERSLNRLQL 98
Cdd:cd19147 45 EAGGNFIDTANNYQDeqsETWIGEWMKSRKN-RDQIVIATKFTTDYKAYEvgkGKAVNYcgnhkrslhvsvRDSLRKLQT 123
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1798692641 99 DYVDLYLIH--QPYGDVHGAWRAMEELQQAGKIRAIGVSN 136
Cdd:cd19147 124 DWIDILYVHwwDYTTSIEEVMDSLHILVQQGKVLYLGVSD 163
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
17-254 |
5.89e-05 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 43.95 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 17 FGVFQMSDAAECER----AVIDAI-DTGYRLIDTAASYQNETQ---VGNALQQTGIaRNELFVTTKLWL---------QD 79
Cdd:cd19146 21 FGEAWKSMMGECDKetafKLLDAFyEQGGNFIDTANNYQGEESerwVGEWMASRGN-RDEMVLATKYTTgyrrggpikIK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 80 TSYEGAKAQ-----FERSLNRLQLDYVDLYLIHqpYGD----VHGAWRAMEELQQAGKIRAIGVSnfhpDRLADLIA--- 147
Cdd:cd19146 100 SNYQGNHAKslrlsVEASLKKLQTSYIDILYVH--WWDyttsIPELMQSLNHLVAAGKVLYLGVS----DTPAWVVSkan 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798692641 148 ----FNKVAP-AVNQIEVNPFNQQLH--AVPWNQSRGIqpeAWAPFAEGKNGLFQHP----------------------- 197
Cdd:cd19146 174 ayarAHGLTQfVVYQGHWSAAFRDFErdILPMCEAEGM---ALAPWGVLGQGQFRTEeefkrrgrsgrkggpqtekerkv 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1798692641 198 --VLTAIGQKYGKSVGQVVLRWIFQRG-----IVslakSVRK-ERMAENINVLDFELSSADMLQI 254
Cdd:cd19146 251 seKLEKVAEEKGTAITSVALAYVMHKApyvfpIV----GGRKvEHLKGNIEALGISLSDEEIQEI 311
|
|
| |
