|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-276 |
0e+00 |
|
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: 510.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 8 TATLHNGVKMPWFGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKVWNA 87
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVG----KGIKESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 88 DLGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQ 167
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 168 VEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENA 247
Cdd:cd19157 157 VEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENA 236
|
250 260
....*....|....*....|....*....
gi 1457282850 248 SVFDFELTQGDMNRIDALNENLRVGPDPD 276
Cdd:cd19157 237 DVFDFELSQEDMDKIDALNENLRVGPDPD 265
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
13-276 |
3.61e-157 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 437.95 E-value: 3.61e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 13 NGVKMPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQqgidEAGISREDLFITSKVWNADLGYE 92
Cdd:COG0656 1 NGVEIPALGLGTWQLP-GEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHGYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 93 ETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVEFHP 172
Cdd:COG0656 76 DTLAAFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 173 RLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDF 252
Cdd:COG0656 156 YLQQRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDF 235
|
250 260
....*....|....*....|....
gi 1457282850 253 ELTQGDMNRIDALNENLRVGPDPD 276
Cdd:COG0656 236 ELSDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-266 |
3.39e-142 |
|
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: 399.89 E-value: 3.39e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKVWNADL 89
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVG----EAIRESGVPREELFVTTKLWNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVE 169
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 170 FHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASV 249
Cdd:cd19126 158 FHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADI 237
|
250
....*....|....*..
gi 1457282850 250 FDFELTQGDMNRIDALN 266
Cdd:cd19126 238 FDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
10-278 |
9.00e-139 |
|
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: 391.50 E-value: 9.00e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQgideAGISREDLFITSKVWNADL 89
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE----SGVPREEVFVTTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVE 169
Cdd:cd19156 78 GYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 170 FHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASV 249
Cdd:cd19156 158 LHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDV 237
|
250 260
....*....|....*....|....*....
gi 1457282850 250 FDFELTQGDMNRIDALNENLRVGPDPDNF 278
Cdd:cd19156 238 FDFELTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
17-263 |
1.20e-123 |
|
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: 352.55 E-value: 1.20e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 17 MPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQqgidEAGISREDLFITSKVWNADLGYEETLA 96
Cdd:cd19071 1 MPLIGLGTYKLKPE-ETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIR----ESGVPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 97 AFETSLSKLGLDYLDLYLIHWPVEGK-------YKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVE 169
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKeggskeaRLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 170 FHPRLTQKELMAYCQKQGIQMEAWSPLMQG--QLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENA 247
Cdd:cd19071 156 LHPYLQQKELVEFCKEHGIVVQAYSPLGRGrrPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENL 235
|
250
....*....|....*.
gi 1457282850 248 SVFDFELTQGDMNRID 263
Cdd:cd19071 236 DVFDFELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-266 |
2.46e-121 |
|
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: 347.05 E-value: 2.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 8 TATLHNGVKMPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKVWNA 87
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVS-NDEAASAVREALEVGYRSIDTAAIYGNEEGVG----KAIRASGVPREELFITTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 88 DLGYEETLAAFETSLSKLGLDYLDLYLIHWPV--EGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMI 165
Cdd:cd19131 76 DQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 166 NQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKE 245
Cdd:cd19131 156 NQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAE 235
|
250 260
....*....|....*....|.
gi 1457282850 246 NASVFDFELTQGDMNRIDALN 266
Cdd:cd19131 236 NFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-266 |
6.96e-118 |
|
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: 338.40 E-value: 6.96e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKVWNADL 89
Cdd:cd19133 2 TLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVG----RAIKKSGIPREELFITTKLWIQDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPVeGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVE 169
Cdd:cd19133 78 GYEKAKKAFERSLKRLGLDYLDLYLIHQPF-GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 170 FHPRLTQKELMAYCQKQGIQMEAWSPLMQGQ--LLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENA 247
Cdd:cd19133 157 THPFNQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENF 236
|
250
....*....|....*....
gi 1457282850 248 SVFDFELTQGDMNRIDALN 266
Cdd:cd19133 237 DIFDFELSDEDMEAIAALD 255
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-265 |
6.02e-113 |
|
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: 326.13 E-value: 6.02e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 17 MPWFGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLGYEETLA 96
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 97 AFETSLSKLGLDYLDLYLIHWP-VEGKY----------KEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMI 165
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgVQGLKpsdprnaelrRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 166 NQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQL--LDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRI 243
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLrlLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 1457282850 244 KENASVFDFELTQGDMNRIDAL 265
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-265 |
5.80e-110 |
|
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: 318.50 E-value: 5.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 7 ATATLHNGVKMPWFGLGVFQVeeGTELVNAVRTAIVH-GYRSIDTAAIYGNEAGVGEGlqqgIDEAGISREDLFITSKVW 85
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTSHS--GGYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKA----IKESGVPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 86 NADLGYEETLAAFETSLSKLGLDYLDLYLIHWP---VEGKYK-----EAWRALETLYKEGRVKAIGVSNFQIHHLEDLMT 157
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPdcpSSGKNVketraETWRALEELYDEGLCRAIGVSNFLIEHLEQLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 158 AAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKS 237
Cdd:cd19135 157 DCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKS 236
|
250 260
....*....|....*....|....*...
gi 1457282850 238 TKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19135 237 TKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-266 |
7.87e-107 |
|
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: 310.88 E-value: 7.87e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEgTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQgideAGISREDLFITSKVWNADL 89
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPP-EETADAVATALADGYRLIDTAAAYGNEREVGEGIRR----SGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYK---EAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMIN 166
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDrtiQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 167 QVEFHPRLTQKELMAYCQKQGIQMEAWSPL------------MQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITI 234
Cdd:cd19127 157 QVELHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAI 236
|
250 260 270
....*....|....*....|....*....|..
gi 1457282850 235 PKSTKEHRIKENASVFDFELTQGDMNRIDALN 266
Cdd:cd19127 237 PKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
6-278 |
4.06e-97 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 286.20 E-value: 4.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 6 QATATLHNGVKMPWFGLGVFQVEEgTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQqgidEAGISREDLFITSKVW 85
Cdd:PRK11565 4 PTVIKLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALK----EASVAREELFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 86 NADlgYEETLAAFETSLSKLGLDYLDLYLIHWPV--EGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKP 163
Cdd:PRK11565 79 NDD--HKRPREALEESLKKLQLDYVDLYLMHWPVpaIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 164 MINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQG--QLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEH 241
Cdd:PRK11565 157 VINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPS 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 1457282850 242 RIKENASVFDFELTQGDMNRIDALNENLRVGPDPDNF 278
Cdd:PRK11565 237 RIAENFDVFDFRLDKDELGEIAKLDQGKRLGPDPDQF 273
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-266 |
2.95e-96 |
|
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: 283.39 E-value: 2.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 11 LHNGVKMPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQgideAGISREDLFITSKVWNADLG 90
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLK-GDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRHHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 91 YEETLAAFETSLSKLGLDYLDLYLIHWPV--EGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQV 168
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHWPNpsRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 169 EFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQ-LLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENA 247
Cdd:cd19132 156 ELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSgLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENL 235
|
250
....*....|....*....
gi 1457282850 248 SVFDFELTQGDMNRIDALN 266
Cdd:cd19132 236 AIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
11-271 |
3.35e-95 |
|
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: 282.25 E-value: 3.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 11 LHNGVKMPWFGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLG 90
Cdd:cd19116 5 LNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 91 YEETLAAFETSLSKLGLDYLDLYLIHWPVEGK-----------------YKEAWRALETLYKEGRVKAIGVSNFQIHHLE 153
Cdd:cd19116 85 REQVEPALRESLKRLGLDYVDLYLIHWPVAFKenndsesngdgslsdidYLETWRGMEDLVKLGLTRSIGVSNFNSEQIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 154 DLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL----MQGQL-----LDHPVLADIAQTYNKSVAQIILR 224
Cdd:cd19116 165 RLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvPRGQTnppprLDDPTLVAIAKKYGKTTAQIVLR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1457282850 225 WDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRV 271
Cdd:cd19116 245 YLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
11-271 |
2.55e-93 |
|
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: 277.73 E-value: 2.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 11 LHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEA-GISREDLFITSKVWNADL 89
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPG-QVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPVEGK--------------------YKEAWRALETLYKEGRVKAIGVSNFQI 149
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFErgdnpfpknpdgtirydsthYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 150 HHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL----------MQGQLLDHPVLADIAQTYNKSVA 219
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwakpDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1457282850 220 QIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRV 271
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
10-271 |
1.01e-90 |
|
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: 270.37 E-value: 1.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADL 89
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADPG-VVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPVEGK---------------YKEAWRALETLYKEGRVKAIGVSNFQIHHLED 154
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKkgahmpepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 155 LMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL-------MQGQLLDHPVLADIAQTYNKSVAQIILRWDL 227
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgttwVKKNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1457282850 228 QHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRV 271
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
17-263 |
3.48e-88 |
|
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: 262.59 E-value: 3.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 17 MPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQqgidEAGISREDLFITSKVWNADLGYEETLA 96
Cdd:cd19073 1 IPALGLGTWQLR-GDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIA----ESGVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 97 AFETSLSKLGLDYLDLYLIHWPVEGK-YKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVEFHPRLT 175
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWPNPTVpLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 176 QKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELT 255
Cdd:cd19073 156 QAELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELT 235
|
....*...
gi 1457282850 256 QGDMNRID 263
Cdd:cd19073 236 SEDVAKID 243
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
10-271 |
1.00e-87 |
|
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: 263.50 E-value: 1.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADL 89
Cdd:cd19154 5 TLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWP-----VEGKYK---------------EAWRALETLYKEGRVKAIGVSNFQI 149
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPaafkdDEGESGtmengmsihdavdveDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 150 HHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL---------------MQGQLLDHPVLADIAQTY 214
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgranftkstgvsPAPNLLQDPIVKAIAEKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1457282850 215 NKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRV 271
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-266 |
1.15e-85 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 256.76 E-value: 1.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGlqqgIDEAGISREDLFITSKVWNADL 89
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPA-DTQRAVATALEVGYRHIDTAAIYGNEEGVGAA----IAASGIPRDELFVTTKLWNDRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPV--EGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQ 167
Cdd:cd19130 78 DGDEPAAAFAESLAKLGLDQVDLYLVHWPTpaAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 168 VEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENA 247
Cdd:cd19130 158 IELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNL 237
|
250
....*....|....*....
gi 1457282850 248 SVFDFELTQGDMNRIDALN 266
Cdd:cd19130 238 DVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
7-270 |
1.17e-85 |
|
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: 258.11 E-value: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 7 ATATLHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWN 86
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKPG-EVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 87 ADLGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGK--------------YKEA-----WRALETLYKEGRVKAIGVSNF 147
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKkgvgfpesgedllsLSPIpledtWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 148 QIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQ------------LLDHPVLADIAQTYN 215
Cdd:cd19123 161 SVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepvLLEDPVINKIAEKHG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1457282850 216 KSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLR 270
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
12-265 |
7.31e-84 |
|
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: 251.79 E-value: 7.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 12 HNGVKMPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGlqqgIDEAGISREDLFITSKVWNADLGY 91
Cdd:cd19140 3 VNGVRIPALGLGTYPLT-GEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA----IAASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 92 EETLAAFETSLSKLGLDYLDLYLIHWP-VEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVEF 170
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWPnKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 171 HPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDL-QHGIITIPKSTKEHRIKENASV 249
Cdd:cd19140 158 HPYLDQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDI 237
|
250
....*....|....*.
gi 1457282850 250 FDFELTQGDMNRIDAL 265
Cdd:cd19140 238 FDFTLSDEEMARIAAL 253
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-272 |
1.32e-83 |
|
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: 251.70 E-value: 1.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 8 TATLHNGVKMPWFGLGVFQVEEgTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKVWNA 87
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSD-DEAERSVSAALEAGYRLIDTAAAYGNEAAVG----RAIAASGIPRGELFVTTKLATP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 88 DLGYEETLAAFETSLSKLGLDYLDLYLIHWPV--EGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMI 165
Cdd:cd19134 77 DQGFTASQAACRASLERLGLDYVDLYLIHWPAgrEGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 166 NQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKE 245
Cdd:cd19134 157 NQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIAS 236
|
250 260
....*....|....*....|....*..
gi 1457282850 246 NASVFDFELTQGDMNRIDALNENLRVG 272
Cdd:cd19134 237 NLDVFDFELTADHMDALDGLDDGTRFR 263
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
14-264 |
5.17e-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: 242.52 E-value: 5.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGV-------FQVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQqgidEAGISREDLFITSKVWN 86
Cdd:cd19120 1 GSKIPAIAFGTgtawyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 87 adlGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYK-----EAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEI 161
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGgptlaEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 162 KPMINQVEFHPRLT--QKELMAYCQKQGIQMEAWSPL------MQGQLLdhPVLADIAQTYNKSVAQIILRWDLQHGIIT 233
Cdd:cd19120 154 KPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLspltrdAGGPLD--PVLEKIAEKYGVTPAQVLLRWALQKGIVV 231
|
250 260 270
....*....|....*....|....*....|.
gi 1457282850 234 IPKSTKEHRIKENASVFDFELTQGDMNRIDA 264
Cdd:cd19120 232 VTTSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
13-265 |
2.85e-78 |
|
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: 238.71 E-value: 2.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 13 NGVKMPWFGLGVF-QVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGI-SREDLFITSKVWNADLG 90
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 91 YEETLAAFETSLSKLGLDYLDLYLIHWPV---EGKY--------------KEAWRALETLYKEGRVKAIGVSNFQIHHLE 153
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVslkPGKFsfpieeedflpfdiKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 154 DLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL-----MQG--QLLDHPVLADIAQTYNKSVAQIILRWD 226
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgapgtKWGsnAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1457282850 227 LQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-270 |
6.83e-76 |
|
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: 233.53 E-value: 6.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 7 ATATLHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWN 86
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPG-EIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 87 ADLGYeeTLAAFETSLSKLGLDYLDLYLIHWPVEGKY------------------------KEAWRALETLYKEGRVKAI 142
Cdd:cd19112 80 SDHGH--VIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvgttgsalgedgvldidvtislETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 143 GVSNFQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQG----------QLLDHPVLADIAQ 212
Cdd:cd19112 158 GISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsvSPLDDPVLKDLAK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1457282850 213 TYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLR 270
Cdd:cd19112 238 KYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
14-271 |
1.18e-72 |
|
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: 225.38 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADlgYEE 93
Cdd:cd19107 1 GAKMPILGLGTWKSPPG-QVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTF--HEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 94 TL--AAFETSLSKLGLDYLDLYLIHWPV--------------------EGKYKEAWRALETLYKEGRVKAIGVSNFQIHH 151
Cdd:cd19107 78 GLvkGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 152 LEDLMTAAEIK--PMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL----------MQGQLLDHPVLADIAQTYNKSVA 219
Cdd:cd19107 158 IERILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwakpEDPSLLEDPKIKEIAAKHNKTTA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1457282850 220 QIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRV 271
Cdd:cd19107 238 QVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRA 289
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-265 |
6.51e-72 |
|
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: 222.37 E-value: 6.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 5 LQATATLHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKV 84
Cdd:cd19117 2 SSKTFKLNTGAEIPAVGLGTWQSKPN-EVAKAVEAALKAGYRHIDTAAIYGNEEEVG----QGIKDSGVPREEIFITTKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 85 WNADlgYEETLAAFETSLSKLGLDYLDLYLIHWPV----------------------EGKYKEAWRALETLYKEGRVKAI 142
Cdd:cd19117 77 WCTW--HRRVEEALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkkddgtkdhepDWDFIKTWELMQKLPATGKVKAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 143 GVSNFQIHHLEDLMTA--AEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL--MQGQLLDHPVLADIAQTYNKSV 218
Cdd:cd19117 155 GVSNFSIKNLEKLLASpsAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgsTNAPLLKEPVIIKIAKKHGKTP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1457282850 219 AQIILRWDLQHGIITIPKSTKEHRIKENASVfdFELTQGDMNRIDAL 265
Cdd:cd19117 235 AQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
11-265 |
7.71e-71 |
|
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: 219.59 E-value: 7.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 11 LHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGI-SREDLFITSKVWNADL 89
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPG-EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGvKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPV-------------------------EGKYKEAWRALETLYKEGRVKAIGV 144
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVafkptgdlnpltavptnggevdldlSVSLVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 145 SNFQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL---MQGQ--LLDHPVLADIAQTYNKSVA 219
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLplLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1457282850 220 QIILRWDLQHGIITIPKSTKEHRIKENASvfDFELTQGDMNRIDAL 265
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-270 |
8.41e-71 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 220.40 E-value: 8.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 8 TATLHNGVKMPWFGLGVFQVEEGTeLVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNA 87
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNAT-AADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 88 DLGYEETLAAFETSLSKLGLDYLDLYLIHWPV-------EGKYK-------------------EAWRALETLYKEGRVKA 141
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIafkfvpiEEKYPpgfycgdgdnfvyedvpilDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 142 IGVSNFQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSP--------LMQGQ------LLDHPVL 207
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSfgpqsfveLNQGRalntptLFEHDTI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1457282850 208 ADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLR 270
Cdd:cd19113 241 KSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
7-278 |
1.44e-70 |
|
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: 219.98 E-value: 1.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 7 ATATLHNGVKMPWFGLGVFQVEEGTeLVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWN 86
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLWKVNNDT-CADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 87 ADLGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKY-------------------------KEAWRALETLYKEGRVKA 141
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYvdpavryppgwfydgkkvefsnapiQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 142 IGVSNFQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWS---PL------MQGQ-----LLDHPVL 207
Cdd:cd19115 162 IGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgPQsfleldLPGAkdtppLFEHDVI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1457282850 208 ADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRVGpDPDNF 278
Cdd:cd19115 242 KSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFN-NPLNY 311
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
14-270 |
8.01e-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: 217.37 E-value: 8.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLGYEE 93
Cdd:cd19111 1 GFPMPVIGLGTYQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 94 TLAAFETSLSKLGLDYLDLYLIHWPVEGKYK--------------EAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAA 159
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVNKkdkgerelassdvtSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 160 EIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL------------MQGQLLDHPVLADIAQTYNKSVAQIILRWDL 227
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgspgranqslwpDQPDLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1457282850 228 QHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLR 270
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-270 |
2.24e-68 |
|
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: 214.31 E-value: 2.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEgTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADL 89
Cdd:cd19155 5 TFNNGEKMPVVGLGTWQSSP-EEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKE----------------------AWRALETLYKEGRVKAIGVSNF 147
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEddsgkldptgehkqdyttdlldIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 148 QIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL-----------------MQGQLLDHPVLADI 210
Cdd:cd19155 164 NREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQDPVVKAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 211 AQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLR 270
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-275 |
2.79e-68 |
|
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: 213.67 E-value: 2.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 16 KMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLGYEETL 95
Cdd:cd19110 3 DIPAVGLGTWKASPG-EVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 96 AAFETSLSKLGLDYLDLYLIHWPVEGK--------------------YKEAWRALETLYKEGRVKAIGVSNFQIHHLEDL 155
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 156 MTAA--EIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL---MQG-QLLDHPVLADIAQTYNKSVAQIILRWDLQH 229
Cdd:cd19110 162 LNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLggsCEGvDLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1457282850 230 GIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRVGPDP 275
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
17-265 |
1.27e-66 |
|
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: 207.59 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 17 MPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKVWNADLGYEETLA 96
Cdd:cd19139 1 IPAFGLGTFRLK-DDVVIDSVRTALELGYRHIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 97 AFETSLSKLGLDYLDLYLIHWP---VEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMI-NQVEFHP 172
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWPspnDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAtNQIELSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 173 RLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDF 252
Cdd:cd19139 156 YLQNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDL 235
|
250
....*....|...
gi 1457282850 253 ELTQGDMNRIDAL 265
Cdd:cd19139 236 TLDADDMAAIAAL 248
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-274 |
4.60e-66 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 206.80 E-value: 4.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 16 KMPWFGLGVFQVEeGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGeglqQGIDEAGISREDLFITSKVWNADLGYEETL 95
Cdd:PRK11172 2 SIPAFGLGTFRLK-DQVVIDSVKTALELGYRAIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLAKDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 96 AAFETSLSKLGLDYLDLYLIHWPVEGK---YKEAWRALETLYKEGRVKAIGVSNFQIHHLE---DLMTAAEIKpmINQVE 169
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPSPNDevsVEEFMQALLEAKKQGLTREIGISNFTIALMKqaiAAVGAENIA--TNQIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 170 FHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASV 249
Cdd:PRK11172 155 LSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLA 234
|
250 260
....*....|....*....|....*.
gi 1457282850 250 FDFELTQGDMNRIDALNENLR-VGPD 274
Cdd:PRK11172 235 QDLQLDAEDMAAIAALDRNGRlVSPE 260
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
11-273 |
2.18e-65 |
|
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: 206.31 E-value: 2.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 11 LHNGVKMPWFGLGVFQVEE--GTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNAD 88
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 89 LGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKEA--------------------WRALETLYKEGRVKAIGVSNFQ 148
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEElfpkdengklifdtvdlcatWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 149 IHHLEDLMTAAEIK--PMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLmqGQ-------------LLDHPVLADIAQT 213
Cdd:cd19108 165 RRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSAL--GSqrdkewvdqnspvLLEDPVLCALAKK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 214 YNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRVGP 273
Cdd:cd19108 243 HKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
10-265 |
4.27e-65 |
|
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: 205.07 E-value: 4.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFQVEEGtELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDeAGISREDLFITSKVWNADl 89
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAG-EVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIA-GGVKREDLFVTTKLWSTY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 gYEETLAAFETSLSKLGLDYLDLYLIHWPV---------------EGK--------YKEAWRALETLYKEGRVKAIGVSN 146
Cdd:cd19121 82 -HRRVELCLDRSLKSLGLDYVDLYLVHWPVllnpngnhdlfptlpDGSrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 147 FQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL--MQGQLLDHPVLADIAQTYNKSVAQIILR 224
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1457282850 225 WDLQHGIITIPKSTKEHRIKENASVFDFelTQGDMNRIDAL 265
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
14-270 |
2.70e-64 |
|
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: 203.88 E-value: 2.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQVEEGT---ELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLG 90
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 91 YEETLAAFETSLSKLGLDYLDLYLIHWPV-------------EGKYK-------EAWRALETLYKEGRVKAIGVSNFQIH 150
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMafkpgdeiyprdeNGKWLyhktnlcATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 151 HLEDLMTAAEIK--PMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQ-----------LLDHPVLADIAQTYNKS 217
Cdd:cd19109 161 QLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1457282850 218 VAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLR 270
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
14-270 |
8.73e-64 |
|
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: 202.40 E-value: 8.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQV--EEGTElvnAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLGY 91
Cdd:cd19114 1 GDKMPLVGFGTAKIkaNETEE---VIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 92 EETLAAFETSLSKLGLDYLDLYLIHWPVEGKY--------------------------KEAWRALETLYKEGRVKAIGVS 145
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYvdpaenypflwkdkelkkfpleqspmQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 146 NFQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQG-------------QLLDHPVLADIAQ 212
Cdd:cd19114 158 NFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkhftNLLEHPVVKKLAD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1457282850 213 TYNKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLR 270
Cdd:cd19114 238 KHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
11-267 |
2.32e-63 |
|
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: 200.80 E-value: 2.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 11 LHNGVKMPWFGLGVFQ-VEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWnaDL 89
Cdd:cd19119 6 LNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVW--PT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWPV--------------------------EGKYKEAWRALETLYKEGRVKAIG 143
Cdd:cd19119 84 FYDEVERSLDESLKALGLDYVDLLLVHWPVcfekdsddsgkpftpvnddgktryaaSGDHITTYKQLEKIYLDGRAKAIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 144 VSNFQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL--MQGQLLDHPVLADIAQTYNKSVAQI 221
Cdd:cd19119 164 VSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLgsHGAPNLKNPLVKKIAEKYNVSTGDI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1457282850 222 ILRWDLQHGIITIPKSTKEHRIKENASVfdFELTQGDMNRIDALNE 267
Cdd:cd19119 244 LISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-267 |
8.34e-60 |
|
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: 191.68 E-value: 8.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 10 TLHNGVKMPWFGLGVFqVEEGT--ELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDE-AGISREDLFITSKVWN 86
Cdd:cd19122 2 TLNNGVKIPAVGFGTF-ANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKEnPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 87 ADLGYEETLAAFETSLSKLGLDYLDLYLIHWPV--------------EGKY----------KEAWRALETLYKEGRVKAI 142
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaekndqrspklgpDGKYvilkdltenpEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 143 GVSNFQIHHLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL-MQGQ-------LLDHPVLADIAQTY 214
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgSQNQvpstgerVSENPTLNEVAEKG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1457282850 215 NKSVAQIILRWDLQHGIITIPKSTKEHRIKENASVfdFELTQGDMNRIDALNE 267
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQVAK 291
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
14-263 |
1.59e-58 |
|
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: 187.44 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQVEEGT--------ELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLqqgideAGISREDLFITS 82
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdysddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI------KGFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 83 KVWNADLGYEETLAAFETSLSKLGLDYLDLYLIHWPV-EGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEI 161
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNpSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 162 KPMI-NQVEFH--PRLTQKELMAYCQKQGIQMEAWSPLMQGQLL---DHPVLADIAQTYNKSVAQIILRWDLQH-GIITI 234
Cdd:cd19072 155 GPIVaNQVEYNlfDREEESGLLPYCQKNGIAIIAYSPLEKGKLSnakGSPLLDEIAKKYGKTPAQIALNWLISKpNVIAI 234
|
250 260
....*....|....*....|....*....
gi 1457282850 235 PKSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19072 235 PKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
12-270 |
1.50e-56 |
|
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: 183.43 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 12 HNGVKMPWFGLGVFqVEEGTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLGY 91
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 92 EETLAAFETSLSKLGLDYLDLYLIHWPV--------------------EG-KYKEAWRALETLYKEGRVKAIGVSNFQIH 150
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFafqpgdeqdprdangnviydDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 151 HLEDLMTAAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPL---MQGQLLDHPVLADIAQTYNKSVAQIILRWDL 227
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLghgMEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1457282850 228 QHGIITIPKSTKEHRIKENasvfdFELTQGDMNRIDALNENLR 270
Cdd:cd19129 240 QRGTALLTTSKTPSRIREN-----FDISTLPEDAMREINEGIK 277
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
18-265 |
8.16e-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: 178.49 E-value: 8.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 18 PWFGLGVFQVEEgTELVNAVRTAIVHGYRSIDTAAIYGNEAGVGEGLQQGIDEAGISREDLFITSKVWNADLGYEETLAA 97
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 98 FETSLSKLGLDYLDLYLIHWPVE------------------GKY--KEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMT 157
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAfdmdtdgdprddnqiqslSKKplEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 158 AAEIKPMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQ------LLDHPVLADIAQTYNKSVAQIILRWDLQHGI 231
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYgdgnltFLNDSELKALATKYNTTPPQVIIAWHLQKWP 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1457282850 232 IT---IPKSTKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19128 241 KNysvIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-263 |
8.98e-54 |
|
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: 175.51 E-value: 8.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 8 TATLHNGVKMPWFGLGVFQVEEGTEL----VNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLqqgideAGIsREDLFI 80
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMGEDPAKraqeIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAI------RGR-RDKVFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 81 TSKV--WNAdlGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTA 158
Cdd:cd19138 75 VSKVlpSNA--SRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 159 AEIKPM-INQVEFH--PRLTQKELMAYCQKQGIQMEAWSPLMQGQLLD-----HPVLADIAQTYNKSVAQIILRWDLQHG 230
Cdd:cd19138 153 PGGGNCaANQVLYNlgSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRrglleNPTLKEIAARHGATPAQVALAWVLRDG 232
|
250 260 270
....*....|....*....|....*....|....
gi 1457282850 231 -IITIPKSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19138 233 nVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
32-266 |
1.45e-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: 172.88 E-value: 1.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLQqgidEAGISREDLFITSKV------WNADLGYEETLAAFETSL 102
Cdd:pfam00248 19 EALEALRAALEAGINFIDTAEVYGdgkSEELLGEALK----DYPVKRDKVVIATKVpdgdgpWPSGGSKENIRKSLEESL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 103 SKLGLDYLDLYLIHWP-VEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVEFHP--RLTQKEL 179
Cdd:pfam00248 95 KRLGTDYIDLYYLHWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNLlrRRQEEEL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 180 MAYCQKQGIQMEAWSPLMQG---------------------------QLLDHPVLADIAQTYNKSVAQIILRWDLQH--G 230
Cdd:pfam00248 175 LEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkgtplNLEALEALEEIAKEHGVSPAQVALRWALSKpgV 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 1457282850 231 IITIPKSTKEHRIKENASVFDFELTQGDMNRIDALN 266
Cdd:pfam00248 255 TIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
14-263 |
5.40e-46 |
|
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: 155.42 E-value: 5.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQV--------EEGTELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLQQgideagISREDLFITS 82
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 83 KVWNADLGYEETLAAFETSLSKLGLDYLDLYLIHWP-VEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEI 161
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPnPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 162 KPMINQVEFH---PRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQH-GIITIPKS 237
Cdd:cd19137 155 PIVCNQVKYNledRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKA 234
|
250 260
....*....|....*....|....*.
gi 1457282850 238 TKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19137 235 GRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
32-269 |
1.67e-38 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 136.56 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQgideagiSREDLFITSKVWNADLGYEETLAAFETSLSKLGLD 108
Cdd:cd19085 24 ESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSPDNLTPEDVRKSCERSLKRLGTD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 109 YLDLYLIHWPVEG-KYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKpmINQVEFHP--RLTQKELMAYCQK 185
Cdd:cd19085 97 YIDLYQIHWPSSDvPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQLPYNLlwRAIEYEILPFCRE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 186 QGIQMEAWSPLMQGQL---------------------LDHP-----------VLADIAQTYNKSVAQIILRWDLQHGIIT 233
Cdd:cd19085 175 HGIGVLAYSPLAQGLLtgkfssaedfppgdartrlfrHFEPgaeeetfealeKLKEIADELGVTMAQLALAWVLQQPGVT 254
|
250 260 270
....*....|....*....|....*....|....*....
gi 1457282850 234 IP---KSTKEHrIKENASVFDFELTQGDMNRIDALNENL 269
Cdd:cd19085 255 SVivgARNPEQ-LEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
32-263 |
1.15e-35 |
|
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: 129.18 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQqgideaGIsREDLFITSKV---WN------ADLGYEETLAAFE 99
Cdd:cd19084 26 ESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALK------GR-RDDVVIATKCglrWDggkgvtKDLSPESIRKEVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 100 TSLSKLGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIkpMINQVEFHP-- 172
Cdd:cd19084 99 QSLRRLQTDYIDLYQIHWpdpntPIE----ETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMle 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 173 RLTQKELMAYCQKQGIQMEAWSPLMQGQL----------------LDHP---------------VLADIAQTYNKSVAQI 221
Cdd:cd19084 173 REIEEELLPYCRENGIGVLPYGPLAQGLLtgkykkeptfppddrrSRFPffrgenfeknleivdKLKEIAEKYGKSLAQL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1457282850 222 ILRWDLQHGIIT--IPKSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19084 253 AIAWTLAQPGVTsaIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
32-263 |
9.43e-35 |
|
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: 126.96 E-value: 9.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQGIDeagisREDLFITSKVWNA--DLGYEETLAAFETSLSKLG 106
Cdd:cd19093 27 DLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELGD-----RDEVVIATKFAPLpwRLTRRSVVKALKASLERLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 107 LDYLDLYLIHWPVE--GKYKEAWRALETLYKEGRVKAIGVSNFQIHHLE---DLMTAAEIKPMINQVEF---HPRLTQKE 178
Cdd:cd19093 102 LDSIDLYQLHWPGPwySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRrahKALKERGVPLASNQVEYsllYRDPEQNG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 179 LMAYCQKQGIQMEAWSPLMQGQL-----LDHP----------------------VLADIAQTYNKSVAQIILRWDLQHGI 231
Cdd:cd19093 182 LLPACDELGITLIAYSPLAQGLLtgkysPENPppggrrrlfgrknlekvqplldALEEIAEKYGKTPAQVALNWLIAKGV 261
|
250 260 270
....*....|....*....|....*....|..
gi 1457282850 232 ITIPKSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19093 262 VPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
20-275 |
2.86e-33 |
|
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: 123.36 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 20 FGLGVFQVEEgTELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLqqgideAGISREDLFITSKV--------WNAD 88
Cdd:COG0667 23 FGGPWGGVDE-AEAIAILDAALDAGINFFDTADVYGpgrSEELLGEAL------KGRPRDDVVIATKVgrrmgpgpNGRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 89 LGYEETLAAFETSLSklgldyldlylIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKP 163
Cdd:COG0667 96 LSREHIRRAVEASLRrlgtdyidlyqLHRpdpdtPIE----ETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 164 MI--NQVEFHP--RLTQKELMAYCQKQGIQMEAWSPLMQG--------------------------------QLLDhpVL 207
Cdd:COG0667 172 PIvaVQNEYSLldRSAEEELLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdraatnfvqgylternlALVD--AL 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 208 ADIAQTYNKSVAQIILRWDLQHGIIT--IPKSTKEHRIKENASVFDFELTQGDMNRIDALnenLRVGPDP 275
Cdd:COG0667 250 RAIAAEHGVTPAQLALAWLLAQPGVTsvIPGARSPEQLEENLAAADLELSAEDLAALDAA---LAAVPAP 316
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
32-255 |
5.17e-31 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 117.17 E-value: 5.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQqgidEAGISREDLFITSKV---------WNA----DLGYEETL 95
Cdd:COG4989 32 EAAALIEAALELGITTFDHADIYGGytcEALFGEALK----LSPSLREKIELQTKCgirlpsearDNRvkhyDTSKEHII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 96 AAFETSLSKLGLDYLDLYLIHWP-----VEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVEF 170
Cdd:COG4989 108 ASVEGSLRRLGTDYLDLLLLHRPdplmdPE----EVAEAFDELKASGKVRHFGVSNFTPSQFELLQSALDQPLVTNQIEL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 171 HprLTQKELM-----AYCQKQGIQMEAWSPLMQGQLLD---------HPVLADIAQTYNKSVAQIILRWDLQH--GIITI 234
Cdd:COG4989 184 S--LLHTDAFddgtlDYCQLNGITPMAWSPLAGGRLFGgfdeqfprlRAALDELAEKYGVSPEAIALAWLLRHpaGIQPV 261
|
250 260
....*....|....*....|.
gi 1457282850 235 PKSTKEHRIKENASVFDFELT 255
Cdd:COG4989 262 IGTTNPERIKAAAAALDIELT 282
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
28-262 |
8.06e-30 |
|
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: 113.81 E-value: 8.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 28 EEGTELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQqgidEAGISREDLFITSK-------------VWNADLGY 91
Cdd:cd19092 21 ESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALA----LNPGLREKIEIQTKcgirlgddprpgrIKHYDTSK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 92 EETLAAFETSLSKLGLDYLDLYLIHWP---VEgkYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQV 168
Cdd:cd19092 97 EHILASVEGSLKRLGTDYLDLLLLHRPdplMD--PEEVAEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 169 EF---HPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLD---------HPVLADIAQTYNKSVAQIILRWDLQH--GIITI 234
Cdd:cd19092 175 ELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGgfderfqrlRAALEELAEEYGVTIEAIALAWLLRHpaRIQPI 254
|
250 260
....*....|....*....|....*...
gi 1457282850 235 PKSTKEHRIKENASVFDFELTQGDMNRI 262
Cdd:cd19092 255 LGTTNPERIRSAVKALDIELTREEWYEI 282
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
36-248 |
7.81e-26 |
|
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: 101.83 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 36 AVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQqgideAGISREDLFITSKV--------WNADLGYEETLAAFETSLSK 104
Cdd:cd06660 22 LLDAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKGghppggdpSRSRLSPEHIRRDLEESLRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 105 LGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAE----IKPMINQVEF---HP 172
Cdd:cd06660 97 LGTDYIDLYYLHRddpstPVE----ETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPGFAAVQPQYsllDR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1457282850 173 RLTQKELMAYCQKQGIQMEAWSPLMQGqlldhpvladiaqtynksVAQIILRWDLQH--GIITIPKSTKEHRIKENAS 248
Cdd:cd06660 173 SPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-265 |
1.20e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 94.66 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 19 WFGLGVfqvEEGTELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLQQgideagiSREDLFITSK---VWNAD---- 88
Cdd:cd19102 17 GGGWGP---QDDRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKG-------LRDRPIVATKcglLWDEEgrir 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 89 --LGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGK-YKEAWRALETLYKEGRVKAIGVSNF---QIHHLEDLMTAAEIK 162
Cdd:cd19102 87 rsLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEpIEEAWGALAELKEEGKVRAIGVSNFsvdQMKRCQAIHPIASLQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 163 PMINQVEfhpRLTQKELMAYCQKQGIQMEAWSPlMQGQLL---------------DHP-------------------VLA 208
Cdd:cd19102 167 PPYSLLR---RGIEAEILPFCAEHGIGVIVYSP-MQSGLLtgkmtpervaslpadDWRrrspffqepnlarnlalvdALR 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1457282850 209 DIAQTYNKSVAQIILRWDLQHGIIT--IPKSTKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19102 243 PIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
32-264 |
2.04e-22 |
|
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: 94.26 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQgideagiSREDLFITSK---VW----------------NADL 89
Cdd:cd19149 34 ESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVLATKcglRWdreggsfffvrdgvtvYKNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 90 GYEETLAAFETSLSKLGLDYLDLYLIHWP-VEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKpmINQV 168
Cdd:cd19149 107 SPESIREEVEQSLKRLGTDYIDLYQTHWQdVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLD--IIQE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 169 EFH--PRLTQKELMAYCQKQGIQMEAWSPLMQGQLL----------------DHP---------VLA------DIAQTYN 215
Cdd:cd19149 185 KYSmlDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTgkitpdrefdagdarsGIPwfspenrekVLAllekwkPLCEKYG 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1457282850 216 KSVAQIILRWDL-QHGIIT-IPKSTKEHRIKENASVFDFELTQGDMNRIDA 264
Cdd:cd19149 265 CTLAQLVIAWTLaQPGITSaLCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
18-263 |
2.64e-20 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 88.41 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 18 PWfglgVFQVEEGTELVnavRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQGIDeagisREDLFITSKVWN-------- 86
Cdd:cd19079 29 PW----VLDEEESRPII---KRALDLGINFFDTANVYSGgasEEILGRALKEFAP-----RDEVVIATKVYFpmgdgpng 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 87 ADLGYEETLAAFETSLSKLGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEI 161
Cdd:cd19079 97 RGLSRKHIMAEVDASLKRLGTDYIDLYQIHRwdyetPIE----ETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 162 K------PMINQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQL---------------------------LDHPVLA 208
Cdd:cd19079 173 NgwtkfvSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLarpwgdtterrrsttdtaklkydyfteADKEIVD 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 209 ---DIAQTYNKSVAQIILRWDLQHGIITIP--KSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19079 253 rveEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
30-265 |
7.67e-20 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 86.98 E-value: 7.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 30 GTELVNAVRT---AIVHGYRSIDTAAIYG---NEAGVGEGLqqgidEAGISREDLFITSKV---WNADLGY------EET 94
Cdd:cd19148 21 GTDEKEAIETihkALDLGINLIDTAPVYGfglSEEIVGKAL-----KEYGKRDRVVIATKVgleWDEGGEVvrnsspARI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 95 LAAFETSLSKLGLDYLDLYLIHWPVEGK-YKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEI---KPMINQVEf 170
Cdd:cd19148 96 RKEVEDSLRRLQTDYIDLYQVHWPDPLVpIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLhtvQPPYNLFE- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 171 hpRLTQKELMAYCQKQGIQMEAWSPLMQGQL------------------------------------LDHpvladIAQT- 213
Cdd:cd19148 175 --REIEKDVLPYARKHNIVTLAYGALCRGLLsgkmtkdtkfegddlrrtdpkfqeprfsqylaaveeLDK-----LAQEr 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1457282850 214 YNKSVAQIILRWDLQHGIITIP--KSTKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19148 248 YGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
28-265 |
1.03e-19 |
|
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: 86.70 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 28 EEGTELVnavRTAIVHGYRSIDTAAIYG---NEAGVGEGLQqgideaGISREDLFITSKVWNADLGYEETL--------A 96
Cdd:cd19083 33 EEGKDLV---REALDNGVNLLDTAFIYGlgrSEELVGEVLK------EYNRNEVVIATKGAHKFGGDGSVLnnspeflrS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 97 AFETSLSKLGLDYLDLYLIHWPVEGKYK-EAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVEFHPRLT 175
Cdd:cd19083 104 AVEKSLKRLNTDYIDLYYIHFPDGETPKaEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQREA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 176 QKELMAYCQKQGIQMEAWSPLMQGQL---------LD--------------------HPV--LADIAQTYNKSVAQIILR 224
Cdd:cd19083 184 EEDILPYCVENNISFIPYFPLASGLLagkytkdtkFPdndlrndkplfkgerfsenlDKVdkLKSIADEKGVTVAHLALA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1457282850 225 WDLQHGIIT--IPKSTKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19083 264 WYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
17-255 |
1.46e-18 |
|
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: 82.65 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 17 MPWFGLGVFQV----EEGTELVnavRTAIVHGYRSIDTAAIYGneAGVGEGLqqgIDEA-GISREDLFITSKV------- 84
Cdd:cd19088 9 MRLTGPGIWGPpadrEEAIAVL---RRALELGVNFIDTADSYG--PDVNERL---IAEAlHPYPDDVVIATKGglvrtgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 85 --WNADLGYEETLAAFETSLSKLGLDYLDLYLIHWP-VEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEdlmTAAEI 161
Cdd:cd19088 81 gwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIdPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIE---EARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 162 KPMIN-QVEFHPRLTQKE-LMAYCQKQGIQMEAWSPLMQGQLLDH-PVLADIAQTYNKSVAQIILRWDLQHG--IITIPK 236
Cdd:cd19088 158 VRIVSvQNRYNLANRDDEgVLDYCEAAGIAFIPWFPLGGGDLAQPgGLLAEVAARLGATPAQVALAWLLARSpvMLPIPG 237
|
250
....*....|....*....
gi 1457282850 237 STKEHRIKENASVFDFELT 255
Cdd:cd19088 238 TSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-264 |
8.26e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 81.49 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 34 VNAVRTAIVHGYRSIDTAAIYGN-EAGVGEGLQQGIDEAGiSREDLFITSKvWNADLG-----YEETLAAFETSLSKLGL 107
Cdd:cd19101 26 VRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERD-AADDVQIHTK-WVPDPGeltmtRAYVEAAIDRSLKRLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 108 DYLDLYLIHW--PVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAeIKPMINQVEFH--PRLTQKELMAYC 183
Cdd:cd19101 104 DRLDLVQFHWwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG-VPIVSNQVQYSllDRRPENGMAALC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 184 QKQGIQMEAWSPLMQGQL----LDHP---------------------------------VLADIAQTYNKSVAQIILRWD 226
Cdd:cd19101 183 EDHGIKLLAYGTLAGGLLsekyLGVPeptgpaletrslqkyklmidewggwdlfqellrTLKAIADKHGVSIANVAVRWV 262
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1457282850 227 LQH----GIItIPKSTKEHrIKENASVFDFELTQGDMNRIDA 264
Cdd:cd19101 263 LDQpgvaGVI-VGARNSEH-IDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
8-265 |
1.32e-17 |
|
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: 81.12 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 8 TATLhnGVKMPWFG-LGVFQVEEGTELVNAvrtAIVHGYRSIDTAAIYGN---EAGVGEGLQQgideagiSREDLFITSK 83
Cdd:cd19091 20 TMTF--GGGGGFFGaWGGVDQEEADRLVDI---ALDAGINFFDTADVYSEgesEEILGKALKG-------RRDDVLIATK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 84 V--WNAD------LGYEETLAAFETSLSKLGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIH 150
Cdd:cd19091 88 VrgRMGEgpndvgLSRHHIIRAVEASLKRLGTDYIDLYQLHGfdaltPLE----ETLRALDDLVRQGKVRYIGVSNFSAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 151 HLEDLMTAAE----IKPMINQVEFHP--RLTQKELMAYCQKQGIQMEAWSPLMQGQL--------------------LDH 204
Cdd:cd19091 164 QIMKALGISErrglARFVALQAYYSLlgRDLEHELMPLALDQGVGLLVWSPLAGGLLsgkyrrgqpapegsrlrrtgFDF 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1457282850 205 P------------VLADIAQTYNKSVAQIILRWDLQHGIIT--IPKSTKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19091 244 PpvdrergydvvdALREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
32-263 |
8.58e-17 |
|
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: 78.43 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLQQgideagiSREDLFITSK-VWNADLGYEETL----------AA 97
Cdd:cd19078 26 EMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKP-------FRDQVVIATKfGFKIDGGKPGPLgldsrpehirKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 98 FETSLSKLGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQihhLEDLMTAAEIKPMIN-QVEFH 171
Cdd:cd19078 99 VEGSLKRLQTDYIDLYYQHRvdpnvPIE----EVAGTMKELIKEGKIRHWGLSEAG---VETIRRAHAVCPVTAvQSEYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 172 --PRLTQKELMAYCQKQGIQMEAWSPLMQG---------------------------------QLLDhpVLADIAQTYNK 216
Cdd:cd19078 172 mmWREPEKEVLPTLEELGIGFVPFSPLGKGfltgkidentkfdegddraslprftpealeanqALVD--LLKEFAEEKGA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1457282850 217 SVAQIILRWDLQHG--IITIPKSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19078 250 TPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-212 |
6.45e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 74.83 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 20 FGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGN-EAGVGEGLQQGideagisREDLFITSKVWNADlgYEETLAAF 98
Cdd:cd19100 16 FGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARD--YEGAKRDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 99 ETSLSKLGLDYLDLYLIH-------WPVEGKYKEAWRALETLYKEGRVKAIGVSNfqiHHLEDLMTAAEIKPM------I 165
Cdd:cd19100 87 ERSLKRLGTDYIDLYQLHavdteedLDQVFGPGGALEALLEAKEEGKIRFIGISG---HSPEVLLRALETGEFdvvlfpI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1457282850 166 NQVEFHPRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLaDIAQ 212
Cdd:cd19100 164 NPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPL-DPEQ 209
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-270 |
7.60e-16 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 76.40 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 12 HNGVKMPWFGLGV--FQVEEGTELVNAVRTAIVHGYRSIDTAAIYGN-EAGVGEGLQQgideagiSREDLFITSK--VWN 86
Cdd:COG1453 8 KTGLEVSVLGFGGmrLPRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVILATKlpPWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 87 ADlgYEETLAAFETSLSKLGLDYLDLYLIH-------WPVEGKYKEAWRALETLYKEGRVKAIGVSNfqiHHLEDLmtaa 159
Cdd:COG1453 81 RD--PEDMRKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPGGALEALEKAKAEGKIRHIGFST---HGSLEV---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 160 eIKPMIN-------QVEFHPRLTQ----KELMAYCQKQGIQ---MEawsPLMQGQLLDHP-VLADIAQTyNKSVAQIILR 224
Cdd:COG1453 152 -IKEAIDtgdfdfvQLQYNYLDQDnqagEEALEAAAEKGIGviiMK---PLKGGRLANPPeKLVELLCP-PLSPAEWALR 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1457282850 225 WDLQHGIITIPKS---TKEHrIKENASVFD-FE-LTQGDMNRIDALNENLR 270
Cdd:COG1453 227 FLLSHPEVTTVLSgmsTPEQ-LDENLKTADnLEpLTEEELAILERLAEELG 276
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-249 |
5.85e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 72.62 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQveEGTELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQqgideaGISREDLFITSKVWNAD-- 88
Cdd:cd19105 10 GLKVSRLGFGGGG--LPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKASPRLdk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 89 LGYEETLAAFETSLSKLGLDYLDLYLIH---WPVEGKYKEAW-RALETLYKEGRVKAIGVS-NFQIHHLedLMTAAEIKP 163
Cdd:cd19105 82 KDKAELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELlEALEKLKKEGKVRFIGFStHDNMAEV--LQAAIESGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 164 ----MI--NQVEFHPRLtqKELMAYCQKQGIQMEAwsplM--QGQLLDHPVLADIAQTYNKSVAQIILRWDLQHGIIT-- 233
Cdd:cd19105 160 fdviMVayNFLNQPAEL--EEALAAAAEKGIGVVA----MktLAGGYLQPALLSVLKAKGFSLPQAALKWVLSNPRVDtv 233
|
250
....*....|....*.
gi 1457282850 234 IPKSTKEHRIKENASV 249
Cdd:cd19105 234 VPGMRNFAELEENLAA 249
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-265 |
4.79e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 70.83 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 31 TELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLQQgideagISREDLFITSKV--WNADLGYEETLAAFETSLSKL 105
Cdd:cd19103 32 DTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR------YPREDYIISTKFtpQIAGQSADPVADMLEGSLARL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 106 GLDYLDLYLIHWPVEgkyKEAWRA-LETLYKEGRVKAIGVSNF---QIHHLEDLMTAAEIKpmINQVEFHPRLTQKE--- 178
Cdd:cd19103 106 GTDYIDIYWIHNPAD---VERWTPeLIPLLKSGKVKHVGVSNHnlaEIKRANEILAKAGVS--LSAVQNHYSLLYRSsee 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 179 --LMAYCQKQGIQMEAWSPLMQGQLLD-----HP-----------------------VLADIAQTYNKSVAQIILRWDLQ 228
Cdd:cd19103 181 agILDYCKENGITFFAYMVLEQGALSGkydtkHPlpegsgraetynpllpqleeltaVMAEIGAKHGASIAQVAIAWAIA 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 1457282850 229 HGIITIPKSTKEHRIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19103 261 KGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-247 |
7.77e-14 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 69.57 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQVEEGTELVNavrTAIVHGYRSIDTAAIYGN-EAGVGEGLqqgideAGISREDLFITSKVW------- 85
Cdd:cd19095 6 GTSGIGRVWGVPSEAEAARLLN---TALDLGINLIDTAPAYGRsEERLGRAL------AGLRRDDLFIATKVGthgeggr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 86 -NADLGYEETLAAFETSLSKLGLDYLDLYLIHWP-VEGKYKEAWRALETLYKEGRVKAIGVSnfqiHHLEDLMTAAEIKP 163
Cdd:cd19095 77 dRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPsDDELTGEVLETLEDLKAAGKVRYIGVS----GDGEELEAAIASGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 164 --MInQVEFHP-RLTQKELMAYCQKQGIQMEAWSPLMQGQLLD-----------HPVLADIAQTYNKSVAQIILRWDLQH 229
Cdd:cd19095 153 fdVV-QLPYNVlDREEEELLPLAAEAGLGVIVNRPLANGRLRRrvrrrplyadyARRPEFAAEIGGATWAQAALRFVLSH 231
|
250 260
....*....|....*....|
gi 1457282850 230 GIIT--IPKSTKEHRIKENA 247
Cdd:cd19095 232 PGVSsaIVGTTNPEHLEENL 251
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
20-263 |
4.18e-13 |
|
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: 68.01 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 20 FGLGVF--QVEEGT--ELVNAVRTAivhGYRSIDTAAIYGNEAgvgEGLQQGIDEAGIS--------REDLFITSKV--W 85
Cdd:cd19081 14 LGTMVFgwTADEETsfALLDAFVDA---GGNFIDTADVYSAWV---PGNAGGESETIIGrwlksrgkRDRVVIATKVgfP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 86 NAD----LGYEETLAAFETSLSKLGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLM 156
Cdd:cd19081 88 MGPngpgLSRKHIRRAVEASLRRLQTDYIDLYQAHWddpatPLE----ETLGALNDLIRQGKVRYIGASNYSAWRLQEAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 157 TAAE---------IKPMINQVEFHPrlTQKELMAYCQKQGIQMEAWSPLMQG---------------------------- 199
Cdd:cd19081 164 ELSRqhglpryvsLQPEYNLVDRES--FEGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakrylne 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1457282850 200 ---QLLDhpVLADIAQTYNKSVAQIILRWDLQHGIITIP--KSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19081 242 rglRILD--ALDEVAAEHGATPAQVALAWLLARPGVTAPiaGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
37-251 |
1.10e-12 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 66.05 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 37 VRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQGideagiSREDLFITSKV-WNADLGYEETLAAFETSLSKLGLDYLDL 112
Cdd:cd19096 27 IRYAIDAGINYFDTAYGYGGgksEEILGEALKEG------PREKFYLATKLpPWSVKSAEDFRRILEESLKRLGVDYIDF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 113 YLIHWPVEGKYKE------AWRALETLYKEGRVKAIGVSnfqIHhledlMTAAEIKPMIN-------QVEFH----PRLT 175
Cdd:cd19096 101 YLLHGLNSPEWLEkarkggLLEFLEKAKKEGLIRHIGFS---FH-----DSPELLKEILDsydfdfvQLQYNyldqENQA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 176 QKELMAYCQKQG---IQMEawsPLMQGQLLDHP-VLADIAQTYNKSVAQIILRWDLQHGIIT---IPKSTKEHrIKENAS 248
Cdd:cd19096 173 GRPGIEYAAKKGmgvIIME---PLKGGGLANNPpEALAILCGAPLSPAEWALRFLLSHPEVTtvlSGMSTPEQ-LDENIA 248
|
...
gi 1457282850 249 VFD 251
Cdd:cd19096 249 AAD 251
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-232 |
1.22e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 66.40 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 20 FGL--GVF----QVEEgTELVNAVRTAIVHGYRSIDTAAIYGN-EAGVGEglqqgideAGISREDLFITSKV----WNAD 88
Cdd:cd19097 10 FGLdyGIAnksgKPSE-KEAKKILEYALKAGINTLDTAPAYGDsEKVLGK--------FLKRLDKFKIITKLpplkEDKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 89 LGYEETLAAFETSLSKLGLDYLDLYLIHWP--VEGKYKEAWRALETLYKEGRVKAIGVSnfqIHHLEDLMTAAEIKPM-I 165
Cdd:cd19097 81 EDEAAIEASVEASLKRLKVDSLDGLLLHNPddLLKHGGKLVEALLELKKEGLIRKIGVS---VYSPEELEKALESFKIdI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 166 NQVEFHP---RLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHPV---------------LADIAQTYNKSVAQIILRWDL 227
Cdd:cd19097 158 IQLPFNIldqRFLKSGLLAKLKKKGIEIHARSVFLQGLLLMEPDklpakfapakpllkkLHELAKKLGLSPLELALGFVL 237
|
....*
gi 1457282850 228 QHGII 232
Cdd:cd19097 238 SLPEI 242
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
40-262 |
1.61e-12 |
|
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: 66.47 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 40 AIVHGYRSIDTAAIYG---NEAGVGEGLQQGideagisREDLFITSK---VWNADLGY-------EETLAAFETSLSKLG 106
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKfgiVRDPGSGFrgvdgrpEYVRAACEASLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 107 LDYLDLYLIH-----WPVEgkykEAWRALETLYKEGRVKAIGVSNFQIhhlEDLMTAAEIKPMIN-QVEFHP--RLTQKE 178
Cdd:cd19076 114 TDVIDLYYQHrvdpnVPIE----ETVGAMAELVEEGKVRYIGLSEASA---DTIRRAHAVHPITAvQSEYSLwtRDIEDE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 179 LMAYCQKQGIQMEAWSPL--------------------------MQGQLLDHPV-LAD----IAQTYNKSVAQIILRWDL 227
Cdd:cd19076 187 VLPTCRELGIGFVAYSPLgrgfltgaikspedlpeddfrrnnprFQGENFDKNLkLVEkleaIAAEKGCTPAQLALAWVL 266
|
250 260 270
....*....|....*....|....*....|....*..
gi 1457282850 228 QHG--IITIPKSTKEHRIKENASVFDFELTQGDMNRI 262
Cdd:cd19076 267 AQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
17-246 |
2.55e-12 |
|
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: 65.66 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 17 MPWFGLGVFQ-VEEGTELVNAVRtaiVHGYRSIDTAAIYGNeaGVGEGLqqgIDEAGISREDLFITSKV---WNADLGYE 92
Cdd:cd19075 8 MTFGSQGRFTtAEAAAELLDAFL---ERGHTEIDTARVYPD--GTSEEL---LGELGLGERGFKIDTKAnpgVGGGLSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 93 ETLAAFETSLSKLGLDYLDLYLIHWP-----VEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAE----IKP 163
Cdd:cd19075 80 NVRKQLETSLKRLKVDKVDVFYLHAPdrstpLE----ETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 164 MINQVEFHP--RLTQKELMAYCQKQGIQMEAWSPL-------------------------MQGQLL----DHP------- 205
Cdd:cd19075 156 TVYQGMYNAitRQVETELFPCLRKLGIRFYAYSPLaggfltgkykysedkagggrfdpnnALGKLYrdryWKPsyfeale 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1457282850 206 VLADIAQTYNKSVAQIILRWDLQH---------GIItIPKSTKEHrIKEN 246
Cdd:cd19075 236 KVEEAAEKEGISLAEAALRWLYHHsaldgekgdGVI-LGASSLEQ-LEEN 283
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
48-271 |
5.38e-12 |
|
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: 64.77 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 48 IDTAAIYG-NEAGVGEGLQQgideAGISREDLFITSKVWN----------ADLGYEETLAAFETSLSKLGLDYLDLYLIH 116
Cdd:cd19144 51 WDTADIYGdSEELIGRWFKQ----NPGKREKIFLATKFGIeknvetgeysVDGSPEYVKKACETSLKRLGVDYIDLYYQH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 117 -----WPVEGKYKeawrALETLYKEGRVKAIGVSNFQIhhlEDLMTAAEIKPMIN-QVEFHPRLT-----QKELMAYCQK 185
Cdd:cd19144 127 rvdgkTPIEKTVA----AMAELVQEGKIKHIGLSECSA---ETLRRAHAVHPIAAvQIEYSPFSLdierpEIGVLDTCRE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 186 QGIQMEAWSPLMQG---------------------------------QLLDHpvLADIAQTYNKSVAQIILRWDLQHG-- 230
Cdd:cd19144 200 LGVAIVAYSPLGRGfltgairspddfeegdfrrmaprfqaenfpknlELVDK--IKAIAKKKNVTAGQLTLAWLLAQGdd 277
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1457282850 231 IITIPKSTKEHRIKENASVFDFELTQGDMNRIDALNENLRV 271
Cdd:cd19144 278 IIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEV 318
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
34-254 |
5.82e-12 |
|
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: 64.50 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 34 VNAVRTAIVHGYRSIDTAAIYGN-EAGVGEGLQqgideaGISREDLFITSKV-----WNADLGYEETLAAFETSLSKLGL 107
Cdd:cd19090 23 VATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKVgrlpeDTADYSADRVRRSVEESLERLGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 108 DYLDLYLIH------WPVEGKYKEAWRALETLYKEGRVKAIGVSnfqihhledLMTAAEIKPMINQVEF-----HPRLT- 175
Cdd:cd19090 97 DRIDLLMIHdpervpWVDILAPGGALEALLELKEEGLIKHIGLG---------GGPPDLLRRAIETGDFdvvltANRYTl 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 176 -----QKELMAYCQKQGIQMEAWSPLMQGQLLDHPV--------------------LADIAQTYNKSVAQIILRWDLQH- 229
Cdd:cd19090 168 ldqsaADELLPAAARHGVGVINASPLGMGLLAGRPPervrytyrwlspelldrakrLYELCDEHGVPLPALALRFLLRDp 247
|
250 260
....*....|....*....|....*..
gi 1457282850 230 GIITIP--KSTKEHrIKENASVFDFEL 254
Cdd:cd19090 248 RISTVLvgASSPEE-LEQNVAAAEGPL 273
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-225 |
1.90e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 63.11 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 20 FGLGVFQVEEG----TELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQGIDEAGISREDLFITSKVwnadlGY- 91
Cdd:cd19099 6 LGLGTYRGDSDdetdEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKA-----GYi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 92 ----EETLAAFETSLSKLGLDYLDLYL---------------------------------IHWPVEG-----------KY 123
Cdd:cd19099 81 pgdgDEPLRPLKYLEEKLGRGLIDVADsaglrhcispayledqierslkrlgldtidlylLHNPEEQllelgeeefydRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 124 KEAWRALETLYKEGRVKAIGVS----------NFQIHHLEDLMTAAEIK------------PMiNQVE---FHPRLTQK- 177
Cdd:cd19099 161 EEAFEALEEAVAEGKIRYYGIStwdgfrappaLPGHLSLEKLVAAAEEVggdnhhfkviqlPL-NLLEpeaLTEKNTVKg 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1457282850 178 ---ELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADI-AQTYNKSVAQIILRW 225
Cdd:cd19099 240 ealSLLEAAKELGLGVIASRPLNQGQLLGELRLADLlALPGGATLAQRALQF 291
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
21-249 |
8.30e-11 |
|
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: 60.57 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 21 GLGVFQ--------VEEgTELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQGideagisREDLFITSKV----- 84
Cdd:cd19086 7 GFGTWGlggdwwgdVDD-AEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 85 ----WNADLGYEETLAAFETSLSKLGLDYLDLYLIH-WPVEGKYK-EAWRALETLYKEGRVKAIGVSnfqIHHLEDLMTA 158
Cdd:cd19086 79 ggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNdELFEALEKLKQEGKIRAYGVS---VGDPEEALAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 159 AEiKPMIN--QVEFHP--RLTQKELMAYCQKQGIQMEAWSPLMQGqLLDHpvladiaqtynkSVAQIILRWDLQHGIIT- 233
Cdd:cd19086 156 LR-RGGIDvvQVIYNLldQRPEEELFPLAEEHGVGVIARVPLASG-LLTG------------KLAQAALRFILSHPAVSt 221
|
250
....*....|....*..
gi 1457282850 234 -IPKSTKEHRIKENASV 249
Cdd:cd19086 222 vIPGARSPEQVEENAAA 238
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
37-256 |
1.95e-10 |
|
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: 60.30 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 37 VRTAIVHGYRSIDTAAIYGN---EAGVGEGLqqgideAGISREDLFITSKV-WNAD-------LGYEETLAAFETSLSKL 105
Cdd:cd19074 28 VRKAYDLGINFFDTADVYAAgqaEEVLGKAL------KGWPRESYVISTKVfWPTGpgpndrgLSRKHIFESIHASLKRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 106 GLDYLDLYLIH-----WPVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAE----IKPMINQVEFH--PRL 174
Cdd:cd19074 102 QLDYVDIYYCHrydpeTPLE----ETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYNmlWRE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 175 TQKELMAYCQKQGIQMEAWSPLMQGQL------------------------------------LDHpvLADIAQTYNKSV 218
Cdd:cd19074 178 IEEEVIPLCEKNGIGLVVWSPLAQGLLtgkyrdgipppsrsratdednrdkkrrlltdenlekVKK--LKPIADELGLTL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1457282850 219 AQIILRWDLQHGIIT--IPKSTKEHRIKENASVFDFELTQ 256
Cdd:cd19074 256 AQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
128-263 |
4.84e-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: 59.17 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 128 RALETLYKEGRVKAIGVSNFQihhLEDLMTAAEIKPM-INQVEFHPRLTQKE---LMAYCQKQGIQMEAWSPLMQGQL-- 201
Cdd:cd19077 132 KALKELVKEGKIRGIGLSEVS---AETIRRAHAVHPIaAVEVEYSLFSREIEengVLETCAELGIPIIAYSPLGRGLLtg 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 202 ------------------------LDH-----PVLADIAQTYNKSVAQIILRWDLQHG---IITIPKSTKEHRIKENASV 249
Cdd:cd19077 209 riksladipegdfrrhldrfngenFEKnlklvDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKA 288
|
170
....*....|....
gi 1457282850 250 FDFELTQGDMNRID 263
Cdd:cd19077 289 ANVELTDEELKEIN 302
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
23-255 |
1.15e-09 |
|
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: 57.95 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 23 GVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQqgideaGISREDLFITSKV------WNA--DLGY 91
Cdd:cd19163 25 GVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK------GIPRDSYYLATKVgrygldPDKmfDFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 92 EETLAAFETSLSKLGLDYLDLYLIHWPVEGKYK-----EAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKpmIN 166
Cdd:cd19163 99 ERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLdqilnETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSPVK--ID 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 167 QVEFHPRLTQ-----KELMAYCQKQGIQMEAWSPLMQGQLLD------HPV----------LADIAQTYNKSVAQIILRW 225
Cdd:cd19163 177 TVLSYCHYTLndtslLELLPFFKEKGVGVINASPLSMGLLTErgppdwHPAspeikeacakAAAYCKSRGVDISKLALQF 256
|
250 260 270
....*....|....*....|....*....|..
gi 1457282850 226 DLQHGII--TIPKSTKEHRIKENASVFDFELT 255
Cdd:cd19163 257 ALSNPDIatTLVGTASPENLRKNLEAAEEPLD 288
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
14-249 |
2.30e-09 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 56.88 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 14 GVKMPWFGLGVFQ-------VEEGTELVnavRTAIVHGYRSIDTAAIYGNEAG-----VGEGLQQgidEAGISREDLFIT 81
Cdd:cd19089 8 GLHLPAISLGLWHnfgdytsPEEARELL---RTAFDLGITHFDLANNYGPPPGsaeenFGRILKR---DLRPYRDELVIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 82 SKVwnadlGYE-------------ETLAAFETSLSKLGLDYLDLYLIH-----WPVEgkykEAWRALETLYKEGRVKAIG 143
Cdd:cd19089 82 TKA-----GYGmwpgpygdggsrkYLLASLDQSLKRMGLDYVDIFYHHrydpdTPLE----ETMTALADAVRSGKALYVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 144 VSNF---QIHHLEDLMTAAEIKPMINQVEFH--PRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDHP------------- 205
Cdd:cd19089 153 ISNYpgaKARRAIALLRELGVPLIIHQPRYSllDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYlngippdsrraae 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1457282850 206 ------------------VLADIAQTYNKSVAQIILRWDLQHGIIT---IPKSTKEHRIKENASV 249
Cdd:cd19089 233 skflteealtpekleqlrKLNKIAAKRGQSLAQLALSWVLRDPRVTsvlIGASSPSQLEDNVAAL 297
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
48-201 |
5.88e-09 |
|
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: 55.66 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 48 IDTAAIYGN---EAGVGEGLQQgideagiSREDLFITSKVwnadlgYEET--------------LAAFETSLSKLGLDYL 110
Cdd:cd19087 47 FDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKV------FGPMgddpndrglsrrhiRRAVEASLRRLQTDYI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 111 DLYLIH-WPVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHL---------EDLMTAAEIKPMINQVEFHPRLtqkELM 180
Cdd:cd19087 114 DLYQMHhFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIakaqgiaarRGLLRFVSEQPMYNLLKRQAEL---EIL 190
|
170 180
....*....|....*....|.
gi 1457282850 181 AYCQKQGIQMEAWSPLMQGQL 201
Cdd:cd19087 191 PAARAYGLGVIPYSPLAGGLL 211
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
18-229 |
6.50e-09 |
|
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: 55.44 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 18 PWFGLGVFQV----EEG-TELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLqqgideAGISREDLFITSKV----- 84
Cdd:cd19162 1 PRLGLGAASLgnlaRAGeDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAAL------ARHPRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 85 -------------WnaDLGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYK---EAWRALETLYKEGRVKAIGVSNFQ 148
Cdd:cd19162 75 pgaagrpagadrrF--DFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQaltDAFPALEELRAEGVVGAIGVGVTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 149 ---------IHHLEDLMTAAEikpminqvefHPRLTQ---KELMAYCQKQGIQMEAWSPLMQGQLL-DHPV--------- 206
Cdd:cd19162 153 waallraarRADVDVVMVAGR----------YTLLDRraaTELLPLCAAKGVAVVAAGVFNSGILAtDDPAgdrydyrpa 222
|
250 260 270
....*....|....*....|....*....|...
gi 1457282850 207 ----------LADIAQTYNKSVAQIILRWDLQH 229
Cdd:cd19162 223 tpevlararrLAAVCRRYGVPLPAAALQFPLRH 255
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
48-263 |
1.02e-08 |
|
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: 54.92 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 48 IDTAAIYGNEAG---VGEGLQQgideagiSREDLFITSK-VWNADLG--------YEETLAAFETSLSKLGLDYLDLYLI 115
Cdd:cd19080 48 IDTANNYTNGTSerlLGEFIAG-------NRDRIVLATKyTMNRRPGdpnaggnhRKNLRRSVEASLRRLQTDYIDLLYV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 116 HW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIK---PMIN-QVEFH--PRLTQKELMAYCQ 184
Cdd:cd19080 121 HAwdfttPVE----EVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRgwsPFVAlQIEYSllERTPERELLPMAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 185 KQGIQMEAWSPLMQGQL-------------------LDHP-----------VLADIAQTYNKSVAQIILRWDLQHGIITI 234
Cdd:cd19080 197 ALGLGVTPWSPLGGGLLtgkyqrgeegrageakgvtVGFGklternwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVI 276
|
250 260 270
....*....|....*....|....*....|.
gi 1457282850 235 P--KSTKEHRIKENASVFDFELTQGDMNRID 263
Cdd:cd19080 277 PiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
31-262 |
3.98e-08 |
|
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: 53.21 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 31 TELVNAVRTAIVHGYRSIDTAAIYG---NEAGVGEGLQQGIdeagisREDLFITSKVWNADLGYEETL---------AAF 98
Cdd:cd19145 33 EEGIALIHHAFNSGVTFLDTSDIYGpntNEVLLGKALKDGP------REKVQLATKFGIHEIGGSGVEvrgdpayvrAAC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 99 ETSLSKLGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIhhlEDLMTAAEIKPMIN-QVEFH- 171
Cdd:cd19145 107 EASLKRLDVDYIDLYYQHRidttvPIE----ITMGELKKLVEEGKIKYIGLSEASA---DTIRRAHAVHPITAvQLEWSl 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 172 -PRLTQKELMAYCQKQGIQMEAWSPL--------------------------MQGQLLDH-----PVLADIAQTYNKSVA 219
Cdd:cd19145 180 wTRDIEEEIIPTCRELGIGIVPYSPLgrgffagkakleellensdvrkshprFQGENLEKnkvlyERVEALAKKKGCTPA 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1457282850 220 QIILRWDLQHG--IITIPKSTKEHRIKENASVFDFELTQGDMNRI 262
Cdd:cd19145 260 QLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
12-233 |
8.75e-08 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 52.41 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 12 HNGVKMPWFGLGVFQVEEGTELV-NA---VRTAIVHGYRSIDTAAIYGNEAGVGEG-----LQQgiDEAGIsREDLFITS 82
Cdd:cd19151 7 RSGLKLPAISLGLWHNFGDVDRYeNSramLRRAFDLGITHFDLANNYGPPPGSAEEnfgriLKE--DLKPY-RDELIIST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 83 K----VWNA---DLGYEETL-AAFETSLSKLGLDYLDLYLIHWP-VEGKYKEAWRALETLYKEGRVKAIGVSNFQ----- 148
Cdd:cd19151 84 KagytMWPGpygDWGSKKYLiASLDQSLKRMGLDYVDIFYHHRPdPETPLEETMGALDQIVRQGKALYVGISNYPpeear 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 149 --IHHLEDLMTAAEI-KP---MINqvefhpRLTQKELMAYCQKQGIQMEAWSPLMQGQLLDH-----PV----------- 206
Cdd:cd19151 164 eaAAILKDLGTPCLIhQPkysMFN------RWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRylngiPEdsraakgssfl 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1457282850 207 ---------------LADIAQTYNKSVAQIILRWDLQHGIIT 233
Cdd:cd19151 238 kpeqiteeklakvrrLNEIAQARGQKLAQMALAWVLRNKRVT 279
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
23-164 |
1.70e-07 |
|
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: 51.38 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 23 GVFQVE-EGTELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQgideAGISREDLFITSKV-----WNADLGYEE 93
Cdd:cd19153 24 GVYGDGlEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAA----LQVPRSSYTVATKVgryrdSEFDYSAER 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1457282850 94 TLAAFETSLSKLGLDYLDLYLIHwPVE-GKY----KEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPM 164
Cdd:cd19153 100 VRASVATSLERLHTTYLDVVYLH-DIEfVDYdtlvDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSL 174
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-246 |
1.90e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 51.18 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 43 HGYRSIDTAAIYG----------NEAGVGEGL-QQGideagiSREDLFITSKV---------WNAD---LGYEETLAAFE 99
Cdd:cd19752 29 AGGNFLDTANNYAfwteggvggeSERLIGRWLkDRG------NRDDVVIATKVgagprdpdgGPESpegLSAETIEQEID 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 100 TSLSKLGLDYLDLYLIH-----WPVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAE-------------- 160
Cdd:cd19752 103 KSLRRLGTDYIDLYYAHvddrdTPLE----ETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARqqgwaefsaiqqrh 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 161 --IKPMINQVEFHPRLTQKELMAYCQKQG-IQMEAWSPLMQGQL----------LDHP-------VLADIAQTYNKSVAQ 220
Cdd:cd19752 179 syLRPRPGADFGVQRIVTDELLDYASSRPdLTLLAYSPLLSGAYtrpdrplpeqYDGPdsdarlaVLEEVAGELGATPNQ 258
|
250 260
....*....|....*....|....*....
gi 1457282850 221 IILRWDLQHGIITIP---KSTKEHrIKEN 246
Cdd:cd19752 259 VVLAWLLHRTPAIIPllgASTVEQ-LEEN 286
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
36-253 |
3.23e-07 |
|
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: 50.69 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 36 AVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQqgideaGISREDLFITSKV------------------WNA------- 87
Cdd:cd19152 25 TLVAAWDLGIRYFDTAPWYGAglsEERLGAALR------ELGREDYVISTKVgrllvplqeveptfepgfWNPlpfdavf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 88 DLGYEETLAAFETSLSKLGLDYLDLYLIHWPVEGKYKEAW------------RALETLYKEGRVKAIGV-SNF-----QI 149
Cdd:cd19152 99 DYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgafRALEELREEGVIKAIGLgVNDwevilRI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 150 HHLEDL---MTAAEIKPMInqvefHPRLTqkELMAYCQKQGIQMEAWSPLMQGQL-------------LDHPVLA----- 208
Cdd:cd19152 179 LEEADLdwvMLAGRYTLLD-----HSAAR--ELLPECEKRGVKVVNAGPFNSGFLaggdnfdyyeygpAPPELIArrdri 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1457282850 209 -DIAQTYNKSVAQIILRWDLQHGIIT--IPKSTKEHRIKENASVFDFE 253
Cdd:cd19152 252 eALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVALLATE 299
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
20-235 |
4.79e-07 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 49.86 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 20 FGLGVFQVEEGTELVNAVRTAIV-HGYRSIDTAAIYGN-------EAGVGEGLQQ-GIdeagisREDLFITSK------- 83
Cdd:cd19082 5 LGTADFGTRIDEEEAFALLDAFVeLGGNFIDTARVYGDwvergasERVIGEWLKSrGN------RDKVVIATKgghpdle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 84 -VWNADLGYEETLAAFETSLSKLGLDYLDLYLIHW-----PVEgkykEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMT 157
Cdd:cd19082 79 dMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRddpsvPVG----EIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 158 AAEIK----PMINQVEF------HPRL------------------TQKELMAY-CQKQG-----IQMEAWSPLMQGQLLD 203
Cdd:cd19082 155 YAKAHglpgFAASSPQWslarpnEPPWpgptlvamdeemrawheeNQLPVFAYsSQARGffskrAAGGAEDDSELRRVYY 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 1457282850 204 HPV-------LADIAQTYNKSVAQIILRWDLQHGIITIP 235
Cdd:cd19082 235 SEEnferlerAKELAEEKGVSPTQIALAYVLNQPFPTVP 273
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
75-265 |
1.19e-06 |
|
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: 49.10 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 75 REDLFITSKV--------W----NADLGYEETLAAFETSLSKLGLDYLDLYLIHWPV-------EGKYK----------- 124
Cdd:cd19094 67 RDKVVLATKVagpgegitWprggGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgGGYYTepseeedsvsf 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 125 -EAWRALETLYKEGRVKAIGVSN---FQIHHLEDLMTAAEIKPMIN-QVEFHpRLTQK---ELMAYCQKQGIQMEAWSPL 196
Cdd:cd19094 147 eEQLEALGELVKAGKIRHIGLSNetpWGVMKFLELAEQLGLPRIVSiQNPYS-LLNRNfeeGLAEACHRENVGLLAYSPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 197 MQGQL----LDHP----------------------------VLADIAQTYNKSVAQIILRWDLQHGIIT---IPKSTKEh 241
Cdd:cd19094 226 AGGVLtgkyLDGAarpeggrlnlfpgymaryrspqaleavaEYVKLARKHGLSPAQLALAWVRSRPFVTstiIGATTLE- 304
|
250 260
....*....|....*....|....
gi 1457282850 242 RIKENASVFDFELTQGDMNRIDAL 265
Cdd:cd19094 305 QLKENIDAFDVPLSDELLAEIDAV 328
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
36-266 |
8.62e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 43.03 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 36 AV-RTAIVHGYRSIDTAAIYG----NeagvgeglqQGIDEA-GISREDLFITSKV---------WNADLGYEETLAAFET 100
Cdd:PRK10376 44 AVlREAVALGVNHIDTSDFYGphvtN---------QLIREAlHPYPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 101 SLSKLGLDYL------DLYLIHWPVEGKYKEAWRALETLYKEGRVKAIGVSNFQIHHLEDLMTAAEIKPMINQVEFHPRl 174
Cdd:PRK10376 115 NLRNLGLDVLdvvnlrLMGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHR- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 175 TQKELMAYCQKQGIQMEAWSPLMQGQLLDHPVLADIAQTYNKSVAQIILRWDLQHG--IITIPKSTKEHRIKENASVFDF 252
Cdd:PRK10376 194 ADDALIDALARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAAAEL 273
|
250
....*....|....
gi 1457282850 253 ELTQGDMNRIDALN 266
Cdd:PRK10376 274 VLSEEVLAELDGIA 287
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
20-84 |
1.34e-03 |
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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: 39.57 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1457282850 20 FGLGVFQVEEGTELVNAVRTAIVHGYRSIDTAAIYGN-EAGVGEGLQqgIDEAGISREDLFITSKV 84
Cdd:cd19164 23 FSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGPsEIILGRALK--ALRDEFPRDTYFIITKV 86
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| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-145 |
2.80e-03 |
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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: 38.79 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457282850 32 ELVNAVRTAIVHGYRSIDTAAIYGN---EAGVGEGLQQgideagiSREDLFITSKVW--NADLG--YEETLAAFETSLSK 104
Cdd:cd19104 33 EQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKG-------LPAGPYITTKVRldPDDLGdiGGQIERSVEKSLKR 105
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1457282850 105 LGLDYLDLYLIH--------WPVEGK--------YKEAWRALETLYKEGRVKAIGVS 145
Cdd:cd19104 106 LKRDSVDLLQLHnrigderdKPVGGTlsttdvlgLGGVADAFERLRSEGKIRFIGIT 162
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| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
36-99 |
3.49e-03 |
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ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380511 [Multi-domain] Cd Length: 268 Bit Score: 38.30 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1457282850 36 AVRTAIVHGYRSIdtAAIYGNEAGVG-----EGLQQGIDEAGISREDLFITSKVWNADLGYEETLAAFE 99
Cdd:cd06288 107 ATRHLIEAGHRRI--AFIGGPEDSLAtrlrlAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLS 173
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