|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-273 |
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: 537.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 10 TTLHNGVKMPWFGLGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYE 89
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 90 TTLQAFETTLEKLGLEYLDLYLVHWPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHP 169
Cdd:cd19157 82 STLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 170 RLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDF 249
Cdd:cd19157 162 RLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDF 241
|
250 260
....*....|....*....|....
gi 446977558 250 ELSSDDMKAIQALNENHRVGPDPD 273
Cdd:cd19157 242 ELSQEDMDKIDALNENLRVGPDPD 265
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
14-273 |
1.58e-178 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 491.49 E-value: 1.58e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 14 NGVKMPWFGLGVFKVeDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETTLQ 93
Cdd:COG0656 1 NGVEIPALGLGTWQL-PGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 94 AFETTLEKLGLEYLDLYLVHWPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQ 173
Cdd:COG0656 80 AFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 174 EELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSS 253
Cdd:COG0656 160 RELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSD 239
|
250 260
....*....|....*....|
gi 446977558 254 DDMKAIQALNENHRVGPDPD 273
Cdd:COG0656 240 EDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
11-275 |
9.60e-160 |
|
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: 444.65 E-value: 9.60e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYET 90
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPR 170
Cdd:cd19156 82 TLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 171 LAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFE 250
Cdd:cd19156 162 LTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFE 241
|
250 260
....*....|....*....|....*
gi 446977558 251 LSSDDMKAIQALNENHRVGPDPDNF 275
Cdd:cd19156 242 LTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
11-263 |
3.60e-159 |
|
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: 442.65 E-value: 3.60e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYET 90
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPR 170
Cdd:cd19126 82 TEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 171 LAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFE 250
Cdd:cd19126 162 LTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFE 241
|
250
....*....|...
gi 446977558 251 LSSDDMKAIQALN 263
Cdd:cd19126 242 LSEDDMTAIDALN 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
11-263 |
1.20e-144 |
|
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: 405.99 E-value: 1.20e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYET 90
Cdd:cd19131 3 TLNDGNTIPQLGLGVWQVSN-DEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPV--KEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYH 168
Cdd:cd19131 82 TLRAFDESLRKLGLDYVDLYLIHWPVpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 169 PRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFD 248
Cdd:cd19131 162 PRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFD 241
|
250
....*....|....*
gi 446977558 249 FELSSDDMKAIQALN 263
Cdd:cd19131 242 FELDADDMQAIAGLD 256
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
18-259 |
1.25e-142 |
|
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: 400.70 E-value: 1.25e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 18 MPWFGLGVFKVeDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETTLQAFET 97
Cdd:cd19071 1 MPLIGLGTYKL-KPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 98 TLEKLGLEYLDLYLVHWPV-------KEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPR 170
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVpgkeggsKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 171 LAQEELHAFCKEHNIQLEAWSPLMQG--QLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFD 248
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGRGrrPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|.
gi 446977558 249 FELSSDDMKAI 259
Cdd:cd19071 240 FELSEEDMAAI 250
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-263 |
2.07e-133 |
|
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: 377.30 E-value: 2.07e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 10 TTLHNGVKMPWFGLGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYE 89
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 90 TTLQAFETTLEKLGLEYLDLYLVHWPVKEkYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHP 169
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPFGD-VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 170 RLAQEELHAFCKEHNIQLEAWSPLMQGQ--LLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIF 247
Cdd:cd19133 160 FNQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIF 239
|
250
....*....|....*.
gi 446977558 248 DFELSSDDMKAIQALN 263
Cdd:cd19133 240 DFELSDEDMEAIAALD 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-263 |
6.67e-122 |
|
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: 349.01 E-value: 6.67e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 10 TTLHNGVKMPWFGLGVFKVEdGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYE 89
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP-PEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 90 TTLQAFETTLEKLGLEYLDLYLVHWPVK---EKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVE 166
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPVPndfDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 167 YHPRLAQEELHAFCKEHNIQLEAWSPL------------MQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKS 234
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKS 239
|
250 260
....*....|....*....|....*....
gi 446977558 235 IKEHRIIENANIFDFELSSDDMKAIQALN 263
Cdd:cd19127 240 VHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
12-262 |
8.55e-122 |
|
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: 348.54 E-value: 8.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 12 LHNGVKMPWFGLGVFKVedGSEVIDSVKAAIKN-GYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYET 90
Cdd:cd19135 7 LSNGVEMPILGLGTSHS--GGYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWP--------VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMV 162
Cdd:cd19135 85 TKQAFEASLKRLGVDYLDLYLLHWPdcpssgknVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 163 NQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIE 242
Cdd:cd19135 165 NQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKE 244
|
250 260
....*....|....*....|
gi 446977558 243 NANIFDFELSSDDMKAIQAL 262
Cdd:cd19135 245 NCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
18-262 |
1.52e-121 |
|
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: 347.70 E-value: 1.52e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 18 MPWFGLGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRES----GIPREELFITSKVWNSDQGYETTLQ 93
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 94 AFETTLEKLGLEYLDLYLVHWPVKEKYT-----------ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMV 162
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKpsdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 163 NQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQGQL--LDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRI 240
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLrlLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 446977558 241 IENANIFDFELSSDDMKAIQAL 262
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
11-276 |
1.28e-113 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 328.19 E-value: 1.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGyeT 90
Cdd:PRK11565 8 KLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHK--R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPV--KEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYH 168
Cdd:PRK11565 85 PREALEESLKKLQLDYVDLYLMHWPVpaIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 169 PRLAQEELHAFCKEHNIQLEAWSPLMQG--QLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANI 246
Cdd:PRK11565 165 PLMQQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDV 244
|
250 260 270
....*....|....*....|....*....|
gi 446977558 247 FDFELSSDDMKAIQALNENHRVGPDPDNFN 276
Cdd:PRK11565 245 FDFRLDKDELGEIAKLDQGKRLGPDPDQFG 274
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-263 |
1.64e-111 |
|
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: 321.91 E-value: 1.64e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 12 LHNGVKMPWFGLGVFKVeDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETT 91
Cdd:cd19132 1 LNDGTQIPAIGFGTYPL-KGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 92 LQAFETTLEKLGLEYLDLYLVHWPV--KEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHP 169
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHWPNpsRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 170 RLAQEELHAFCKEHNIQLEAWSPLMQGQ-LLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFD 248
Cdd:cd19132 160 YFPQAEQRAYHREHGIVTQSWSPLGRGSgLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFD 239
|
250
....*....|....*
gi 446977558 249 FELSSDDMKAIQALN 263
Cdd:cd19132 240 FELSDEDMAAIAALD 254
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
12-268 |
2.13e-108 |
|
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: 315.86 E-value: 2.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 12 LHNGVKMPWFGLGVFKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRES-----GIPREELFITSKVWNSDQ 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPG-QVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 87 GYETTLQAFETTLEKLGLEYLDLYLVHWPVKEK--------------------YTESWKALEKLYKDGRVRAIGVSNFHI 146
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFErgdnpfpknpdgtirydsthYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 147 HHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL----------MQGQLLDHPTLQEIATKYSKSTA 216
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwakpDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446977558 217 QVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRV 268
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-259 |
3.78e-108 |
|
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: 313.05 E-value: 3.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 18 MPWFGLGVFKVEdGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETTLQAFET 97
Cdd:cd19073 1 IPALGLGTWQLR-GDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 98 TLEKLGLEYLDLYLVHWPVKEK-YTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEEL 176
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWPNPTVpLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 177 HAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDM 256
Cdd:cd19073 160 LEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDV 239
|
...
gi 446977558 257 KAI 259
Cdd:cd19073 240 AKI 242
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
11-269 |
5.11e-106 |
|
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: 308.32 E-value: 5.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYET 90
Cdd:cd19134 4 TLNDDNTMPVIGLGVGELSD-DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPVKE--KYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYH 168
Cdd:cd19134 83 SQAACRASLERLGLDYVDLYLIHWPAGRegKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIELH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 169 PRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFD 248
Cdd:cd19134 163 PLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFD 242
|
250 260
....*....|....*....|.
gi 446977558 249 FELSSDDMKAIQALNENHRVG 269
Cdd:cd19134 243 FELTADHMDALDGLDDGTRFR 263
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
9-267 |
7.23e-101 |
|
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: 296.63 E-value: 7.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 9 YTTLHNGVKMPWFGLGVFKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAI----RESGIPREELFITSKVWNS 84
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKPG-EVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGYETTLQAFETTLEKLGLEYLDLYLVHWPV-----------KEKY--------TESWKALEKLYKDGRVRAIGVSNFH 145
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPValkkgvgfpesGEDLlslspiplEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 146 IHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQGQ------------LLDHPTLQEIATKYSK 213
Cdd:cd19123 162 VKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepvLLEDPVINKIAEKHGA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446977558 214 STAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHR 267
Cdd:cd19123 242 SPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
12-268 |
4.83e-100 |
|
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: 294.19 E-value: 4.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 12 LHNGVKMPWFGLGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRE----SGIPREELFITSKVWNSDQG 87
Cdd:cd19116 5 LNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREkiaeGVVKREDLFITTKLWNSYHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 88 YETTLQAFETTLEKLGLEYLDLYLVHWPVKEK-----------------YTESWKALEKLYKDGRVRAIGVSNFHIHHLQ 150
Cdd:cd19116 85 REQVEPALRESLKRLGLDYVDLYLIHWPVAFKenndsesngdgslsdidYLETWRGMEDLVKLGLTRSIGVSNFNSEQIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 151 DVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL----MQGQL-----LDHPTLQEIATKYSKSTAQVILR 221
Cdd:cd19116 165 RLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvPRGQTnppprLDDPTLVAIAKKYGKTTAQIVLR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446977558 222 WDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRV 268
Cdd:cd19116 245 YLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-268 |
1.69e-99 |
|
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: 292.71 E-value: 1.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 8 DYTTLHNGVKMPWFGLGVFKvEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESG----IPREELFITSKVWN 83
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQ-ADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 84 SDQGYETTLQAFETTLEKLGLEYLDLYLVHWPVKEK---------------YTESWKALEKLYKDGRVRAIGVSNFHIHH 148
Cdd:cd19125 80 TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKkgahmpepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 149 LQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL-------MQGQLLDHPTLQEIATKYSKSTAQVILR 221
Cdd:cd19125 160 LEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgttwVKKNVLKDPIVTKVAEKLGKTPAQVALR 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446977558 222 WDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRV 268
Cdd:cd19125 240 WGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
11-263 |
4.92e-97 |
|
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: 285.27 E-value: 4.92e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYET 90
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPP-ADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPV--KEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYH 168
Cdd:cd19130 82 PAAAFAESLAKLGLDQVDLYLVHWPTpaAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 169 PRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFD 248
Cdd:cd19130 162 PAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFD 241
|
250
....*....|....*
gi 446977558 249 FELSSDDMKAIQALN 263
Cdd:cd19130 242 FDLTDTEIAAIDALD 256
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
11-268 |
9.22e-96 |
|
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: 283.92 E-value: 9.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEdGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRE---SGI-PREELFITSKVWNSDQ 86
Cdd:cd19154 5 TLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 87 GYETTLQAFETTLEKLGLEYLDLYLVH--WPVKE------------------KYTESWKALEKLYKDGRVRAIGVSNFHI 146
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHapAAFKDdegesgtmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 147 HHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL---------------MQGQLLDHPTLQEIATKY 211
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgranftkstgvsPAPNLLQDPIVKAIAEKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446977558 212 SKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRV 268
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-262 |
1.19e-95 |
|
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: 281.84 E-value: 1.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 13 HNGVKMPWFGLGVFKVEdGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETTL 92
Cdd:cd19140 3 VNGVRIPALGLGTYPLT-GEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 93 QAFETTLEKLGLEYLDLYLVHWPVKE-KYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPRL 171
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWPNKDvPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 172 AQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNE-VVTIPKSIKEHRIIENANIFDFE 250
Cdd:cd19140 162 DQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQEgVAAIPKATNPERLEENLDIFDFT 241
|
250
....*....|..
gi 446977558 251 LSSDDMKAIQAL 262
Cdd:cd19140 242 LSDEEMARIAAL 253
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
15-267 |
3.60e-94 |
|
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: 278.35 E-value: 3.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGV-------FKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQg 87
Cdd:cd19120 1 GSKIPAIAFGTgtawyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 88 yeTTLQAFETTLEKLGLEYLDLYLVHWP--VKEKYT---ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMV 162
Cdd:cd19120 80 --DPREALRKSLAKLGVDYVDLYLIHSPffAKEGGPtlaEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 163 NQVEYHPRLA--QEELHAFCKEHNIQLEAWSPL------MQGQLLdhPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKS 234
Cdd:cd19120 158 NQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLspltrdAGGPLD--PVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTS 235
|
250 260 270
....*....|....*....|....*....|...
gi 446977558 235 IKEHRIIENANIFDFELSSDDMKAIQALNENHR 267
Cdd:cd19120 236 SKEERMKEYLEAFDFELTEEEVEEIDKAGKQKH 268
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-262 |
2.97e-88 |
|
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: 263.89 E-value: 2.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 12 LHNGVKMPWFGLGVFKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRES-----GIPREELFITSKVWNSDQ 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPG-EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 87 GYETTLQAFETTLEKLGLEYLDLYLVHWPV-------------------------KEKYTESWKALEKLYKDGRVRAIGV 141
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVafkptgdlnpltavptnggevdldlSVSLVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 142 SNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL---MQGQ--LLDHPTLQEIATKYSKSTA 216
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLplLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446977558 217 QVILRWDLQNEVVTIPKSIKEHRIIENANifDFELSSDDMKAIQAL 262
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
14-262 |
6.86e-85 |
|
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: 255.27 E-value: 6.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 14 NGVKMPWFGLGVFKVEDGSEVI-DSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRE---SG--IPREELFITSKVWNSDQG 87
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPEDIkAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGlvKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 88 YETTLQAFETTLEKLGLEYLDLYLVHWPVKEK-----------------YTESWKALEKLYKDGRVRAIGVSNFHIHHLQ 150
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKpgkfsfpieeedflpfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 151 DVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL-----MQG--QLLDHPTLQEIATKYSKSTAQVILRWD 223
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgapgtKWGsnAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 446977558 224 LQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQAL 262
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
11-266 |
2.85e-83 |
|
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: 251.26 E-value: 2.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQgyET 90
Cdd:cd19117 7 KLNTGAEIPAVGLGTWQSKPN-EVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWH--RR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPV-----------------KEKYTE-----SWKALEKLYKDGRVRAIGVSNFHIHH 148
Cdd:cd19117 84 VEEALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkkddgtKDHEPDwdfikTWELMQKLPATGKVKAIGVSNFSIKN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 149 LQDVF--EIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL--MQGQLLDHPTLQEIATKYSKSTAQVILRWDL 224
Cdd:cd19117 164 LEKLLasPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgsTNAPLLKEPVIIKIAKKHGKTPAQVIISWGL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446977558 225 QNEVVTIPKSIKEHRIIENANIfdFELSSDDMKAIQALNENH 266
Cdd:cd19117 244 QRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHKEY 283
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
11-276 |
5.57e-82 |
|
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: 248.94 E-value: 5.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESG----IPREELFITSKVWNSDQ 86
Cdd:cd19112 4 TLNSGHKMPVIGLGVWRMEPG-EIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWNSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 87 GYetTLQAFETTLEKLGLEYLDLYLVHWPVKEKYT------------------------ESWKALEKLYKDGRVRAIGVS 142
Cdd:cd19112 83 GH--VIEACKDSLKKLQLDYLDLYLVHFPVATKHTgvgttgsalgedgvldidvtisleTTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 143 NFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQG----------QLLDHPTLQEIATKYS 212
Cdd:cd19112 161 NYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsvSPLDDPVLKDLAKKYG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446977558 213 KSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRVGpDPDNFN 276
Cdd:cd19112 241 KSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTN-QPAKFW 303
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-268 |
1.85e-78 |
|
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: 240.01 E-value: 1.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVFKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAI----RESGIPREELFITSKVWNSDQGYET 90
Cdd:cd19107 1 GAKMPILGLGTWKSPPG-QVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPV--------------------KEKYTESWKALEKLYKDGRVRAIGVSNFHihHLQ 150
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFN--HLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 151 dvfeIAEI--------KPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL----------MQGQLLDHPTLQEIATKYS 212
Cdd:cd19107 158 ----IERIlnkpglkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwakpEDPSLLEDPKIKEIAAKHN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446977558 213 KSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRV 268
Cdd:cd19107 234 KTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRA 289
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
17-271 |
8.24e-78 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 236.84 E-value: 8.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 17 KMPWFGLGVFKVEdGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETTLQAFE 96
Cdd:PRK11172 2 SIPAFGLGTFRLK-DQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 97 TTLEKLGLEYLDLYLVHWPVKEK---YTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEI---AEIKpmVNQVEYHPR 170
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWPSPNDevsVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAvgaENIA--TNQIELSPY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 171 LAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFE 250
Cdd:PRK11172 159 LQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQ 238
|
250 260
....*....|....*....|..
gi 446977558 251 LSSDDMKAIQALNENHR-VGPD 271
Cdd:PRK11172 239 LDAEDMAAIAALDRNGRlVSPE 260
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-262 |
3.74e-77 |
|
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: 235.50 E-value: 3.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 9 YTTLHNGVKMPWFGLGVFKvEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRES---GIPREELFITSKVWNSd 85
Cdd:cd19121 3 SFKLNTGASIPAVGLGTWQ-AKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWST- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 86 qgYETTLQ-AFETTLEKLGLEYLDLYLVHWPV-------KEKY----------------TESWKALEKLYKDGRVRAIGV 141
Cdd:cd19121 81 --YHRRVElCLDRSLKSLGLDYVDLYLVHWPVllnpngnHDLFptlpdgsrdldwdwnhVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 142 SNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL--MQGQLLDHPTLQEIATKYSKSTAQVI 219
Cdd:cd19121 159 SNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446977558 220 LRWDLQNEVVTIPKSIKEHRIIENANIFDFElsSDDMKAIQAL 262
Cdd:cd19121 239 ISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
18-262 |
5.34e-77 |
|
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: 234.17 E-value: 5.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 18 MPWFGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETTLQAFET 97
Cdd:cd19139 1 IPAFGLGTFRLKD-DVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 98 TLEKLGLEYLDLYLVHWP---VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMV-NQVEYHPRLAQ 173
Cdd:cd19139 80 SLEKLRTDYVDLTLIHWPspnDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAtNQIELSPYLQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 174 EELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSS 253
Cdd:cd19139 160 RKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDA 239
|
....*....
gi 446977558 254 DDMKAIQAL 262
Cdd:cd19139 240 DDMAAIAAL 248
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
12-270 |
1.44e-76 |
|
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: 234.82 E-value: 1.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 12 LHNGVKMPWFGLGVFKVED--GSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIR---ESG-IPREELFITSKVWNSD 85
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRskiADGtVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 86 QGYETTLQAFETTLEKLGLEYLDLYLVHWPVKEKYTE--------------------SWKALEKLYKDGRVRAIGVSNFH 145
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEelfpkdengklifdtvdlcaTWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 146 IHHLQDVFEIAEIK--PMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPLmqGQ-------------LLDHPTLQEIATK 210
Cdd:cd19108 165 RRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSAL--GSqrdkewvdqnspvLLEDPVLCALAKK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 211 YSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRVGP 270
Cdd:cd19108 243 HKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-267 |
4.42e-74 |
|
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: 228.15 E-value: 4.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVFKVEdGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIR---ESG-IPREELFITSKVWNSDQGYET 90
Cdd:cd19111 1 GFPMPVIGLGTYQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 91 TLQAFETTLEKLGLEYLDLYLVHWPVKEKY--------------TESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIA 156
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVNkkdkgerelassdvTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 157 EIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL------------MQGQLLDHPTLQEIATKYSKSTAQVILRWDL 224
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgspgranqslwpDQPDLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446977558 225 QNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHR 267
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
10-275 |
5.11e-74 |
|
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: 228.84 E-value: 5.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 10 TTLHNGVKMPWFGLGVFKVeDGSEVIDSVKAAIKNGYRSIDTAAIYQNE----EGVGQAIRESGIPREELFITSKVWNSD 85
Cdd:cd19115 5 VKLNSGYDMPLVGFGLWKV-NNDTCADQVYNAIKAGYRLFDGACDYGNEveagQGVARAIKEGIVKREDLFIVSKLWNTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 86 QGYETTLQAFETTLEKLGLEYLDLYLVHWPVKEKYT-------------------------ESWKALEKLYKDGRVRAIG 140
Cdd:cd19115 84 HDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVdpavryppgwfydgkkvefsnapiqETWTAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 141 VSNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWS---PL------MQGQ-----LLDHPTLQE 206
Cdd:cd19115 164 VSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgPQsfleldLPGAkdtppLFEHDVIKS 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446977558 207 IATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRVGpDPDNF 275
Cdd:cd19115 244 IAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFN-NPLNY 311
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-267 |
9.35e-74 |
|
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: 228.10 E-value: 9.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 9 YTTLHNGVKMPWFGLGVFKVeDGSEVIDSVKAAIKNGYRSIDTAAIYQNE----EGVGQAIRESGIPREELFITSKVWNS 84
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKL-DNATAADQIYQAIKAGYRLFDGAEDYGNEkevgEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGYETTLQAFETTLEKLGLEYLDLYLVHWPV-------KEKY-------------------TESWKALEKLYKDGRVRA 138
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIafkfvpiEEKYppgfycgdgdnfvyedvpiLDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 139 IGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSP--------LMQGQLLDHPTLQE---- 206
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSfgpqsfveLNQGRALNTPTLFEhdti 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446977558 207 --IATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHR 267
Cdd:cd19113 241 ksIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-267 |
1.17e-70 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 220.09 E-value: 1.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 7 KDYTTLHNGVKMPWFGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRE---SG-IPREELFITSKV- 81
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQSSP-EEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 82 --WNSDQGYETTLQAfetTLEKLGLEYLDLYLVHWPVKEKYTES----------------------WKALEKLYKDGRVR 137
Cdd:cd19155 80 pgGNRREKVEKFLLK---SLEKLQLDYVDLYLIHFPVGSLSKEDdsgkldptgehkqdyttdlldiWKAMEAQVDQGLTR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 138 AIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL-----------------MQGQLLD 200
Cdd:cd19155 157 SIGLSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446977558 201 HPTLQEIATKYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHR 267
Cdd:cd19155 237 DPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-259 |
2.58e-70 |
|
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: 217.48 E-value: 2.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVFKV--------EDGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIResGIPREELFITSKVWN 83
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 84 SDQGYETTLQAFETTLEKLGLEYLDLYLVHWP---VKEKytESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE-IK 159
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPnpsIPIE--ETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKkGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 160 PMVNQVEYH--PRLAQEELHAFCKEHNIQLEAWSPLMQGQLL---DHPTLQEIATKYSKSTAQVILRWDLQNE-VVTIPK 233
Cdd:cd19072 157 IVANQVEYNlfDREEESGLLPYCQKNGIAIIAYSPLEKGKLSnakGSPLLDEIAKKYGKTPAQIALNWLISKPnVIAIPK 236
|
250 260
....*....|....*....|....*.
gi 446977558 234 SIKEHRIIENANIFDFELSSDDMKAI 259
Cdd:cd19072 237 ASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-257 |
2.77e-70 |
|
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: 218.52 E-value: 2.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 8 DYTTLHNGVKMPWFGLGVFK-VEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIR----ESGIPREELFITSKVW 82
Cdd:cd19119 2 ISFKLNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 83 NSdqGYETTLQAFETTLEKLGLEYLDLYLVHWPV---KEK-----------------------YTESWKALEKLYKDGRV 136
Cdd:cd19119 82 PT--FYDEVERSLDESLKALGLDYVDLLLVHWPVcfeKDSddsgkpftpvnddgktryaasgdHITTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 137 RAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL--MQGQLLDHPTLQEIATKYSKS 214
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLgsHGAPNLKNPLVKKIAEKYNVS 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446977558 215 TAQVILRWDLQNEVVTIPKSIKEHRIIENANIfdFELSSDDMK 257
Cdd:cd19119 240 TGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQ 280
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
17-272 |
5.75e-70 |
|
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: 217.90 E-value: 5.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 17 KMPWFGLGVFKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIR----ESGIPREELFITSKVWNSDQGYETTL 92
Cdd:cd19110 3 DIPAVGLGTWKASPG-EVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekikEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 93 QAFETTLEKLGLEYLDLYLVHWPVKEK--------------------YTESWKALEKLYKDGRVRAIGVSNFHIHHLQDV 152
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 153 FEIA--EIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL---MQG-QLLDHPTLQEIATKYSKSTAQVILRWDLQN 226
Cdd:cd19110 162 LNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLggsCEGvDLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446977558 227 EVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRVGPDP 272
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-259 |
1.75e-68 |
|
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: 212.88 E-value: 1.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 9 YTTLHNGVKMPWFGLGVFKVEDG----SEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESgipREELFITSKV 81
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMGEDpakrAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 82 WNSDQGYETTLQAFETTLEKLGLEYLDLYLVHWPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPM 161
Cdd:cd19138 79 LPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 162 V-NQVEYH--PRLAQEELHAFCKEHNIQLEAWSPLMQG-----QLLDHPTLQEIATKYSKSTAQVILRWDL-QNEVVTIP 232
Cdd:cd19138 159 AaNQVLYNlgSRGIEYDLLPWCREHGVPVMAYSPLAQGgllrrGLLENPTLKEIAARHGATPAQVALAWVLrDGNVIAIP 238
|
250 260
....*....|....*....|....*..
gi 446977558 233 KSIKEHRIIENANIFDFELSSDDMKAI 259
Cdd:cd19138 239 KSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
15-267 |
4.01e-68 |
|
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: 213.19 E-value: 4.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVFKV--EDGSEVIDSvkaAIKNGYRSIDTAAIYQNEEGVG----QAIRESGIPREELFITSKVWNSDQGY 88
Cdd:cd19114 1 GDKMPLVGFGTAKIkaNETEEVIYN---AIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 89 ETTLQAFETTLEKLGLEYLDLYLVHWPVKEKYT--------------------------ESWKALEKLYKDGRVRAIGVS 142
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVdpaenypflwkdkelkkfpleqspmqECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 143 NFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQG-------------QLLDHPTLQEIAT 209
Cdd:cd19114 158 NFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkhftNLLEHPVVKKLAD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446977558 210 KYSKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHR 267
Cdd:cd19114 238 KHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
15-267 |
5.64e-68 |
|
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: 213.12 E-value: 5.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVF---KVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRES----GIPREELFITSKVWNSDQG 87
Cdd:cd19109 1 GNSIPIIGLGTYsepKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 88 YETTLQAFETTLEKLGLEYLDLYLVHWPVKEK---------------YTES-----WKALEKLYKDGRVRAIGVSNFHIH 147
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiyprdengkwlYHKTnlcatWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 148 HLQDVFEIAEIK--PMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQGQ-----------LLDHPTLQEIATKYSKS 214
Cdd:cd19109 161 QLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446977558 215 TAQVILRWDLQNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHR 267
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
11-264 |
1.92e-67 |
|
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: 211.33 E-value: 1.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 11 TLHNGVKMPWFGLGVFkVEDGS--EVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRE-----SGIPREELFITSKVWN 83
Cdd:cd19122 2 TLNNGVKIPAVGFGTF-ANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 84 SDQGYETTLQAFETTLEKLGLEYLDLYLVHWPV--------------------KEKYTE----SWKALEKLYKDGRVRAI 139
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaekndqrspklgpdgkyviLKDLTEnpepTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 140 GVSNFHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL-MQGQ-------LLDHPTLQEIATKY 211
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgSQNQvpstgerVSENPTLNEVAEKG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446977558 212 SKSTAQVILRWDLQNEVVTIPKSIKEHRIIENANIfdFELSSDDMKAIQALNE 264
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQVAK 291
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-264 |
4.81e-66 |
|
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: 207.70 E-value: 4.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 13 HNGVKMPWFGLGVFkVEDGSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRE----SGIPREELFITSKVWNSDQGY 88
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 89 ETTLQAFETTLEKLGLEYLDLYLVHWPVKEK---------------------YTESWKALEKLYKDGRVRAIGVSNFHIH 147
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFAFQpgdeqdprdangnviyddgvtLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 148 HLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPL---MQGQLLDHPTLQEIATKYSKSTAQVILRWDL 224
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLghgMEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446977558 225 QNEVVTIPKSIKEHRIIENanifdFELSSDDMKAIQALNE 264
Cdd:cd19129 240 QRGTALLTTSKTPSRIREN-----FDISTLPEDAMREINE 274
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
19-262 |
4.90e-65 |
|
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: 204.68 E-value: 4.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 19 PWFGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIYQNEEGVGQAIRE----SGIPREELFITSKVWNSDQGYETTLQA 94
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 95 FETTLEKLGLEYLDLYLVHWPVK------------------EKYT--ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFE 154
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAfdmdtdgdprddnqiqslSKKPleDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 155 IAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQGQ------LLDHPTLQEIATKYSKSTAQVILRWDLQ--- 225
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYgdgnltFLNDSELKALATKYNTTPPQVIIAWHLQkwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 446977558 226 NEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQAL 262
Cdd:cd19128 241 KNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
32-263 |
1.18e-64 |
|
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: 204.08 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 32 SEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESGIPREELFITSKVWNSDQGY------ETTLQAFETTLEKL 102
Cdd:pfam00248 18 EEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWpsggskENIRKSLEESLKRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 103 GLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHP--RLAQEELHAF 179
Cdd:pfam00248 98 GTDYIDLYYLHWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNLlrRRQEEELLEY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 180 CKEHNIQLEAWSPLMQG---------------------------QLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVT-- 230
Cdd:pfam00248 178 CKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkgtplNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTip 257
|
250 260 270
....*....|....*....|....*....|...
gi 446977558 231 IPKSIKEHRIIENANIFDFELSSDDMKAIQALN 263
Cdd:pfam00248 258 IPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
15-259 |
4.10e-58 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 186.24 E-value: 4.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVFKV--------EDGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIREsgIPREELFITSKVWN 83
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 84 SDQGYETTLQAFETTLEKLGLEYLDLYLVHWPVKE-KYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMV 162
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNiPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 163 NQVEYH---PRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLQEIATKYSKSTAQVILRWDLQNE-VVTIPKSIKEH 238
Cdd:cd19137 159 NQVKYNledRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPnVVAIPKAGRVE 238
|
250 260
....*....|....*....|.
gi 446977558 239 RIIENANIFDFELSSDDMKAI 259
Cdd:cd19137 239 HLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
27-259 |
7.26e-49 |
|
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: 163.47 E-value: 7.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 27 KVEDgSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESgipREELFITSKV---WNSDQGY------ETTLQA 94
Cdd:cd19084 21 EVDD-QESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKCglrWDGGKGVtkdlspESIRKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 95 FETTLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIkpMVNQVEYHP--RL 171
Cdd:cd19084 97 VEQSLRRLQTDYIDLYQIHWPdPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMleRE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 172 AQEELHAFCKEHNIQLEAWSPLMQGQL----------------LDHP---------------TLQEIATKYSKSTAQVIL 220
Cdd:cd19084 175 IEEELLPYCRENGIGVLPYGPLAQGLLtgkykkeptfppddrrSRFPffrgenfeknleivdKLKEIAEKYGKSLAQLAI 254
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446977558 221 RWDLQNEVVTI----PKSIKEhrIIENANIFDFELSSDDMKAI 259
Cdd:cd19084 255 AWTLAQPGVTSaivgAKNPEQ--LEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
30-259 |
3.75e-48 |
|
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: 161.60 E-value: 3.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 30 DGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIREsgiPREELFITSKVWNSDQGYETTLQAFETTLEKLGLEY 106
Cdd:cd19085 21 DDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNLTPEDVRKSCERSLKRLGTDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 107 LDLYLVHWPV-KEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKpmVNQVEYHP--RLAQEELHAFCKEH 183
Cdd:cd19085 98 IDLYQIHWPSsDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQLPYNLlwRAIEYEILPFCREH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 184 NIQLEAWSPLMQGqLL-------------DHPT--------------------LQEIATKYSKSTAQVILRWDLQNEVVT 230
Cdd:cd19085 176 GIGVLAYSPLAQG-LLtgkfssaedfppgDARTrlfrhfepgaeeetfealekLKEIADELGVTMAQLALAWVLQQPGVT 254
|
250 260 270
....*....|....*....|....*....|.
gi 446977558 231 --IPKSIKEHRIIENANIFDFELSSDDMKAI 259
Cdd:cd19085 255 svIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
21-272 |
6.68e-47 |
|
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: 159.19 E-value: 6.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 21 FGLGVFKVEDgSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIResGIPREELFITSKV--------WNSDQGYE 89
Cdd:COG0667 23 FGGPWGGVDE-AEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVVIATKVgrrmgpgpNGRGLSRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 90 TTLQAFETTLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMV--NQVE 166
Cdd:COG0667 100 HIRRAVEASLRRLGTDYIDLYQLHRPdPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIvaVQNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 167 YHP--RLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPT------------------------------LQEIATKYSKS 214
Cdd:COG0667 180 YSLldRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRrgatfpegdraatnfvqgylternlalvdaLRAIAAEHGVT 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446977558 215 TAQVILRWDLQNEVVTIPksI----KEHRIIENANIFDFELSSDDMKAIQALnenHRVGPDP 272
Cdd:COG0667 260 PAQLALAWLLAQPGVTSV--IpgarSPEQLEENLAAADLELSAEDLAALDAA---LAAVPAP 316
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
33-259 |
3.24e-45 |
|
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: 153.92 E-value: 3.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 33 EVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESGiPREELFITSKVWN--SDQGYETTLQAFETTLEKLGLEYL 107
Cdd:cd19093 27 DLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKFAPlpWRLTRRSVVKALKASLERLGLDSI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 108 DLYLVHWPVK--EKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDV---FEIAEIKPMVNQVEY---HPRLAQEELHAF 179
Cdd:cd19093 106 DLYQLHWPGPwySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAhkaLKERGVPLASNQVEYsllYRDPEQNGLLPA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 180 CKEHNIQLEAWSPLMQGQL-----LDHP----------------------TLQEIATKYSKSTAQVILRWDLQNEVVTIP 232
Cdd:cd19093 186 CDELGITLIAYSPLAQGLLtgkysPENPppggrrrlfgrknlekvqplldALEEIAEKYGKTPAQVALNWLIAKGVVPIP 265
|
250 260
....*....|....*....|....*....
gi 446977558 233 --KSIKehRIIENANIFDFELSSDDMKAI 259
Cdd:cd19093 266 gaKNAE--QAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
30-232 |
4.53e-42 |
|
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: 144.20 E-value: 4.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 30 DGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESGIpREELFITSKVWNSDQGY--------ETTLQAFETT 98
Cdd:cd06660 15 DEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDpsrsrlspEHIRRDLEES 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 99 LEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE----IKPMVNQVEY---HPR 170
Cdd:cd06660 94 LRRLGTDYIDLYYLHRDdPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPGFAAVQPQYsllDRS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446977558 171 LAQEELHAFCKEHNIQLEAWSPLMQGqlldhptlqeiatkysksTAQVILRWDLQNEVVTIP 232
Cdd:cd06660 174 PMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPFVTVP 217
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-262 |
1.31e-36 |
|
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: 132.03 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 20 WFGLGVfkvEDGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESgipREELFITSK---VWNSD----QGY- 88
Cdd:cd19102 17 GGGWGP---QDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWDEEgrirRSLk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 89 -ETTLQAFETTLEKLGLEYLDLYLVHWPV-KEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKpmVNQVE 166
Cdd:cd19102 91 pASIRAECEASLRRLGVDVIDLYQIHWPDpDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIA--SLQPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 167 Y---HPRLAQEELhAFCKEHNIQLEAWSPlMQGQLL---------------DHP-------------------TLQEIAT 209
Cdd:cd19102 169 YsllRRGIEAEIL-PFCAEHGIGVIVYSP-MQSGLLtgkmtpervaslpadDWRrrspffqepnlarnlalvdALRPIAE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446977558 210 KYSKSTAQVILRWDLQNEVVT--IPKSIKEHRIIENANIFDFELSSDDMKAIQAL 262
Cdd:cd19102 247 RHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-259 |
1.99e-36 |
|
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: 131.55 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 8 DYTTL-HNGVKMPWFGLG------------VFKVEDGSEVIdsvKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESgIP 71
Cdd:cd19079 1 EYVRLgNSGLKVSRLCLGcmsfgdpkwrpwVLDEEESRPII---KRALDLGINFFDTANVYSGgasEEILGRALKEF-AP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 72 REELFITSKVWN-SDQGY-------ETTLQAFETTLEKLGLEYLDLYLVHW-----PVKEkyteSWKALEKLYKDGRVRA 138
Cdd:cd19079 77 RDEVVIATKVYFpMGDGPngrglsrKHIMAEVDASLKRLGTDYIDLYQIHRwdyetPIEE----TLEALHDVVKSGKVRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 139 IGVSNFHIHHLQDVFEIAEIK---PMVNQVEYHPRLAQEELHA---FCKEHNIQLEAWSPLMQGQL-------------- 198
Cdd:cd19079 153 IGASSMYAWQFAKALHLAEKNgwtKFVSMQNHYNLLYREEEREmipLCEEEGIGVIPWSPLARGRLarpwgdtterrrst 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 199 -------------LDHPTL---QEIATKYSKSTAQVILRWDLQNEVVTIPksI----KEHRIIENANIFDFELSSDDMKA 258
Cdd:cd19079 233 tdtaklkydyfteADKEIVdrvEEVAKERGVSMAQVALAWLLSKPGVTAP--IvgatKLEHLEDAVAALDIKLSEEEIKY 310
|
.
gi 446977558 259 I 259
Cdd:cd19079 311 L 311
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
30-259 |
8.06e-32 |
|
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: 119.68 E-value: 8.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 30 DGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESgipREELFITSK---VWNSDQGY--------------- 88
Cdd:cd19149 31 DDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcglRWDREGGSfffvrdgvtvyknls 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 89 -ETTLQAFETTLEKLGLEYLDLYLVHWPVKE-KYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKpmVNQVE 166
Cdd:cd19149 108 pESIREEVEQSLKRLGTDYIDLYQTHWQDVEtPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLD--IIQEK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 167 YH--PRLAQEELHAFCKEHNIQLEAWSPLMQGQL--------------------LDHPT-----------LQEIATKYSK 213
Cdd:cd19149 186 YSmlDRGIEKELLPYCKKNNIAFQAYSPLEQGLLtgkitpdrefdagdarsgipWFSPEnrekvlallekWKPLCEKYGC 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446977558 214 STAQVILRWDLQ--NEVVTIPKSIKEHRIIENANIFDFELSSDDMKAI 259
Cdd:cd19149 266 TLAQLVIAWTLAqpGITSALCGARKPEQAEENAKAGDIRLSAEDIATM 313
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-272 |
3.70e-31 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 118.77 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 9 YTTL-HNGVKMPWFGLGV--FKVEDGSEVIDSVKAAIKNGYRSIDTAAIY-QNEEGVGQAIREsgiPREELFITSK--VW 82
Cdd:COG1453 3 YRRLgKTGLEVSVLGFGGmrLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKG---PRDKVILATKlpPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 83 NSDqgYETTLQAFETTLEKLGLEYLDLYLVHWPVKEKYTES-------WKALEKLYKDGRVRAIGVSNfhiHHLQDVF-E 154
Cdd:COG1453 80 VRD--PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKvlkpggaLEALEKAKAEGKIRHIGFST---HGSLEVIkE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 155 IAEIKPM-VNQVEYHPRL----AQEELHAFCKEHNIQLEAWSPLMQGQLLDHP-TLQEIATKySKSTAQVILRWDLQNEV 228
Cdd:COG1453 155 AIDTGDFdFVQLQYNYLDqdnqAGEEALEAAAEKGIGVIIMKPLKGGRLANPPeKLVELLCP-PLSPAEWALRFLLSHPE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446977558 229 VTIP----KSIKEhrIIENANIFD-FE-LSSDDMKAIQAL-NENHRVGPDP 272
Cdd:COG1453 234 VTTVlsgmSTPEQ--LDENLKTADnLEpLTEEELAILERLaEELGELLKDF 282
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
29-255 |
5.83e-31 |
|
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: 116.50 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 29 EDGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESGIPREELFITSK---------VWNSDQGYETT----L 92
Cdd:cd19092 21 ESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgirlgddpRPGRIKHYDTSkehiL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 93 QAFETTLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEYHPrL 171
Cdd:cd19092 101 ASVEGSLKRLGTDYLDLLLLHRPdPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIELSL-L 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 172 AQEELHA----FCKEHNIQLEAWSPLMQGQLLD---------HPTLQEIATKYSKSTAQVILRWDLQN--EVVTIPKSIK 236
Cdd:cd19092 180 HTEAIDDgtldYCQLLDITPMAWSPLGGGRLFGgfderfqrlRAALEELAEEYGVTIEAIALAWLLRHpaRIQPILGTTN 259
|
250
....*....|....*....
gi 446977558 237 EHRIIENANIFDFELSSDD 255
Cdd:cd19092 260 PERIRSAVKALDIELTREE 278
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
30-262 |
8.81e-31 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 116.75 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 30 DGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESGipREELFITSKVWNSDQGYETTL--------QAFETT 98
Cdd:cd19083 31 DEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEYN--RNEVVIATKGAHKFGGDGSVLnnspeflrSAVEKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 99 LEKLGLEYLDLYLVHWPVKEKYT-ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKpmVNQVEYH--PRLAQEE 175
Cdd:cd19083 109 LKRLNTDYIDLYYIHFPDGETPKaEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVD--VLQGEYNllQREAEED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 176 LHAFCKEHNIQLEAWSPLMQGQL---------------------LDHPT----------LQEIATKYSKSTAQVILRWDL 224
Cdd:cd19083 187 ILPYCVENNISFIPYFPLASGLLagkytkdtkfpdndlrndkplFKGERfsenldkvdkLKSIADEKGVTVAHLALAWYL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446977558 225 QNEVVT--IPKSIKEHRIIENANIFDFELSSDDMKAIQAL 262
Cdd:cd19083 267 TRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
30-262 |
2.66e-30 |
|
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: 115.10 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 30 DGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESGiPREELFITSKV---WNSDQGY------ETTLQAFET 97
Cdd:cd19148 23 DEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGEVvrnsspARIRKEVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 98 TLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLqDVFE----IAEIKPMVNQVEyhpRLA 172
Cdd:cd19148 102 SLRRLQTDYIDLYQVHWPdPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQM-ETFRkvapLHTVQPPYNLFE---REI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 173 QEELHAFCKEHNIQLEAWSPLMQGQLLDHPT-------------------------------LQEIA-TKYSKSTAQVIL 220
Cdd:cd19148 178 EKDVLPYARKHNIVTLAYGALCRGLLSGKMTkdtkfegddlrrtdpkfqeprfsqylaaveeLDKLAqERYGKSVIHLAV 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446977558 221 RWDLQNEVVTIP--KSIKEHRIIENANIFDFELSSDDMKAIQAL 262
Cdd:cd19148 258 RWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-245 |
7.75e-28 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 107.18 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 19 PWFGlgvfKVEDGsEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIREsgiPREELFITSKVWNSDQGY------- 88
Cdd:cd19086 16 DWWG----DVDDA-EAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFGNRFDGGperpqdf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 89 --ETTLQAFETTLEKLGLEYLDLYLVH-WPVKEKYT-ESWKALEKLYKDGRVRAIGVSnfhIHHLQDVFEIAEI-KPMVN 163
Cdd:cd19086 88 spEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNdELFEALEKLKQEGKIRAYGVS---VGDPEEALAALRRgGIDVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 164 QVEYHP--RLAQEELHAFCKEHNIQLEAWSPLMQGQLldhptlqeiatkySKSTAQVILRWDLQNEVVT--IP--KSIKE 237
Cdd:cd19086 165 QVIYNLldQRPEEELFPLAEEHGVGVIARVPLASGLL-------------TGKLAQAALRFILSHPAVStvIPgaRSPEQ 231
|
....*...
gi 446977558 238 hrIIENAN 245
Cdd:cd19086 232 --VEENAA 237
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-259 |
1.60e-27 |
|
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: 107.69 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 14 NGVKMPWFGLGV------FKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQ---NEEGVGQAIREsgiPREELFITSK---V 81
Cdd:cd19076 8 QGLEVSALGLGCmgmsafYGPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVIATKfgiV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 82 WNSDQGY-------ETTLQAFETTLEKLGLEYLDLYLVH-----WPVKEkyteSWKALEKLYKDGRVRAIGVSNF---HI 146
Cdd:cd19076 85 RDPGSGFrgvdgrpEYVRAACEASLKRLGTDVIDLYYQHrvdpnVPIEE----TVGAMAELVEEGKVRYIGLSEAsadTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 147 HHLQDVFEIAEIkpmvnQVEYHP--RLAQEELHAFCKEHNIQLEAWSPL--------------------------MQGQL 198
Cdd:cd19076 161 RRAHAVHPITAV-----QSEYSLwtRDIEDEVLPTCRELGIGFVAYSPLgrgfltgaikspedlpeddfrrnnprFQGEN 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446977558 199 LDH-----PTLQEIATKYSKSTAQVILRWDLQ--NEVVTIPKSIKEHRIIENANIFDFELSSDDMKAI 259
Cdd:cd19076 236 FDKnlklvEKLEAIAAEKGCTPAQLALAWVLAqgDDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
15-262 |
3.38e-27 |
|
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: 107.31 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFG-LGVFKVEDGSEVidsVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESgipREELFITSKVW-------- 82
Cdd:cd19091 24 GGGGGFFGaWGGVDQEEADRL---VDIALDAGINFFDTADVYsegESEEILGKALKGR---RDDVLIATKVRgrmgegpn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 83 NSDQGYETTLQAFETTLEKLGLEYLDLYLVHW-----PVKekytESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE 157
Cdd:cd19091 98 DVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGfdaltPLE----ETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 158 ----IKPMVNQVEYHP--RLAQEELHAFCKEHNIQLEAWSPLMQGQL--------------------LDHP--------- 202
Cdd:cd19091 174 rrglARFVALQAYYSLlgRDLEHELMPLALDQGVGLLVWSPLAGGLLsgkyrrgqpapegsrlrrtgFDFPpvdrergyd 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446977558 203 ---TLQEIATKYSKSTAQVILRWDLQNEVVTipkSI-----KEHRIIENANIFDFELSSDDMKAIQAL 262
Cdd:cd19091 254 vvdALREIAKETGATPAQVALAWLLSRPTVS---SViigarNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-230 |
1.50e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 103.82 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 9 YTTLHN-GVKMPWFGLGVfkVEDGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIResGIPREELFITSKVWNS 84
Cdd:cd19105 3 YRTLGKtGLKVSRLGFGG--GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGY--ETTLQAFETTLEKLGLEYLDLYLVH---WPVKEKYTESW-KALEKLYKDGRVRAIGVSNfhiHH-LQDVF-EIA 156
Cdd:cd19105 79 LDKKdkAELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELlEALEKLKKEGKVRFIGFST---HDnMAEVLqAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 157 EIKPM-VNQVEYHPRLAQEEL-HAF--CKEHNIQLEAwsplM--QGQLLDHPTLQEIATKYSKSTAQVILRWDLQNEVVT 230
Cdd:cd19105 156 ESGWFdVIMVAYNFLNQPAELeEALaaAAEKGIGVVA----MktLAGGYLQPALLSVLKAKGFSLPQAALKWVLSNPRVD 231
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
18-252 |
6.98e-26 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 102.30 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 18 MPWFGLGVFKV-EDGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESGiprEELFITSKV---------WNS 84
Cdd:cd19088 9 MRLTGPGIWGPpADREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvrtgpgwWGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGYETTLQAFETTLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVN 163
Cdd:cd19088 86 DGSPEYLRQAVEASLRRLGLDRIDLYQLHRIdPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIVSVQN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 164 QveYHPRLAQ-EELHAFCKEHNIQLEAWSPLMQGQLLDH-PTLQEIATKYSKSTAQVILRWDLQ--NEVVTIPKSIKEHR 239
Cdd:cd19088 166 R--YNLANRDdEGVLDYCEAAGIAFIPWFPLGGGDLAQPgGLLAEVAARLGATPAQVALAWLLArsPVMLPIPGTSSVEH 243
|
250
....*....|...
gi 446977558 240 IIENANIFDFELS 252
Cdd:cd19088 244 LEENLAAAGLRLS 256
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
19-254 |
9.08e-26 |
|
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: 103.06 E-value: 9.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 19 PWFGLGVfkveDGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIResGIPREELFITSKV-WN-SDQGYETTL- 92
Cdd:cd19074 13 LTFGGQV----DDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALK--GWPRESYVISTKVfWPtGPGPNDRGLs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 93 -----QAFETTLEKLGLEYLDLYLVHwpvkeKY------TESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE---- 157
Cdd:cd19074 87 rkhifESIHASLKRLQLDYVDIYYCH-----RYdpetplEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARqfgl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 158 IKPMVNQVEYH--PRLAQEELHAFCKEHNIQLEAWSPLMQG-------------------------QLLDHPT------- 203
Cdd:cd19074 162 IPPVVEQPQYNmlWREIEEEVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdKKRRLLTdenlekv 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446977558 204 --LQEIATKYSKSTAQVILRWDLQNEVVT--IPKSIKEHRIIENANIFDFELSSD 254
Cdd:cd19074 242 kkLKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-261 |
3.44e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 101.52 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 27 KVEDGSEVIDSVKAAIKNGYRSIDTAAIYQN-EEGVGQAIRESG----------------IPREELFITskvwnsdqgYE 89
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRrerdaaddvqihtkwvPDPGELTMT---------RA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 90 TTLQAFETTLEKLGLEYLDLYLVHW--PVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEiAEIKPMVNQVEY 167
Cdd:cd19101 89 YVEAAIDRSLKRLGVDRLDLVQFHWwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILD-AGVPIVSNQVQY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 168 H--PRLAQEELHAFCKEHNIQLEAWSPLMQGQL----LDHP---------------------------------TLQEIA 208
Cdd:cd19101 168 SllDRRPENGMAALCEDHGIKLLAYGTLAGGLLsekyLGVPeptgpaletrslqkyklmidewggwdlfqellrTLKAIA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446977558 209 TKYSKSTAQVILRWDLQNEVVtiPKSI-----KEHrIIENANIFDFELSSDDMKAIQA 261
Cdd:cd19101 248 DKHGVSIANVAVRWVLDQPGV--AGVIvgarnSEH-IDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
29-259 |
7.30e-25 |
|
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: 100.75 E-value: 7.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 29 EDGS-EVIDSVKAAiknGYRSIDTAAIY----------QNEEGVGQAIRESGiPREELFITSKV--WNSDQGY----ETT 91
Cdd:cd19081 25 EETSfALLDAFVDA---GGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgfPMGPNGPglsrKHI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 92 LQAFETTLEKLGLEYLDLYLVHWPVKE-KYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE----IKPMVNQVE 166
Cdd:cd19081 101 RRAVEASLRRLQTDYIDLYQAHWDDPAtPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 167 Y---HPRLAQEELHAFCKEHNIQLEAWSPLMQG-------------------------------QLLDhpTLQEIATKYS 212
Cdd:cd19081 181 YnlvDRESFEGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakrylnerglRILD--ALDEVAAEHG 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446977558 213 KSTAQVILRWDLQNEVVTIP----KSIKEHRiiENANIFDFELSSDDMKAI 259
Cdd:cd19081 259 ATPAQVALAWLLARPGVTAPiagaRTVEQLE--DLLAAAGLRLTDEEVARL 307
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
33-230 |
1.72e-24 |
|
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: 98.79 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 33 EVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIREsgIPREELFITSKV-WNSDQGYETTLQAFETTLEKLGLEYLD 108
Cdd:cd19096 22 KAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKE--GPREKFYLATKLpPWSVKSAEDFRRILEESLKRLGVDYID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 109 LYLVHWPVKEKYTES------WKALEKLYKDGRVRAIGVSnFHihhlqDVFEiaEIKPMVN-------QVEYH----PRL 171
Cdd:cd19096 100 FYLLHGLNSPEWLEKarkgglLEFLEKAKKEGLIRHIGFS-FH-----DSPE--LLKEILDsydfdfvQLQYNyldqENQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 172 AQEELHAFCKEHNIQLEAWSPLMQGQLLDHPT-LQEIATKYSKSTAQVILRWDLQNEVVT 230
Cdd:cd19096 172 AGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPeALAILCGAPLSPAEWALRFLLSHPEVT 231
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-230 |
2.03e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 97.94 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 21 FGLGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQN-EEGVGQAIREsgiPREELFITSKVWNSDqgYETTLQAFETTL 99
Cdd:cd19100 16 FGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARD--YEGAKRDLERSL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 100 EKLGLEYLDLYLVH-------WPVKEKYTESWKALEKLYKDGRVRAIGVSNfhiHHLQ------DVFEIAEIKPMVNQVE 166
Cdd:cd19100 91 KRLGTDYIDLYQLHavdteedLDQVFGPGGALEALLEAKEEGKIRFIGISG---HSPEvllralETGEFDVVLFPINPAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446977558 167 YHPRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPTLqeiatkysksTAQVILRWDLQNEVVT 230
Cdd:cd19100 168 DHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPL----------DPEQALRYALSLPPVD 221
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-244 |
5.91e-24 |
|
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: 97.31 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVFKVEDGSEVIDsvkAAIKNGYRSIDTAAIYQN-EEGVGQAIreSGIPREELFITSKVWNSDQG------ 87
Cdd:cd19095 6 GTSGIGRVWGVPSEAEAARLLN---TALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGTHGEGgrdrkd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 88 --YETTLQAFETTLEKLGLEYLDLYLVHWPVKEKYT-ESWKALEKLYKDGRVRAIGVSNFH---IHHLQ-DVFEiaeikp 160
Cdd:cd19095 81 fsPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTgEVLETLEDLKAAGKVRYIGVSGDGeelEAAIAsGVFD------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 161 mVNQVEYHPrLAQEELHAF--CKEHNIQLEAWSPLMQGQLL----------DHPTLQEIATKY-SKSTAQVILRWDLQNE 227
Cdd:cd19095 155 -VVQLPYNV-LDREEEELLplAAEAGLGVIVNRPLANGRLRrrvrrrplyaDYARRPEFAAEIgGATWAQAALRFVLSHP 232
|
250
....*....|....*....
gi 446977558 228 VVT--IPKSIKEHRIIENA 244
Cdd:cd19095 233 GVSsaIVGTTNPEHLEENL 251
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
8-198 |
1.07e-22 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 94.95 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 8 DYTTL-HNGVKMP--WFGLGVFKVE-DGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESgipREELFITSK 80
Cdd:cd19087 2 EYRTLgRTGLKVSrlCLGTMNFGGRtDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 81 V------WNSDQGYET--TLQAFETTLEKLGLEYLDLYLVH-WPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQD 151
Cdd:cd19087 79 VfgpmgdDPNDRGLSRrhIRRAVEASLRRLQTDYIDLYQMHhFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446977558 152 VFEIAE---------IKPMVNQVEyhpRLAQEELHAFCKEHNIQLEAWSPLMQGQL 198
Cdd:cd19087 159 AQGIAArrgllrfvsEQPMYNLLK---RQAELEILPAARAYGLGVIPYSPLAGGLL 211
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-227 |
5.27e-22 |
|
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: 92.61 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 9 YTTL-HNGVKMPWFGLG------VFKVEDGSEVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIResGIPREELFIT 78
Cdd:cd19163 3 YRKLgKTGLKVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 79 SKV------WNS--DQGYETTLQAFETTLEKLGLEYLDLYLVHWPVKEKY-----TESWKALEKLYKDGRVRAIGVSNFH 145
Cdd:cd19163 81 TKVgrygldPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSldqilNETLPALQKLKEEGKVRFIGITGYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 146 IHHLQDVFEIAEIKpmVNQVEYHPRLAQ-----EELHAFCKEHNIQLEAWSPLMQGQLLD------HPTLQEI------A 208
Cdd:cd19163 161 LDVLKEVLERSPVK--IDTVLSYCHYTLndtslLELLPFFKEKGVGVINASPLSMGLLTErgppdwHPASPEIkeacakA 238
|
250 260
....*....|....*....|...
gi 446977558 209 TKYSKS----TAQVILRWDLQNE 227
Cdd:cd19163 239 AAYCKSrgvdISKLALQFALSNP 261
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
20-222 |
1.67e-21 |
|
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: 91.08 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 20 WFGlGVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQN-EEGVGQAIREsgIPREELFITSKV-----WNSDQGYETTLQ 93
Cdd:cd19090 9 GLG-GVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE--LPREPLVLSTKVgrlpeDTADYSADRVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 94 AFETTLEKLGLEYLDLYLVH---WPVKEKYT---ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMVNQVEY 167
Cdd:cd19090 86 SVEESLERLGRDRIDLLMIHdpeRVPWVDILapgGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGDFDVVLTANRY 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446977558 168 HP--RLAQEELHAFCKEHNIQLEAWSPLMQGqLLDHPTLQEIATKYSKSTAQVILRW 222
Cdd:cd19090 166 TLldQSAADELLPAAARHGVGVINASPLGMG-LLAGRPPERVRYTYRWLSPELLDRA 221
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-222 |
2.31e-21 |
|
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: 91.08 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 18 MPWFGLGVF-KVEDGSEVIDSVKAAiknGYRSIDTAAIYQN---EEGVGQAiresGIPREELFITSKVwNSDQG----YE 89
Cdd:cd19075 8 MTFGSQGRFtTAEAAAELLDAFLER---GHTEIDTARVYPDgtsEELLGEL----GLGERGFKIDTKA-NPGVGgglsPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 90 TTLQAFETTLEKLGLEYLDLYLVHWPvkEKYT---ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE----IKPMV 162
Cdd:cd19075 80 NVRKQLETSLKRLKVDKVDVFYLHAP--DRSTpleETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 163 NQVEYHP--RLAQEELHAFCKEHNIQLEAWSPL-------------------------MQGQLL----DHPT-------L 204
Cdd:cd19075 158 YQGMYNAitRQVETELFPCLRKLGIRFYAYSPLaggfltgkykysedkagggrfdpnnALGKLYrdryWKPSyfealekV 237
|
250
....*....|....*...
gi 446977558 205 QEIATKYSKSTAQVILRW 222
Cdd:cd19075 238 EEAAEKEGISLAEAALRW 255
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-222 |
6.30e-21 |
|
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: 90.07 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 29 EDGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRES----GIPREELFITSKV---------------W---- 82
Cdd:cd19099 18 ETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELiekgGIKRDEVVIVTKAgyipgdgdeplrplkYleek 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 83 ----NSDQGYETTL----------QAFETTLEKLGLEYLDLYLVHWP-----------VKEKYTESWKALEKLYKDGRVR 137
Cdd:cd19099 98 lgrgLIDVADSAGLrhcispayleDQIERSLKRLGLDTIDLYLLHNPeeqllelgeeeFYDRLEEAFEALEEAVAEGKIR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 138 AIGVS----------NFHIHHLQDVFEIAEIKPMVN------QVEYHPRLAQ------------EELHAFCKEHNIQLEA 189
Cdd:cd19099 178 YYGIStwdgfrappaLPGHLSLEKLVAAAEEVGGDNhhfkviQLPLNLLEPEaltekntvkgeaLSLLEAAKELGLGVIA 257
|
250 260 270
....*....|....*....|....*....|....
gi 446977558 190 WSPLMQGQLLDHPTLQEI-ATKYSKSTAQVILRW 222
Cdd:cd19099 258 SRPLNQGQLLGELRLADLlALPGGATLAQRALQF 291
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-227 |
2.08e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 87.97 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 21 FGL--GVF----KVEDgSEVIDSVKAAIKNGYRSIDTAAIYQN-EEGVGQAIRESgiprEELFITSKV----WNSDQGYE 89
Cdd:cd19097 10 FGLdyGIAnksgKPSE-KEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL----DKFKIITKLpplkEDKKEDEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 90 TTLQAFETTLEKLGLEYLDLYLVHWP--VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKpMVnQVEY 167
Cdd:cd19097 85 AIEASVEASLKRLKVDSLDGLLLHNPddLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKID-II-QLPF 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446977558 168 HP---RLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHPT---------------LQEIATKYSKSTAQVILRWDLQNE 227
Cdd:cd19097 163 NIldqRFLKSGLLAKLKKKGIEIHARSVFLQGLLLMEPDklpakfapakpllkkLHELAKKLGLSPLELALGFVLSLP 240
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
49-259 |
5.19e-20 |
|
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: 87.27 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 49 IDTAAIYQN---EEGVGQAIRESgipREELFITSK-VWNSDQGYETT--------LQAFETTLEKLGLEYLDLYLVHW-- 114
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAGN---RDRIVLATKyTMNRRPGDPNAggnhrknlRRSVEASLRRLQTDYIDLLYVHAwd 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 115 ---PVKekytESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIK---PMVN-QVEYH--PRLAQEELHAFCKEHNI 185
Cdd:cd19080 125 fttPVE----EVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRgwsPFVAlQIEYSllERTPERELLPMARALGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 186 QLEAWSPLMQGQL-------------------LDHP-----------TLQEIATKYSKSTAQVILRWDLQNEVVTIPksI 235
Cdd:cd19080 201 GVTPWSPLGGGLLtgkyqrgeegrageakgvtVGFGklternwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIP--I 278
|
250 260
....*....|....*....|....*...
gi 446977558 236 KEHRIIE--NANI--FDFELSSDDMKAI 259
Cdd:cd19080 279 IGARTLEqlKDNLgaLDLTLSPEQLARL 306
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
29-232 |
1.19e-19 |
|
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: 86.07 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 29 EDGSEVIDsvkAAIKNGYRSIDTAAIYQNEEG-------VGQAIRESGIpREELFITSK--------VWNSDQGYETTLQ 93
Cdd:cd19082 17 EEAFALLD---AFVELGGNFIDTARVYGDWVErgaservIGEWLKSRGN-RDKVVIATKgghpdledMSRSRLSPEDIRA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 94 AFETTLEKLGLEYLDLYLVHW-----PVKEKYTeswkALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIK----PMVNQ 164
Cdd:cd19082 93 DLEESLERLGTDYIDLYFLHRddpsvPVGEIVD----TLNELVRAGKIRAFGASNWSTERIAEANAYAKAHglpgFAASS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 165 VEY------HPRLA-------QEELHAFCKEHNIQLEAWSPLMQG-----------------QLLDHPT-------LQEI 207
Cdd:cd19082 169 PQWslarpnEPPWPgptlvamDEEMRAWHEENQLPVFAYSSQARGffskraaggaeddselrRVYYSEEnferlerAKEL 248
|
250 260
....*....|....*....|....*
gi 446977558 208 ATKYSKSTAQVILRWDLQNEVVTIP 232
Cdd:cd19082 249 AEEKGVSPTQIALAYVLNQPFPTVP 273
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
40-268 |
3.50e-19 |
|
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: 85.57 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 40 AAIKNGYRSIDTAAIYQ-NEEGVGQAIRESGIPREELFITSKVWNSDQGY----------ETTLQAFETTLEKLGLEYLD 108
Cdd:cd19144 42 AAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFGIEKNVEtgeysvdgspEYVKKACETSLKRLGVDYID 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 109 LYLVH-----WPVkEKyteSWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPMvnQVEYHP-----RLAQEELHA 178
Cdd:cd19144 122 LYYQHrvdgkTPI-EK---TVAAMAELVQEGKIKHIGLSECSAETLRRAHAVHPIAAV--QIEYSPfsldiERPEIGVLD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 179 FCKEHNIQLEAWSPLMQG---------------------------------QLLDhpTLQEIATKYSKSTAQVILRWDL- 224
Cdd:cd19144 196 TCRELGVAIVAYSPLGRGfltgairspddfeegdfrrmaprfqaenfpknlELVD--KIKAIAKKKNVTAGQLTLAWLLa 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446977558 225 -QNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQALNENHRV 268
Cdd:cd19144 274 qGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEV 318
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-262 |
1.54e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 83.15 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 38 VKAAIKNGYRSIDTAAIYqneeGVGQAIRESG-----IPREELFITSKV--WNSDQGYETTLQAFETTLEKLGLEYLDLY 110
Cdd:cd19103 38 FDKAMAAGLNLWDTAAVY----GMGASEKILGeflkrYPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 111 LVHWPVK-EKYTESwkaLEKLYKDGRVRAIGVSNFHIHHLQDVFEI-AEIKPMVNQVEYHPRL---AQEE--LHAFCKEH 183
Cdd:cd19103 114 WIHNPADvERWTPE---LIPLLKSGKVKHVGVSNHNLAEIKRANEIlAKAGVSLSAVQNHYSLlyrSSEEagILDYCKEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 184 NIQLEAWSPLMQGQLLD-----HP-----------------------TLQEIATKYSKSTAQVILRWDLQNEVVTIPKSI 235
Cdd:cd19103 191 GITFFAYMVLEQGALSGkydtkHPlpegsgraetynpllpqleeltaVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVT 270
|
250 260
....*....|....*....|....*..
gi 446977558 236 KEHRIIENANIFDFELSSDDMKAIQAL 262
Cdd:cd19103 271 KPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
33-260 |
5.15e-18 |
|
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: 81.90 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 33 EVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIREsgiPREELFITSK-VWNSDQG----------YETTLQAFETT 98
Cdd:cd19078 26 EMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKfGFKIDGGkpgplgldsrPEHIRKAVEGS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 99 LEKLGLEYLDLYLVHW-----PVKEKYteswKALEKLYKDGRVRAIGVSNF---HIHHLQDVFEIAEIkpmvnQVEYH-- 168
Cdd:cd19078 103 LKRLQTDYIDLYYQHRvdpnvPIEEVA----GTMKELIKEGKIRHWGLSEAgveTIRRAHAVCPVTAV-----QSEYSmm 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 169 PRLAQEELHAFCKEHNIQLEAWSPLMQGQL---LDHPT----------------------------LQEIATKYSKSTAQ 217
Cdd:cd19078 174 WREPEKEVLPTLEELGIGFVPFSPLGKGFLtgkIDENTkfdegddraslprftpealeanqalvdlLKEFAEEKGATPAQ 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446977558 218 VILRWDLQNE--VVTIPKSIKEHRIIENANIFDFELSSDDMKAIQ 260
Cdd:cd19078 254 IALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-232 |
2.60e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 79.68 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 44 NGYRSIDTAAIY----------QNEEGVGQAIRESGIpREELFITSKV---------WNSD---QGYETTLQAFETTLEK 101
Cdd:cd19752 29 AGGNFLDTANNYafwteggvggESERLIGRWLKDRGN-RDDVVIATKVgagprdpdgGPESpegLSAETIEQEIDKSLRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 102 LGLEYLDLYLVHwpVKEKYT---ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE----------------IKPMV 162
Cdd:cd19752 108 LGTDYIDLYYAH--VDDRDTpleETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARqqgwaefsaiqqrhsyLRPRP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 163 NQVEYHPRLAQEELHAFCKEH-NIQLEAWSPLMQGQL----------LDHP-------TLQEIATKYSKSTAQVILRWDL 224
Cdd:cd19752 186 GADFGVQRIVTDELLDYASSRpDLTLLAYSPLLSGAYtrpdrplpeqYDGPdsdarlaVLEEVAGELGATPNQVVLAWLL 265
|
....*...
gi 446977558 225 QNEVVTIP 232
Cdd:cd19752 266 HRTPAIIP 273
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
29-262 |
5.51e-15 |
|
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: 73.75 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 29 EDGSEVIDsvkAAIKNGYRSIDTAAIY----------QNEEGVGQAIRESGiPREELFITSKV--------W----NSDQ 86
Cdd:cd19094 18 AEAHEQLD---YAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWprggGTRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 87 GYETTLQAFETTLEKLGLEYLDLYLVHWPvkEKYT---------------------ESWKALEKLYKDGRVRAIGVSN-- 143
Cdd:cd19094 94 DRENIREAVEGSLKRLGTDYIDLYQLHWP--DRYTplfgggyytepseeedsvsfeEQLEALGELVKAGKIRHIGLSNet 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 144 ------FHihhlqdvfEIAE---IKPMVN-QVEYH--PRLAQEELHAFCKEHNIQLEAWSPLMQGQL-------LDHPT- 203
Cdd:cd19094 172 pwgvmkFL--------ELAEqlgLPRIVSiQNPYSllNRNFEEGLAEACHRENVGLLAYSPLAGGVLtgkyldgAARPEg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 204 ------------------------LQEIATKYSKSTAQVILRWDLQNEVVTipkSIkehrII---------ENANIFDFE 250
Cdd:cd19094 244 grlnlfpgymaryrspqaleavaeYVKLARKHGLSPAQLALAWVRSRPFVT---ST----IIgattleqlkENIDAFDVP 316
|
330
....*....|..
gi 446977558 251 LSSDDMKAIQAL 262
Cdd:cd19094 317 LSDELLAEIDAV 328
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
33-259 |
9.50e-15 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 72.85 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 33 EVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIResGIPREELFITSKVWNSDQGYETTL---------QAFETTLE 100
Cdd:cd19145 34 EGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQLATKFGIHEIGGSGVEvrgdpayvrAACEASLK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 101 KLGLEYLDLYLVHW-----PVKEKYTEswkaLEKLYKDGRVRAIGVSNFH---IHHLQDVFEIAEIkpmvnQVEYH--PR 170
Cdd:cd19145 112 RLDVDYIDLYYQHRidttvPIEITMGE----LKKLVEEGKIKYIGLSEASadtIRRAHAVHPITAV-----QLEWSlwTR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 171 LAQEELHAFCKEHNIQLEAWSPLMQG---------QLLD-------HPTLQE---------------IATKYSKSTAQVI 219
Cdd:cd19145 183 DIEEEIIPTCRELGIGIVPYSPLGRGffagkakleELLEnsdvrksHPRFQGenleknkvlyerveaLAKKKGCTPAQLA 262
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446977558 220 LRWDLQ--NEVVTIPKSIKEHRIIENANIFDFELSSDDMKAI 259
Cdd:cd19145 263 LAWVLHqgEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
32-260 |
9.78e-15 |
|
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: 72.66 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 32 SEVIDSVKAAIKNGYRSIDTAAIY------QNEEGVGQAIRESGIPREELFITSKV-WNS-----DQGYETTLQAFETTL 99
Cdd:cd19077 25 EEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKGgLDPdtlrpDGSPEAVRKSIENIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 100 EKLG-LEYLDLYLV-----HWPVkekyTESWKALEKLYKDGRVRAIGVSNFHihhLQDVFEIAEIKPMV-NQVEYHPrLA 172
Cdd:cd19077 105 RALGgTKKIDIFEParvdpNVPI----EETIKALKELVKEGKIRGIGLSEVS---AETIRRAHAVHPIAaVEVEYSL-FS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 173 QEELH----AFCKEHNIQLEAWSPLMQG------------------QLLDHPT-------------LQEIATKYSKSTAQ 217
Cdd:cd19077 177 REIEEngvlETCAELGIPIIAYSPLGRGlltgriksladipegdfrRHLDRFNgenfeknlklvdaLQELAEKKGCTPAQ 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446977558 218 VILRWDL---QNEVVTIPKSIKEHRIIENANIFDFELSSDDMKAIQ 260
Cdd:cd19077 257 LALAWILaqsGPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
30-262 |
9.98e-15 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 72.63 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 30 DGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESGIPREELFITSKV-WNSDQGYETT--------LQAFET 97
Cdd:cd19143 29 DVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGGGGPPPNDrglsrkhiVEGTKA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 98 TLEKLGLEYLDLYLVHWPVKEkyT---ESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE----IKPMVNQVEY--- 167
Cdd:cd19143 109 SLKRLQLDYVDLVFCHRPDPA--TpieETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQYnlf 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 168 HPRLAQEELHAFCKEHNIQLEAWSPLMQGQL-------------LDHPT---------------------LQEIATKYSK 213
Cdd:cd19143 187 HRERVEVEYAPLYEKYGLGTTTWSPLASGLLtgkynngipegsrLALPGyewlkdrkeelgqekiekvrkLKPIAEELGC 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446977558 214 STAQVILRWDLQNEVV--TIPKSIKEHRIIENanifdfelssddMKAIQAL 262
Cdd:cd19143 267 SLAQLAIAWCLKNPNVstVITGATKVEQLEEN------------LKALEVL 305
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
30-161 |
8.44e-14 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 69.87 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 30 DGSEVIDS---VKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESGIPREELFITSKVWN-SDQGYETTL----QAFETT 98
Cdd:cd19153 28 DGLEQDEAvaiVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVGRyRDSEFDYSAervrASVATS 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446977558 99 LEKLGLEYLDLYLVHWPVKEKY----TESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEIKPM 161
Cdd:cd19153 108 LERLHTTYLDVVYLHDIEFVDYdtlvDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSL 174
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-245 |
2.48e-13 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 68.82 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGV---FKVEDGSEVIDS-VKAAIKNGYRSIDTAAIYQNEEG-----VGQAIRESGIP-REELFITSKVwns 84
Cdd:cd19089 8 GLHLPAISLGLwhnFGDYTSPEEARElLRTAFDLGITHFDLANNYGPPPGsaeenFGRILKRDLRPyRDELVISTKA--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 dqGYET-------------TLQAFETTLEKLGLEYLDLYLVHWPVKE-KYTESWKALEKLYKDGRVRAIGVSNF---HIH 147
Cdd:cd19089 85 --GYGMwpgpygdggsrkyLLASLDQSLKRMGLDYVDIFYHHRYDPDtPLEETMTALADAVRSGKALYVGISNYpgaKAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 148 HLQDVFEIAEIKPMVNQVEYH--PRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDHP----------------------- 202
Cdd:cd19089 163 RAIALLRELGVPLIIHQPRYSllDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYlngippdsrraaeskflteealt 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446977558 203 --------TLQEIATKYSKSTAQVILRWDLQNEVVT---IPKSIKEHrIIENAN 245
Cdd:cd19089 243 pekleqlrKLNKIAAKRGQSLAQLALSWVLRDPRVTsvlIGASSPSQ-LEDNVA 295
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
38-203 |
1.67e-12 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 66.23 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 38 VKAAIKNGYRSIDTAAIY---QNEEGVGQAIResGIPREELFITSKV------------------WnsDQGYETTLQAFE 96
Cdd:cd19162 25 LDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgaagrpagadrrF--DFSADGIRRSIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 97 TTLEKLGLEYLDLYLVHWP---VKEKYTESWKALEKLYKDGRVRAIGVS--------NFHIHHLQDVFEIAEIKPMVNQV 165
Cdd:cd19162 101 ASLERLGLDRLDLVFLHDPdrhLLQALTDAFPALEELRAEGVVGAIGVGvtdwaallRAARRADVDVVMVAGRYTLLDRR 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 446977558 166 eyhprlAQEELHAFCKEHNIQLEAWSPLMQGQLL-DHPT 203
Cdd:cd19162 181 ------AATELLPLCAAKGVAVVAAGVFNSGILAtDDPA 213
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
13-257 |
1.25e-11 |
|
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: 63.58 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 13 HNGVKMPWFGLGVFKVEDGSEVIDSVKAAIKN----GYRSIDTAAIY-----QNEEGVGQAIRESGIP-REELFITSK-- 80
Cdd:cd19151 7 RSGLKLPAISLGLWHNFGDVDRYENSRAMLRRafdlGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 81 --VWNS---DQGYETTLQA-FETTLEKLGLEYLDLYLVHWPVKEK-YTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVF 153
Cdd:cd19151 87 ytMWPGpygDWGSKKYLIAsLDQSLKRMGLDYVDIFYHHRPDPETpLEETMGALDQIVRQGKALYVGISNYPPEEAREAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 154 EIAE---IKPMVNQVEYH--PRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDH-----PT-------------------- 203
Cdd:cd19151 167 AILKdlgTPCLIHQPKYSmfNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRylngiPEdsraakgssflkpeqiteek 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446977558 204 ------LQEIATKYSKSTAQVILRWDLQNEVVT---IPKSiKEHRIIENANIFD-FELSSDDMK 257
Cdd:cd19151 247 lakvrrLNEIAQARGQKLAQMALAWVLRNKRVTsvlIGAS-KPSQIEDAVGALDnREFSEEELA 309
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-142 |
1.96e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 63.05 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 33 EVIDSVKAAIKNGYRSIDTAAIY---QNEEGVGQAIRESgipREELFITSKV----WNSDQGYETTLQAFETTLEKLGLE 105
Cdd:cd19104 33 EQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL---PAGPYITTKVrldpDDLGDIGGQIERSVEKSLKRLKRD 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446977558 106 YLDLYLVH--------WPVKEKYT--------ESWKALEKLYKDGRVRAIGVS 142
Cdd:cd19104 110 SVDLLQLHnrigderdKPVGGTLSttdvlglgGVADAFERLRSEGKIRFIGIT 162
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
24-254 |
4.67e-11 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 61.86 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 24 GVFKVEDGSEVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIREsgIPREELFITSKV------------------W 82
Cdd:cd19152 12 NLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE--LGREDYVISTKVgrllvplqeveptfepgfW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 83 NS-------DQGYETTLQAFETTLEKLGLEYLDLYLVHWPVKEKYTESWK------------ALEKLYKDGRVRAIGV-S 142
Cdd:cd19152 90 NPlpfdavfDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafrALEELREEGVIKAIGLgV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 143 NF-----HIHHLQ--DVFEIAEIKPMVNQVEYHPRLAQeelhafCKEHNIQLEAWSPLMQGQLLDHPT------------ 203
Cdd:cd19152 170 NDwevilRILEEAdlDWVMLAGRYTLLDHSAARELLPE------CEKRGVKVVNAGPFNSGFLAGGDNfdyyeygpappe 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 204 -------LQEIATKYSKSTAQVILRWDLQNEVVT--IPKSIKEHRIIENANIFDFELSSD 254
Cdd:cd19152 244 liarrdrIEALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
14-193 |
7.05e-11 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 61.71 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 14 NGVKMPWFGLG---VFKVEDGSEVIDS-VKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESGIPREELFITSKV-WN-- 83
Cdd:cd19142 9 SGLRVSNVGLGtwsTFSTAISEEQAEEiVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIyWSyg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 84 -SDQGY--ETTLQAFETTLEKLGLEYLDLYLVH-----WPVKEKYteswKALEKLYKDGRVRAIGVSNFHIHHLQDVFEI 155
Cdd:cd19142 89 sEERGLsrKHIIESVRASLRRLQLDYIDIVIIHkadpmCPMEEVV----RAMSYLIDNGLIMYWGTSRWSPVEIMEAFSI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446977558 156 AE----IKPMVNQVEYHPrlaqeelhaFCKEH------------NIQLEAWSPL 193
Cdd:cd19142 165 ARqfncPTPICEQSEYHM---------FCREKmelympelynkvGVGLITWSPL 209
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
13-198 |
8.37e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 61.41 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 13 HNGVKMPWFGLGVFKV-EDGSEViDS---VKAAIKNGYRSIDTAAIYQ----------NEEGVGQAIRESGiPREELFIT 78
Cdd:PRK10625 8 HSSLEVSTLGLGTMTFgEQNSEA-DAhaqLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 79 SKV----WNSDQGY--------ETTLQAFETTLEKLGLEYLDLYLVHWPVKE---------KYT---------ESWKALE 128
Cdd:PRK10625 86 SKVsgpsRNNDKGIrpnqaldrKNIREALHDSLKRLQTDYLDLYQVHWPQRPtncfgklgySWTdsapavsllETLDALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446977558 129 KLYKDGRVRAIGVSN------FHIHHLQDVFEIAEIKPMVNQVEYHPRLAQEELHAFCKEHNIQLEAWSPLMQGQL 198
Cdd:PRK10625 166 EQQRAGKIRYIGVSNetafgvMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTL 241
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
33-221 |
1.20e-10 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 60.80 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 33 EVIDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIREsgIPREELFITSKV-----------------W--------NS 84
Cdd:cd19161 21 DADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkparegsvpdpngFvdplpfeiVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGYETTLQAFETTLEKLGLEYLDLYLVH-----WPVKEKYTESW--------KALEKLYKDGRVRAI--GVSNFHIhhL 149
Cdd:cd19161 99 DYSYDGIMRSFEDSLQRLGLNRIDILYVHdigvyTHGDRKERHHFaqlmsggfKALEELKKAGVIKAFglGVNEVQI--C 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446977558 150 QDVFEIAEIKPMVNQVEYH--PRLAQEELHAFCKEHNIQLEAWSPLMQGqLLDHPTLQEIATKYSKSTAQVILR 221
Cdd:cd19161 177 LEALDEADLDCFLLAGRYSllDQSAEEEFLPRCEQRGTSLVIGGVFNSG-ILATGTKSGAKFNYGDAPAEIISR 249
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
14-196 |
1.15e-09 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 58.13 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 14 NGVKMPWFGLGVFkVEDGSEVIDSVKA-----AIKNGYRSIDTAAIY---QNEEGVGQAIRESGIPREELFITSKV-WNS 84
Cdd:cd19159 9 SGLRVSCLGLGTW-VTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGYETTL------QAFETTLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE 157
Cdd:cd19159 88 KAETERGLsrkhiiEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446977558 158 ----IKPMVNQVEYHpRLAQEELHAFCKE--HNIQLEA--WSPLMQG 196
Cdd:cd19159 168 qfnmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACG 213
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
14-196 |
3.36e-09 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 56.63 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 14 NGVKMPWFGLGVFkVEDGSEVIDSVKA-----AIKNGYRSIDTAAIY---QNEEGVGQAIRESGIPREELFITSKV-WNS 84
Cdd:cd19158 9 SGLRVSCLGLGTW-VTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGYETTL------QAFETTLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE 157
Cdd:cd19158 88 KAETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPdPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446977558 158 ----IKPMVNQVEYHpRLAQEELHAFCKE--HNIQLEA--WSPLMQG 196
Cdd:cd19158 168 qfnlIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACG 213
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
35-142 |
3.58e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 56.32 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 35 IDSVKAAIKNGYRSIDTAAIYQN---EEGVGQAIRESGIPREELFITSKVWNSDQGY----ETTLQAFETTLEKLGLEYL 107
Cdd:PLN02587 34 IASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCGRYGEGFdfsaERVTKSVDESLARLQLDYV 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 446977558 108 DLYLVH----WPVKEKYTESWKALEKLYKDGRVRAIGVS 142
Cdd:PLN02587 114 DILHCHdiefGSLDQIVNETIPALQKLKESGKVRFIGIT 152
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
14-259 |
8.24e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 52.68 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 14 NGVKMPWFGLGVFKVEDGSEVIDSVKAAIKN----GYRSIDTAAIY-----QNEEGVGQAIRESGIP-REELFITSK--- 80
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGHVNALESQRAILRKafdlGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 81 -VWNSDQGYETT----LQAFETTLEKLGLEYLDLYLVHwPVKEK--YTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVF 153
Cdd:PRK09912 101 dMWPGPYGSGGSrkylLASLDQSLKRMGLEYVDIFYSH-RVDENtpMEETASALAHAVQSGKALYVGISSYSPERTQKMV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 154 EIA---EIKPMVNQVEY---HPRLAQEELHAFCKEHNIQLEAWSPLMQGQLLDH-----PT------------------- 203
Cdd:PRK09912 180 ELLrewKIPLLIHQPSYnllNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKylngiPQdsrmhregnkvrgltpkml 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446977558 204 ----------LQEIATKYSKSTAQVILRWDLQNEVVT--IPKSIKEHRIIENANIF-DFELSSDDMKAI 259
Cdd:PRK09912 260 teanlnslrlLNEMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVQALnNLTFSTEELAQI 328
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
22-263 |
8.99e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 52.28 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 22 GLGVF---KVEDGSevIDSVKAAIKNGYRSIDTAAIY----QNeegvgQAIRESGIP-REELFITSKV---------WNS 84
Cdd:PRK10376 29 GPGVFgppKDRDAA--IAVLREAVALGVNHIDTSDFYgphvTN-----QLIREALHPyPDDLTIVTKVgarrgedgsWLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 85 DQGYETTLQAFETTLEKLGLEYLDL------YLVHWPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAEI 158
Cdd:PRK10376 102 AFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 159 KPMVNQveYHprLAQEELHAFCKEHNIQ---------LEAWSPLMQGqlldhpTLQEIATKYSKSTAQVILRWDLQN--E 227
Cdd:PRK10376 182 VCVQNH--YN--LAHRADDALIDALARDgiayvpffpLGGFTPLQSS------TLSDVAASLGATPMQVALAWLLQRspN 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 446977558 228 VVTIP--KSIKEHRiiENANIFDFELSSDDMKAIQALN 263
Cdd:PRK10376 252 ILLIPgtSSVAHLR--ENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
13-230 |
2.95e-07 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 50.53 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 13 HNGVKMPWFGLGVFKVEDGSEVIDSVKAAIKN----GYRSIDTAAIY-----QNEEGVGQAIRESGIP-REELFITSK-- 80
Cdd:cd19150 7 KSGLKLPALSLGLWHNFGDDTPLETQRAILRTafdlGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 81 --VWNSDQG----YETTLQAFETTLEKLGLEYLDLYLVH-WPVKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVF 153
Cdd:cd19150 87 ydMWPGPYGewgsRKYLLASLDQSLKRMGLDYVDIFYSHrFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 154 EI-AEIK-P-MVNQVEYH--PRLAQE-ELHAFCKEHNIQLEAWSPLMQGQL----------------------------- 198
Cdd:cd19150 167 AIlRELGtPlLIHQPSYNmlNRWVEEsGLLDTLQELGVGCIAFTPLAQGLLtdkylngipegsraskerslspkmltean 246
|
250 260 270
....*....|....*....|....*....|...
gi 446977558 199 LDH-PTLQEIATKYSKSTAQVILRWDLQNEVVT 230
Cdd:cd19150 247 LNSiRALNEIAQKRGQSLAQMALAWVLRDGRVT 279
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
15-198 |
3.29e-07 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 50.52 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 15 GVKMPWFGLGVFkVEDGSEVIDSV-----KAAIKNGYRSIDTAAIY---QNEEGVGQAIRESGIPREELFITSKV-W--- 82
Cdd:cd19141 9 GLRVSCLGLGTW-VTFGSQISDEVaeelvTLAYENGINLFDTAEVYaagKAEIVLGKILKKKGWRRSSYVITTKIfWggk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 83 -NSDQGY--ETTLQAFETTLEKLGLEYLDLYLVHWP-VKEKYTESWKALEKLYKDGRVRAIGVSNFHIHHLQDVFEIAE- 157
Cdd:cd19141 88 aETERGLsrKHIIEGLKASLERLQLEYVDIVFANRPdPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446977558 158 ---IKPMVNQVEYHpRLAQEELHAFCKE--HNIQLEA--WSPLMQGQL 198
Cdd:cd19141 168 fnlIPPIVEQAEYH-LFQREKVEMQLPElfHKIGVGAmtWSPLACGIL 214
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
21-143 |
4.91e-05 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 44.05 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 21 FGLGVFKVEDGSEVIDSVKAAiknGYRSIDTAAIYQNEEG---VGQAIRESGIpREELFITSKVWNSDQGYE-------- 89
Cdd:cd19147 26 GFMGSMDKEQAFELLDAFYEA---GGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDYKAYEvgkgkavn 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446977558 90 -------TTLQAFETTLEKLGLEYLDLYLVH-WPVKEKYTESWKALEKLYKDGRVRAIGVSN 143
Cdd:cd19147 102 ycgnhkrSLHVSVRDSLRKLQTDWIDILYVHwWDYTTSIEEVMDSLHILVQQGKVLYLGVSD 163
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-142 |
5.50e-03 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 37.71 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446977558 40 AAIKNGYRSIDTAAIY-QNEEGVGQAIRESGIPREELFITSKvWnsdqGYETT--------------------LQAFETT 98
Cdd:cd19098 43 AAWAAGVRYFDAARSYgRAEEFLGSWLRSRNIAPDAVFVGSK-W----GYTYTadwqvdaavhevkdhslarlLKQWEET 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446977558 99 LEKLGlEYLDLYLVHWPVKE----KYTESWKALEKLYKDGrvRAIGVS 142
Cdd:cd19098 118 RSLLG-KHLDLYQIHSATLEsgvlEDADVLAALAELKAEG--VKIGLS 162
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
42-96 |
7.00e-03 |
|
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: 37.14 E-value: 7.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446977558 42 IKNGYRSI-------DTAAIYQNEEGVGQAIRESGIPREELFITSKVWNSDQGYETTLQAFE 96
Cdd:cd06288 112 IEAGHRRIafiggpeDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLS 173
|
|
| |
