|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
9-277 |
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: 543.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGiqaaGISREALFVTSKVWNA 88
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKES----GIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQ 168
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 169 VEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENA 248
Cdd:cd19157 157 VEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENA 236
|
250 260
....*....|....*....|....*....
gi 1992844687 249 AVFDFELTKEEMEQIDRLNQNLRVGPDPD 277
Cdd:cd19157 237 DVFDFELSQEDMDKIDALNENLRVGPDPD 265
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
14-277 |
3.24e-176 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 486.10 E-value: 3.24e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 14 NGVKMPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADLGYE 93
Cdd:COG0656 1 NGVEIPALGLGTWQLP-GEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA----SGVPREELFVTTKVWNDNHGYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 94 STLKAYETSLEKLGLEYLDLYLIHWPVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVEYHP 173
Cdd:COG0656 76 DTLAAFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 174 RLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDF 253
Cdd:COG0656 156 YLQQRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDF 235
|
250 260
....*....|....*....|....
gi 1992844687 254 ELTKEEMEQIDRLNQNLRVGPDPD 277
Cdd:COG0656 236 ELSDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
11-267 |
2.38e-155 |
|
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: 433.02 E-value: 2.38e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADL 90
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVE 170
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 171 YHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAV 250
Cdd:cd19126 158 FHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADI 237
|
250
....*....|....*..
gi 1992844687 251 FDFELTKEEMEQIDRLN 267
Cdd:cd19126 238 FDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
11-279 |
3.41e-152 |
|
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: 425.78 E-value: 3.41e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADL 90
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE----SGVPREEVFVTTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVE 170
Cdd:cd19156 78 GYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 171 YHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAV 250
Cdd:cd19156 158 LHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDV 237
|
250 260
....*....|....*....|....*....
gi 1992844687 251 FDFELTKEEMEQIDRLNQNLRVGPDPDNF 279
Cdd:cd19156 238 FDFELTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
18-264 |
2.78e-140 |
|
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: 394.93 E-value: 2.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 18 MPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADLGYESTLK 97
Cdd:cd19071 1 MPLIGLGTYKLKPE-ETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRE----SGVPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 98 AYETSLEKLGLEYLDLYLIHWPVEGK-------YKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVE 170
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKeggskeaRLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 171 YHPRLTQKELQAFCREQGIQMEAWSPLMQG--QLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENA 248
Cdd:cd19071 156 LHPYLQQKELVEFCKEHGIVVQAYSPLGRGrrPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENL 235
|
250
....*....|....*.
gi 1992844687 249 AVFDFELTKEEMEQID 264
Cdd:cd19071 236 DVFDFELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-267 |
3.96e-138 |
|
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: 389.81 E-value: 3.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIRegiqAAGISREALFVTSKVWNA 88
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVS-NDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIHWPV--EGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMI 166
Cdd:cd19131 76 DQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 167 NQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAE 246
Cdd:cd19131 156 NQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAE 235
|
250 260
....*....|....*....|.
gi 1992844687 247 NAAVFDFELTKEEMEQIDRLN 267
Cdd:cd19131 236 NFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-267 |
1.46e-130 |
|
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: 370.37 E-value: 1.46e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 10 TTLNNGVKMPWFGLGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNAD 89
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK----SGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 90 LGYESTLKAYETSLEKLGLEYLDLYLIHWPVeGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQV 169
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPF-GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 170 EYHPRLTQKELQAFCREQGIQMEAWSPLMQGQ--LLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAEN 247
Cdd:cd19133 156 ETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAEN 235
|
250 260
....*....|....*....|
gi 1992844687 248 AAVFDFELTKEEMEQIDRLN 267
Cdd:cd19133 236 FDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-267 |
8.11e-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: 348.63 E-value: 8.11e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 10 TTLNNGVKMPWFGLGVFKVEEgPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNAD 89
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPP-EETADAVATALADGYRLIDTAAAYGNEREVGEGIRR----SGVDRSDIFVTTKLWISD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 90 LGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKD---AWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMI 166
Cdd:cd19127 76 YGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRtiqAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 167 NQVEYHPRLTQKELQAFCREQGIQMEAWSPL------------MQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVT 234
Cdd:cd19127 156 NQVELHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSA 235
|
250 260 270
....*....|....*....|....*....|...
gi 1992844687 235 IPKSTKEHRIAENAAVFDFELTKEEMEQIDRLN 267
Cdd:cd19127 236 IPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
18-266 |
9.62e-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: 345.77 E-value: 9.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 18 MPWFGLGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLGYESTLK 97
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 98 AYETSLEKLGLEYLDLYLIHWP-VEGKY----------KDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMI 166
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgVQGLKpsdprnaelrRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 167 NQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQL--LDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRI 244
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLrlLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 1992844687 245 AENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-266 |
6.57e-118 |
|
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: 338.91 E-value: 6.57e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 8 DTTTLNNGVKMPWFGLGVFKVeeGPELVNAVKTAIQH-GYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVW 86
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTSHS--GGYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 87 NADLGYESTLKAYETSLEKLGLEYLDLYLIHWP---VEGKYK-----DAWKALETLYKDGRVKAIGVSNFQIHHLEDLMK 158
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPdcpSSGKNVketraETWRALEELYDEGLCRAIGVSNFLIEHLEQLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 159 DAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKS 238
Cdd:cd19135 157 DCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKS 236
|
250 260
....*....|....*....|....*...
gi 1992844687 239 TKEHRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19135 237 TKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
11-279 |
5.22e-109 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 316.63 E-value: 5.22e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKVEEgPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIregiQAAGISREALFVTSKVWNADl 90
Cdd:PRK11565 8 KLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKAL----KEASVAREELFITTKLWNDD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 gYESTLKAYETSLEKLGLEYLDLYLIHWPV--EGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQ 168
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVpaIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 169 VEYHPRLTQKELQAFCREQGIQMEAWSPLMQG--QLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAE 246
Cdd:PRK11565 161 IELHPLMQQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAE 240
|
250 260 270
....*....|....*....|....*....|...
gi 1992844687 247 NAAVFDFELTKEEMEQIDRLNQNLRVGPDPDNF 279
Cdd:PRK11565 241 NFDVFDFRLDKDELGEIAKLDQGKRLGPDPDQF 273
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
12-272 |
3.16e-108 |
|
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: 315.38 E-value: 3.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 12 LNNGVKMPWFGLGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLG 91
Cdd:cd19116 5 LNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 92 YESTLKAYETSLEKLGLEYLDLYLIHWPVEGK-----------------YKDAWKALETLYKDGRVKAIGVSNFQIHHLE 154
Cdd:cd19116 85 REQVEPALRESLKRLGLDYVDLYLIHWPVAFKenndsesngdgslsdidYLETWRGMEDLVKLGLTRSIGVSNFNSEQIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 155 DLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL----MQGQL-----LDNEVLAEIAQKHNKSTAQVILR 225
Cdd:cd19116 165 RLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvPRGQTnppprLDDPTLVAIAKKYGKTTAQIVLR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1992844687 226 WDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRV 272
Cdd:cd19116 245 YLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-268 |
4.01e-108 |
|
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: 313.44 E-value: 4.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 12 LNNGVKMPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADLG 91
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLK-GDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRHHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 92 YESTLKAYETSLEKLGLEYLDLYLIHWPV--EGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQV 169
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHWPNpsRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 170 EYHPRLTQKELQAFCREQGIQMEAWSPLMQGQ-LLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENA 248
Cdd:cd19132 156 ELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSgLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENL 235
|
250 260
....*....|....*....|
gi 1992844687 249 AVFDFELTKEEMEQIDRLNQ 268
Cdd:cd19132 236 AIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
11-272 |
1.26e-104 |
|
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: 305.81 E-value: 1.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADL 90
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADPG-VVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWPVEGK---------------YKDAWKALETLYKDGRVKAIGVSNFQIHHLED 155
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKkgahmpepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 156 LMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL-------MQGQLLDNEVLAEIAQKHNKSTAQVILRWDL 228
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgttwVKKNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1992844687 229 QNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRV 272
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
12-272 |
1.04e-102 |
|
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: 301.61 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 12 LNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGI-QAAGISREALFVTSKVWNADL 90
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPG-QVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWPVEGK--------------------YKDAWKALETLYKDGRVKAIGVSNFQI 150
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFErgdnpfpknpdgtirydsthYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 151 HHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL----------MQGQLLDNEVLAEIAQKHNKSTA 220
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwakpDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1992844687 221 QVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRV 272
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-264 |
4.59e-101 |
|
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: 295.33 E-value: 4.59e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 18 MPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADLGYESTLK 97
Cdd:cd19073 1 IPALGLGTWQLR-GDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAE----SGVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 98 AYETSLEKLGLEYLDLYLIHWPVEGK-YKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVEYHPRLT 176
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWPNPTVpLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 177 QKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELT 256
Cdd:cd19073 156 QAELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELT 235
|
....*...
gi 1992844687 257 KEEMEQID 264
Cdd:cd19073 236 SEDVAKID 243
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
9-273 |
4.98e-100 |
|
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: 293.30 E-value: 4.98e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIRegiqAAGISREALFVTSKVWNA 88
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDD-EAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA----ASGIPRGELFVTTKLATP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIHWPV--EGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMI 166
Cdd:cd19134 77 DQGFTASQAACRASLERLGLDYVDLYLIHWPAgrEGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 167 NQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAE 246
Cdd:cd19134 157 NQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIAS 236
|
250 260
....*....|....*....|....*..
gi 1992844687 247 NAAVFDFELTKEEMEQIDRLNQNLRVG 273
Cdd:cd19134 237 NLDVFDFELTADHMDALDGLDDGTRFR 263
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
9-271 |
4.35e-99 |
|
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: 292.39 E-value: 4.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNA 88
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKPG-EVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIHWPV-------------------EGKYKDAWKALETLYKDGRVKAIGVSNFQ 149
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPValkkgvgfpesgedllslsPIPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 150 IHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQ------------LLDNEVLAEIAQKHNK 217
Cdd:cd19123 162 VKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepvLLEDPVINKIAEKHGA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1992844687 218 STAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLR 271
Cdd:cd19123 242 SPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
11-267 |
7.73e-95 |
|
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: 279.87 E-value: 7.73e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGqgirEGIQAAGISREALFVTSKVWNADL 90
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPA-DTQRAVATALEVGYRHIDTAAIYGNEEGVG----AAIAASGIPRDELFVTTKLWNDRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWPV--EGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQ 168
Cdd:cd19130 78 DGDEPAAAFAESLAKLGLDQVDLYLVHWPTpaAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 169 VEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENA 248
Cdd:cd19130 158 IELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNL 237
|
250
....*....|....*....
gi 1992844687 249 AVFDFELTKEEMEQIDRLN 267
Cdd:cd19130 238 DVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
14-268 |
2.78e-94 |
|
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: 279.54 E-value: 2.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 14 NGVKMPWFGLGVFKVEEGPE-LVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGI-SREALFVTSKVWNADLG 91
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPEdIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 92 YESTLKAYETSLEKLGLEYLDLYLIHWPV---EGKY--------------KDAWKALETLYKDGRVKAIGVSNFQIHHLE 154
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVslkPGKFsfpieeedflpfdiKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 155 DLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL-----MQG--QLLDNEVLAEIAQKHNKSTAQVILRWD 227
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgapgtKWGsnAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1992844687 228 LQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQ 268
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
15-265 |
7.83e-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: 277.96 E-value: 7.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGV-------FKVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWN 87
Cdd:cd19120 1 GSKIPAIAFGTgtawyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKE----SGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 88 adlGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKD-----AWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEI 162
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGptlaeAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 163 KPMINQVEYHPRLT--QKELQAFCREQGIQMEAWSPL------MQGQLLDneVLAEIAQKHNKSTAQVILRWDLQNGVVT 234
Cdd:cd19120 154 KPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLspltrdAGGPLDP--VLEKIAEKYGVTPAQVLLRWALQKGIVV 231
|
250 260 270
....*....|....*....|....*....|.
gi 1992844687 235 IPKSTKEHRIAENAAVFDFELTKEEMEQIDR 265
Cdd:cd19120 232 VTTSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
11-272 |
1.26e-93 |
|
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: 278.53 E-value: 1.26e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADL 90
Cdd:cd19154 5 TLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWP-----VEGKYK---------------DAWKALETLYKDGRVKAIGVSNFQI 150
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPaafkdDEGESGtmengmsihdavdveDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 151 HHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL---------------MQGQLLDNEVLAEIAQKH 215
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgranftkstgvsPAPNLLQDPIVKAIAEKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1992844687 216 NKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRV 272
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
14-266 |
1.85e-93 |
|
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: 276.45 E-value: 1.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 14 NGVKMPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIRegiqAAGISREALFVTSKVWNADLGYE 93
Cdd:cd19140 4 NGVRIPALGLGTYPLT-GEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIA----ASGVPRDELFLTTKVWPDNYSPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 94 STLKAYETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVEYH 172
Cdd:cd19140 79 DFLASVEESLRKLRTDYVDLLLLHWPnKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 173 PRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDL-QNGVVTIPKSTKEHRIAENAAVF 251
Cdd:cd19140 159 PYLDQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIF 238
|
250
....*....|....*
gi 1992844687 252 DFELTKEEMEQIDRL 266
Cdd:cd19140 239 DFTLSDEEMARIAAL 253
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-266 |
7.32e-86 |
|
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: 258.20 E-value: 7.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 5 NLQDTTTLNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIRegiqAAGISREALFVTSK 84
Cdd:cd19117 1 PSSKTFKLNTGAEIPAVGLGTWQSKPN-EVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 85 VWNADlgYESTLKAYETSLEKLGLEYLDLYLIHWPV----------------------EGKYKDAWKALETLYKDGRVKA 142
Cdd:cd19117 76 LWCTW--HRRVEEALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkkddgtkdhepDWDFIKTWELMQKLPATGKVKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 143 IGVSNFQIHHLEDLMKD--AEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL--MQGQLLDNEVLAEIAQKHNKS 218
Cdd:cd19117 154 IGVSNFSIKNLEKLLASpsAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgsTNAPLLKEPVIIKIAKKHGKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1992844687 219 TAQVILRWDLQNGVVTIPKSTKEHRIAENAAVfdFELTKEEMEQIDRL 266
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
11-266 |
2.43e-85 |
|
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: 256.69 E-value: 2.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKvEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIqAAGISREALFVTSKVWNADl 90
Cdd:cd19121 5 KLNTGASIPAVGLGTWQ-AKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 gYESTLKAYETSLEKLGLEYLDLYLIHWPV---------------EGK--------YKDAWKALETLYKDGRVKAIGVSN 147
Cdd:cd19121 82 -HRRVELCLDRSLKSLGLDYVDLYLVHWPVllnpngnhdlfptlpDGSrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 148 FQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL--MQGQLLDNEVLAEIAQKHNKSTAQVILR 225
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1992844687 226 WDLQNGVVTIPKSTKEHRIAENAAVFDFelTKEEMEQIDRL 266
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-266 |
7.01e-85 |
|
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: 255.41 E-value: 7.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 12 LNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGI-SREALFVTSKVWNADL 90
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPG-EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGvKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWPV-------------------------EGKYKDAWKALETLYKDGRVKAIGV 145
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVafkptgdlnpltavptnggevdldlSVSLVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 146 SNFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL---MQGQ--LLDNEVLAEIAQKHNKSTA 220
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLplLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1992844687 221 QVILRWDLQNGVVTIPKSTKEHRIAENAAvfDFELTKEEMEQIDRL 266
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
12-274 |
4.88e-83 |
|
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: 251.38 E-value: 4.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 12 LNNGVKMPWFGLGVFKVEEGP--ELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNAD 89
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEEVPksKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 90 LGYESTLKAYETSLEKLGLEYLDLYLIHWPV-------------EGK-------YKDAWKALETLYKDGRVKAIGVSNFQ 149
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPValkpgeelfpkdeNGKlifdtvdLCATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 150 IHHLEDLMKDAEIK--PMINQVEYHPRLTQKELQAFCREQGIQMEAWSPLmqGQ-------------LLDNEVLAEIAQK 214
Cdd:cd19108 165 RRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSAL--GSqrdkewvdqnspvLLEDPVLCALAKK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 215 HNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRVGP 274
Cdd:cd19108 243 HKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-271 |
8.80e-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: 248.55 E-value: 8.80e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNA 88
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRMEPG-EIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYesTLKAYETSLEKLGLEYLDLYLIHWPVEGKY------------------------KDAWKALETLYKDGRVKAIG 144
Cdd:cd19112 81 DHGH--VIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvgttgsalgedgvldidvtislETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 145 VSNFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQG----------QLLDNEVLAEIAQK 214
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsvSPLDDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1992844687 215 HNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLR 271
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-271 |
7.43e-81 |
|
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: 246.20 E-value: 7.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNA 88
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNA-TAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIHWPV-------EGKYK-------------------DAWKALETLYKDGRVKA 142
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIafkfvpiEEKYPpgfycgdgdnfvyedvpilDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 143 IGVSNFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSP--------LMQGQ------LLDNEVL 208
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSfgpqsfveLNQGRalntptLFEHDTI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992844687 209 AEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLR 271
Cdd:cd19113 241 KSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-272 |
8.85e-81 |
|
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: 245.79 E-value: 8.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADlgYES 94
Cdd:cd19107 1 GAKMPILGLGTWKSPPG-QVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTF--HEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 95 TL--KAYETSLEKLGLEYLDLYLIHWPV--------------------EGKYKDAWKALETLYKDGRVKAIGVSNFQIHH 152
Cdd:cd19107 78 GLvkGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 153 LEDLMKDAEIK--PMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL----------MQGQLLDNEVLAEIAQKHNKSTA 220
Cdd:cd19107 158 IERILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwakpEDPSLLEDPKIKEIAAKHNKTTA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1992844687 221 QVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRV 272
Cdd:cd19107 238 QVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRA 289
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-271 |
6.34e-80 |
|
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: 243.97 E-value: 6.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 7 QDTTTLNNGVKMPWFGLGVFKVEEgPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVW 86
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQSSP-EEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 87 NADLGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYK----------------------DAWKALETLYKDGRVKAIG 144
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKeddsgkldptgehkqdyttdllDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 145 VSNFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL-----------------MQGQLLDNEV 207
Cdd:cd19155 160 LSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQDPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1992844687 208 LAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLR 271
Cdd:cd19155 240 VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-271 |
6.88e-78 |
|
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: 237.78 E-value: 6.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLGYES 94
Cdd:cd19111 1 GFPMPVIGLGTYQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 95 TLKAYETSLEKLGLEYLDLYLIHWPVEGKYK--------------DAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDA 160
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVNKkdkgerelassdvtSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 161 EIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL------------MQGQLLDNEVLAEIAQKHNKSTAQVILRWDL 228
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgspgranqslwpDQPDLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1992844687 229 QNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLR 271
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-279 |
7.70e-78 |
|
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: 238.47 E-value: 7.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEEgPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNA 88
Cdd:cd19115 4 TVKLNSGYDMPLVGFGLWKVNN-DTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKD-------------------------AWKALETLYKDGRVKAI 143
Cdd:cd19115 83 FHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDpavryppgwfydgkkvefsnapiqeTWTAMEKLVDKGLARSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 144 GVSNFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWS---PL------MQGQ-----LLDNEVLA 209
Cdd:cd19115 163 GVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgPQsfleldLPGAkdtppLFEHDVIK 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 210 EIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRVGpDPDNF 279
Cdd:cd19115 243 SIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFN-NPLNY 311
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
12-266 |
3.05e-76 |
|
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: 233.93 E-value: 3.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 12 LNNGVKMPWFGLGVFK-VEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWnaDL 90
Cdd:cd19119 6 LNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVW--PT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWPV--------------------------EGKYKDAWKALETLYKDGRVKAIG 144
Cdd:cd19119 84 FYDEVERSLDESLKALGLDYVDLLLVHWPVcfekdsddsgkpftpvnddgktryaaSGDHITTYKQLEKIYLDGRAKAIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 145 VSNFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL--MQGQLLDNEVLAEIAQKHNKSTAQV 222
Cdd:cd19119 164 VSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLgsHGAPNLKNPLVKKIAEKYNVSTGDI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1992844687 223 ILRWDLQNGVVTIPKSTKEHRIAENAAVfdFELTKEEMEQIDRL 266
Cdd:cd19119 244 LISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
17-276 |
3.33e-76 |
|
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: 234.08 E-value: 3.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 17 KMPWFGLGVFKVEEGpELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLGYESTL 96
Cdd:cd19110 3 DIPAVGLGTWKASPG-EVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 97 KAYETSLEKLGLEYLDLYLIHWPVEGK--------------------YKDAWKALETLYKDGRVKAIGVSNFQIHHLEDL 156
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 157 MKDA--EIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL---MQG-QLLDNEVLAEIAQKHNKSTAQVILRWDLQN 230
Cdd:cd19110 162 LNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLggsCEGvDLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1992844687 231 GVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLRVGPDP 276
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
17-275 |
9.45e-75 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 229.14 E-value: 9.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 17 KMPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADLGYESTL 96
Cdd:PRK11172 2 SIPAFGLGTFRLK-DQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLAKDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 97 KAYETSLEKLGLEYLDLYLIHWPVEGK---YKDAWKALETLYKDGRVKAIGVSNFQIhhleDLMKDA-------EIKpmI 166
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPSPNDevsVEEFMQALLEAKKQGLTREIGISNFTI----ALMKQAiaavgaeNIA--T 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 167 NQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAE 246
Cdd:PRK11172 151 NQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLAS 230
|
250 260 270
....*....|....*....|....*....|
gi 1992844687 247 NAAVFDFELTKEEMEQIDRLNQNLR-VGPD 275
Cdd:PRK11172 231 NLLAQDLQLDAEDMAAIAALDRNGRlVSPE 260
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
15-271 |
5.28e-74 |
|
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: 228.92 E-value: 5.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGVFKVEEGP---ELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLG 91
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 92 YESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKDA--------------------WKALETLYKDGRVKAIGVSNFQIH 151
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEiyprdengkwlyhktnlcatWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 152 HLEDLMKDAEIK--PMINQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQ-----------LLDNEVLAEIAQKHNKS 218
Cdd:cd19109 161 QLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1992844687 219 TAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLR 271
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
18-266 |
1.47e-72 |
|
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: 223.00 E-value: 1.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 18 MPWFGLGVFKVEeGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREgiqaAGISREALFVTSKVWNADLGYESTLK 97
Cdd:cd19139 1 IPAFGLGTFRLK-DDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 98 AYETSLEKLGLEYLDLYLIHWP---VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLE---DLMKDAEIkpMINQVEY 171
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWPspnDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDeaiAVVGAGAI--ATNQIEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 172 HPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVF 251
Cdd:cd19139 154 SPYLQNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLAL 233
|
250
....*....|....*
gi 1992844687 252 DFELTKEEMEQIDRL 266
Cdd:cd19139 234 DLTLDADDMAAIAAL 248
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-264 |
2.38e-69 |
|
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: 215.19 E-value: 2.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTLNNGVKMPWFGLGVFKVEEGPEL----VNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREgiqaagiSREALFV 81
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMGEDPAKraqeIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 82 TSKV--WNAdlGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKD 159
Cdd:cd19138 75 VSKVlpSNA--SRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 160 AEIKPM-INQVEYH--PRLTQKELQAFCREQGIQMEAWSPLMQGQLLD-----NEVLAEIAQKHNKSTAQVILRWDL-QN 230
Cdd:cd19138 153 PGGGNCaANQVLYNlgSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRrglleNPTLKEIAARHGATPAQVALAWVLrDG 232
|
250 260 270
....*....|....*....|....*....|....
gi 1992844687 231 GVVTIPKSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19138 233 NVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-264 |
8.28e-69 |
|
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: 214.02 E-value: 8.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGVFKVEEGP--------ELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIRegiqaaGISREALFVTS 83
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdysddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 84 KVWNADLGYESTLKAYETSLEKLGLEYLDLYLIHWPV-EGKYKDAWKALETLYKDGRVKAIGVSNF---QIHHLEDLMKD 159
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNpSIPIEETLRAMEELVEEGKIRYIGVSNFsleELEEAQSYLKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 160 AEIkpMINQVEYH--PRLTQKELQAFCREQGIQMEAWSPLMQGQLL---DNEVLAEIAQKHNKSTAQVILRWDL-QNGVV 233
Cdd:cd19072 155 GPI--VANQVEYNlfDREEESGLLPYCQKNGIAIIAYSPLEKGKLSnakGSPLLDEIAKKYGKTPAQIALNWLIsKPNVI 232
|
250 260 270
....*....|....*....|....*....|.
gi 1992844687 234 TIPKSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19072 233 AIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
15-271 |
2.48e-67 |
|
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: 211.65 E-value: 2.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGVFKV--EEGPElvnAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLGY 92
Cdd:cd19114 1 GDKMPLVGFGTAKIkaNETEE---VIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 93 ESTLKAYETSLEKLGLEYLDLYLIHWPVEGKY--------------------------KDAWKALETLYKDGRVKAIGVS 146
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYvdpaenypflwkdkelkkfpleqspmQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 147 NFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQG-------------QLLDNEVLAEIAQ 213
Cdd:cd19114 158 NFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkhftNLLEHPVVKKLAD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1992844687 214 KHNKSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQNLR 271
Cdd:cd19114 238 KHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
11-266 |
1.36e-66 |
|
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: 209.40 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFGLGVFKVEEGP-ELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGI-QAAGISREALFVTSKVWNA 88
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAKgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLkENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIHWPV--------------EGKY----------KDAWKALETLYKDGRVKAIG 144
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaekndqrspklgpDGKYvilkdltenpEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 145 VSNFQIHHLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL-MQGQ-------LLDNEVLAEIAQKHN 216
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgSQNQvpstgerVSENPTLNEVAEKGG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1992844687 217 KSTAQVILRWDLQNGVVTIPKSTKEHRIAENAAVfdFELTKEEMEQIDRL 266
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQV 289
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-265 |
2.25e-64 |
|
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: 203.46 E-value: 2.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 13 NNGVKMPWFGLGVFkVEEGPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLGY 92
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 93 ESTLKAYETSLEKLGLEYLDLYLIHWPV--------------------EG-KYKDAWKALETLYKDGRVKAIGVSNFQIH 151
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFafqpgdeqdprdangnviydDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 152 HLEDLMKDAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL---MQGQLLDNEVLAEIAQKHNKSTAQVILRWDL 228
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLghgMEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1992844687 229 QNGVVTIPKSTKEHRIAENaavFDFE-LTKEEMEQIDR 265
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), ... |
19-266 |
3.77e-63 |
|
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: 200.06 E-value: 3.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 19 PWFGLGVFKVEEgPELVNAVKTAIQHGYRSIDTAAIYGNEEGVGQGIREGIQAAGISREALFVTSKVWNADLGYESTLKA 98
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 99 YETSLEKLGLEYLDLYLIHWPVE------------------GKY--KDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMK 158
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAfdmdtdgdprddnqiqslSKKplEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 159 DAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEV------LAEIAQKHNKSTAQVILRWDLQ--- 229
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTflndseLKALATKYNTTPPQVIIAWHLQkwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1992844687 230 NGVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19128 241 KNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
32-267 |
3.01e-62 |
|
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: 197.92 E-value: 3.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 32 PELVNAVKTAIQHGYRSIDTAAIYG---NEEGVGqgirEGIQAAGISREALFVTSKV------WNADLGYESTLKAYETS 102
Cdd:pfam00248 18 EEALEALRAALEAGINFIDTAEVYGdgkSEELLG----EALKDYPVKRDKVVIATKVpdgdgpWPSGGSKENIRKSLEES 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 103 LEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVEYHP--RLTQKE 179
Cdd:pfam00248 94 LKRLGTDYIDLYYLHWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNLlrRRQEEE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 180 LQAFCREQGIQMEAWSPLMQG---------------------------QLLDNEVLAEIAQKHNKSTAQVILRWDLQN-- 230
Cdd:pfam00248 174 LLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkgtplNLEALEALEEIAKEHGVSPAQVALRWALSKpg 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 1992844687 231 GVVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLN 267
Cdd:pfam00248 254 VTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
15-264 |
8.31e-55 |
|
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: 178.15 E-value: 8.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGVFKV--------EEGPELVNAVKTAIQHGYRSIDTAAIYG---NEEGVGQGIREgiqaagISREALFVTS 83
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 84 KVWNADLGYESTLKAYETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEI 162
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPnPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 163 KPMINQVEYH---PRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLAEIAQKHNKSTAQVILRWDLQN-GVVTIPKS 238
Cdd:cd19137 155 PIVCNQVKYNledRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKA 234
|
250 260
....*....|....*....|....*.
gi 1992844687 239 TKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19137 235 GRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
37-276 |
8.78e-50 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 166.51 E-value: 8.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 37 AVKTAIQHGYRSIDTAAIYG---NEEGVGQGIRegiqaaGISREALFVTSKV--------WNADLGYESTLKAYETSLEK 105
Cdd:COG0667 38 ILDAALDAGINFFDTADVYGpgrSEELLGEALK------GRPRDDVVIATKVgrrmgpgpNGRGLSREHIRRAVEASLRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 106 LGLEYLDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMI--NQVEYHP--RLT 176
Cdd:COG0667 112 LGTDYIDLYQLHRpdpdtPIE----ETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIvaVQNEYSLldRSA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 177 QKELQAFCREQGIQMEAWSPLMQGQLLDN------------------------------EVLAEIAQKHNKSTAQVILRW 226
Cdd:COG0667 188 EEELLPAARELGVGVLAYSPLAGGLLTGKyrrgatfpegdraatnfvqgylternlalvDALRAIAAEHGVTPAQLALAW 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1992844687 227 DLQNGVVT--IPKSTKEHRIAENAAVFDFELTKEEMEQIDRLnqnLRVGPDP 276
Cdd:COG0667 268 LLAQPGVTsvIPGARSPEQLEENLAAADLELSAEDLAALDAA---LAAVPAP 316
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
32-264 |
1.06e-49 |
|
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: 165.86 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 32 PELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGIQaagisREALFVTSKVWNA--DLGYESTLKAYETSLEKL 106
Cdd:cd19093 26 EDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELGD-----RDEVVIATKFAPLpwRLTRRSVVKALKASLERL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 107 GLEYLDLYLIHWPVE--GKYKDAWKALETLYKDGRVKAIGVSNFQIHHLE---DLMKDAEIKPMINQVEY---HPRLTQK 178
Cdd:cd19093 101 GLDSIDLYQLHWPGPwySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRrahKALKERGVPLASNQVEYsllYRDPEQN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 179 ELQAFCREQGIQMEAWSPLMQGQL-----LDN----------------------EVLAEIAQKHNKSTAQVILRWDLQNG 231
Cdd:cd19093 181 GLLPACDELGITLIAYSPLAQGLLtgkysPENpppggrrrlfgrknlekvqpllDALEEIAEKYGKTPAQVALNWLIAKG 260
|
250 260 270
....*....|....*....|....*....|...
gi 1992844687 232 VVTIPKSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19093 261 VVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
33-264 |
5.88e-47 |
|
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: 158.84 E-value: 5.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREgiqaagiSREALFVTSKV---WN------ADLGYESTLKAYE 100
Cdd:cd19084 26 ESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATKCglrWDggkgvtKDLSPESIRKEVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 101 TSLEKLGLEYLDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIkpMINQVEYHP-- 173
Cdd:cd19084 99 QSLRRLQTDYIDLYQIHWpdpntPIE----ETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMle 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 174 RLTQKELQAFCREQGIQMEAWSPLMQGqLL------------------------DN--------EVLAEIAQKHNKSTAQ 221
Cdd:cd19084 173 REIEEELLPYCRENGIGVLPYGPLAQG-LLtgkykkeptfppddrrsrfpffrgENfeknleivDKLKEIAEKYGKSLAQ 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1992844687 222 VILRWDLQNGVVT--IPKSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19084 252 LAIAWTLAQPGVTsaIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
33-270 |
5.97e-47 |
|
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: 158.52 E-value: 5.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIrEGIqaagisREALFVTSKVWNADLGYESTLKAYETSLEKLGLE 109
Cdd:cd19085 24 ESIATIHAALDAGINFFDTAEAYGDghsEEVLGKAL-KGR------RDDVVIATKVSPDNLTPEDVRKSCERSLKRLGTD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 110 YLDLYLIHWPVEG-KYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKpmINQVEYHP--RLTQKELQAFCRE 186
Cdd:cd19085 97 YIDLYQIHWPSSDvPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQLPYNLlwRAIEYEILPFCRE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 187 QGIQMEAWSPLMQGqLL-------------DN--------------------EVLAEIAQKHNKSTAQVILRWDLQNGVV 233
Cdd:cd19085 175 HGIGVLAYSPLAQG-LLtgkfssaedfppgDArtrlfrhfepgaeeetfealEKLKEIADELGVTMAQLALAWVLQQPGV 253
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1992844687 234 TIP---KSTKEHrIAENAAVFDFELTKEEMEQIDRLNQNL 270
Cdd:cd19085 254 TSVivgARNPEQ-LEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
33-259 |
4.43e-40 |
|
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: 140.77 E-value: 4.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQ------GIREGIQ---AAGISREALFVTSKVWNADLGYESTLKAYE 100
Cdd:cd19092 25 ELLSLIEAALELGITTFDHADIYGGgkcEELFGEalalnpGLREKIEiqtKCGIRLGDDPRPGRIKHYDTSKEHILASVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 101 TSLEKLGLEYLDLYLIHWP---VEgkYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVE---YHPR 174
Cdd:cd19092 105 GSLKRLGTDYLDLLLLHRPdplMD--PEEVAEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIElslLHTE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 175 LTQKELQAFCREQGIQMEAWSPLMQGQLLD---------NEVLAEIAQKHNKSTAQVILRWDLQN--GVVTIPKSTKEHR 243
Cdd:cd19092 183 AIDDGTLDYCQLLDITPMAWSPLGGGRLFGgfderfqrlRAALEELAEEYGVTIEAIALAWLLRHpaRIQPILGTTNPER 262
|
250
....*....|....*.
gi 1992844687 244 IAENAAVFDFELTKEE 259
Cdd:cd19092 263 IRSAVKALDIELTREE 278
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
33-259 |
6.53e-39 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 137.98 E-value: 6.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGqgirEGIQAAGISREALFVTSK--VWNADLGYESTLKAY-------- 99
Cdd:COG4989 32 EAAALIEAALELGITTFDHADIYGGytcEALFG----EALKLSPSLREKIELQTKcgIRLPSEARDNRVKHYdtskehii 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 100 ---ETSLEKLGLEYLDLYLIHWPvegkykDAW-------KALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQV 169
Cdd:COG4989 108 asvEGSLRRLGTDYLDLLLLHRP------DPLmdpeevaEAFDELKASGKVRHFGVSNFTPSQFELLQSALDQPLVTNQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 170 E---YHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLD---------NEVLAEIAQKHNKSTAQVILRWDLQN--GVVTI 235
Cdd:COG4989 182 ElslLHTDAFDDGTLDYCQLNGITPMAWSPLAGGRLFGgfdeqfprlRAALDELAEKYGVSPEAIALAWLLRHpaGIQPV 261
|
250 260
....*....|....*....|....
gi 1992844687 236 PKSTKEHRIAENAAVFDFELTKEE 259
Cdd:COG4989 262 IGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
37-249 |
5.83e-35 |
|
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: 125.71 E-value: 5.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 37 AVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGIQaagisREALFVTSKV--------WNADLGYESTLKAYETSLEK 105
Cdd:cd06660 22 LLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-----RDDVVIATKGghppggdpSRSRLSPEHIRRDLEESLRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 106 LGLEYLDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAE----IKPMINQVEY---HP 173
Cdd:cd06660 97 LGTDYIDLYYLHRddpstPVE----ETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPGFAAVQPQYsllDR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1992844687 174 RLTQKELQAFCREQGIQMEAWSPLMQGqlldnevlaeiaqkhnksTAQVILRWDLQNGVVT--IPKSTKEHRIAENAA 249
Cdd:cd06660 173 SPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPFVTvpIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-266 |
2.31e-33 |
|
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: 123.55 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 35 VNAVKTAIQHGYRSIDTAAIYG---NEEGVGQGIREgiqaagiSREALFVTSK---VWNAD------LGYESTLKAYETS 102
Cdd:cd19102 29 IAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKG-------LRDRPIVATKcglLWDEEgrirrsLKPASIRAECEAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 103 LEKLGLEYLDLYLIHWPV-EGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEI---KPMINQVEyhpRLTQK 178
Cdd:cd19102 102 LRRLGVDVIDLYQIHWPDpDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIaslQPPYSLLR---RGIEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 179 ELQAFCREQGIQMEAWSPLMQGQL---LDNEVLA------------------------------EIAQKHNKSTAQVILR 225
Cdd:cd19102 179 EILPFCAEHGIGVIVYSPMQSGLLtgkMTPERVAslpaddwrrrspffqepnlarnlalvdalrPIAERHGRTVAQLAIA 258
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1992844687 226 WDLQNGVVT--IPKSTKEHRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19102 259 WVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-266 |
5.50e-31 |
|
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: 117.33 E-value: 5.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 11 TLNNGVKMPWFG-LGVFKVEEGPELVNAvktAIQHGYRSIDTAAIYGN---EEGVGQGIREGIQAAGISREALFVTSKVW 86
Cdd:cd19091 20 TMTFGGGGGFFGaWGGVDQEEADRLVDI---ALDAGINFFDTADVYSEgesEEILGKALKGRRDDVLIATKVRGRMGEGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 87 NAD-LGYESTLKAYETSLEKLGLEYLDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDA 160
Cdd:cd19091 97 NDVgLSRHHIIRAVEASLKRLGTDYIDLYQLHGfdaltPLE----ETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGIS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 161 E----IKPMINQVEYHP--RLTQKELQAFCREQGIQMEAWSPLMQGQL-------------------------LDNE--- 206
Cdd:cd19091 173 ErrglARFVALQAYYSLlgRDLEHELMPLALDQGVGLLVWSPLAGGLLsgkyrrgqpapegsrlrrtgfdfppVDRErgy 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1992844687 207 ----VLAEIAQKHNKSTAQVILRWDLQNGVVT--IPKSTKEHRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19091 253 dvvdALREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
38-264 |
4.94e-30 |
|
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: 114.99 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 38 VKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGIqaagiSREALFVTSKVWN--------ADLGYESTLKAYETSLEKL 106
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFpmgdgpngRGLSRKHIMAEVDASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 107 GLEYLDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIK---PMINQVEYHP---RL 175
Cdd:cd19079 116 GTDYIDLYQIHRwdyetPIE----ETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNgwtKFVSMQNHYNllyRE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 176 TQKELQAFCREQGIQMEAWSPLMQGQL---------------------------LDNEVLA---EIAQKHNKSTAQVILR 225
Cdd:cd19079 192 EEREMIPLCEEEGIGVIPWSPLARGRLarpwgdtterrrsttdtaklkydyfteADKEIVDrveEVAKERGVSMAQVALA 271
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1992844687 226 WDLQNGVVTIP--KSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19079 272 WLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
33-264 |
1.33e-29 |
|
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: 113.91 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREgiqaagiSREALFVTSK---VW----------------NADL 90
Cdd:cd19149 34 ESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVLATKcglRWdreggsfffvrdgvtvYKNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 91 GYESTLKAYETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKpmINQV 169
Cdd:cd19149 107 SPESIREEVEQSLKRLGTDYIDLYQTHWQdVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLD--IIQE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 170 EYH--PRLTQKELQAFCREQGIQMEAWSPLMQGQLLDN-------------------------------EVLAEIAQKHN 216
Cdd:cd19149 185 KYSmlDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKitpdrefdagdarsgipwfspenrekvlallEKWKPLCEKYG 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1992844687 217 KSTAQVILRWDL-QNGVVT-IPKSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19149 265 CTLAQLVIAWTLaQPGITSaLCGARKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
41-263 |
4.92e-29 |
|
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: 111.92 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 41 AIQHGYRSIDTAAIYG---NEEGVGQGIREGiqaagisREALFVTSK---VWNADLGY-------ESTLKAYETSLEKLG 107
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKfgiVRDPGSGFrgvdgrpEYVRAACEASLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 108 LEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIGVSNFQIhhlEDLMKDAEIKPMIN-QVEYHP--RLTQKE 179
Cdd:cd19076 114 TDVIDLYYQHrvdpnVPIE----ETVGAMAELVEEGKVRYIGLSEASA---DTIRRAHAVHPITAvQSEYSLwtRDIEDE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 180 LQAFCREQGIQMEAWSPL--------------------------MQGQLLDN-----EVLAEIAQKHNKSTAQVILRWDL 228
Cdd:cd19076 187 VLPTCRELGIGFVAYSPLgrgfltgaikspedlpeddfrrnnprFQGENFDKnlklvEKLEAIAAEKGCTPAQLALAWVL 266
|
250 260 270
....*....|....*....|....*....|....*..
gi 1992844687 229 QNG--VVTIPKSTKEHRIAENAAVFDFELTKEEMEQI 263
Cdd:cd19076 267 AQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-266 |
6.17e-29 |
|
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: 111.74 E-value: 6.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 29 EEGPELVnavKTAIQHGYRSIDTAAIYG---NEEGVGQGIREgiqaagISREALFVTSKVWNADLGYESTL--------K 97
Cdd:cd19083 33 EEGKDLV---REALDNGVNLLDTAFIYGlgrSEELVGEVLKE------YNRNEVVIATKGAHKFGGDGSVLnnspeflrS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 98 AYETSLEKLGLEYLDLYLIHWPVEGKYKD-AWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMinQVEYHprLT 176
Cdd:cd19083 104 AVEKSLKRLNTDYIDLYYIHFPDGETPKAeAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDVL--QGEYN--LL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 177 QKELQA----FCREQGIQMEAWSPLMQGQL--------------LDNEV-----------------LAEIAQKHNKSTAQ 221
Cdd:cd19083 180 QREAEEdilpYCVENNISFIPYFPLASGLLagkytkdtkfpdndLRNDKplfkgerfsenldkvdkLKSIADEKGVTVAH 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1992844687 222 VILRWDLQNGVVT--IPKSTKEHRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19083 260 LALAWYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-264 |
1.71e-28 |
|
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: 110.38 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 27 KVEEGPELVNAVKTAIQHGYRSIDTAAIYGN-EEGVGQgIREGIQAAGISREALFVTSKvWNADLGYESTLKAY-----E 100
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGE-FRKRLRRERDAADDVQIHTK-WVPDPGELTMTRAYveaaiD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 101 TSLEKLGLEYLDLYLIHW--PVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMkDAEIKPMINQVEYH--PRLT 176
Cdd:cd19101 96 RSLKRLGVDRLDLVQFHWwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL-DAGVPIVSNQVQYSllDRRP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 177 QKELQAFCREQGIQMEAWSPLMQG---------------------------------------QLLdnEVLAEIAQKHNK 217
Cdd:cd19101 175 ENGMAALCEDHGIKLLAYGTLAGGllsekylgvpeptgpaletrslqkyklmidewggwdlfqELL--RTLKAIADKHGV 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1992844687 218 STAQVILRWDL-QNGV--VTIPKSTKEHrIAENAAVFDFELTKEEMEQID 264
Cdd:cd19101 253 SIANVAVRWVLdQPGVagVIVGARNSEH-IDDNVRAFSFRLDDEDRAAID 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
13-271 |
6.36e-28 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.29 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 13 NNGVKMPWFGLGV--FKVEEGPELVNAVKTAIQHGYRSIDTAAIYGN-EEGVGQGIREgiqaagiSREALFVTSK--VWN 87
Cdd:COG1453 8 KTGLEVSVLGFGGmrLPRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVILATKlpPWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 88 ADlgYESTLKAYETSLEKLGLEYLDLYLIH-------WPVEGKYKDAWKALETLYKDGRVKAIGVSNfqiHHLEDLMKDA 160
Cdd:COG1453 81 RD--PEDMRKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPGGALEALEKAKAEGKIRHIGFST---HGSLEVIKEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 161 eikpmIN-------QVEYHPRLTQ----KELQAFCREQGIQ---MEawsPLMQGQLLD-NEVLAEIAqKHNKSTAQVILR 225
Cdd:COG1453 156 -----IDtgdfdfvQLQYNYLDQDnqagEEALEAAAEKGIGviiMK---PLKGGRLANpPEKLVELL-CPPLSPAEWALR 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1992844687 226 WDLQNGVVTIPKS---TKEHrIAENAAVFD-FE-LTKEEMEQIDRLNQNLR 271
Cdd:COG1453 227 FLLSHPEVTTVLSgmsTPEQ-LDENLKTADnLEpLTEEELAILERLAEELG 276
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
31-266 |
2.17e-25 |
|
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: 102.00 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 31 GPELVNAVKT---AIQHGYRSIDTAAIYG---NEEGVGQGIREGIQaagisREALFVTSKV---WNADLGY------EST 95
Cdd:cd19148 21 GTDEKEAIETihkALDLGINLIDTAPVYGfglSEEIVGKALKEYGK-----RDRVVIATKVgleWDEGGEVvrnsspARI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 96 LKAYETSLEKLGLEYLDLYLIHWPVEGK-YKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEI---KPMINQVEy 171
Cdd:cd19148 96 RKEVEDSLRRLQTDYIDLYQVHWPDPLVpIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLhtvQPPYNLFE- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 172 hpRLTQKELQAFCREQGIQMEAWSPLMQGQL--------------LDN-----------------EVLAEIAQKH-NKST 219
Cdd:cd19148 175 --REIEKDVLPYARKHNIVTLAYGALCRGLLsgkmtkdtkfegddLRRtdpkfqeprfsqylaavEELDKLAQERyGKSV 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1992844687 220 AQVILRWDLQNGVVTIP--KSTKEHRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19148 253 IHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
33-265 |
3.78e-25 |
|
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: 101.54 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYG---NEEGVGQGI---REGIQAA---GISREAlfvTSKVWNA-DLGYESTLKAYETS 102
Cdd:cd19078 26 EMIELIRKAVELGITFFDTAEVYGpytNEELVGEALkpfRDQVVIAtkfGFKIDG---GKPGPLGlDSRPEHIRKAVEGS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 103 LEKLGLEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIGVSNFQihhLEDLMKDAEIKPMIN-QVEYH--PR 174
Cdd:cd19078 103 LKRLQTDYIDLYYQHrvdpnVPIE----EVAGTMKELIKEGKIRHWGLSEAG---VETIRRAHAVCPVTAvQSEYSmmWR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 175 LTQKELQAFCREQGIQMEAWSPLMQGQLLDN-------------------------------EVLAEIAQKHNKSTAQVI 223
Cdd:cd19078 176 EPEKEVLPTLEELGIGFVPFSPLGKGFLTGKidentkfdegddraslprftpealeanqalvDLLKEFAEEKGATPAQIA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1992844687 224 LRWDLQNG--VVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDR 265
Cdd:cd19078 256 LAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-264 |
6.43e-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: 101.14 E-value: 6.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 42 IQHGYRSIDTAAIY-----GNEEGVGQGIREGIQAAGISREALFVTSKV--WNAD----LGYESTLKAYETSLEKLGLEY 110
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpGNAGGESETIIGRWLKSRGKRDRVVIATKVgfPMGPngpgLSRKHIRRAVEASLRRLQTDY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 111 LDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLE---DLMKDAEIKPMIN-QVEY---HPRLTQK 178
Cdd:cd19081 116 IDLYQAHWddpatPLE----ETLGALNDLIRQGKVRYIGASNYSAWRLQealELSRQHGLPRYVSlQPEYnlvDRESFEG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 179 ELQAFCREQGIQMEAWSPLMQGQL----------------------LDNE-------VLAEIAQKHNKSTAQVILRWDLQ 229
Cdd:cd19081 192 ELLPLCREEGIGVIPYSPLAGGFLtgkyrseadlpgstrrgeaakrYLNErglrildALDEVAAEHGATPAQVALAWLLA 271
|
250 260 270
....*....|....*....|....*....|....*..
gi 1992844687 230 NGVVTIP--KSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19081 272 RPGVTAPiaGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
18-256 |
6.95e-25 |
|
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: 99.60 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 18 MPWFGLGVFKVEEGPE-LVNAVKTAIQHGYRSIDTAAIYG---NEEGvgqgIREGIQAAGisrEALFVTSKV-------- 85
Cdd:cd19088 9 MRLTGPGIWGPPADREeAIAVLRRALELGVNFIDTADSYGpdvNERL----IAEALHPYP---DDVVIATKGglvrtgpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 86 -WNADLGYESTLKAYETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIK 163
Cdd:cd19088 82 wWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIdPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 164 PMINQveYHPRLTQKE-LQAFCREQGIQMEAWSPLMQGQLLDNEV-LAEIAQKHNKSTAQVILRWDLQ--NGVVTIPKST 239
Cdd:cd19088 162 SVQNR--YNLANRDDEgVLDYCEAAGIAFIPWFPLGGGDLAQPGGlLAEVAARLGATPAQVALAWLLArsPVMLPIPGTS 239
|
250
....*....|....*..
gi 1992844687 240 KEHRIAENAAVFDFELT 256
Cdd:cd19088 240 SVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
9-272 |
4.14e-24 |
|
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: 99.05 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTL-NNGVKMPWFGLGV--FKVEEGPELVNA-----VKTAIQHGYRSIDTAAIYG-NEEGVGQGIRegiQAAGiSREAL 79
Cdd:cd19144 3 TRTLgRNGPSVPALGFGAmgLSAFYGPPKPDEerfavLDAAFELGCTFWDTADIYGdSEELIGRWFK---QNPG-KREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 80 FVTSKVWN----------ADLGYESTLKAYETSLEKLGLEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIG 144
Cdd:cd19144 79 FLATKFGIeknvetgeysVDGSPEYVKKACETSLKRLGVDYIDLYYQHrvdgkTPIE----KTVAAMAELVQEGKIKHIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 145 VSNFQIhhlEDLMKDAEIKPMIN-QVEYHPRLTQKE------LQAfCREQGIQMEAWSPLMQG----------------- 200
Cdd:cd19144 155 LSECSA---ETLRRAHAVHPIAAvQIEYSPFSLDIErpeigvLDT-CRELGVAIVAYSPLGRGfltgairspddfeegdf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 201 ----------------QLLDNevLAEIAQKHNKSTAQVILRWDLQNG--VVTIPKSTKEHRIAENAAVFDFELTKEEMEQ 262
Cdd:cd19144 231 rrmaprfqaenfpknlELVDK--IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKE 308
|
330
....*....|
gi 1992844687 263 IDRLNQNLRV 272
Cdd:cd19144 309 IREIAEEAEV 318
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-250 |
6.38e-24 |
|
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: 96.78 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 19 PWFGlgvfKVEEGpELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGiqaagisREALFVTSKV---------W 86
Cdd:cd19086 16 DWWG----DVDDA-EAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFgnrfdggpeR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 87 NADLGYESTLKAYETSLEKLGLEYLDLYLIH-WPVEGKYKD-AWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKP 164
Cdd:cd19086 84 PQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDeLFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGIDV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 165 MinQVEYHP--RLTQKELQAFCREQGIQMEAWSPLMQGqLLDNEvLAEIAqkhnkstaqviLRWDLQNGVVT--IPKSTK 240
Cdd:cd19086 164 V--QVIYNLldQRPEEELFPLAEEHGVGVIARVPLASG-LLTGK-LAQAA-----------LRFILSHPAVStvIPGARS 228
|
250
....*....|
gi 1992844687 241 EHRIAENAAV 250
Cdd:cd19086 229 PEQVEENAAA 238
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-250 |
1.42e-22 |
|
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: 93.45 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 15 GVKMPWFGLGVFKVEEGPELVNavkTAIQHGYRSIDTAAIYGNEEgvgqgIREGIQAAGISREALFVTSKVW-------- 86
Cdd:cd19095 6 GTSGIGRVWGVPSEAEAARLLN---TALDLGINLIDTAPAYGRSE-----ERLGRALAGLRRDDLFIATKVGthgeggrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 87 NADLGYESTLKAYETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQiHHLEDLMKDAEIKpM 165
Cdd:cd19095 78 RKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPsDDELTGEVLETLEDLKAAGKVRYIGVSGDG-EELEAAIASGVFD-V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 166 InQVEYHPrLTQKELQAF--CREQGIQMEAWSPLMQGQLLDNE-----------VLAEIAQKHNKSTAQVILRWDLQNGV 232
Cdd:cd19095 156 V-QLPYNV-LDREEEELLplAAEAGLGVIVNRPLANGRLRRRVrrrplyadyarRPEFAAEIGGATWAQAALRFVLSHPG 233
|
250 260
....*....|....*....|
gi 1992844687 233 VT--IPKSTKEHRIAENAAV 250
Cdd:cd19095 234 VSsaIVGTTNPEHLEENLAA 253
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
38-258 |
2.42e-22 |
|
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: 93.81 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 38 VKTAIQHGYRSIDTAAIYGN---EEGVGQGIRegiqaaGISREALFVTSKV-WNADLG-YESTL------KAYETSLEKL 106
Cdd:cd19074 28 VRKAYDLGINFFDTADVYAAgqaEEVLGKALK------GWPRESYVISTKVfWPTGPGpNDRGLsrkhifESIHASLKRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 107 GLEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAE----IKPMINQVEYH--PRL 175
Cdd:cd19074 102 QLDYVDIYYCHrydpeTPLE----ETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYNmlWRE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 176 TQKELQAFCREQGIQMEAWSPLMQG----------------------------QLLDNEVLA------EIAQKHNKSTAQ 221
Cdd:cd19074 178 IEEEVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrRLLTDENLEkvkklkPIADELGLTLAQ 257
|
250 260 270
....*....|....*....|....*....|....*....
gi 1992844687 222 VILRWDLQNGVVT--IPKSTKEHRIAENAAVFDFELTKE 258
Cdd:cd19074 258 LALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-226 |
2.53e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 93.92 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 21 FGLGVFKVEEG----PELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGIQAAGISREALFVTSKV-------- 85
Cdd:cd19099 6 LGLGTYRGDSDdetdEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 86 ---------WNADLGYESTLK-----------AY-----ETSLEKLGLEYLDLYLIHWPVEG-----------KYKDAWK 129
Cdd:cd19099 86 eplrplkylEEKLGRGLIDVAdsaglrhcispAYledqiERSLKRLGLDTIDLYLLHNPEEQllelgeeefydRLEEAFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 130 ALETLYKDGRVKAIGVS----------NFQIHHLEDLMKDAEIKPMIN------QVEYHPRLTQ------------KELQ 181
Cdd:cd19099 166 ALEEAVAEGKIRYYGIStwdgfrappaLPGHLSLEKLVAAAEEVGGDNhhfkviQLPLNLLEPEaltekntvkgeaLSLL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1992844687 182 AFCREQGIQMEAWSPLMQGQLLDNEVLAEI-AQKHNKSTAQVILRW 226
Cdd:cd19099 246 EAAKELGLGVIASRPLNQGQLLGELRLADLlALPGGATLAQRALQF 291
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-266 |
2.53e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 93.94 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGneEGVGQGIReGIQAAGISREALFVTSKV--WNADLGYESTLKAYETSLEKLGLEY 110
Cdd:cd19103 33 TLKAVFDKAMAAGLNLWDTAAVYG--MGASEKIL-GEFLKRYPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 111 LDLYLIHWP--VEGkykdaW-KALETLYKDGRVKAIGVSNF---QIHHLEDLMKDAEIKpmINQVEYHPRLTQKE----- 179
Cdd:cd19103 110 IDIYWIHNPadVER-----WtPELIPLLKSGKVKHVGVSNHnlaEIKRANEILAKAGVS--LSAVQNHYSLLYRSseeag 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 180 LQAFCREQGIQMEAWSPLMQGQLLD----------------------------NEVLAEIAQKHNKSTAQVILRWDLQNG 231
Cdd:cd19103 183 ILDYCKENGITFFAYMVLEQGALSGkydtkhplpegsgraetynpllpqleelTAVMAEIGAKHGASIAQVAIAWAIAKG 262
|
250 260 270
....*....|....*....|....*....|....*
gi 1992844687 232 VVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19103 263 TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-249 |
2.33e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 89.85 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 21 FGLGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGN-EEGVGQGIREGiqaagisREALFVTSKVWNADlgYESTLKAY 99
Cdd:cd19100 16 FGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARD--YEGAKRDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 100 ETSLEKLGLEYLDLYLIH-------WPVEGKYKDAWKALETLYKDGRVKAIGVSNfqiHHLEDLMKDAEIKPM------I 166
Cdd:cd19100 87 ERSLKRLGTDYIDLYQLHavdteedLDQVFGPGGALEALLEAKEEGKIRFIGISG---HSPEVLLRALETGEFdvvlfpI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 167 NQVEYHPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEVLaeiaqkhnksTAQVILRWDLQNGVVTIP----KSTKEh 242
Cdd:cd19100 164 NPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPL----------DPEQALRYALSLPPVDVVivgmDSPEE- 232
|
....*..
gi 1992844687 243 rIAENAA 249
Cdd:cd19100 233 -LDENLA 238
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
32-263 |
2.41e-21 |
|
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: 91.34 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 32 PELVNAVKTAIQHGYRSIDTAAIYG---NEEGVGQ----GIREGIQAA---GIsREALFVTSKVwNADLGYesTLKAYET 101
Cdd:cd19145 33 EEGIALIHHAFNSGVTFLDTSDIYGpntNEVLLGKalkdGPREKVQLAtkfGI-HEIGGSGVEV-RGDPAY--VRAACEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 102 SLEKLGLEYLDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIhhlEDLMKDAEIKPMIN-QVEYH--P 173
Cdd:cd19145 109 SLKRLDVDYIDLYYQHRidttvPIE----ITMGELKKLVEEGKIKYIGLSEASA---DTIRRAHAVHPITAvQLEWSlwT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 174 RLTQKELQAFCREQGIQMEAWSPL--------------------------MQGQLLD-NEVLAE----IAQKHNKSTAQV 222
Cdd:cd19145 182 RDIEEEIIPTCRELGIGIVPYSPLgrgffagkakleellensdvrkshprFQGENLEkNKVLYErveaLAKKKGCTPAQL 261
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1992844687 223 ILRWDLQNG--VVTIPKSTKEHRIAENAAVFDFELTKEEMEQI 263
Cdd:cd19145 262 ALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-234 |
4.10e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 89.57 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 9 TTTL-NNGVKMPWFGLGVfkVEEGPELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIRegiqaaGISREALFVTSK 84
Cdd:cd19105 3 YRTLgKTGLKVSRLGFGG--GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 85 VWNAD--LGYESTLKAYETSLEKLGLEYLDLYLIH---WPVEGKYKDAW-KALETLYKDGRVKAIGVS--NFQIHHLEDL 156
Cdd:cd19105 75 ASPRLdkKDKAELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELlEALEKLKKEGKVRFIGFSthDNMAEVLQAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 157 MKDAE---IKPMINQVEYHPRLtqKELQAFCREQGI---QMEAWSPLMQGQLLDNEVLAEIAqkhnkSTAQVILRWDLQN 230
Cdd:cd19105 155 IESGWfdvIMVAYNFLNQPAEL--EEALAAAAEKGIgvvAMKTLAGGYLQPALLSVLKAKGF-----SLPQAALKWVLSN 227
|
....
gi 1992844687 231 GVVT 234
Cdd:cd19105 228 PRVD 231
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
13-259 |
1.26e-20 |
|
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: 89.24 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 13 NNGVKMPWFGLGV---FKVEEGPELVNA-VKTAIQHGYRSIDTAAIYGNEEG-----VGQGIREGIQAagiSREALFVTS 83
Cdd:cd19089 6 RSGLHLPAISLGLwhnFGDYTSPEEARElLRTAFDLGITHFDLANNYGPPPGsaeenFGRILKRDLRP---YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 84 KV----WNADLGYESTLK----AYETSLEKLGLEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIGVSNF-- 148
Cdd:cd19089 83 KAgygmWPGPYGDGGSRKyllaSLDQSLKRMGLDYVDIFYHHrydpdTPLE----ETMTALADAVRSGKALYVGISNYpg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 149 -QIHHLEDLMKDAEIKPMINQVEYH--PRLTQKELQAFCREQGIQMEAWSPLMQGQLLDN-------------------- 205
Cdd:cd19089 159 aKARRAIALLRELGVPLIIHQPRYSllDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKylngippdsrraaeskflte 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1992844687 206 -----------EVLAEIAQKHNKSTAQVILRWDLQNGVVT---IPKSTKEHRIAENAAVFDFELTKEE 259
Cdd:cd19089 239 ealtpekleqlRKLNKIAAKRGQSLAQLALSWVLRDPRVTsvlIGASSPSQLEDNVAALKNLDFSEEE 306
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
38-252 |
1.32e-20 |
|
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: 88.39 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 38 VKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGiqaagiSREALFVTSKV-WNADLGYESTLKAYETSLEKLGLEYLDL 113
Cdd:cd19096 27 IRYAIDAGINYFDTAYGYGGgksEEILGEALKEG------PREKFYLATKLpPWSVKSAEDFRRILEESLKRLGVDYIDF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 114 YLIHWPVEGKYKD------AWKALETLYKDGRVKAIGVSnfqIHhledlMKDAEIKPMIN-------QVEYH----PRLT 176
Cdd:cd19096 101 YLLHGLNSPEWLEkarkggLLEFLEKAKKEGLIRHIGFS---FH-----DSPELLKEILDsydfdfvQLQYNyldqENQA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 177 QKELQAFCREQG---IQMEawsPLMQGQLLDN-EVLAEIAQKHNKSTAQVILRWDLQNG---VVTIPKSTKEHrIAENAA 249
Cdd:cd19096 173 GRPGIEYAAKKGmgvIIME---PLKGGGLANNpPEALAILCGAPLSPAEWALRFLLSHPevtTVLSGMSTPEQ-LDENIA 248
|
...
gi 1992844687 250 VFD 252
Cdd:cd19096 249 AAD 251
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-226 |
1.96e-20 |
|
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: 88.77 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 18 MPWFGLGVF-KVEEGPELVNAVKtaiQHGYRSIDTAAIYGN---EEGVGQgIREGIQAAGISREALFVTSKvwnaDLGYE 93
Cdd:cd19075 8 MTFGSQGRFtTAEAAAELLDAFL---ERGHTEIDTARVYPDgtsEELLGE-LGLGERGFKIDTKANPGVGG----GLSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 94 STLKAYETSLEKLGLEYLDLYLIHWP-----VEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAE----IKP 164
Cdd:cd19075 80 NVRKQLETSLKRLKVDKVDVFYLHAPdrstpLE----ETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 165 MINQVEYHP--RLTQKELQAFCREQGIQMEAWSPL-------------------------MQGQLLDN-----------E 206
Cdd:cd19075 156 TVYQGMYNAitRQVETELFPCLRKLGIRFYAYSPLaggfltgkykysedkagggrfdpnnALGKLYRDrywkpsyfealE 235
|
250 260
....*....|....*....|
gi 1992844687 207 VLAEIAQKHNKSTAQVILRW 226
Cdd:cd19075 236 KVEEAAEKEGISLAEAALRW 255
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
49-264 |
2.05e-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: 88.82 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 49 IDTAAIYGN---EEGVGQGIREgiqaagiSREALFVTSK-VWNADLG--------YESTLKAYETSLEKLGLEYLDLYLI 116
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKyTMNRRPGdpnaggnhRKNLRRSVEASLRRLQTDYIDLLYV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 117 HW-----PVEgkykDAWKALETLYKDGRVKAIGVSNF------------QIHHLEdlmkdaeikPMIN-QVEYH--PRLT 176
Cdd:cd19080 121 HAwdfttPVE----EVMRALDDLVRAGKVLYVGISDTpawvvarantlaELRGWS---------PFVAlQIEYSllERTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 177 QKELQAFCREQGIQMEAWSPLMQGQL------------------------LDN------EVLAEIAQKHNKSTAQVILRW 226
Cdd:cd19080 188 ERELLPMARALGLGVTPWSPLGGGLLtgkyqrgeegrageakgvtvgfgkLTErnwaivDVVAAVAEELGRSAAQVALAW 267
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1992844687 227 DLQNGVVTIP--KSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19080 268 VRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
20-255 |
8.44e-19 |
|
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: 83.76 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 20 WFGlGVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGN-EEGVGQGIREgiqaagISREALFVTSKV-----WNADLGYE 93
Cdd:cd19090 9 GLG-GVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeDTADYSAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 94 STLKAYETSLEKLGLEYLDLYLIH------WPVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMIN 167
Cdd:cd19090 82 RVRRSVEESLERLGRDRIDLLMIHdpervpWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGDFDVVLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 168 QVEYHPrLTQKELQAF---CREQGIQMEAWSPLMQG---------------QLLDNEV-----LAEIAQKHNKSTAQVIL 224
Cdd:cd19090 162 ANRYTL-LDQSAADELlpaAARHGVGVINASPLGMGllagrppervrytyrWLSPELLdrakrLYELCDEHGVPLPALAL 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1992844687 225 RWDLQN----GVVTIPkSTKEHrIAENAAVFDFEL 255
Cdd:cd19090 241 RFLLRDprisTVLVGA-SSPEE-LEQNVAAAEGPL 273
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-230 |
4.78e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 81.42 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 38 VKTAIQHGYRSIDTAAIYGN-EEGVGQgiregiqaAGISREALFVTSKV----WNADLGYESTLKAYETSLEKLGLEYLD 112
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGDsEKVLGK--------FLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 113 LYLIHWP--VEGKYKDAWKALETLYKDGRVKAIGVSnfqIHHLEDLmKDAEIKPMIN--QVEYHP---RLTQKELQAFCR 185
Cdd:cd19097 104 GLLLHNPddLLKHGGKLVEALLELKKEGLIRKIGVS---VYSPEEL-EKALESFKIDiiQLPFNIldqRFLKSGLLAKLK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 186 EQGIQMEAWSPLMQGQLLDNEV---------------LAEIAQKHNKSTAQVILRWDLQN 230
Cdd:cd19097 180 KKGIEIHARSVFLQGLLLMEPDklpakfapakpllkkLHELAKKLGLSPLELALGFVLSL 239
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
13-261 |
5.29e-18 |
|
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: 81.83 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 13 NNGVKMPWFGLG------VFK-VEEGpELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIRegiqaaGISREALFVT 82
Cdd:cd19163 8 KTGLKVSKLGFGasplggVFGpVDEE-EAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK------GIPRDSYYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 83 SKV------WNA--DLGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKD-----AWKALETLYKDGRVKAIGVSNFQ 149
Cdd:cd19163 81 TKVgrygldPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDqilneTLPALQKLKEEGKVRFIGITGYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 150 IHHLEDLMKDAEIKpmINQVEYHPRLTQ-----KELQAFCREQGIQMEAWSPLMQGQLLDN----------EV------L 208
Cdd:cd19163 161 LDVLKEVLERSPVK--IDTVLSYCHYTLndtslLELLPFFKEKGVGVINASPLSMGLLTERgppdwhpaspEIkeacakA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1992844687 209 AEIAQKHNKSTAQVILRWDLQN--GVVTIPKSTKEHRIAENAAVFDFELTKEEME 261
Cdd:cd19163 239 AAYCKSRGVDISKLALQFALSNpdIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
40-236 |
6.48e-18 |
|
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: 81.45 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 40 TAIQHGYRSIDTAAIYGNEEGVG---QGIREGIQAAGIsREALFVTSK--------VWNADLGYESTLKAYETSLEKLGL 108
Cdd:cd19082 25 AFVELGGNFIDTARVYGDWVERGaseRVIGEWLKSRGN-RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 109 EYLDLYLIHW-----PVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIK----PMINQVEY------HP 173
Cdd:cd19082 104 DYIDLYFLHRddpsvPVG----EIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHglpgFAASSPQWslarpnEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 174 RL-------TQKELQAFCREQGIQMEAWSPLMQG-----------------QLLDNEV-------LAEIAQKHNKSTAQV 222
Cdd:cd19082 180 PWpgptlvaMDEEMRAWHEENQLPVFAYSSQARGffskraaggaeddselrRVYYSEEnferlerAKELAEEKGVSPTQI 259
|
250
....*....|....
gi 1992844687 223 ILRWDLQNGVVTIP 236
Cdd:cd19082 260 ALAYVLNQPFPTVP 273
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
13-261 |
2.45e-17 |
|
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: 80.14 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 13 NNGVKMPWFGLGVF-------KVEEGPELVnavKTAIQHGYRSIDTAAIYG-----NEEGVGQGIREGIQAagiSREALF 80
Cdd:cd19151 7 RSGLKLPAISLGLWhnfgdvdRYENSRAML---RRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKP---YRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 81 VTSK----VWNA---DLGYESTLKA-YETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNF--- 148
Cdd:cd19151 81 ISTKagytMWPGpygDWGSKKYLIAsLDQSLKRMGLDYVDIFYHHRPdPETPLEETMGALDQIVRQGKALYVGISNYppe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 149 QIHHLEDLMKDAEIKPMINQVEYH--PRLTQKELQAFCREQGIQMEAWSPLMQGQLLDN--------------------- 205
Cdd:cd19151 161 EAREAAAILKDLGTPCLIHQPKYSmfNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRylngipedsraakgssflkpe 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1992844687 206 ----EVLA------EIAQKHNKSTAQVILRWDLQNGVVT--IPKSTKEHRIAEN-AAVFDFELTKEEME 261
Cdd:cd19151 241 qiteEKLAkvrrlnEIAQARGQKLAQMALAWVLRNKRVTsvLIGASKPSQIEDAvGALDNREFSEEELA 309
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
33-249 |
8.33e-17 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 78.55 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGneEGVGQgIREGIQAAGISREALFVTSKV------------------WnaDLGYES 94
Cdd:cd19162 20 EAAATLDAAWDAGIRYFDTAPLYG--LGLSE-RRLGAALARHPRAEYVVSTKVgrllepgaagrpagadrrF--DFSADG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 95 TLKAYETSLEKLGLEYLDLYLIHWPVEGKYK---DAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQVEY 171
Cdd:cd19162 95 IRRSIEASLERLGLDRLDLVFLHDPDRHLLQaltDAFPALEELRAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGRY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 172 H--PRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEV--------------------LAEIAQKHNKSTAQVILRWDLQ 229
Cdd:cd19162 175 TllDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPagdrydyrpatpevlararrLAAVCRRYGVPLPAAALQFPLR 254
|
250 260
....*....|....*....|....
gi 1992844687 230 N----GVVTIPKSTKEhrIAENAA 249
Cdd:cd19162 255 HpavaSVVVGAASPAE--LRDNLA 276
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
49-266 |
7.75e-16 |
|
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: 76.07 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 49 IDTAAIYGN---EEGVGQGIREgiqaagiSREALFVTSKVwnadlgYEST--------------LKAYETSLEKLGLEYL 111
Cdd:cd19087 47 FDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKV------FGPMgddpndrglsrrhiRRAVEASLRRLQTDYI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 112 DLYLIH-WPVEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHL---------EDLMKDAEIKPMINQVEYHPRLtqkELQ 181
Cdd:cd19087 114 DLYQMHhFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIakaqgiaarRGLLRFVSEQPMYNLLKRQAEL---EIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 182 AFCREQGIQMEAWSPL---------------MQGQLLDNEV----------------LAEIAQKHNKSTAQVILRWDLQN 230
Cdd:cd19087 191 PAARAYGLGVIPYSPLagglltgkygkgkrpESGRLVERARyqarygleeyrdiaerFEALAAEAGLTPASLALAWVLSH 270
|
250 260 270
....*....|....*....|....*....|....*....
gi 1992844687 231 GVVTIP---KSTKEHrIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19087 271 PAVTSPiigPRTLEQ-LEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
41-266 |
1.04e-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: 75.68 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 41 AIQHGYRSIDTAAIY---GNEEGVGQG---IREGIQAAGiSREALFVTSKV--------W----NADLGYESTLKAYETS 102
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvpPSPETQGRTeeiIGSWLKKKG-NRDKVVLATKVagpgegitWprggGTRLDRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 103 LEKLGLEYLDLYLIHWPV-------EGKYKDAWK------------ALETLYKDGRVKAIGVSN---FQIHHLEDLMKDA 160
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPDrytplfgGGYYTEPSEeedsvsfeeqleALGELVKAGKIRHIGLSNetpWGVMKFLELAEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 161 EIKPMIN-QVEYHpRLTQK---ELQAFCREQGIQMEAWSPLMQGQL----LDNE-------------------------- 206
Cdd:cd19094 186 GLPRIVSiQNPYS-LLNRNfeeGLAEACHRENVGLLAYSPLAGGVLtgkyLDGAarpeggrlnlfpgymaryrspqalea 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1992844687 207 --VLAEIAQKHNKSTAQVILRWDLQNGVVT---IPKSTKEhRIAENAAVFDFELTKEEMEQIDRL 266
Cdd:cd19094 265 vaEYVKLARKHGLSPAQLALAWVRSRPFVTstiIGATTLE-QLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
37-264 |
1.29e-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: 75.35 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 37 AVKTAIQHGYRSIDTAAIYGNEEGVG--QGIREGIQAAGISREALFVTSKV-WN-----ADLGYESTLKAYETSLEKLG- 107
Cdd:cd19077 30 TMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKGgLDpdtlrPDGSPEAVRKSIENILRALGg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 108 LEYLDLYLI-----HWPVEgkykDAWKALETLYKDGRVKAIGVSNFQihhLEDLMKDAEIKPM-INQVEYHPRLTQKE-- 179
Cdd:cd19077 110 TKKIDIFEParvdpNVPIE----ETIKALKELVKEGKIRGIGLSEVS---AETIRRAHAVHPIaAVEVEYSLFSREIEen 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 180 -LQAFCREQGIQMEAWSPLMQG------------------QLLDN-------------EVLAEIAQKHNKSTAQVILRWD 227
Cdd:cd19077 183 gVLETCAELGIPIIAYSPLGRGlltgriksladipegdfrRHLDRfngenfeknlklvDALQELAEKKGCTPAQLALAWI 262
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1992844687 228 LQNG---VVTIPKSTKEHRIAENAAVFDFELTKEEMEQID 264
Cdd:cd19077 263 LAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-249 |
2.55e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 74.29 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 42 IQHGYRSIDTAAIYG--NEEGVG----QGIREGIQAAGiSREALFVTSKV---------WNAD---LGYESTLKAYETSL 103
Cdd:cd19752 27 VAAGGNFLDTANNYAfwTEGGVGgeseRLIGRWLKDRG-NRDDVVIATKVgagprdpdgGPESpegLSAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 104 EKLGLEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAE----------------I 162
Cdd:cd19752 106 RRLGTDYIDLYYAHvddrdTPLE----ETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARqqgwaefsaiqqrhsyL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 163 KPMINQVEYHPRLTQKELQAFCREQG-IQMEAWSPLMQGQLLDNE-----------------VLAEIAQKHNKSTAQVIL 224
Cdd:cd19752 182 RPRPGADFGVQRIVTDELLDYASSRPdLTLLAYSPLLSGAYTRPDrplpeqydgpdsdarlaVLEEVAGELGATPNQVVL 261
|
250 260
....*....|....*....|....*...
gi 1992844687 225 RWDLQNGVVTIP---KSTKEHrIAENAA 249
Cdd:cd19752 262 AWLLHRTPAIIPllgASTVEQ-LEENLA 288
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
29-165 |
5.50e-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: 70.64 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 29 EEGPELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIRegiqAAGISREALFVTSKV-----WNADLGYESTLKAYE 100
Cdd:cd19153 30 LEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALA----ALQVPRSSYTVATKVgryrdSEFDYSAERVRASVA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 101 TSLEKLGLEYLDLYLIHwPVE-GKY----KDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPM 165
Cdd:cd19153 106 TSLERLHTTYLDVVYLH-DIEfVDYdtlvDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSL 174
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
24-254 |
1.75e-12 |
|
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: 66.09 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 24 GVFKVEEGPELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREgiqaagISREALFVTSKV--------------- 85
Cdd:cd19152 12 NLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE------LGREDYVISTKVgrllvplqeveptfe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 86 ---WNA-------DLGYESTLKAYETSLEKLGLEYLDLYLIHWPVEGKYKDAWK------------ALETLYKDGRVKAI 143
Cdd:cd19152 86 pgfWNPlpfdavfDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafrALEELREEGVIKAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 144 GV-SNF-----QIHHLEDLmkDAEikpMI-NQveYHPrLTQKELQAF---CREQGIQMEAWSPLMQGQL----------- 202
Cdd:cd19152 166 GLgVNDwevilRILEEADL--DWV---MLaGR--YTL-LDHSAARELlpeCEKRGVKVVNAGPFNSGFLaggdnfdyyey 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1992844687 203 --LDNEVLA------EIAQKHNKSTAQVILRWDLQNGVVT--IPKSTKEHRIAENAAVFDFE 254
Cdd:cd19152 238 gpAPPELIArrdrieALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVALLATE 299
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-266 |
7.86e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 64.59 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 33 ELVNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREgiqaagiSREALFVTSKVwnaDLGYESTLKAY-------ETS 102
Cdd:cd19104 33 EQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKG-------LPAGPYITTKV---RLDPDDLGDIGgqiersvEKS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 103 LEKLGLEYLDLYLIH--------WPVEGK--------YKDAWKALETLYKDGRVKAIGVSNF-QIHHLEDLMKDAeiKPM 165
Cdd:cd19104 103 LKRLKRDSVDLLQLHnrigderdKPVGGTlsttdvlgLGGVADAFERLRSEGKIRFIGITGLgNPPAIRELLDSG--KFD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 166 INQVEY--------------HPRLTQKELQAFCREQGIQMEAWSPLMQGQLLDNEV----------------------LA 209
Cdd:cd19104 181 AVQVYYnllnpsaaearprgWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTTSLDrgreapptsdsdvaidfrraaaFR 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1992844687 210 EIAQKHNKSTAQVILRWDLQN-GVVTIP---KSTKEHRIAENAAVFDfELTKEEMEQIDRL 266
Cdd:cd19104 261 ALAREWGETLAQLAHRFALSNpGVSTVLvgvKNREELEEAVAAEAAG-PLPAENLARLEAL 320
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
38-264 |
1.03e-11 |
|
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: 64.15 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 38 VKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGiqaaGISREALFVTSKV-WNADLGYEST--------LKAYETSLEK 105
Cdd:cd19143 37 MKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKEL----GWPRSDYVVSTKIfWGGGGPPPNDrglsrkhiVEGTKASLKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 106 LGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSN---FQI---------HHLedlmkdaeIKPMINQVEY- 171
Cdd:cd19143 113 LQLDYVDLVFCHRPdPATPIEETVRAMNDLIDQGKAFYWGTSEwsaQQIeeaheiadrLGL--------IPPVMEQPQYn 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 172 --HPRLTQKELQAFCREQGIQMEAWSPLMQGQL---------------------LDNEV-------------LAEIAQKH 215
Cdd:cd19143 185 lfHRERVEVEYAPLYEKYGLGTTTWSPLASGLLtgkynngipegsrlalpgyewLKDRKeelgqekiekvrkLKPIAEEL 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1992844687 216 NKSTAQVILRWDLQNGVV--TIPKSTKEHRIAENAAVFDF--ELTKEEMEQID 264
Cdd:cd19143 265 GCSLAQLAIAWCLKNPNVstVITGATKVEQLEENLKALEVlpKLTPEVMEKIE 317
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
14-265 |
4.09e-11 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 62.70 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 14 NGVKMPWFGLGVFK----VEEGPELVNAVKTAIQHGYRSIDTAAIYG-----NEEGVGQGIREGIQAAgisREALFVTSK 84
Cdd:PRK09912 21 SGLRLPALSLGLWHnfghVNALESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAY---RDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 85 ----VWNADLGYEST----LKAYETSLEKLGLEYLDLYLIHWPVEGK-YKDAWKALETLYKDGRVKAIGVSNF---QIHH 152
Cdd:PRK09912 98 agydMWPGPYGSGGSrkylLASLDQSLKRMGLEYVDIFYSHRVDENTpMEETASALAHAVQSGKALYVGISSYspeRTQK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 153 LEDLMKDAEIKPMINQVEYH--PRLTQKE-LQAFCREQGIQMEAWSPLMQGQLLDN------------------------ 205
Cdd:PRK09912 178 MVELLREWKIPLLIHQPSYNllNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdsrmhregnkvrgltpk 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992844687 206 ----------EVLAEIAQKHNKSTAQVILRWDLQNGVVT--IPKSTKEHRIAEN-AAVFDFELTKEEMEQIDR 265
Cdd:PRK09912 258 mlteanlnslRLLNEMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENvQALNNLTFSTEELAQIDQ 330
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
38-261 |
1.31e-10 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 60.93 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 38 VKTAIQHGYRSIDTAAIYG-----NEEGVGQGIREGIQAagiSREALFVTSK----VWNADLG----YESTLKAYETSLE 104
Cdd:cd19150 36 LRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAG---YRDELIISTKagydMWPGPYGewgsRKYLLASLDQSLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 105 KLGLEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIGVSNF---QIHHLEDLMKDAEIKPMINQVEYH--PR 174
Cdd:cd19150 113 RMGLDYVDIFYSHrfdpdTPLE----ETMGALDHAVRSGKALYVGISSYspeRTREAAAILRELGTPLLIHQPSYNmlNR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 175 LTQK-ELQAFCREQGIQMEAWSPLMQGQLLDN------------------------------EVLAEIAQKHNKSTAQVI 223
Cdd:cd19150 189 WVEEsGLLDTLQELGVGCIAFTPLAQGLLTDKylngipegsraskerslspkmlteanlnsiRALNEIAQKRGQSLAQMA 268
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1992844687 224 LRWDLQNGVVT---IPKSTKEhRIAENAAVFD-FELTKEEME 261
Cdd:cd19150 269 LAWVLRDGRVTsalIGASRPE-QLEENVGALDnLTFSADELA 309
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-267 |
1.34e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 57.67 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 1 MTAKNLQDTTTL-NNGVK------MPWFGLGVFKVEEGPELVNAV-KTAIQHGYRSIDTAAIYG----NeegvgQGIREG 68
Cdd:PRK10376 1 MSTIMSSGTFTLgGRSVNrlgygaMQLAGPGVFGPPKDRDAAIAVlREAVALGVNHIDTSDFYGphvtN-----QLIREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 69 IQAagiSREALFVTSKV---------WNADLGYESTLKAYETSLEKLGLEYLDL------YLIHWPVEGKYKDAWKALET 133
Cdd:PRK10376 76 LHP---YPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEGSIEEPLTVLAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 134 LYKDGRVKAIGVSNFQIHHLEDLMKDAEIKPMINQveYHprLTQKELQAFC---REQGIQMEAWSPLMQGQLLDNEVLAE 210
Cdd:PRK10376 153 LQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNH--YN--LAHRADDALIdalARDGIAYVPFFPLGGFTPLQSSTLSD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1992844687 211 IAQKHNKSTAQVILRWDLQNG--VVTIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLN 267
Cdd:PRK10376 229 VAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
37-270 |
3.66e-09 |
|
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: 56.57 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 37 AVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREgiqaagISREALFVTSKV-----------------W--------NA 88
Cdd:cd19161 25 TLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE------KPRDEFVLSTKVgrllkparegsvpdpngFvdplpfeiVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 89 DLGYESTLKAYETSLEKLGLEYLDLYLIH-----WPVEGKYKDAW--------KALETLYKDGRVKAI--GVSNFQIhhL 153
Cdd:cd19161 99 DYSYDGIMRSFEDSLQRLGLNRIDILYVHdigvyTHGDRKERHHFaqlmsggfKALEELKKAGVIKAFglGVNEVQI--C 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 154 EDLMKDAEIKPMINQVEYH--PRLTQKELQAFCREQGIQMEAWSPLMQGqLLDNEVLAEIAQKHNKSTAQVILRwdlqng 231
Cdd:cd19161 177 LEALDEADLDCFLLAGRYSllDQSAEEEFLPRCEQRGTSLVIGGVFNSG-ILATGTKSGAKFNYGDAPAEIISR------ 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1992844687 232 VVTIPKSTKEHRIAENAAVFDFELTKEEMEQI-------DRLNQNL 270
Cdd:cd19161 250 VMEIEKICDAYNVPLAAAALQFPLRHPAVASVltgarnpAQLRQNV 295
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
41-268 |
5.63e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 41 AIQHGYRSIDTAAIYG-NEEGVGQGIREG-----IQAAGiSREALFVTSKVWNADLGYESTLK------------AYETS 102
Cdd:PRK10625 39 AVAQGINLIDVAEMYPvPPRPETQGLTETyignwLAKRG-SREKLIIASKVSGPSRNNDKGIRpnqaldrknireALHDS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 103 LEKLGLEYLDLYLIHWPVE-----GKYKDAWKA-------LETL------YKDGRVKAIGVSN------FQIHHLEDLMK 158
Cdd:PRK10625 118 LKRLQTDYLDLYQVHWPQRptncfGKLGYSWTDsapavslLETLdalaeqQRAGKIRYIGVSNetafgvMRYLHLAEKHD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 159 DAEIKPMINQVEYHPRLTQKELQAFCREQGIQMEAWSPL----MQGQLLD-----------------------NEVLAE- 210
Cdd:PRK10625 198 LPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLafgtLTGKYLNgakpagarntlfsrftrysgeqtQKAVAAy 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1992844687 211 --IAQKHNKSTAQVILRWDLQNGVV--TIPKSTKEHRIAENAAVFDFELTKEEMEQIDRLNQ 268
Cdd:PRK10625 278 vdIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
14-197 |
2.00e-07 |
|
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: 51.31 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 14 NGVKMPWFGLGVFKV------EEGPELVnaVKTAIQHGYRSIDTAAIYGN---EEGVGQGIREGiqaaGISREALFVTSK 84
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaisEEQAEEI--VTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 85 V-WN-----ADLGYESTLKAYETSLEKLGLEYLDLYLIH-----WPVEgkykDAWKALETLYKDGRVKAIGVSNFQIHHL 153
Cdd:cd19142 83 IyWSygseeRGLSRKHIIESVRASLRRLQLDYIDIVIIHkadpmCPME----EVVRAMSYLIDNGLIMYWGTSRWSPVEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 154 EDLMKDAE----IKPMINQVEYHPrltqkelqaFCREQ------------GIQMEAWSPL 197
Cdd:cd19142 159 MEAFSIARqfncPTPICEQSEYHM---------FCREKmelympelynkvGVGLITWSPL 209
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
21-146 |
7.85e-07 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 49.58 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 21 FGLGVF--KVEEGPE---LVNAVKTAIQHGYRSIDTAAIYGNEEGV-GQGIRegIQAAGISREALFVTSKV-----WNAD 89
Cdd:cd19164 18 FGAATFsyQYTTDPEsipPVDIVRRALELGIRAFDTSPYYGPSEIIlGRALK--ALRDEFPRDTYFIITKVgrygpDDFD 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1992844687 90 LGYESTLKAYETSLEKLGLEYLDLYLIHwPVE----GKYKDAWKALETLYKDGRVKAIGVS 146
Cdd:cd19164 96 YSPEWIRASVERSLRRLHTDYLDLVYLH-DVEfvadEEVLEALKELFKLKDEGKIRNVGIS 155
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
35-146 |
1.81e-05 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 45.15 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 35 VNAVKTAIQHGYRSIDTAAIYGN---EEGVGQGIRegiqAAGISREALFVTSK----VWNADLGYESTLKAYETSLEKLG 107
Cdd:PLN02587 34 IASVREAFRLGINFFDTSPYYGGtlsEKVLGKALK----ALGIPREKYVVSTKcgryGEGFDFSAERVTKSVDESLARLQ 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1992844687 108 LEYLDLYLIHwPVEGKYKD-----AWKALETLYKDGRVKAIGVS 146
Cdd:PLN02587 110 LDYVDILHCH-DIEFGSLDqivneTIPALQKLKESGKVRFIGIT 152
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
14-200 |
6.32e-05 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 43.88 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 14 NGVKMPWFGLGVFkVEEGPELVNAV-----KTAIQHGYRSIDTAAIY--GNEEGVGQGIregIQAAGISREALFVTSKV- 85
Cdd:cd19159 9 SGLRVSCLGLGTW-VTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaaGKAEVILGSI---IKKKGWRRSSLVITTKLy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 86 WNAD------LGYESTLKAYETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMK 158
Cdd:cd19159 85 WGGKaetergLSRKHIIEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1992844687 159 DAE----IKPMINQVEYHprLTQKE-----LQAFCREQGIQMEAWSPLMQG 200
Cdd:cd19159 165 VARqfnmIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACG 213
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
14-200 |
1.06e-04 |
|
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: 43.15 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 14 NGVKMPWFGLGVFKVEEGP---ELVNAVKT-AIQHGYRSIDTAAIY--GNEEGVGQGIregIQAAGISREALFVTSKV-W 86
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQitdEMAEHLMTlAYDNGINLFDTAEVYaaGKAEVVLGNI---IKKKGWRRSSLVITTKIfW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992844687 87 NAD------LGYESTLKAYETSLEKLGLEYLDLYLIHWP-VEGKYKDAWKALETLYKDGRVKAIGVSNFQIHHLEDLMKD 159
Cdd:cd19158 86 GGKaetergLSRKHIIEGLKASLERLQLEYVDVVFANRPdPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1992844687 160 AE----IKPMINQVEYHPRLTQK---ELQAFCREQGIQMEAWSPLMQG 200
Cdd:cd19158 166 ARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLACG 213
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
37-97 |
7.18e-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: 7.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1992844687 37 AVKTAIQHGYRSIdtAAIYGNEEGVG-----QGIREGIQAAGISREALFVTSKVWNADLGYESTLK 97
Cdd:cd06288 107 ATRHLIEAGHRRI--AFIGGPEDSLAtrlrlAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKR 170
|
|
| |
