|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-263 |
2.49e-141 |
|
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: 398.10 E-value: 2.49e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 5 ILSNNLKMPMVGFGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATglctREELFITSKLWVQDM 84
Cdd:cd19133 2 TLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIP----REELFITTKLWIQDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 aNYDLAKAGIEASLKKSGLDYFDLYLLHQAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVE 164
Cdd:cd19133 78 -GYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 165 LHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENF 244
Cdd:cd19133 157 THPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENF 236
|
250
....*....|....*....
gi 446378920 245 AIWDFSLTDNEMAQINALD 263
Cdd:cd19133 237 DIFDFELSDEDMEAIAALD 255
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-266 |
2.05e-128 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 365.53 E-value: 2.05e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 8 NNLKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAiatGLcTREELFITSKLWVQDMAnY 87
Cdd:COG0656 1 NGVEIPALGLGTWQLPG-EEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS---GV-PREELFVTTKVWNDNHG-Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 88 DLAKAGIEASLKKSGLDYFDLYLLHQAM-GDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVELH 166
Cdd:COG0656 75 DDTLAAFEESLERLGLDYLDLYLIHWPGpGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 167 PYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAI 246
Cdd:COG0656 155 PYLQQRELLAFCREHGIVVEAYSPLGRG--KLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDA 232
|
250 260
....*....|....*....|
gi 446378920 247 WDFSLTDNEMAQINALDLGY 266
Cdd:COG0656 233 FDFELSDEDMAAIDALDRGE 252
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
12-260 |
2.20e-117 |
|
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: 337.15 E-value: 2.20e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIatglCTREELFITSKLWVQDMAnYDLAK 91
Cdd:cd19071 1 MPLIGLGTYKLKP-EETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHG-YERVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AGIEASLKKSGLDYFDLYLLH--------QAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQV 163
Cdd:cd19071 75 EALEESLKDLGLDYLDLYLIHwpvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 164 ELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEEN 243
Cdd:cd19071 155 ELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKEN 234
|
250
....*....|....*..
gi 446378920 244 FAIWDFSLTDNEMAQIN 260
Cdd:cd19071 235 LDVFDFELSEEDMAAID 251
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-263 |
8.21e-104 |
|
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: 303.54 E-value: 8.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREaiatGLCTREELFITSKLWVQDMA 85
Cdd:cd19157 4 LNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNADQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 nYDLAKAGIEASLKKSGLDYFDLYLLHQAMGD-YFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVE 164
Cdd:cd19157 80 -YDSTLKAFEASLERLGLDYLDLYLIHWPVKGkYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 165 LHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENF 244
Cdd:cd19157 159 FHPRLTQKELRDYCKKQGIQLEAWSPLMQG--QLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENA 236
|
250
....*....|....*....
gi 446378920 245 AIWDFSLTDNEMAQINALD 263
Cdd:cd19157 237 DVFDFELSQEDMDKIDALN 255
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-263 |
5.51e-100 |
|
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: 293.19 E-value: 5.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREaiaTGLcTREELFITSKLWVQDMa 85
Cdd:cd19126 3 LNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE---SGV-PREELFVTTKLWNDDQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NYDLAKAGIEASLKKSGLDYFDLYLLH-QAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVE 164
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHwPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 165 LHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENF 244
Cdd:cd19126 158 FHPYLTQKELRGYCKSKGIVVEAWSPLGQG--GLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENA 235
|
250
....*....|....*....
gi 446378920 245 AIWDFSLTDNEMAQINALD 263
Cdd:cd19126 236 DIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-263 |
1.24e-99 |
|
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: 292.77 E-value: 1.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREaiaTGLcTREELFITSKLWVQDMA 85
Cdd:cd19127 3 LNNGVEMPALGLGVFQ-TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRR---SGV-DRSDIFVTTKLWISDYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 nYDLAKAGIEASLKKSGLDYFDLYLLHQAMGDYF----SAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVN 161
Cdd:cd19127 78 -YDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFdrtiQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 162 QVELHPYFAQPAALETMKHYNVQPEAWAPLGG----------GRHKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVI 231
Cdd:cd19127 157 QVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAI 236
|
250 260 270
....*....|....*....|....*....|..
gi 446378920 232 PKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19127 237 PKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
12-262 |
8.15e-99 |
|
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: 290.69 E-value: 8.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDMAnYDLAK 91
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQG-YEKAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AGIEASLKKSGLDYFDLYLLH----QAMGDYFSA--------WRALEDAYEAGKLKAIGVSNF-YAHV--LANFCETVri 156
Cdd:cd19136 80 AACLGSLERLGTDYLDLYLIHwpgvQGLKPSDPRnaelrresWRALEDLYKEGKLRAIGVSNYtVRHLeeLLKYCEVP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 157 tPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTR 236
Cdd:cd19136 158 -PAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTN 236
|
250 260
....*....|....*....|....*.
gi 446378920 237 QERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19136 237 PERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
6-263 |
4.19e-97 |
|
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: 286.34 E-value: 4.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREaiaTGLcTREELFITSKLWVQDMA 85
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE---SGV-PREEVFVTTKLWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 nYDLAKAGIEASLKKSGLDYFDLYLLHQAMGD-YFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVE 164
Cdd:cd19156 79 -YESTLAAFEESLEKLGLDYVDLYLIHWPVKGkFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 165 LHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENF 244
Cdd:cd19156 158 LHPLLTQEPLRKFCKEKNIAVEAWSPLGQG--KLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENF 235
|
250
....*....|....*....
gi 446378920 245 AIWDFSLTDNEMAQINALD 263
Cdd:cd19156 236 DVFDFELTAEEIRQIDGLN 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
6-263 |
7.43e-95 |
|
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: 280.41 E-value: 7.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAiatGLcTREELFITSKLWvQDMA 85
Cdd:cd19131 4 LNDGNTIPQLGLGVWQVSN-DEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRAS---GV-PREELFITTKLW-NSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NYDLAKAGIEASLKKSGLDYFDLYLLHQAM---GDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQ 162
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWPVpaqDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 163 VELHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEE 242
Cdd:cd19131 158 IELHPRFQQRELRAFHAKHGIQTESWSPLGQG--GLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAE 235
|
250 260
....*....|....*....|.
gi 446378920 243 NFAIWDFSLTDNEMAQINALD 263
Cdd:cd19131 236 NFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
6-263 |
9.48e-93 |
|
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: 274.92 E-value: 9.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREA-IAtglctREELFITSKLWVQDM 84
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKG-DEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSgVP-----REELFVTTKLPGRHH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 AnYDLAKAGIEASLKKSGLDYFDLYLLH---QAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVN 161
Cdd:cd19132 75 G-YEEALRTIEESLYRLGLDYVDLYLIHwpnPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 162 QVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIE 241
Cdd:cd19132 154 QIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS-GLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQR 232
|
250 260
....*....|....*....|..
gi 446378920 242 ENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19132 233 ENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
6-266 |
5.06e-91 |
|
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: 271.85 E-value: 5.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWvQDMA 85
Cdd:cd19116 5 LNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW-NSYH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NYDLAKAGIEASLKKSGLDYFDLYLLHQAMG------------------DYFSAWRALEDAYEAGKLKAIGVSNFYAHVL 147
Cdd:cd19116 84 EREQVEPALRESLKRLGLDYVDLYLIHWPVAfkenndsesngdgslsdiDYLETWRGMEDLVKLGLTRSIGVSNFNSEQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 148 ANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLggGRHKP---------YENVMLQRIADAHQKTIAQV 218
Cdd:cd19116 164 NRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPF--GRLVPrgqtnppprLDDPTLVAIAKKYGKTTAQI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446378920 219 VLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALDLGY 266
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQ 289
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-266 |
2.06e-85 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 257.72 E-value: 2.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSILSNNLKMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLW 80
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWK-SKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 81 VQDMANYDLAKAgIEASLKKSGLDYFDLYLLH------------QAMGDYFS--------AWRALEDAYEAGKLKAIGVS 140
Cdd:cd19123 80 NNSHAPEDVLPA-LEKTLADLQLDYLDLYLMHwpvalkkgvgfpESGEDLLSlspipledTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 141 NFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLG-GGRHKPY---------ENVMLQRIADA 210
Cdd:cd19123 159 NFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGsGDRPAAMkaegepvllEDPVINKIAEK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446378920 211 HQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALDLGY 266
Cdd:cd19123 239 HGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHH 294
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
6-262 |
1.88e-83 |
|
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: 251.47 E-value: 1.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVtdKEECQQSVLSAIR-SGYRLIDTAAVYGNEDAVGDAVREAiatGLcTREELFITSKLWVQDM 84
Cdd:cd19135 7 LSNGVEMPILGLGTSHS--GGYSHEAVVYALKeCGYRHIDTAKRYGCEELLGKAIKES---GV-PREDLFLTTKLWPSDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 AnYDLAKAGIEASLKKSGLDYFDLYLLH------------QAMGDyfsAWRALEDAYEAGKLKAIGVSNFYAHVLANFCE 152
Cdd:cd19135 81 G-YESTKQAFEASLKRLGVDYLDLYLLHwpdcpssgknvkETRAE---TWRALEELYDEGLCRAIGVSNFLIEHLEQLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 153 TVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIP 232
Cdd:cd19135 157 DCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKG--KALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIP 234
|
250 260 270
....*....|....*....|....*....|
gi 446378920 233 KSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19135 235 KSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
6-263 |
4.21e-83 |
|
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: 251.95 E-value: 4.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDMA 85
Cdd:cd19154 6 LSNGVKMPLIGLGTWQSKG-AEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NYDLAKAgIEASLKKSGLDYFDLYLLH---------------QAMGDYFSA------WRALEDAYEAGKLKAIGVSNFYA 144
Cdd:cd19154 85 PEDVEEA-LRESLKKLQLEYVDLYLIHapaafkddegesgtmENGMSIHDAvdvedvWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 145 HVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG-GR--------HKPYENVM----LQRIADAH 211
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpGRanftkstgVSPAPNLLqdpiVKAIAEKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446378920 212 QKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIE 295
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-265 |
1.38e-82 |
|
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: 249.39 E-value: 1.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 5 ILSNNLKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVReaiATGLcTREELFITSKLWVQDM 84
Cdd:cd19134 4 TLNDDNTMPVIGLGVGELSD-DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASGI-PRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 AnYDLAKAGIEASLKKSGLDYFDLYLLHQAMGD---YFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVN 161
Cdd:cd19134 79 G-FTASQAACRASLERLGLDYVDLYLIHWPAGRegkYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 162 QVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRhkPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIE 241
Cdd:cd19134 158 QIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR--LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIA 235
|
250 260
....*....|....*....|....
gi 446378920 242 ENFAIWDFSLTDNEMAQINALDLG 265
Cdd:cd19134 236 SNLDVFDFELTADHMDALDGLDDG 259
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-262 |
2.43e-81 |
|
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: 246.80 E-value: 2.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGVF-KVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGL-CTREELFITSKLWVQDmANYD 88
Cdd:cd19124 4 TMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLvKSRDELFVTSKLWCSD-AHPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 89 LAKAGIEASLKKSGLDYFDLYLLH-------------------QAMgDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLAN 149
Cdd:cd19124 83 LVLPALKKSLRNLQLEYVDLYLIHwpvslkpgkfsfpieeedfLPF-DIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 150 FCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG-----GRHKPYENVMLQRIADAHQKTIAQVVLRWNV 224
Cdd:cd19124 162 LLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGApgtkwGSNAVMESDVLKEIAAAKGKTVAQVSLRWVY 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 446378920 225 QRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19124 242 EQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
6-263 |
1.31e-80 |
|
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: 245.76 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCT-REELFITSKLWVQDM 84
Cdd:cd19106 1 LHTGQKMPLIGLGTWK-SKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVpREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 ANYDLAKAgIEASLKKSGLDYFDLYLLHQAMG---------------------DYFSAWRALEDAYEAGKLKAIGVSNFY 143
Cdd:cd19106 80 HPEDVEPA-LRKTLKDLQLDYLDLYLIHWPYAfergdnpfpknpdgtirydstHYKETWKAMEKLVDKGLVKAIGLSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 144 AHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRH---KPYENVML-----QRIADAHQKTI 215
Cdd:cd19106 159 SRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRpwaKPDEPVLLeepkvKALAKKYNKSP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446378920 216 AQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALN 286
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
12-265 |
1.37e-78 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 239.59 E-value: 1.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREaiaTGLcTREELFITSKLWVQDMANydlAK 91
Cdd:PRK11565 15 MPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE---ASV-AREELFITTKLWNDDHKR---PR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AGIEASLKKSGLDYFDLYLLH---QAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVELHPY 168
Cdd:PRK11565 87 EALEESLKKLQLDYVDLYLMHwpvPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 169 FAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWD 248
Cdd:PRK11565 167 MQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFD 246
|
250
....*....|....*..
gi 446378920 249 FSLTDNEMAQINALDLG 265
Cdd:PRK11565 247 FRLDKDELGEIAKLDQG 263
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
5-263 |
2.44e-78 |
|
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: 238.27 E-value: 2.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 5 ILSNNLKMPMVGFGVFKVTDKEEcQQSVLSAIRSGYRLIDTAAVYGNEDAVGdavrEAIATGLCTREELFITSKLWvQDM 84
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPADT-QRAVATALEVGYRHIDTAAIYGNEEGVG----AAIAASGIPRDELFVTTKLW-NDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 ANYDLAKAGIEASLKKSGLDYFDLYLLH---QAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVN 161
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHwptPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 162 QVELHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIE 241
Cdd:cd19130 157 QIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG--KLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERME 234
|
250 260
....*....|....*....|..
gi 446378920 242 ENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19130 235 DNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
11-260 |
2.16e-77 |
|
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: 236.86 E-value: 2.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDMANYDLA 90
Cdd:cd19125 10 KIPAVGLGTWQ-ADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAPEDVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KAgIEASLKKSGLDYFDLYLLH--------QAMG--------DYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETV 154
Cdd:cd19125 89 PA-LEKTLKDLQLDYLDLYLIHwpvrlkkgAHMPepeevlppDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 155 RITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGG-----RHKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVT 229
Cdd:cd19125 168 RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPgttwvKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQRGTS 247
|
250 260 270
....*....|....*....|....*....|.
gi 446378920 230 VIPKSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19125 248 VLPKSTNEERIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
7-262 |
5.07e-77 |
|
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: 234.85 E-value: 5.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 7 SNNLKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREA-IAtglctREELFITSKLWVQDMA 85
Cdd:cd19140 3 VNGVRIPALGLGTYPLTG-EECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASgVP-----RDELFLTTKVWPDNYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NYDLAKAgIEASLKKSGLDYFDLYLLHQAMGDYFSAW--RALEDAYEAGKLKAIGVSNFYAhvlANFCETVRITP---MV 160
Cdd:cd19140 77 PDDFLAS-VEESLRKLRTDYVDLLLLHWPNKDVPLAEtlGALNEAQEAGLARHIGVSNFTV---ALLREAVELSEaplFT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 161 NQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYEnvMLQRIADAHQKTIAQVVLRWNVQR-GVTVIPKSTRQER 239
Cdd:cd19140 153 NQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGEVLKDP--VLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNPER 230
|
250 260
....*....|....*....|...
gi 446378920 240 IEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19140 231 LEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
6-263 |
9.15e-77 |
|
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: 236.23 E-value: 9.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVtDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDma 85
Cdd:cd19112 5 LNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 nYDLAKAGIEASLKKSGLDYFDLYLLH--------------QAMGD-----------YFSAWRALEDAYEAGKLKAIGVS 140
Cdd:cd19112 82 -HGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgSALGEdgvldidvtisLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 141 NFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG--------GRHKPYENVMLQRIADAHQ 212
Cdd:cd19112 161 NYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGaaanaewfGSVSPLDDPVLKDLAKKYG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446378920 213 KTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19112 241 KSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLD 291
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
12-260 |
7.69e-75 |
|
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: 228.69 E-value: 7.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATglctREELFITSKLWVQDMANYDLAK 91
Cdd:cd19073 1 IPALGLGTWQLRG-DDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVP----REDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AgIEASLKKSGLDYFDLYLLH-----QAMGDYFSAwraLEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVELH 166
Cdd:cd19073 76 S-VDRSLEKLGTDYVDLLLIHwpnptVPLEETLGA---LKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 167 PYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAI 246
Cdd:cd19073 152 PFLYQAELLEYCRENDIVITAYSPLARG--EVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAI 229
|
250
....*....|....
gi 446378920 247 WDFSLTDNEMAQIN 260
Cdd:cd19073 230 FDWELTSEDVAKID 243
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-265 |
3.29e-74 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 229.61 E-value: 3.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVtDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWvqdma 85
Cdd:cd19115 7 LNSGYDMPLVGFGLWKV-NNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NYDLAKAGIEASLKKS----GLDYFDLYLLH------------------QAMGD--YFS------AWRALEDAYEAGKLK 135
Cdd:cd19115 81 NTFHDGERVEPICRKQladwGIDYFDLFLIHfpialkyvdpavryppgwFYDGKkvEFSnapiqeTWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 136 AIGVSNFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLG----------GGRHKP--YENVM 203
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldlpGAKDTPplFEHDV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446378920 204 LQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALDLG 265
Cdd:cd19115 241 IKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIG 302
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-265 |
3.69e-74 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 229.64 E-value: 3.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVtDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLW--VQD 83
Cdd:cd19113 5 LNSGYKMPSVGFGCWKL-DNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWnnFHD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 84 MANYDLAkagIEASLKKSGLDYFDLYLLHQAM-------------------GDYFS--------AWRALEDAYEAGKLKA 136
Cdd:cd19113 84 PKNVETA---LNKTLSDLKLDYVDLFLIHFPIafkfvpieekyppgfycgdGDNFVyedvpildTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 137 IGVSNFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQ--------PEAWAPLGGGRHKP----YENVML 204
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITitayssfgPQSFVELNQGRALNtptlFEHDTI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446378920 205 QRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALDLG 265
Cdd:cd19113 241 KSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIG 301
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-261 |
2.41e-71 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 220.95 E-value: 2.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGV-------FKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAiatgLCTREELFITSKLWVqD 83
Cdd:cd19120 3 KIPAIAFGTgtawyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSP-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 84 MANydlAKAGIEASLKKSGLDYFDLYLLH------QAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRIT 157
Cdd:cd19120 78 IKD---PREALRKSLAKLGVDYVDLYLIHspffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 158 PMVNQVELHPYFA--QPAALETMKHYNVQPEAW---APLGGGRHKPYENVmLQRIADAHQKTIAQVVLRWNVQRGVTVIP 232
Cdd:cd19120 155 PAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYsplSPLTRDAGGPLDPV-LEKIAEKYGVTPAQVLLRWALQKGIVVVT 233
|
250 260
....*....|....*....|....*....
gi 446378920 233 KSTRQERIEENFAIWDFSLTDNEMAQINA 261
Cdd:cd19120 234 TSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-263 |
2.10e-67 |
|
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: 211.59 E-value: 2.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDMANYDLA 90
Cdd:cd19111 3 PMPVIGLGTYQ-SPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KaGIEASLKKSGLDYFDLYLLHQAMG---------------DYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVR 155
Cdd:cd19111 82 K-SLEKSLENLKLPYVDLYLIHHPCGfvnkkdkgerelassDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 156 ITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG-GRHKPY----------ENVMLQrIADAHQKTIAQVVLRWNV 224
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSlwpdqpdlleDPTVLA-IAKELDKTPAQVLLRFVL 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 446378920 225 QRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLD 278
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-263 |
2.72e-67 |
|
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: 211.97 E-value: 2.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVF---KVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDMANyD 88
Cdd:cd19109 4 IPIIGLGTYsepKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHPP-E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 89 LAKAGIEASLKKSGLDYFDLYLLHQAM----GDYF-----------------SAWRALEDAYEAGKLKAIGVSNFYAHVL 147
Cdd:cd19109 83 LVRPTLERTLKVLQLDYVDLYIIEMPMafkpGDEIyprdengkwlyhktnlcATWEALEACKDAGLVKSIGVSNFNRRQL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 148 ANFCET--VRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENV---------MLQRIADAHQKTIA 216
Cdd:cd19109 163 ELILNKpgLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVsspplledpLLNSIGKKYNKTAA 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446378920 217 QVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19109 243 QVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALN 289
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-268 |
7.06e-67 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 210.84 E-value: 7.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 8 NNLKMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDMANY 87
Cdd:cd19155 8 NGEKMPVVGLGTWQ-SSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGNRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 88 DLAKAgIEASLKKSGLDYFDLYLLHQAMG-----------------------DYFSAWRALEDAYEAGKLKAIGVSNFYA 144
Cdd:cd19155 87 KVEKF-LLKSLEKLQLDYVDLYLIHFPVGslskeddsgkldptgehkqdyttDLLDIWKAMEAQVDQGLTRSIGLSNFNR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 145 HVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG-GRH--------------KPYENVMLQRIAD 209
Cdd:cd19155 166 EQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpGAAhfspgtgspsgsspDLLQDPVVKAIAE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 210 AHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALDLGYVG 268
Cdd:cd19155 246 RHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
6-262 |
1.38e-66 |
|
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: 209.28 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVReaiATGLcTREELFITSKLWVQDMA 85
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKP-NEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSGV-PREEIFITTKLWCTWHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NydlAKAGIEASLKKSGLDYFDLYLLHQAMG-----------------------DYFSAWRALEDAYEAGKLKAIGVSNF 142
Cdd:cd19117 83 R---VEEALDQSLKKLGLDYVDLYLMHWPVPldpdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIGVSNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 143 YAHVLANFCET--VRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQKTIAQVVL 220
Cdd:cd19117 160 SIKNLEKLLASpsAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTPAQVII 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446378920 221 RWNVQRGVTVIPKSTRQERIEENFAIWdfSLTDNEMAQINAL 262
Cdd:cd19117 240 SWGLQRGYSVLPKSVTPSRIESNFKLF--TLSDEEFKEIDEL 279
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-262 |
4.99e-66 |
|
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: 207.77 E-value: 4.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSILSNNLKMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLcTREELFITSKLW 80
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQ-AKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGV-KREDLFVTTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 81 vqdmANY-DLAKAGIEASLKKSGLDYFDLYLLH-----QAMG-------------------DYFSAWRALEDAYEAGKLK 135
Cdd:cd19121 79 ----STYhRRVELCLDRSLKSLGLDYVDLYLVHwpvllNPNGnhdlfptlpdgsrdldwdwNHVDTWKQMEKVLKTGKTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 136 AIGVSNFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQKTI 215
Cdd:cd19121 155 AIGVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446378920 216 AQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFslTDNEMAQINAL 262
Cdd:cd19121 235 GTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-278 |
3.52e-64 |
|
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: 203.80 E-value: 3.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQDMANyDLA 90
Cdd:cd19107 3 KMPILGLGTWK-SPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEK-GLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KAGIEASLKKSGLDYFDLYLLHQAMG---------------------DYFSAWRALEDAYEAGKLKAIGVSNFyahvlaN 149
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGfkpgkelfpldesgnvipsdtTFLDTWEAMEELVDEGLVKAIGVSNF------N 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 150 FCETVRI--------TPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRH---KPYENVMLQ-----RIADAHQK 213
Cdd:cd19107 155 HLQIERIlnkpglkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwaKPEDPSLLEdpkikEIAAKHNK 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446378920 214 TIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALDLGY----VGEAVKH----FNPEF 278
Cdd:cd19107 235 TTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWracaLLSCSSHkdypFHAEY 307
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
6-262 |
2.67e-63 |
|
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: 200.71 E-value: 2.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKvTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIAT-GLCTREELFITSKLWVQDM 84
Cdd:cd19118 1 LNTGNKIPAIGLGTWQ-AEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 ANYDLaKAGIEASLKKSGLDYFDLYLLH-----QAMGDYFS---------------------AWRALEDAYEAGKLKAIG 138
Cdd:cd19118 80 RPEYV-EPALDDTLKELGLDYLDLYLIHwpvafKPTGDLNPltavptnggevdldlsvslvdTWKAMVELKKTGKVKSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 139 VSNFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG---GRHKPYENVMLQRIADAHQKTI 215
Cdd:cd19118 159 VSNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNnlaGLPLLVQHPEVKAIAAKLGKTP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446378920 216 AQVVLRWNVQRGVTVIPKSTRQERIEENFAiwDFSLTDNEMAQINAL 262
Cdd:cd19118 239 AQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-266 |
5.35e-62 |
|
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: 197.72 E-value: 5.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFK-VTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVqdm 84
Cdd:cd19119 6 LNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 ANYDLAKAGIEASLKKSGLDYFDLYLLH---------------------------QAMGDYFSAWRALEDAYEAGKLKAI 137
Cdd:cd19119 83 TFYDEVERSLDESLKALGLDYVDLLLVHwpvcfekdsddsgkpftpvnddgktryAASGDHITTYKQLEKIYLDGRAKAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 138 GVSNFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQKTIAQ 217
Cdd:cd19119 163 GVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKYNVSTGD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446378920 218 VVLRWNVQRGVTVIPKSTRQERIEENFAIwdFSLTDNEMAQINALDLGY 266
Cdd:cd19119 243 ILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGEKY 289
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
13-262 |
9.30e-62 |
|
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: 196.59 E-value: 9.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 13 PMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWvQDMANYDLAKA 92
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLW-PTMHQPENVKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 93 GIEASLKKSGLDYFDLYLLHQ-------AMGDYFSA--------------WRALEDAYEAGKLKAIGVSNFYAHVLANFC 151
Cdd:cd19128 80 QLLITLQDLQLEYLDLFLIHWplafdmdTDGDPRDDnqiqslskkpledtWRAMEQCVDEKLTKNIGVSNYSTKLLTDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 152 ETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG----GRHKPYENVMLQRIADAHQKTIAQVVLRWNVQR- 226
Cdd:cd19128 160 NYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGsygdGNLTFLNDSELKALATKYNTTPPQVIIAWHLQKw 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 446378920 227 --GVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19128 240 pkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-263 |
3.09e-61 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 196.24 E-value: 3.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGVFKVTDKEeCQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWvQDMANYDLA 90
Cdd:cd19114 3 KMPLVGFGTAKIKANE-TEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLW-NNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KAGIEASLKKSGLDYFDLYLLHQAMGDYF---------------------------SAWRALEDAYEAGKLKAIGVSNFY 143
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAYvdpaenypflwkdkelkkfpleqspmqECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 144 AHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRH-------KPYENVM----LQRIADAHQ 212
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYtkvtkhlKHFTNLLehpvVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446378920 213 KTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELE 291
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
12-262 |
2.11e-59 |
|
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: 189.49 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREaiaTGLcTREELFITSKLWVQDMANYDLAK 91
Cdd:cd19139 1 IPAFGLGTFRLKD-DVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE---SGV-PRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AgIEASLKKSGLDYFDLYLLH-------QAMGDYFSAwraLEDAYEAGKLKAIGVSNFYAHVLANFCETV---RITpmVN 161
Cdd:cd19139 76 S-LEESLEKLRTDYVDLTLIHwpspndeVPVEEYIGA---LAEAKEQGLTRHIGVSNFTIALLDEAIAVVgagAIA--TN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 162 QVELHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIE 241
Cdd:cd19139 150 QIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYG--KVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLR 227
|
250 260
....*....|....*....|.
gi 446378920 242 ENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19139 228 SNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
11-263 |
6.18e-59 |
|
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: 190.17 E-value: 6.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGVFKVTDKEeCQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQdMANYDLA 90
Cdd:cd19110 3 DIPAVGLGTWKASPGE-VTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCT-CHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KAGIEASLKKSGLDYFDLYLLHQAMG---------------------DYFSAWRALEDAYEAGKLKAIGVSNFYAHVLAN 149
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGfkpgepdlpldrsgmvipsdtDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 150 FCET--VRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGG---GRHKpYENVMLQRIADAHQKTIAQVVLRWNV 224
Cdd:cd19110 161 LLNKpgLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGsceGVDL-IDDPVIQRIAKKHGKSPAQILIRFQI 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 446378920 225 QRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19110 240 QRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLD 278
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-263 |
2.07e-58 |
|
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: 188.98 E-value: 2.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVTD--KEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWVQD 83
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 84 MANyDLAKAGIEASLKKSGLDYFDLYLLHQAM-----GDYF----------------SAWRALEDAYEAGKLKAIGVSNF 142
Cdd:cd19108 85 HRP-ELVRPALEKSLKKLQLDYVDLYLIHFPValkpgEELFpkdengklifdtvdlcATWEAMEKCKDAGLAKSIGVSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 143 yahvlaNFCETVRI--------TPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHK-------PY--ENVMLQ 205
Cdd:cd19108 164 ------NRRQLEMIlnkpglkyKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKewvdqnsPVllEDPVLC 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446378920 206 RIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:cd19108 238 ALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLN 295
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
7-260 |
1.21e-56 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 184.20 E-value: 1.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 7 SNNLKMPMVGFGVFkVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCTREELFITSKLWvqdMAN 86
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLW---NTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 87 Y--DLAKAGIEASLKKSGLDYFDLYLLHQAM----GD------------------YFSAWRALEDAYEAGKLKAIGVSNF 142
Cdd:cd19129 77 HrpERVKPAFEASLKRLQLDYLDLYLIHTPFafqpGDeqdprdangnviyddgvtLLDTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 143 YAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLG-GGRHKPYENVMLQRIADAHQKTIAQVVLR 221
Cdd:cd19129 157 SLEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGhGMEPKLLEDPVITAIARRVNKTPAQVLLA 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 446378920 222 WNVQRGVTVIPKSTRQERIEENFAIwdFSLTDNEMAQIN 260
Cdd:cd19129 237 WAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREIN 273
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
10-265 |
2.56e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 177.14 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 10 LKMPMVGFGVFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGdavrEAIATGLCTREELFITSKLWVQDMANYDL 89
Cdd:PRK11172 1 MSIPAFGLGTFRLKD-QVVIDSVKTALELGYRAIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 90 AkAGIEASLKKSGLDYFDLYLLHQ-------AMGDYFSAwraLEDAYEAGKLKAIGVSNFYAHVLANFCETV---RITpm 159
Cdd:PRK11172 76 I-PSLKESLQKLRTDYVDLTLIHWpspndevSVEEFMQA---LLEAKKQGLTREIGISNFTIALMKQAIAAVgaeNIA-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 160 VNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGrhKPYENVMLQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQER 239
Cdd:PRK11172 150 TNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYG--KVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKREN 227
|
250 260
....*....|....*....|....*.
gi 446378920 240 IEENFAIWDFSLTDNEMAQINALDLG 265
Cdd:PRK11172 228 LASNLLAQDLQLDAEDMAAIAALDRN 253
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
6-258 |
7.21e-54 |
|
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: 176.66 E-value: 7.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 6 LSNNLKMPMVGFGVFKVT-DKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVGDAVREAIATGLCT-REELFITSKLWvQD 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEgAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSVkREDLFICTKVW-NH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 84 MANYDLAKAGIEASLKKSGLDYFDLYLLHQAM---------------GDYF----------SAWRALEDAYEAGKLKAIG 138
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaekndqrspklgpdGKYVilkdltenpePTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 139 VSNFYAHVLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPY------ENVMLQRIADAHQ 212
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPStgervsENPTLNEVAEKGG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446378920 213 KTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQ 258
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFEAIN 287
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-263 |
1.73e-46 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 157.86 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 17 FGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGdavrEAIATGLCTREELFITSKLW-VQDMANYDLAKA 92
Cdd:pfam00248 9 GGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLG----EALKDYPVKRDKVVIATKVPdGDGPWPSGGSKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 93 GI----EASLKKSGLDYFDLYLLHQAMGD--YFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQVELH 166
Cdd:pfam00248 85 NIrkslEESLKRLGTDYIDLYYLHWPDPDtpIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 167 PYFAQPAA--LETMKHYNVQPEAWAPLGGG-------RHKPYENVM------------------LQRIADAHQKTIAQVV 219
Cdd:pfam00248 165 LLRRRQEEelLEYCKKNGIPLIAYSPLGGGlltgkytRDPDKGPGErrrllkkgtplnlealeaLEEIAKEHGVSPAQVA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446378920 220 LRW--NVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINALD 263
Cdd:pfam00248 245 LRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-260 |
3.87e-45 |
|
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: 153.56 E-value: 3.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 5 ILSNNLKMPMVGFGVFKV----TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatglcTREELFITS 77
Cdd:cd19138 4 TLPDGTKVPALGQGTWYMgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 78 KLWVQDmANYDLAKAGIEASLKKSGLDYFDLYLLHqamgdyfsaWR----------ALEDAYEAGKLKAIGVSNFYahvL 147
Cdd:cd19138 77 KVLPSN-ASRQGTVRACERSLRRLGTDYLDLYLLH---------WRggvplaetvaAMEELKKEGKIRAWGVSNFD---T 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 148 ANFCETVRI----TPMVNQVELHpyFAQPAA----LETMKHYNVQPEAWAPLGGG---RHKPYENVMLQRIADAHQKTIA 216
Cdd:cd19138 144 DDMEELWAVpgggNCAANQVLYN--LGSRGIeydlLPWCREHGVPVMAYSPLAQGgllRRGLLENPTLKEIAARHGATPA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446378920 217 QVVLRWNV-QRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19138 222 QVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
9-260 |
1.58e-44 |
|
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: 151.61 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 9 NLKMPMVGFGVFKV--------TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAIatglctREELFITS 77
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKGFD------REDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 78 KLWvQDMANYDLAKAGIEASLKKSGLDYFDLYLLHQ--AMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVR 155
Cdd:cd19072 75 KVS-PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWpnPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 156 ITPMV-NQVELHPYF--AQPAALETMKHYNVQPEAWAPLG-GGRHKPYENVMLQRIADAHQKTIAQVVLRWNVQR-GVTV 230
Cdd:cd19072 154 KGPIVaNQVEYNLFDreEESGLLPYCQKNGIAIIAYSPLEkGKLSNAKGSPLLDEIAKKYGKTPAQIALNWLISKpNVIA 233
|
250 260 270
....*....|....*....|....*....|
gi 446378920 231 IPKSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19072 234 IPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-262 |
3.51e-39 |
|
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: 139.16 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSILSN-NLKMPMVGFG------VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREAiatglcTR 70
Cdd:COG0667 1 MEYRRLGRsGLKVSRLGLGtmtfggPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 71 EELFITSK---LWVQDMANYDLAKAGI----EASLKKSGLDYFDLYLLH-----QAMGDyfsAWRALEDAYEAGKLKAIG 138
Cdd:COG0667 75 DDVVIATKvgrRMGPGPNGRGLSREHIrravEASLRRLGTDYIDLYQLHrpdpdTPIEE---TLGALDELVREGKIRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 139 VSNFYAHVLANFCETVR-ITPMV-NQVELHPYFAQPAA--LETMKHYNVQPEAWAPLGGGR------------------- 195
Cdd:COG0667 152 VSNYSAEQLRRALAIAEgLPPIVaVQNEYSLLDRSAEEelLPAARELGVGVLAYSPLAGGLltgkyrrgatfpegdraat 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446378920 196 --HKPYENV-------MLQRIADAHQKTIAQVVLRWNVQRG--VTVIPKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:COG0667 232 nfVQGYLTErnlalvdALRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-260 |
6.92e-39 |
|
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: 138.13 E-value: 6.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 17 FGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatgLCTREELFITSKLWV--QDMANYDLAK 91
Cdd:cd19093 17 WWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKE-----LGDRDEVVIATKFAPlpWRLTRRSVVK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AgIEASLKKSGLDYFDLYLLHQAMGDYFSA---WRALEDAYEAGKLKAIGVSNFYAHVLANFCETVR---ITPMVNQVE- 164
Cdd:cd19093 92 A-LKASLERLGLDSIDLYQLHWPGPWYSQIealMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKergVPLASNQVEy 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 165 --LHPYFAQPAALETMKHYNVQPEAWAPLGGGR--------------------HKPYENV-----MLQRIADAHQKTIAQ 217
Cdd:cd19093 171 slLYRDPEQNGLLPACDELGITLIAYSPLAQGLltgkyspenpppggrrrlfgRKNLEKVqplldALEEIAEKYGKTPAQ 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446378920 218 VVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19093 251 VALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-260 |
6.07e-35 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 126.92 E-value: 6.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 11 KMPMVGFGVFKV--------TDKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREAiatglcTREELFITSKL 79
Cdd:cd19137 3 KIPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKDF------PREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 80 WVQDMANYDLAKAgIEASLKKSGLDYFDLYLLHQAMGD--YFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRIT 157
Cdd:cd19137 77 WPTNLRYDDLLRS-LQNSLRRLDTDYIDLYLIHWPNPNipLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 158 PMVNQVELHPYFAQP---AALETMKHYNVQPEAWAPLGGGRHKpyENVMLQRIADAHQKTIAQVVLRWNVQR-GVTVIPK 233
Cdd:cd19137 156 IVCNQVKYNLEDRDPerdGLLEYCQKNGITVVAYSPLRRGLEK--TNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPK 233
|
250 260
....*....|....*....|....*..
gi 446378920 234 STRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19137 234 AGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
9-260 |
1.40e-31 |
|
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: 118.78 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 9 NLKMPMVGFG-------VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatglcTREELFITSK 78
Cdd:cd19084 1 DLKVSRIGLGtwaiggtWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 79 ---LWVQD-MANYDLAKAGI----EASLKKSGLDYFDLYLLHqamgdyfsaWR-----------ALEDAYEAGKLKAIGV 139
Cdd:cd19084 74 cglRWDGGkGVTKDLSPESIrkevEQSLRRLQTDYIDLYQIH---------WPdpntpieetaeALEKLKKEGKIRYIGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 140 SNFYAHVLANFCETVRITpmVNQVelhPY--FAQPAALETM---KHYNVQPEAWAPLGGG------------------RH 196
Cdd:cd19084 145 SNFSVEQLEEARKYGPIV--SLQP---PYsmLEREIEEELLpycRENGIGVLPYGPLAQGlltgkykkeptfppddrrSR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446378920 197 KPY------ENVM-----LQRIADAHQKTIAQVVLRWNVQR-GVT-VIPKSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19084 220 FPFfrgenfEKNLeivdkLKEIAEKYGKSLAQLAIAWTLAQpGVTsAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
23-245 |
2.41e-28 |
|
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: 108.76 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 23 TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAIAtglctREELFITSKL---WVQDMANYDLAKAGIEA 96
Cdd:cd06660 14 GDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-----RDDVVIATKGghpPGGDPSRSRLSPEHIRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 97 SLKKS----GLDYFDLYLLH-----QAMGDyfsAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVR----ITPMVNQV 163
Cdd:cd06660 89 DLEESlrrlGTDYIDLYYLHrddpsTPVEE---TLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPGFAAVQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 164 E---LHPYFAQPAALETMKHYNVQPEAWAPLGGGrhkpyenvmlqriadahqktIAQVVLRW--NVQRGVTVIPKSTRQE 238
Cdd:cd06660 166 QyslLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------PAQLALAWllSQPFVTVPIVGARSPE 225
|
....*..
gi 446378920 239 RIEENFA 245
Cdd:cd06660 226 QLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
23-242 |
1.70e-27 |
|
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: 107.64 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 23 TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAiaTGLctREELFITSK----LWVQDMAN----YDLAK 91
Cdd:cd19092 21 ESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN--PGL--REKIEIQTKcgirLGDDPRPGrikhYDTSK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AGI----EASLKKSGLDYFDLYLLHQAmgDY-FSAW---RALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPMVNQV 163
Cdd:cd19092 97 EHIlasvEGSLKRLGTDYLDLLLLHRP--DPlMDPEevaEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 164 ELHPYFAQPAA---LETMKHYNVQPEAWAPLGGGR-----HKPYENVM--LQRIADAHQKTIAQVVLRWNVQRGVTVIP- 232
Cdd:cd19092 175 ELSLLHTEAIDdgtLDYCQLLDITPMAWSPLGGGRlfggfDERFQRLRaaLEELAEEYGVTIEAIALAWLLRHPARIQPi 254
|
250
....*....|.
gi 446378920 233 -KSTRQERIEE 242
Cdd:cd19092 255 lGTTNPERIRS 265
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
24-261 |
2.58e-26 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 104.59 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 24 DKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatglcTREELFITSKLWVQDMANYDLAKAgIEASLKK 100
Cdd:cd19085 21 DDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSPDNLTPEDVRKS-CERSLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 101 SGLDYFDLYLLHQAMGD-----YFSAwraLEDAYEAGKLKAIGVSNFYAHVLANFCETVRITpmVNQV-----------E 164
Cdd:cd19085 93 LGTDYIDLYQIHWPSSDvpleeTMEA---LEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQLpynllwraieyE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 165 LHPY----------------------FAQPAALETM----KHYNV-QPEAWAPLGGGRHKpyenvmLQRIADAHQKTIAQ 217
Cdd:cd19085 168 ILPFcrehgigvlaysplaqglltgkFSSAEDFPPGdartRLFRHfEPGAEEETFEALEK------LKEIADELGVTMAQ 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446378920 218 VVLRWNVQR-GVT-VIPKSTRQERIEENFAIWDFSLTDNEMAQINA 261
Cdd:cd19085 242 LALAWVLQQpGVTsVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-282 |
6.71e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 104.90 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSIL-SNNLKMPMVGFGV--FKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN-EDAVGDAVREaiatglcTREELFIT 76
Cdd:COG1453 1 MQYRRLgKTGLEVSVLGFGGmrLPRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 77 SKL--WVQDMANydlAKAGIEASLKKSGLDYFDLYLLH---------QAMGDyFSAWRALEDAYEAGKLKAIGVSNfyaH 145
Cdd:COG1453 74 TKLppWVRDPED---MRKDLEESLKRLQTDYIDLYLIHglnteedleKVLKP-GGALEALEKAKAEGKIRHIGFST---H 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 146 ----VLANFCETVRITpMVNqveLHPYFA---QPAALE-------------TMKhynvqpeawaPLGGGR-HKPYENVMl 204
Cdd:COG1453 147 gsleVIKEAIDTGDFD-FVQ---LQYNYLdqdNQAGEEaleaaaekgigviIMK----------PLKGGRlANPPEKLV- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 205 qRIADAhQKTIAQVVLR--WNVQRGVTVIPKSTRQERIEENFAIWD--FSLTDNEMAQINAldlgyVGEAVKHFNPEFVR 280
Cdd:COG1453 212 -ELLCP-PLSPAEWALRflLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILER-----LAEELGELLKDFCT 284
|
..
gi 446378920 281 GC 282
Cdd:COG1453 285 GC 286
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-262 |
1.36e-23 |
|
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: 97.68 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSILSNN-LKMPMVGFG---------VFKV---TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAia 64
Cdd:cd19091 1 MEYRTLGRSgLKVSELALGtmtfgggggFFGAwggVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 65 tglctREELFITSK--LWVQDMAN-YDLAK----AGIEASLKKSGLDYFDLYLLHQ--AMGDYFSAWRALEDAYEAGKLK 135
Cdd:cd19091 79 -----RDDVLIATKvrGRMGEGPNdVGLSRhhiiRAVEASLKRLGTDYIDLYQLHGfdALTPLEETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 136 AIGVSNFYAHVLAN---FCETVRITPMV-NQV-----------ELHPyFAQPAALETMkhynvqpeAWAPLGGGR----H 196
Cdd:cd19091 154 YIGVSNFSAWQIMKalgISERRGLARFVaLQAyysllgrdlehELMP-LALDQGVGLL--------VWSPLAGGLlsgkY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 197 KPYENV--------------------------MLQRIADAHQKTIAQVVLRWNVQR--GVTVIPKSTRQERIEENFAIWD 248
Cdd:cd19091 225 RRGQPApegsrlrrtgfdfppvdrergydvvdALREIAKETGATPAQVALAWLLSRptVSSVIIGARNEEQLEDNLGAAG 304
|
330
....*....|....
gi 446378920 249 FSLTDNEMAQINAL 262
Cdd:cd19091 305 LSLTPEEIARLDKV 318
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-262 |
5.22e-23 |
|
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: 95.82 E-value: 5.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 32 VLSAIRSGYRLIDTAAVYG---NEDAVGDAVREaiatglcTREELFITSK---LWVQD-MANYDLAKAGI----EASLKK 100
Cdd:cd19102 32 IRAALDLGINWIDTAAVYGlghSEEVVGRALKG-------LRDRPIVATKcglLWDEEgRIRRSLKPASIraecEASLRR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 101 SGLDYFDLYLLHQAMGD--YFSAWRALEDAYEAGKLKAIGVSNFYAHVLANfCETVR----ITPMVNQV------ELHPY 168
Cdd:cd19102 105 LGVDVIDLYQIHWPDPDepIEEAWGALAELKEEGKVRAIGVSNFSVDQMKR-CQAIHpiasLQPPYSLLrrgieaEILPF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 169 FAQ---------P--AALETMKhynVQPEAWAPLGGGRHKPYENVM--------------LQRIADAHQKTIAQVVLRWN 223
Cdd:cd19102 184 CAEhgigvivysPmqSGLLTGK---MTPERVASLPADDWRRRSPFFqepnlarnlalvdaLRPIAERHGRTVAQLAIAWV 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446378920 224 VQR-GVT-VIPKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19102 261 LRRpEVTsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
16-262 |
8.47e-23 |
|
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: 95.56 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 16 GFGVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREAiatglcTREELFITSKLWVQDMANY----- 87
Cdd:cd19083 23 GHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEY------NRNEVVIATKGAHKFGGDGsvlnn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 88 --DLAKAGIEASLKKSGLDYFDLYLLHQAMGDYF--SAWRALEDAYEAGKLKAIGVSNFYAHVL--AN---FCETVR--- 155
Cdd:cd19083 97 spEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPkaEAVGALQELKDEGKIRAIGVSNFSLEQLkeANkdgYVDVLQgey 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 156 ----------ITPMV--NQVELHPYFAQPAALETMKH---YNVQPEAWAPLGGGRHKP-YENVM-----LQRIADAHQKT 214
Cdd:cd19083 177 nllqreaeedILPYCveNNISFIPYFPLASGLLAGKYtkdTKFPDNDLRNDKPLFKGErFSENLdkvdkLKSIADEKGVT 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446378920 215 IAQVVLRWNVQRGV--TVIPKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19083 257 VAHLALAWYLTRPAidVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-245 |
2.58e-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: 93.07 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 15 VGFGVFK------VTDKEECQQSVLSAIRSGYRLIDTAAVYGN-EDAVGDAVREAIatglctREELFITSKLWVQDMAN- 86
Cdd:cd19095 3 LGLGTSGigrvwgVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAGLR------RDDLFIATKVGTHGEGGr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 87 ------YDLAKAGIEASLKKSGLDYFDLYLLHQAMGDYFS--AWRALEDAYEAGKLKAIGVSNFYAHvLANFCETVRITp 158
Cdd:cd19095 77 drkdfsPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTgeVLETLEDLKAAGKVRYIGVSGDGEE-LEAAIASGVFD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 159 mVNQVELHPyfAQPAALETMkhynvqPEAWA---------PLGGGR---------HKPYENVMLQRIADAHQKTIAQVVL 220
Cdd:cd19095 155 -VVQLPYNV--LDREEEELL------PLAAEaglgvivnrPLANGRlrrrvrrrpLYADYARRPEFAAEIGGATWAQAAL 225
|
250 260
....*....|....*....|....*..
gi 446378920 221 RWNV-QRGVT-VIPKSTRQERIEENFA 245
Cdd:cd19095 226 RFVLsHPGVSsAIVGTTNPEHLEENLA 252
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
8-259 |
3.13e-22 |
|
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: 94.05 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 8 NNLKMPMVGFGVFKVT------DKEECQQSVL-SAIRSGYRLIDTAAVYG-NEDAVGdaVREAIATGlcTREELFITSK- 78
Cdd:cd19144 9 NGPSVPALGFGAMGLSafygppKPDEERFAVLdAAFELGCTFWDTADIYGdSEELIG--RWFKQNPG--KREKIFLATKf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 79 ----------LWVQDMANYdlAKAGIEASLKKSGLDYFDLYLLHQAMGD--YFSAWRALEDAYEAGKLKAIGVSNFYAHV 146
Cdd:cd19144 85 gieknvetgeYSVDGSPEY--VKKACETSLKRLGVDYIDLYYQHRVDGKtpIEKTVAAMAELVQEGKIKHIGLSECSAET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 147 LANFCETVRITPMvnQVELHPYF-----AQPAALETMKHYNVQPEAWAPLGGG------------------RHKP----- 198
Cdd:cd19144 163 LRRAHAVHPIAAV--QIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGfltgairspddfeegdfrRMAPrfqae 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 199 --YENVML----QRIADAHQKTIAQVVLRWNVQRG--VTVIPKSTRQERIEENFAIWDFSLTDNEMAQI 259
Cdd:cd19144 241 nfPKNLELvdkiKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-245 |
4.45e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 92.16 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 9 NLKMPMVGFG---VFKVTDkEECQQSVLSAIRSGYRLIDTAAVYGN-EDAVGDAVREAiatglctREELFITSKLWVQDm 84
Cdd:cd19100 8 GLKVSRLGFGggpLGRLSQ-EEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 85 anYDLAKAGIEASLKKSGLDYFDLYLLH---------QAMGDYfSAWRALEDAYEAGKLKAIGVS--NFYAHVLA---NF 150
Cdd:cd19100 79 --YEGAKRDLERSLKRLGTDYIDLYQLHavdteedldQVFGPG-GALEALLEAKEEGKIRFIGISghSPEVLLRAletGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 151 CETVriTPMVNQVELHPYFAQPAALET----------MKhynvqpeawaPLGGGrhkpyenvmlqRIADAHQKTIAQvVL 220
Cdd:cd19100 156 FDVV--LFPINPAGDHIDSFREELLPLarekgvgviaMK----------VLAGG-----------RLLSGDPLDPEQ-AL 211
|
250 260
....*....|....*....|....*..
gi 446378920 221 RWNVQRG--VTVIPKSTRQERIEENFA 245
Cdd:cd19100 212 RYALSLPpvDVVIVGMDSPEELDENLA 238
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-260 |
2.31e-21 |
|
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: 91.49 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 2 EYSILSNN-LKMP-----MVGFGVFK----VTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatgLC 68
Cdd:cd19079 1 EYVRLGNSgLKVSrlclgCMSFGDPKwrpwVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKE-----FA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 69 TREELFITSKLW--VQDMAN-YDLAK----AGIEASLKKSGLDYFDLYLLHQamgdyfsaW----------RALEDAYEA 131
Cdd:cd19079 76 PRDEVVIATKVYfpMGDGPNgRGLSRkhimAEVDASLKRLGTDYIDLYQIHR--------WdyetpieetlEALHDVVKS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 132 GKLKAIGVSNFYAHVLANfcetvritpMVNQVELHPyFAQPAALETmkHYN-VQPE-----------------AWAPLGG 193
Cdd:cd19079 148 GKVRYIGASSMYAWQFAK---------ALHLAEKNG-WTKFVSMQN--HYNlLYREeeremiplceeegigviPWSPLAR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 194 GR---------------------HKPYEN-----VM--LQRIADAHQKTIAQVVLRWNVQRGVTVIP--KSTRQERIEEN 243
Cdd:cd19079 216 GRlarpwgdtterrrsttdtaklKYDYFTeadkeIVdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDA 295
|
330
....*....|....*..
gi 446378920 244 FAIWDFSLTDNEMAQIN 260
Cdd:cd19079 296 VAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
7-259 |
2.88e-21 |
|
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: 91.12 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 7 SNNLKMPMVGFGVFKVT------DKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREAiatglctREELFITS 77
Cdd:cd19076 7 TQGLEVSALGLGCMGMSafygpaDEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 78 KL-WVQDMANYDL--------AKAGIEASLKKSGLDYFDLYLLH---------QAMGdyfsawrALEDAYEAGKLKAIGV 139
Cdd:cd19076 80 KFgIVRDPGSGFRgvdgrpeyVRAACEASLKRLGTDVIDLYYQHrvdpnvpieETVG-------AMAELVEEGKVRYIGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 140 SNFYAhvlanfcETVR-------ITPMvnQVELHPYF--AQPAALETMKHYNVQPEAWAPLGGG---------------- 194
Cdd:cd19076 153 SEASA-------DTIRrahavhpITAV--QSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLGRGfltgaikspedlpedd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 195 --RHKPY---ENVM--------LQRIADAHQKTIAQVVLRWNVQRG--VTVIPKSTRQERIEENFAIWDFSLTDNEMAQI 259
Cdd:cd19076 224 frRNNPRfqgENFDknlklvekLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
23-259 |
8.94e-21 |
|
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: 90.02 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 23 TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVRE-----AIAT--GLCTREELfiTSKLWVQDMA--NYDLA 90
Cdd:cd19149 30 SDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGrrdkvVLATkcGLRWDREG--GSFFFVRDGVtvYKNLS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KAGI----EASLKKSGLDYFDLYLLH---------QAMGdyfsawrALEDAYEAGKLKAIGVSNFYAHVLANFCETVRIT 157
Cdd:cd19149 108 PESIreevEQSLKRLGTDYIDLYQTHwqdvetpieETME-------ALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 158 pmVNQV-----------ELHPYFAQpaaletmkhYNVQPEAWAPLGGG------------------RHKPY---ENV--- 202
Cdd:cd19149 181 --IIQEkysmldrgiekELLPYCKK---------NNIAFQAYSPLEQGlltgkitpdrefdagdarSGIPWfspENRekv 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446378920 203 --MLQR---IADAHQKTIAQVVLRWNVQRG--VTVIPKSTRQERIEENFAIWDFSLTDNEMAQI 259
Cdd:cd19149 250 laLLEKwkpLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATM 313
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
9-260 |
2.66e-20 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 88.44 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 9 NLKMPMVGFGVF-------KVTDKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGdavrEAIATglcTREELFITSK 78
Cdd:cd19078 1 GLEVSAIGLGCMgmshgygPPPDKEEMIELIRKAVELGITFFDTAEVYGpytNEELVG----EALKP---FRDQVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 79 L----------WVQDMANYDLAKAGIEASLKKSGLDYFDLYLLH------------QAMGDYFsawraledayEAGKLKA 136
Cdd:cd19078 74 FgfkidggkpgPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHrvdpnvpieevaGTMKELI----------KEGKIRH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 137 IGVSNfyAHVlanfcETVR----ITPMVN-QVELHPYFAQPAA--LETMKHYNVQPEAWAPLG----GGRHKPY------ 199
Cdd:cd19078 144 WGLSE--AGV-----ETIRrahaVCPVTAvQSEYSMMWREPEKevLPTLEELGIGFVPFSPLGkgflTGKIDENtkfdeg 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 200 -----------ENV--------MLQRIADAHQKTIAQVVLRW--NVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQ 258
Cdd:cd19078 217 ddraslprftpEALeanqalvdLLKEFAEEKGATPAQIALAWllAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELRE 296
|
..
gi 446378920 259 IN 260
Cdd:cd19078 297 IE 298
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
12-252 |
3.55e-20 |
|
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: 87.27 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVFKV-TDKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREA-----IAT-GLCTReelfITSKLWV 81
Cdd:cd19088 9 MRLTGPGIWGPpADREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYpddvvIATkGGLVR----TGPGWWG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 82 QDMANYDLAKAgIEASLKKSGLDYFDLYLLHQ-----AMGDYFSAWRALEDayeAGKLKAIGVSNFYAHVLAnfcETVRI 156
Cdd:cd19088 85 PDGSPEYLRQA-VEASLRRLGLDRIDLYQLHRidpkvPFEEQLGALAELQD---EGLIRHIGLSNVTVAQIE---EARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 157 TPMVN-QVELHPYFAQPAA-LETMKHYNVQPEAWAPLGGGRHKPYEnVMLQRIADAHQKTIAQVVLRWNVQRG--VTVIP 232
Cdd:cd19088 158 VRIVSvQNRYNLANRDDEGvLDYCEAAGIAFIPWFPLGGGDLAQPG-GLLAEVAARLGATPAQVALAWLLARSpvMLPIP 236
|
250 260
....*....|....*....|
gi 446378920 233 KSTRQERIEENFAIWDFSLT 252
Cdd:cd19088 237 GTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-140 |
1.41e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 82.63 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSILSN-NLKMPMVGFGVfkVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAiatglcTREELFIT 76
Cdd:cd19105 1 MPYRTLGKtGLKVSRLGFGG--GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKGL------RRDKVFLA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 77 SK-LWVQDMANYDLAKAGIEASLKKSGLDYFDLYLLHQAMG---DYFSAW--RALEDAYEAGKLKAIGVS 140
Cdd:cd19105 73 TKaSPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTpeeRLLNEEllEALEKLKKEGKVRFIGFS 142
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-245 |
1.77e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 83.52 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 15 VGFGVFKV----TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAIATGLCTREELFITSK--------- 78
Cdd:cd19099 6 LGLGTYRGdsddETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 79 ------LWVQDMAN-------------YDLAKAGIEASLKKS----GLDYFDLYLLHQ--------AMGDYFS----AWR 123
Cdd:cd19099 86 eplrplKYLEEKLGrglidvadsaglrHCISPAYLEDQIERSlkrlGLDTIDLYLLHNpeeqllelGEEEFYDrleeAFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 124 ALEDAYEAGKLKAIGVS-NFYAHVLANFCETVRITPMVN---------------QVELHPYFAQ------------PAAL 175
Cdd:cd19099 166 ALEEAVAEGKIRYYGIStWDGFRAPPALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLEPEaltekntvkgeaLSLL 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446378920 176 ETMKHYNVQPEAWAPLGGGRHKPyENVMLQRIADAHQKTIAQVVLRWNV-QRGV-TVIPKSTRQERIEENFA 245
Cdd:cd19099 246 EAAKELGLGVIASRPLNQGQLLG-ELRLADLLALPGGATLAQRALQFARsTPGVdSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-245 |
1.90e-18 |
|
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: 82.14 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 15 VGFG-------VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatglcTREELFITSKL----- 79
Cdd:cd19086 6 IGFGtwglggdWWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 80 -WVQDMANYDLA--KAGIEASLKKSGLDYFDLYLLHQAMGDYF---SAWRALEDAYEAGKLKAIGVS-----NFYAHVLA 148
Cdd:cd19086 79 gGPERPQDFSPEyiREAVEASLKRLGTDYIDLYQLHNPPDEVLdndELFEALEKLKQEGKIRAYGVSvgdpeEALAALRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 149 NFCETVritpmvnQVELHPYFAQPA--ALETMKHYNVQPEAWAPLGGGrhkpyenvMLQRiadahqkTIAQVVLRWNVQR 226
Cdd:cd19086 159 GGIDVV-------QVIYNLLDQRPEeeLFPLAEEHGVGVIARVPLASG--------LLTG-------KLAQAALRFILSH 216
|
250 260
....*....|....*....|...
gi 446378920 227 -GV-TVIP--KSTRQerIEENFA 245
Cdd:cd19086 217 pAVsTVIPgaRSPEQ--VEENAA 237
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
24-246 |
5.71e-18 |
|
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: 81.07 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 24 DKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAiatglcTREELFITSKLWVQDMANYDLAKAGIEASLKK 100
Cdd:cd19096 19 DEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKEG------PREKFYLATKLPPWSVKSAEDFRRILEESLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 101 SGLDYFDLYLLHqAMGDYFS--------AWRALEDAYEAGKLKAIGVSnfyAHV-LANFCETVRITPM-VNQVELHpYFA 170
Cdd:cd19096 93 LGVDYIDFYLLH-GLNSPEWlekarkggLLEFLEKAKKEGLIRHIGFS---FHDsPELLKEILDSYDFdFVQLQYN-YLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 171 QP-----AALETMKHYNVQPEAWAPLGGGRHKPYENVMLQRIADAHQkTIAQVVLRWNV-QRGVTVI---PKSTRQerIE 241
Cdd:cd19096 168 QEnqagrPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGAPL-SPAEWALRFLLsHPEVTTVlsgMSTPEQ--LD 244
|
....*
gi 446378920 242 ENFAI 246
Cdd:cd19096 245 ENIAA 249
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
23-262 |
4.71e-17 |
|
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: 79.54 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 23 TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatglcTREELFITSK--------LWVQDMANYDLAK 91
Cdd:cd19087 27 TDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKvfgpmgddPNDRGLSRRHIRR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 92 AgIEASLKKSGLDYFDLYLLHQamgdYFSA------WRALEDAYEAGKLKAIGVSNFYAHVLANFCET---------VRI 156
Cdd:cd19087 100 A-VEASLRRLQTDYIDLYQMHH----FDRDtpleetLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIaarrgllrfVSE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 157 TPMVN----QVELHpyfAQPAALetmkHYNVQPEAWAPLGGG------------------RHKPYENVM----------- 203
Cdd:cd19087 175 QPMYNllkrQAELE---ILPAAR----AYGLGVIPYSPLAGGlltgkygkgkrpesgrlvERARYQARYgleeyrdiaer 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446378920 204 LQRIADAHQKTIAQVVLRWNVQR-GVT--VI-PKSTRQerIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19087 248 FEALAAEAGLTPASLALAWVLSHpAVTspIIgPRTLEQ--LEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
18-245 |
1.60e-16 |
|
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: 77.59 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 18 GVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN-EDAVGDAVREAiatglcTREELFITSKL--WVQDMANY--DLAKA 92
Cdd:cd19090 12 GVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAEL------PREPLVLSTKVgrLPEDTADYsaDRVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 93 GIEASLKKSGLDYFDLYLLH--QAMGDYFS-----AWRALEDAYEAGKLKAIGVSNFYAHVLANFCETV---------RI 156
Cdd:cd19090 86 SVEESLERLGRDRIDLLMIHdpERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGdfdvvltanRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 157 TPmVNQVELHPYFaqPAALEtmkhYNVQPEAWAPLGGG----------RHKPYENV--------MLQRIADAHQKTIAQV 218
Cdd:cd19090 166 TL-LDQSAADELL--PAAAR----HGVGVINASPLGMGllagrppervRYTYRWLSpelldrakRLYELCDEHGVPLPAL 238
|
250 260
....*....|....*....|....*....
gi 446378920 219 VLRW--NVQRGVTVIPKSTRQERIEENFA 245
Cdd:cd19090 239 ALRFllRDPRISTVLVGASSPEELEQNVA 267
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
23-260 |
1.92e-16 |
|
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: 77.64 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 23 TDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatglcTREELFITSKlWVQDMANYDLAKAG------ 93
Cdd:cd19080 28 ADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAG-------NRDRIVLATK-YTMNRRPGDPNAGGnhrknl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 94 ---IEASLKKSGLDYFDLYLLHqaMGDYFSA----WRALEDAYEAGKLKAIGVSNFYAHVLANfCETVritpmvnqVELH 166
Cdd:cd19080 100 rrsVEASLRRLQTDYIDLLYVH--AWDFTTPveevMRALDDLVRAGKVLYVGISDTPAWVVAR-ANTL--------AELR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 167 PYfAQPAALETmkHYNV---QPE---------------AWAPLGGG------------RHKPYENVM------------- 203
Cdd:cd19080 169 GW-SPFVALQI--EYSLlerTPErellpmaralglgvtPWSPLGGGlltgkyqrgeegRAGEAKGVTvgfgklternwai 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446378920 204 ---LQRIADAHQKTIAQVVLRWNVQRGVTVIP--KSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19080 246 vdvVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
8-260 |
3.51e-16 |
|
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: 76.87 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 8 NNLKMPMVGFG--VFKVTDKEECQQSVLSA-IRSGYRLIDTAAVYGNEDAVGDAVR-EAI------ATGlcTREELFITS 77
Cdd:cd19081 5 TGLSVSPLCLGtmVFGWTADEETSFALLDAfVDAGGNFIDTADVYSAWVPGNAGGEsETIigrwlkSRG--KRDRVVIAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 78 KL-WVQDMANYDLAKA----GIEASLKKSGLDYFDLYLLHQ--AMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANF 150
Cdd:cd19081 83 KVgFPMGPNGPGLSRKhirrAVEASLRRLQTDYIDLYQAHWddPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 151 CETVRitpmvnQVELHPY-FAQPaaletmkHYN----------VQPEA---------WAPLGGG---------------- 194
Cdd:cd19081 163 LELSR------QHGLPRYvSLQP-------EYNlvdresfegeLLPLCreegigvipYSPLAGGfltgkyrseadlpgst 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 195 ----RHKPYEN-----VM--LQRIADAHQKTIAQVVLRWNVQR-GVT-VIPKSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19081 230 rrgeAAKRYLNerglrILdaLDEVAAEHGATPAQVALAWLLARpGVTaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
8-260 |
7.31e-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: 73.04 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 8 NNLKMPMVGFGVFKVT------DKEECQQSVLSAIRSGYRLIDTAAVYGNEDAVG--DAVREAIATGLCTREELFITSKL 79
Cdd:cd19077 1 NGKLVGPIGLGLMGLTwrpnptPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 80 -WVQDMANYDLAKAGIEASLKKS-----GLDYFDLY---------LLHQAMGdyfsawrALEDAYEAGKLKAIGVSnfya 144
Cdd:cd19077 81 gLDPDTLRPDGSPEAVRKSIENIlralgGTKKIDIFeparvdpnvPIEETIK-------ALKELVKEGKIRGIGLS---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 145 HVLAnfcETVR----ITPMV-NQVELHPYF---AQPAALETMKHYNVQPEAWAPLGGG------------------RHKP 198
Cdd:cd19077 150 EVSA---ETIRrahaVHPIAaVEVEYSLFSreiEENGVLETCAELGIPIIAYSPLGRGlltgriksladipegdfrRHLD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446378920 199 ------YENVM-----LQRIADAHQKTIAQVVLRWNVQRGVTVI---PKSTRQERIEENFAIWDFSLTDNEMAQIN 260
Cdd:cd19077 227 rfngenFEKNLklvdaLQELAEKKGCTPAQLALAWILAQSGPKIipiPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
23-142 |
9.41e-15 |
|
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: 72.72 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 23 TDKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREaiatgLCTREELFITSKL---WVQ-DMANYDLAKAGI- 94
Cdd:cd19148 22 TDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKE-----YGKRDRVVIATKVgleWDEgGEVVRNSSPARIr 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446378920 95 ---EASLKKSGLDYFDLYLLHqamgdyfsaW-----------RALEDAYEAGKLKAIGVSNF 142
Cdd:cd19148 97 kevEDSLRRLQTDYIDLYQVH---------WpdplvpieetaEALKELLDEGKIRAIGVSNF 149
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-254 |
1.12e-14 |
|
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: 72.62 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 10 LKMPMVGFG----VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGNEDA---VGDAVREAiatglcTREELFITSKL-WV 81
Cdd:cd19074 2 LKVSELSLGtwltFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAeevLGKALKGW------PRESYVISTKVfWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 82 QDMANYD--LAKA----GIEASLKKSGLDYFDLYLLHQAmgDYFS----AWRALEDAYEAGKLKAIGVSNFYAHVLANFC 151
Cdd:cd19074 76 TGPGPNDrgLSRKhifeSIHASLKRLQLDYVDIYYCHRY--DPETpleeTVRAMDDLIRQGKILYWGTSEWSAEQIAEAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 152 ETVR----ITPMVNQVELHpYFAQPAALE----TMKHyNVQPEAWAPL---------------GGGRHKPYENVM----- 203
Cdd:cd19074 154 DLARqfglIPPVVEQPQYN-MLWREIEEEviplCEKN-GIGLVVWSPLaqglltgkyrdgippPSRSRATDEDNRdkkrr 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446378920 204 ------------LQRIADAHQKTIAQVVLRWNVQR-GVT-VIPKSTRQERIEENFAIWDFSLTDN 254
Cdd:cd19074 232 lltdenlekvkkLKPIADELGLTLAQLALAWCLRNpAVSsAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-245 |
1.63e-14 |
|
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: 72.20 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 16 GFGVFKVTDKEECQQSVLSAIRS-GYRLIDTAAVYGN---EDAVGDAvreaiatGLCTREeLFITSKL--WVQDMANYDL 89
Cdd:cd19075 9 TFGSQGRFTTAEAAAELLDAFLErGHTEIDTARVYPDgtsEELLGEL-------GLGERG-FKIDTKAnpGVGGGLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 90 AKAGIEASLKKSGLDYFDLYLLHQA-----MGDYFsawRALEDAYEAGKLKAIGVSNFYAHVLANFCETVR----ITPMV 160
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLHAPdrstpLEETL---AAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 161 NQ---------VElhpyfaqPAALETMKHYNVQPEAWAPLGGG----RHKPYENV------------------------- 202
Cdd:cd19075 158 YQgmynaitrqVE-------TELFPCLRKLGIRFYAYSPLAGGfltgKYKYSEDKagggrfdpnnalgklyrdrywkpsy 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446378920 203 -----MLQRIADAHQKTIAQVVLRW-------NVQRGVTVIPKSTRQERIEENFA 245
Cdd:cd19075 231 fealeKVEEAAEKEGISLAEAALRWlyhhsalDGEKGDGVILGASSLEQLEENLA 285
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-140 |
7.06e-14 |
|
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: 70.27 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSILSN-NLKMPMVGFG------VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAiatglcTR 70
Cdd:cd19163 1 MKYRKLGKtGLKVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKGI------PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 71 EELFITSK-----LWVQDMANYDLAK--AGIEASLKKSGLDYFDLYLLHQA-MGDYFS-----AWRALEDAYEAGKLKAI 137
Cdd:cd19163 75 DSYYLATKvgrygLDPDKMFDFSAERitKSVEESLKRLGLDYIDIIQVHDIeFAPSLDqilneTLPALQKLKEEGKVRFI 154
|
...
gi 446378920 138 GVS 140
Cdd:cd19163 155 GIT 157
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
10-257 |
8.99e-13 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 67.28 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 10 LKMPMVGFGVFK----VTDKEECQQSVLSAIRSGYRLIDTAAVYGN-----EDAVGDAVREAIATglcTREELFITSK-- 78
Cdd:cd19089 9 LHLPAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRP---YRDELVISTKag 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 79 --LWVQDMANYDLAK---AGIEASLKKSGLDYFDLYLLH---------QAMGdyfsawrALEDAYEAGKLKAIGVSNF-- 142
Cdd:cd19089 86 ygMWPGPYGDGGSRKyllASLDQSLKRMGLDYVDIFYHHrydpdtpleETMT-------ALADAVRSGKALYVGISNYpg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 143 -YAHVLANFCETVRITPMVNQVE---LHPYfAQPAALETMKHYNVQPEAWAPLGGG--------RHKPYENVM------- 203
Cdd:cd19089 159 aKARRAIALLRELGVPLIIHQPRyslLDRW-AEDGLLEVLEEAGIGFIAFSPLAQGlltdkylnGIPPDSRRAaeskflt 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446378920 204 --------------LQRIADAHQKTIAQVVLRWNVQR-GVT-VIPKSTRQERIEENF-AIWDFSLTDNEMA 257
Cdd:cd19089 238 eealtpekleqlrkLNKIAAKRGQSLAQLALSWVLRDpRVTsVLIGASSPSQLEDNVaALKNLDFSEEELA 308
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-140 |
1.11e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 66.40 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 35 AIRSGYRLIDTAAVYGN-EDAVGDAvreaiatgLCTREELFITSKL---WVQDMANYDLAKAGIEASLKKSGLDYFDLYL 110
Cdd:cd19097 35 ALKAGINTLDTAPAYGDsEKVLGKF--------LKRLDKFKIITKLpplKEDKKEDEAAIEASVEASLKRLKVDSLDGLL 106
|
90 100 110
....*....|....*....|....*....|...
gi 446378920 111 LHQAM---GDYFSAWRALEDAYEAGKLKAIGVS 140
Cdd:cd19097 107 LHNPDdllKHGGKLVEALLELKKEGLIRKIGVS 139
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-262 |
1.31e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 66.59 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 9 NLKMPMV-------------GFGVFKVT-DKEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREAiatglcTRE 71
Cdd:cd19103 1 DKKLPKIalgtwswgsggagGDQVFGNHlDEDTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKRY------PRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 72 ELFITSKLWVQDMANY-DLAKAGIEASLKKSGLDYFDLYLLHQAMGdyFSAWRA-LEDAYEAGKLKAIGVSNFyahvlaN 149
Cdd:cd19103 75 DYIISTKFTPQIAGQSaDPVADMLEGSLARLGTDYIDIYWIHNPAD--VERWTPeLIPLLKSGKVKHVGVSNH------N 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 150 FCETVRITPMVNQVELHPYFAQ------------PAALETMKHYNVQPEAWA-----------------PLGGGRHKPYE 200
Cdd:cd19103 147 LAEIKRANEILAKAGVSLSAVQnhysllyrsseeAGILDYCKENGITFFAYMvleqgalsgkydtkhplPEGSGRAETYN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446378920 201 NVM---------LQRIADAHQKTIAQVVLRWNVQRGVTVIPKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19103 227 PLLpqleeltavMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-261 |
5.64e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 64.92 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 21 KVTDKEECQQSVLSAIRSGYRLIDTAAVYGN-EDAVGDAVREAiATGLCTREELFITSKlWVQDMANYDLAKAGIEA--- 96
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRL-RRERDAADDVQIHTK-WVPDPGELTMTRAYVEAaid 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 97 -SLKKSGLDYFDLYLLH---QAMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETvRITPMVNQVE-------- 164
Cdd:cd19101 96 rSLKRLGVDRLDLVQFHwwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDA-GVPIVSNQVQyslldrrp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 165 --------------LHPYFAQPAALETMKHYNVQPEAWAPLGGGRHKPYENVM---------------LQRIADAHQKTI 215
Cdd:cd19101 175 engmaalcedhgikLLAYGTLAGGLLSEKYLGVPEPTGPALETRSLQKYKLMIdewggwdlfqellrtLKAIADKHGVSI 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446378920 216 AQVVLRWNVQR-GVT-VIPKSTRQERIEENFAIWDFSLTDNEMAQINA 261
Cdd:cd19101 255 ANVAVRWVLDQpGVAgVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
91-262 |
2.78e-11 |
|
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: 62.97 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KAGIEASLKKSGLDYFDLYLLH-------QAMGDYFSAW-------------RALEDAYEAGKLKAIGVSNFYAHVLANF 150
Cdd:cd19094 99 REAVEGSLKRLGTDYIDLYQLHwpdrytpLFGGGYYTEPseeedsvsfeeqlEALGELVKAGKIRHIGLSNETPWGVMKF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 151 CETVR---ITPMV-----------NQVELHPyfaqpaalETMKHYNVQPEAWAPLGGG----------------RHKPYE 200
Cdd:cd19094 179 LELAEqlgLPRIVsiqnpysllnrNFEEGLA--------EACHRENVGLLAYSPLAGGvltgkyldgaarpeggRLNLFP 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 201 NVM--------------LQRIADAHQKTIAQVVLRWNVQR---GVTVIpKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:cd19094 251 GYMaryrspqaleavaeYVKLARKHGLSPAQLALAWVRSRpfvTSTII-GATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
10-260 |
5.45e-11 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 62.31 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 10 LKMPMVGFGV---FKVTDKEECQQSVL-SAIRSGYRLIDTAAVYG-----NEDAVGDAVREAIATglcTREELFITSKlw 80
Cdd:PRK09912 23 LRLPALSLGLwhnFGHVNALESQRAILrKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAA---YRDELIISTK-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 81 vqdmANYDLAK-------------AGIEASLKKSGLDYFDLYLLHQA-----MGDYFSawrALEDAYEAGKLKAIGVSNF 142
Cdd:PRK09912 98 ----AGYDMWPgpygsggsrkyllASLDQSLKRMGLEYVDIFYSHRVdentpMEETAS---ALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 143 YAHVLANFCETVR---ITPMVNQVE---LHPYFAQPAALETMKHYNVQPEAWAPL----------------------GGG 194
Cdd:PRK09912 171 SPERTQKMVELLRewkIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLaqglltgkylngipqdsrmhreGNK 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 195 RHKPYENV----------MLQRIADAHQKTIAQVVLRWNV--QRGVTVIPKSTRQERIEENF-AIWDFSLTDNEMAQIN 260
Cdd:PRK09912 251 VRGLTPKMlteanlnslrLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVqALNNLTFSTEELAQID 329
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
35-259 |
6.78e-11 |
|
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: 61.68 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 35 AIRSGYRLIDTAAVYG---NEDAVGDAVREAIatglctREELFITSKLWVQDMANY--------DLAKAGIEASLKKSGL 103
Cdd:cd19145 42 AFNSGVTFLDTSDIYGpntNEVLLGKALKDGP------REKVQLATKFGIHEIGGSgvevrgdpAYVRAACEASLKRLDV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 104 DYFDLYLLHQ---------AMGdyfsawrALEDAYEAGKLKAIGVSNFYAhvlanfcETVR-------ITPMvnQVE--L 165
Cdd:cd19145 116 DYIDLYYQHRidttvpieiTMG-------ELKKLVEEGKIKYIGLSEASA-------DTIRrahavhpITAV--QLEwsL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 166 HPYFAQPAALETMKHYNVQPEAWAPLGGG-------------------RHKPYE-------NVMLQRIADAHQK---TIA 216
Cdd:cd19145 180 WTRDIEEEIIPTCRELGIGIVPYSPLGRGffagkakleellensdvrkSHPRFQgenleknKVLYERVEALAKKkgcTPA 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446378920 217 QVVLRWNVQRG--VTVIPKSTRQERIEENFAIWDFSLTDNEMAQI 259
Cdd:cd19145 260 QLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
13-140 |
2.27e-10 |
|
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: 60.07 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 13 PMVGFG------VFKVTDkEECQQSVLSAIRSGYRLIDTAAVYG---NEDAVGDAVREAiatglcTREELFITSK---LW 80
Cdd:cd19162 1 PRLGLGaaslgnLARAGE-DEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKvgrLL 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 81 VQDMANY--------DLAKAG----IEASLKKSGLDYFDLYLLH-------QAMGDyfsAWRALEDAYEAGKLKAIGVS 140
Cdd:cd19162 74 EPGAAGRpagadrrfDFSADGirrsIEASLERLGLDRLDLVFLHdpdrhllQALTD---AFPALEELRAEGVVGAIGVG 149
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
12-262 |
2.91e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 59.60 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 12 MPMVGFGVF-KVTDKEECQQSVLSAIRSGYRLIDTAAVYG----NEdavgdAVREAIATGlctREELFITSKL------- 79
Cdd:PRK10376 25 MQLAGPGVFgPPKDRDAAIAVLREAVALGVNHIDTSDFYGphvtNQ-----LIREALHPY---PDDLTIVTKVgarrged 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 80 --WVQDMANYDLAKAgIEASLKKSGLDYFDLYLLhQAMGDYFS-AWRALEDAYEA-------GKLKAIGVSNFYAhvlAN 149
Cdd:PRK10376 97 gsWLPAFSPAELRRA-VHDNLRNLGLDVLDVVNL-RLMGDGHGpAEGSIEEPLTVlaelqrqGLVRHIGLSNVTP---TQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 150 FCETVRITPMV---NQVEL-H------------------PYFaqpaaletmkhynvqpeawaPLGGgrHKPYENVMLQRI 207
Cdd:PRK10376 172 VAEARKIAEIVcvqNHYNLaHraddalidalardgiayvPFF--------------------PLGG--FTPLQSSTLSDV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446378920 208 ADAHQKTIAQVVLRWNVQRG--VTVIPKSTRQERIEENFAIWDFSLTDNEMAQINAL 262
Cdd:PRK10376 230 AASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-140 |
4.60e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 59.20 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 10 LKMPMVGFG------VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREaiatglcTREELFITSKLW 80
Cdd:cd19104 10 LKVSELTFGgggiggLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKG-------LPAGPYITTKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 81 VQDMANYDLA---KAGIEASLKKSGLDYFDLYLLHQAMGD-----------------YFSAWRALEDAYEAGKLKAIGVS 140
Cdd:cd19104 83 LDPDDLGDIGgqiERSVEKSLKRLKRDSVDLLQLHNRIGDerdkpvggtlsttdvlgLGGVADAFERLRSEGKIRFIGIT 162
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-245 |
5.22e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 58.88 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 17 FGVfkVTDKEECQQSVLSAIRSGYRLIDTAAVYG--NEDAVGDAVREAIATGL---CTREELFITSKL------WVQDMA 85
Cdd:cd19752 10 FGT--RTDEETSFAILDRYVAAGGNFLDTANNYAfwTEGGVGGESERLIGRWLkdrGNRDDVVIATKVgagprdPDGGPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 86 NY-----DLAKAGIEASLKKSGLDYFDLYLLH---------QAMGdyfsawrALEDAYEAGKLKAIGVSNFYAHVLANfc 151
Cdd:cd19752 88 SPeglsaETIEQEIDKSLRRLGTDYIDLYYAHvddrdtpleETLE-------AFNELVKAGKVRAIGASNFAAWRLER-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 152 etvritpmVNQVELHPYFAQPAALEtMKHYNVQPEAWAPLGGGR------------HK-----PYENVM----------- 203
Cdd:cd19752 159 --------ARQIARQQGWAEFSAIQ-QRHSYLRPRPGADFGVQRivtdelldyassRPdltllAYSPLLsgaytrpdrpl 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 204 ---------------LQRIADAHQKTIAQVVLRWNVQRGVTVIP--KSTRQERIEENFA 245
Cdd:cd19752 230 peqydgpdsdarlavLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
36-141 |
7.47e-10 |
|
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: 58.33 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 36 IRSGYRLIDTAAVYGneDAVGDAVREAI------ATGLctREELFITSK--------LWVQDMANYDLAKAgIEASLKKS 101
Cdd:cd19082 27 VELGGNFIDTARVYG--DWVERGASERVigewlkSRGN--RDKVVIATKgghpdledMSRSRLSPEDIRAD-LEESLERL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446378920 102 GLDYFDLYLLH-----QAMGDYFSawrALEDAYEAGKLKAIGVSN 141
Cdd:cd19082 102 GTDYIDLYFLHrddpsVPVGEIVD---TLNELVRAGKIRAFGASN 143
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
17-251 |
1.90e-08 |
|
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: 54.21 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 17 FGVFKVTDKEEC--QQSVLSAIRSGYRLIDTAAVYGNEDAV-GDAVReAIATGLcTREELFITSKLWVQDMANYDLAKAG 93
Cdd:cd19164 23 FSYQYTTDPESIppVDIVRRALELGIRAFDTSPYYGPSEIIlGRALK-ALRDEF-PRDTYFIITKVGRYGPDDFDYSPEW 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 94 IEASLKKS----GLDYFDLYLLHQ----AMGDYFSAWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRitpmvnqvel 165
Cdd:cd19164 101 IRASVERSlrrlHTDYLDLVYLHDvefvADEEVLEALKELFKLKDEGKIRNVGISGYPLPVLLRLAELAR---------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 166 HPYFAQPAALETMKHYNVQ-----------------------------------PEAWAPLGGG-RHKPYENVmlqRIAD 209
Cdd:cd19164 171 TTAGRPLDAVLSYCHYTLQnttllayipkflaaagvkvvlnasplsmgllrsqgPPEWHPASPElRAAAAKAA---EYCQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446378920 210 AHQKTIAQV----VLRWNVQRGVTVIPKSTRQErIEENFAIWDFSL 251
Cdd:cd19164 248 AKGTDLADValryALREWGGEGPTVVGCSNVDE-LEEAVEAYWSVL 292
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
13-245 |
1.21e-06 |
|
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: 49.14 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 13 PMVGFG------VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVREAiatglcTREELFITSKL---- 79
Cdd:cd19152 1 PKLGFGtaplgnLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 80 -------------WVQDMAN---YDLAKAGIEASLKKS----GLDYFDLYLLH----------------QAMGDyfsAWR 123
Cdd:cd19152 75 vplqeveptfepgFWNPLPFdavFDYSYDGILRSIEDSlqrlGLSRIDLLSIHdpdedlagaesdehfaQAIKG---AFR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 124 ALEDAYEAGKLKAIGV-SNFyAHVLANFCEtvRITP---MV-NQVELhpyFAQPAALETM----KHyNVQPEAWAP---- 190
Cdd:cd19152 152 ALEELREEGVIKAIGLgVND-WEVILRILE--EADLdwvMLaGRYTL---LDHSAARELLpeceKR-GVKVVNAGPfnsg 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 191 -LGGGRHKPYENV------MLQR------IADAHQKTIAQVVLRWNVQ-RGV-TVIPKSTRQERIEENFA 245
Cdd:cd19152 225 fLAGGDNFDYYEYgpappeLIARrdrieaLCEQHGVSLAAAALQFALApPAVaSVAPGASSPERVEENVA 294
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
32-184 |
2.89e-06 |
|
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: 47.92 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 32 VLSAIRSGYRLIDTAAVYGN---EDAVGDAVREA--------IATGLCT-REELFITSKlwvqdmanyDLAKAGIEASLK 99
Cdd:cd19153 39 VAEAFAAGINHFDTSPYYGAessEAVLGKALAALqvprssytVATKVGRyRDSEFDYSA---------ERVRASVATSLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 100 KSGLDYFDLYLLHQA-MGDYFS----AWRALEDAYEAGKLKAIGVSNFYAHVLANFCETVRITPmvnqvelhpyfaqPAA 174
Cdd:cd19153 110 RLHTTYLDVVYLHDIeFVDYDTlvdeALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS-------------LDA 176
|
170
....*....|
gi 446378920 175 LETMKHYNVQ 184
Cdd:cd19153 177 VLSYCHLTLQ 186
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-261 |
4.15e-06 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 47.21 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 1 MEYSILSNN-LKMPMVGFG---VFKVTDKEECQQSVLSAIR-SGYRLIDTAAVYGN---EDAVGDAVREAiatGLcTREE 72
Cdd:cd19143 1 MEYRRLGRSgLKVSALSFGswvTFGNQVDVDEAKECMKAAYdAGVNFFDNAEVYANgqsEEIMGQAIKEL---GW-PRSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 73 LFITSKL---WVQDMAN-YDLAKA----GIEASLKKSGLDYFDLYLLHQ------------AM------GDYF----SAW 122
Cdd:cd19143 77 YVVSTKIfwgGGGPPPNdRGLSRKhiveGTKASLKRLQLDYVDLVFCHRpdpatpieetvrAMndlidqGKAFywgtSEW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 123 RA--LEDAYE-AGKLKAIGvsnfyahvlanfcetvritPMVNQ------------VELHPYFAQpaaletmkhYNVQPEA 187
Cdd:cd19143 157 SAqqIEEAHEiADRLGLIP-------------------PVMEQpqynlfhrerveVEYAPLYEK---------YGLGTTT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 188 WAPLGGG--------------R--HKPYENVM----------------LQRIADAHQKTIAQVVLRW-----NVQrgvTV 230
Cdd:cd19143 209 WSPLASGlltgkynngipegsRlaLPGYEWLKdrkeelgqekiekvrkLKPIAEELGCSLAQLAIAWclknpNVS---TV 285
|
330 340 350
....*....|....*....|....*....|...
gi 446378920 231 IPKSTRQERIEENFAIWDF--SLTDNEMAQINA 261
Cdd:cd19143 286 ITGATKVEQLEENLKALEVlpKLTPEVMEKIEA 318
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
18-138 |
4.36e-06 |
|
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: 47.32 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 18 GVFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVRE------AIATG----LCTREELFITSKLWVQD- 83
Cdd:cd19161 12 NLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREkprdefVLSTKvgrlLKPAREGSVPDPNGFVDp 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378920 84 ---MANYDLAKAGI----EASLKKSGLDYFDLYLLH-----------------QAMGdyfSAWRALEDAYEAGKLKAIG 138
Cdd:cd19161 92 lpfEIVYDYSYDGImrsfEDSLQRLGLNRIDILYVHdigvythgdrkerhhfaQLMS---GGFKALEELKKAGVIKAFG 167
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
10-257 |
9.68e-06 |
|
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: 46.29 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 10 LKMPMVGFGV---FKVTDKEECQQSVL-SAIRSGYRLIDTAAVYG-----NEDAVGDAVREAIATglcTREELFITSKlw 80
Cdd:cd19150 10 LKLPALSLGLwhnFGDDTPLETQRAILrTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAG---YRDELIISTK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 81 vqdmANYDLAK-------------AGIEASLKKSGLDYFDLYLLH---------QAMGdyfsawrALEDAYEAGKLKAIG 138
Cdd:cd19150 85 ----AGYDMWPgpygewgsrkyllASLDQSLKRMGLDYVDIFYSHrfdpdtpleETMG-------ALDHAVRSGKALYVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 139 VSNFYAHVLANFCETVRI--TP-MVNQVE---LHPYFAQPAALETMKHYNVQPEAWAPLGGG-----------------R 195
Cdd:cd19150 154 ISSYSPERTREAAAILRElgTPlLIHQPSynmLNRWVEESGLLDTLQELGVGCIAFTPLAQGlltdkylngipegsrasK 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446378920 196 HKPYENVM-----------LQRIADAHQKTIAQVVLRWNVQRGV--TVIPKSTRQERIEENF-AIWDFSLTDNEMA 257
Cdd:cd19150 234 ERSLSPKMlteanlnsiraLNEIAQKRGQSLAQMALAWVLRDGRvtSALIGASRPEQLEENVgALDNLTFSADELA 309
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
35-194 |
3.11e-05 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 35 AIRSGYRLIDTAAVYG----------NEDAVGDAVReaiATGlcTREELFITSKL--------------WVQDMANydlA 90
Cdd:PRK10625 39 AVAQGINLIDVAEMYPvpprpetqglTETYIGNWLA---KRG--SREKLIIASKVsgpsrnndkgirpnQALDRKN---I 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 91 KAGIEASLKKSGLDYFDLYLLH--QAMGDYFS----AW-------------RALEDAYEAGKLKAIGVSN-------FYA 144
Cdd:PRK10625 111 REALHDSLKRLQTDYLDLYQVHwpQRPTNCFGklgySWtdsapavslletlDALAEQQRAGKIRYIGVSNetafgvmRYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446378920 145 HvLANFCETVRITPMVNQVELHPYFAQPAALETMKHYNVQPEAWAPLGGG 194
Cdd:PRK10625 191 H-LAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFG 239
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
38-266 |
5.87e-05 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 43.95 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 38 SGYRLIDTAAVYGNEDA---VGD--AVRE-----AIATGLCTREELFITSKLWVQDMANYdlAKA---GIEASLKKSGLD 104
Cdd:cd19146 47 QGGNFIDTANNYQGEESerwVGEwmASRGnrdemVLATKYTTGYRRGGPIKIKSNYQGNH--AKSlrlSVEASLKKLQTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 105 YFDLYLLHqaMGDYFSA----WRALEDAYEAGKLKAIGVS----------NFYA--HVLANFC-------ETVR-----I 156
Cdd:cd19146 125 YIDILYVH--WWDYTTSipelMQSLNHLVAAGKVLYLGVSdtpawvvskaNAYAraHGLTQFVvyqghwsAAFRdferdI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 157 TPMVNQ--VELHPY-------FAQPAALEtmkhynvQPEAWAPLGGGRHKPYENV--MLQRIADAHQKTIAQVVLRWNVQ 225
Cdd:cd19146 203 LPMCEAegMALAPWgvlgqgqFRTEEEFK-------RRGRSGRKGGPQTEKERKVseKLEKVAEEKGTAITSVALAYVMH 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446378920 226 RGVTVIP--KSTRQERIEENFAIWDFSLTDNEMAQINA---LDLGY 266
Cdd:cd19146 276 KAPYVFPivGGRKVEHLKGNIEALGISLSDEEIQEIEDaypFDVGF 321
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
7-147 |
7.37e-05 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 43.61 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 7 SNNLKMPMVGFG------VFKVTDKEECQQSVLSAIRSGYRLIDTAAVYGN---EDAVGDAVReaiaTGLCTREELFITS 77
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALK----ALGIPREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 78 KLWvQDMANYDLAKA----GIEASLKKSGLDYFDLYLLH--------QAMGDYFSAWRALEdayEAGKLKAIGVS----N 141
Cdd:PLN02587 82 KCG-RYGEGFDFSAErvtkSVDESLARLQLDYVDILHCHdiefgsldQIVNETIPALQKLK---ESGKVRFIGITglplA 157
|
....*.
gi 446378920 142 FYAHVL 147
Cdd:PLN02587 158 IFTYVL 163
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
10-142 |
5.16e-04 |
|
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: 40.85 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378920 10 LKMPMVGFGVFK----VTDKEECQQSVLSAIRSGYRLIDTAAVYG-----NEDAVGDAVREAIATglcTREELFITSK-- 78
Cdd:cd19151 10 LKLPAISLGLWHnfgdVDRYENSRAMLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKP---YRDELIISTKag 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446378920 79 --LWVQDMANYDLAK---AGIEASLKKSGLDYFDLYLLH---------QAMGdyfsawrALEDAYEAGKLKAIGVSNF 142
Cdd:cd19151 87 ytMWPGPYGDWGSKKyliASLDQSLKRMGLDYVDIFYHHrpdpetpleETMG-------ALDQIVRQGKALYVGISNY 157
|
|
| |
