|
Name |
Accession |
Description |
Interval |
E-value |
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-275 |
0e+00 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 589.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 1 MANPTIIRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWND 80
Cdd:PRK11565 1 MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 DQKRPREALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQ 160
Cdd:PRK11565 81 DHKRPREALEESLKKLQLDYVDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 161 IELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAE 240
Cdd:PRK11565 161 IELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 445935245 241 NFAVWDFRLDKDELGEIAKLDQGKRLGPDPDQFGG 275
Cdd:PRK11565 241 NFDVFDFRLDKDELGEIAKLDQGKRLGPDPDQFGG 275
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-261 |
6.20e-161 |
|
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: 447.20 E-value: 6.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQ--KR 84
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQgyDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 85 PREALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIELH 164
Cdd:cd19131 82 TLRAFDESLRKLGLDYVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 165 PLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAV 244
Cdd:cd19131 162 PRFQQRELRAFHAKHGIQTESWSPLGQG--GLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDV 239
|
250
....*....|....*..
gi 445935245 245 WDFRLDKDELGEIAKLD 261
Cdd:cd19131 240 FDFELDADDMQAIAGLD 256
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-271 |
3.84e-146 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 409.83 E-value: 3.84e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 11 DGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQ--KRPREA 88
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHgyDDTLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 89 LQESLKKlqldyldlylM----------HWPVPaiDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVI 158
Cdd:COG0656 81 FEESLER----------LgldyldlyliHWPGP--GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 159 NQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRI 238
Cdd:COG0656 149 NQVELHPYLQQRELLAFCREHGIVVEAYSPLGRG--KLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERI 226
|
250 260 270
....*....|....*....|....*....|...
gi 445935245 239 AENFAVWDFRLDKDELGEIAKLDQGKRLGPDPD 271
Cdd:COG0656 227 RENLDAFDFELSDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-258 |
2.11e-116 |
|
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: 334.06 E-value: 2.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQ--KRPREALQES 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHgyERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 93 LKKLQLDYLDLYLMHWPVP-----AIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLM 167
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPgkeggSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 168 QQRQLHAWNATHKIQTESWSPLAQGGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDF 247
Cdd:cd19071 161 QQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDF 240
|
250
....*....|.
gi 445935245 248 RLDKDELGEIA 258
Cdd:cd19071 241 ELSEEDMAAID 251
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
9-262 |
1.65e-114 |
|
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: 329.62 E-value: 1.65e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 9 LQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQKR--PR 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYeeAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 87 EALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPL 166
Cdd:cd19132 81 RTIEESLYRLGLDYVDLYLIHWPNPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 167 MQQRQLHAWNATHKIQTESWSPLAQgGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWD 246
Cdd:cd19132 161 FPQAEQRAYHREHGIVTQSWSPLGR-GSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFD 239
|
250
....*....|....*.
gi 445935245 247 FRLDKDELGEIAKLDQ 262
Cdd:cd19132 240 FELSDEDMAAIAALDR 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-271 |
1.03e-107 |
|
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: 312.79 E-value: 1.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASN-EEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQ--K 83
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQgyD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPREALQESLKKLQLDYLDLYLMHWPVPaiDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIEL 163
Cdd:cd19157 82 STLKAFEASLERLGLDYLDLYLIHWPVK--GKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 164 HPLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFA 243
Cdd:cd19157 160 HPRLTQKELRDYCKKQGIQLEAWSPLMQG--QLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENAD 237
|
250 260
....*....|....*....|....*...
gi 445935245 244 VWDFRLDKDELGEIAKLDQGKRLGPDPD 271
Cdd:cd19157 238 VFDFELSQEDMDKIDALNENLRVGPDPD 265
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-267 |
1.40e-105 |
|
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: 307.17 E-value: 1.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 4 PTIIrLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQ- 82
Cdd:cd19134 1 PTVT-LNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 -KRPREALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQI 161
Cdd:cd19134 80 fTASQAACRASLERLGLDYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 162 ELHPLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAEN 241
Cdd:cd19134 160 ELHPLLNQAELRKVNAQHGIVTQAYSPLGVG--RLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASN 237
|
250 260
....*....|....*....|....*.
gi 445935245 242 FAVWDFRLDKDELGEIAKLDQGKRLG 267
Cdd:cd19134 238 LDVFDFELTADHMDALDGLDDGTRFR 263
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
7-273 |
5.02e-101 |
|
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: 295.97 E-value: 5.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASN-EEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQ--K 83
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQgyE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPREALQESLKKLQLDYLDLYLMHWPVPaiDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIEL 163
Cdd:cd19156 81 STLAAFEESLEKLGLDYVDLYLIHWPVK--GKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 164 HPLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFA 243
Cdd:cd19156 159 HPLLTQEPLRKFCKEKNIAVEAWSPLGQG--KLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFD 236
|
250 260 270
....*....|....*....|....*....|
gi 445935245 244 VWDFRLDKDELGEIAKLDQGKRLGPDPDQF 273
Cdd:cd19156 237 VFDFELTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
7-261 |
1.22e-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: 294.35 E-value: 1.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKA-SNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQK-- 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTpDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRar 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPREALQESLKKLQLDYLDLYLMHWPVPaiDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIEL 163
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHWPGK--DKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 164 HPLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFA 243
Cdd:cd19126 159 HPYLTQKELRGYCKSKGIVVEAWSPLGQG--GLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENAD 236
|
250
....*....|....*...
gi 445935245 244 VWDFRLDKDELGEIAKLD 261
Cdd:cd19126 237 IFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
7-261 |
1.24e-100 |
|
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: 294.48 E-value: 1.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASN-EEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLW--NDDQK 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWiqDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPREALQESLKKLQLDYLDLYLMHWPVpaiDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIEL 163
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPF---GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 164 HPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFA 243
Cdd:cd19133 158 HPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFD 237
|
250
....*....|....*...
gi 445935245 244 VWDFRLDKDELGEIAKLD 261
Cdd:cd19133 238 IFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
7-261 |
1.79e-97 |
|
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: 287.00 E-value: 1.79e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDD--QKR 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDygYDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 85 PREALQESLKKLQLDYLDLYLMHWPVPAI-DHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIEL 163
Cdd:cd19127 81 ALRGFDASLRRLGLDYVDLYLLHWPVPNDfDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 164 HPLMQQRQLHAWNATHKIQTESWSPL----------AQGGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSV 233
Cdd:cd19127 161 HPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgPTGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSV 240
|
250 260
....*....|....*....|....*...
gi 445935245 234 TPSRIAENFAVWDFRLDKDELGEIAKLD 261
Cdd:cd19127 241 HPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-261 |
1.14e-93 |
|
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: 276.79 E-value: 1.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQK--R 84
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDgdE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 85 PREALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIELH 164
Cdd:cd19130 82 PAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 165 PLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAV 244
Cdd:cd19130 162 PAYQQRTIRDWAQAHDVKIEAWSPLGQG--KLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDV 239
|
250
....*....|....*..
gi 445935245 245 WDFRLDKDELGEIAKLD 261
Cdd:cd19130 240 FDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-265 |
1.11e-88 |
|
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: 265.30 E-value: 1.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKA-SNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKAL----KAASVAREELFITTKLWND- 80
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIrekiAEGVVKREDLFITTKLWNSy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 -DQKRPREALQESLKKLQLDYLDLYLMHWPVPAIDH---------------YVDAWKGMIALQKEGLVKSIGVCNFQIHH 144
Cdd:cd19116 83 hEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENndsesngdgslsdidYLETWRGMEDLVKLGLTRSIGVSNFNSEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 145 LQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL-------AQGGEGVFDQKVIRELADKYGKTPAQIV 217
Cdd:cd19116 163 INRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvprgQTNPPPRLDDPTLVAIAKKYGKTTAQIV 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 445935245 218 IRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKR 265
Cdd:cd19116 243 LRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQR 290
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-266 |
1.00e-81 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 248.10 E-value: 1.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 5 TIIRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA----SVAREELFITTKLWND 80
Cdd:cd19154 2 ASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELleegVVKREDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 DQKRP--REALQESLKKLQLDYLDLYLMHWPVP-------------------AIDHyVDAWKGMIALQKEGLVKSIGVCN 139
Cdd:cd19154 82 EHAPEdvEEALRESLKKLQLEYVDLYLIHAPAAfkddegesgtmengmsihdAVDV-EDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 140 FQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLA-------------QGGEGVFDQKVIRELA 206
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGspgranftkstgvSPAPNLLQDPIVKAIA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 207 DKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRL 266
Cdd:cd19154 241 EKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-260 |
1.22e-80 |
|
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: 244.63 E-value: 1.22e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 9 LQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA-----SVAREELFITTKLWNDDQK 83
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPR--EALQESLKKLQLDYLDLYLMHWPVP--------------------AIDHYV---DAWKGMIALQKEGLVKSIGVC 138
Cdd:cd19118 81 PEYvePALDDTLKELGLDYLDLYLIHWPVAfkptgdlnpltavptnggevDLDLSVslvDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 139 NFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL---AQGGEGVFDQKVIRELADKYGKTPAQ 215
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLPLLVQHPEVKAIAAKLGKTPAQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 445935245 216 IVIRWHLDCGLVVIPKSVTPSRIAENFAvwDFRLDKDELGEIAKL 260
Cdd:cd19118 241 VLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-257 |
7.73e-79 |
|
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: 238.32 E-value: 7.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQKRP--REALQES 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEdlKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 93 LKKLQLDYLDLYLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQL 172
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNPTVP-LEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 173 HAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKD 252
Cdd:cd19073 160 LEYCRENDIVITAYSPLARG--EVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSE 237
|
....*
gi 445935245 253 ELGEI 257
Cdd:cd19073 238 DVAKI 242
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-266 |
6.03e-77 |
|
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: 235.77 E-value: 6.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 8 RLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKAL----KAASVAREELFITTKLWNDDQK 83
Cdd:cd19123 5 PLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNNSHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 ----RPreALQESLKKLQLDYLDLYLMHWPVpAIDHYV------------------DAWKGMIALQKEGLVKSIGVCNFQ 141
Cdd:cd19123 85 pedvLP--ALEKTLADLQLDYLDLYLMHWPV-ALKKGVgfpesgedllslspipleDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 142 IHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL----------AQGGEGVFDQKVIRELADKYGK 211
Cdd:cd19123 162 VKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLgsgdrpaamkAEGEPVLLEDPVINKIAEKHGA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 445935245 212 TPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRL 266
Cdd:cd19123 242 SPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
15-260 |
6.68e-77 |
|
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: 234.06 E-value: 6.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKA-SNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA----SVAREELFITTKLWNDDQ--KRPRE 87
Cdd:cd19136 1 MPILGLGTFRLrGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQgyEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 88 ALQESLKKLQLDYLDLYLMHWP-VPAIDHY--------VDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVI 158
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgVQGLKPSdprnaelrRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 159 NQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRI 238
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 445935245 239 AENFAVWDFRLDKDELGEIAKL 260
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-266 |
1.02e-75 |
|
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: 232.24 E-value: 1.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 9 LQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA----SVAREELFITTKLWNDDQ-- 82
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLfedgVVKREDLFITSKLWCTDHap 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 KRPREALQESLKKLQLDYLDLYLMHWPV--------PAIDHYV-----DAWKGMIALQKEGLVKSIGVCNFQIHHLQRLI 149
Cdd:cd19125 85 EDVPPALEKTLKDLQLDYLDLYLIHWPVrlkkgahmPEPEEVLppdipSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 150 DETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEG-----VFDQKVIRELADKYGKTPAQIVIRWHLDC 224
Cdd:cd19125 165 AVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTwvkknVLKDPIVTKVAEKLGKTPAQVALRWGLQR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 445935245 225 GLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRL 266
Cdd:cd19125 245 GTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
6-260 |
1.54e-75 |
|
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: 231.62 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 6 IIRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQKRP 85
Cdd:cd19117 5 TFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 REALQESLKKLQLDYLDLYLMHWPVPAI---------------DHY-----VDAWKGMIALQKEGLVKSIGVCNFQIHHL 145
Cdd:cd19117 85 EEALDQSLKKLGLDYVDLYLMHWPVPLDpdgndflfkkddgtkDHEpdwdfIKTWELMQKLPATGKVKAIGVSNFSIKNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 146 QRLI--DETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQKVIRELADKYGKTPAQIVIRWHLD 223
Cdd:cd19117 165 EKLLasPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTPAQVIISWGLQ 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 445935245 224 CGLVVIPKSVTPSRIAENFAVWDfrLDKDELGEIAKL 260
Cdd:cd19117 245 RGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDEL 279
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-254 |
1.86e-75 |
|
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: 230.67 E-value: 1.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKA---SNEEVIAAIHkalEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQ- 82
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSggySHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 -KRPREALQESLKKLQLDYLDLYLMHWPV-PAIDHYV-----DAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVT 155
Cdd:cd19135 82 yESTKQAFEASLKRLGVDYLDLYLLHWPDcPSSGKNVketraETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 156 PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTP 235
Cdd:cd19135 162 PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKG--KALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKE 239
|
250
....*....|....*....
gi 445935245 236 SRIAENFAVWDFRLDKDEL 254
Cdd:cd19135 240 ERIKENCQVFDFSLSEEDM 258
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-260 |
1.49e-74 |
|
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: 227.91 E-value: 1.49e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQKRPR--EALQES 92
Cdd:cd19140 8 IPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDflASVEES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 93 LKKLQLDYLDLYLMHWPVP--AIDHYVDAwkgMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQR 170
Cdd:cd19140 88 LRKLRTDYVDLLLLHWPNKdvPLAETLGA---LNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYLDQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 171 QLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLD-CGLVVIPKSVTPSRIAENFAVWDFRL 249
Cdd:cd19140 165 KLLDAAREHGIALTAYSPLARG--EVLKDPVLQEIGRKHGKTPAQVALRWLLQqEGVAAIPKATNPERLEENLDIFDFTL 242
|
250
....*....|.
gi 445935245 250 DKDELGEIAKL 260
Cdd:cd19140 243 SDEEMARIAAL 253
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-265 |
1.05e-73 |
|
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: 226.34 E-value: 1.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 12 GNVMPQLGLGV---WKAS-----NEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKlWNDDQK 83
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSgdddiQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTK-VSPGIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPREALQESLKKLQLDYLDLYLMHWPVPAIDHYVD---AWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVINQ 160
Cdd:cd19120 80 DPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTlaeAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAVNQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 161 IELHP--LMQQRQLHAWNATHKIQTESWSPLA---QGGEGVFDqKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTP 235
Cdd:cd19120 160 IEFHPylYPQQPALLEYCREHGIVVSAYSPLSpltRDAGGPLD-PVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKE 238
|
250 260 270
....*....|....*....|....*....|
gi 445935245 236 SRIAENFAVWDFRLDKDELGEIAKLDQGKR 265
Cdd:cd19120 239 ERMKEYLEAFDFELTEEEVEEIDKAGKQKH 268
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-266 |
3.07e-73 |
|
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: 226.50 E-value: 3.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 9 LQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA-----SVAREELFITTKLWNDdQK 83
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNT-KH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RP---REALQESLKKLQLDYLDLYLMHWPVP------------------AIDHYVDAWKGMIALQKEGLVKSIGVCNFQI 142
Cdd:cd19106 80 HPedvEPALRKTLKDLQLDYLDLYLIHWPYAfergdnpfpknpdgtiryDSTHYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 143 HHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL-------AQGGEGV-FDQKVIRELADKYGKTPA 214
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwAKPDEPVlLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 445935245 215 QIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRL 266
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-262 |
1.32e-71 |
|
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: 221.37 E-value: 1.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 11 DGNVMPQLGLG--VWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA-----SVAREELFITTKLWNDDQK 83
Cdd:cd19124 1 SGQTMPVIGMGtaSDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEAlrlglVKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPR--EALQESLKKLQLDYLDLYLMHWPV----------PAIDHYVD-----AWKGMIALQKEGLVKSIGVCNFQIHHLQ 146
Cdd:cd19124 81 PDLvlPALKKSLRNLQLEYVDLYLIHWPVslkpgkfsfpIEEEDFLPfdikgVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 147 RLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL-----AQGGEGVFDQKVIRELADKYGKTPAQIVIRWH 221
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgapgtKWGSNAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 445935245 222 LDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQ 262
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
15-270 |
2.24e-67 |
|
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: 211.36 E-value: 2.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKA----ASVAREELFITTKLWNDDQKRP--REA 88
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREkikeGVVRREDLFIVSKLWCTCHKKSlvKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 89 LQESLKKLQLDYLDLYLMHWP------------------VPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLID 150
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPmgfkpgepdlpldrsgmvIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 151 ETG--VTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGV--FDQKVIRELADKYGKTPAQIVIRWHLDCGL 226
Cdd:cd19110 164 KPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVdlIDDPVIQRIAKKHGKSPAQILIRFQIQRNV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 445935245 227 VVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRLGPDP 270
Cdd:cd19110 244 IVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-265 |
3.35e-67 |
|
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: 211.12 E-value: 3.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKA----LKAASVAREELFITTKLWNDDQKRP--REA 88
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAiqekIKEQVVKREDLFIVSKLWCTFHEKGlvKGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 89 LQESLKKLQLDYLDLYLMHWP------------------VPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLID 150
Cdd:cd19107 84 CQKTLSDLKLDYLDLYLIHWPtgfkpgkelfpldesgnvIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIERILN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 151 ETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPL-------AQGGE-GVFDQKVIRELADKYGKTPAQIVIRW 220
Cdd:cd19107 164 KPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwAKPEDpSLLEDPKIKEIAAKHNKTTAQVLIRF 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 445935245 221 HLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKR 265
Cdd:cd19107 244 PIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
15-260 |
7.60e-67 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 207.98 E-value: 7.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLW--NDDQKRPREALQES 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWidNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 93 LKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIA-LQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVI-NQIELHPLMQQR 170
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDEVPVEEYIGALAeAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAtNQIELSPYLQNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 171 QLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLD 250
Cdd:cd19139 161 KLVAHCKQHGIHVTSYMTLAYG--KVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLD 238
|
250
....*....|
gi 445935245 251 KDELGEIAKL 260
Cdd:cd19139 239 ADDMAAIAAL 248
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-266 |
1.05e-65 |
|
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: 207.38 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALK----AASVAREELFITTKLWNDDQ 82
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwidSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 KRP--REALQESLKKLQLDYLDLYLMHWPVPAI---------------------DHyVDAWKGMIALQKEGLVKSIGVCN 139
Cdd:cd19155 84 RREkvEKFLLKSLEKLQLDYVDLYLIHFPVGSLskeddsgkldptgehkqdyttDL-LDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 140 FQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVF---------------DQKVIRE 204
Cdd:cd19155 163 FNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFspgtgspsgsspdllQDPVVKA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445935245 205 LADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRL 266
Cdd:cd19155 243 IAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-266 |
1.15e-65 |
|
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: 206.58 E-value: 1.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 12 GNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALK----AASVAREELFITTKLW--NDDQKRP 85
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlkNGKLKREEVFITTKLPpvYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 REALQESLKKLQLDYLDLYLMHWPVPAIDH------------YVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETG 153
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKkdkgerelassdVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 154 VTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVF-----------DQKVIrELADKYGKTPAQIVIRWHL 222
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQslwpdqpdlleDPTVL-AIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 445935245 223 DCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRL 266
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
4-247 |
4.38e-65 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 204.69 E-value: 4.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 4 PTIIRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA---SVAREELFITTKLWND 80
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 DQKRPREALQESLKKLQLDYLDLYLMHWPVPAID---------------------HYVDAWKGMIALQKEGLVKSIGVCN 139
Cdd:cd19121 81 YHRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPngnhdlfptlpdgsrdldwdwNHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 140 FQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQKVIRELADKYGKTPAQIVIR 219
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260
....*....|....*....|....*...
gi 445935245 220 WHLDCGLVVIPKSVTPSRIAENFAVWDF 247
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDL 268
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-265 |
5.32e-65 |
|
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: 205.41 E-value: 5.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA----SVAREELFITTKLWNDDQ 82
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAfktgLVKREDLFITTKLWNSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 KRPREALQESLKKLQLDYLDLYLMHWPVPA-------------------IDHYV---DAWKGMIALQKEGLVKSIGVCNF 140
Cdd:cd19112 83 GHVIEACKDSLKKLQLDYLDLYLVHFPVATkhtgvgttgsalgedgvldIDVTIsleTTWHAMEKLVSAGLVRSIGISNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 141 QIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGV--------FDQKVIRELADKYGKT 212
Cdd:cd19112 163 DIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAewfgsvspLDDPVLKDLAKKYGKS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 445935245 213 PAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKR 265
Cdd:cd19112 243 AAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
15-273 |
9.45e-64 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 201.02 E-value: 9.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAASVAREELFITTKLWNDDQKRPR--EALQES 92
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKliPSLKES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 93 LKKLQLDYLDLYLMHWPVPaiDHYVDAWKGMIAL---QKEGLVKSIGVCNFQIHHLQRLIDETGVTPV-INQIELHPLMQ 168
Cdd:PRK11172 83 LQKLRTDYVDLTLIHWPSP--NDEVSVEEFMQALleaKKQGLTREIGISNFTIALMKQAIAAVGAENIaTNQIELSPYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 169 QRQLHAWNATHKIQTESWSPLAQGgeGVFDQKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFR 248
Cdd:PRK11172 161 NRKVVAFAKEHGIHVTSYMTLAYG--KVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQ 238
|
250 260
....*....|....*....|....*
gi 445935245 249 LDKDELGEIAKLDQGKRLgPDPDQF 273
Cdd:PRK11172 239 LDAEDMAAIAALDRNGRL-VSPEGL 262
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
7-270 |
3.63e-62 |
|
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: 198.05 E-value: 3.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNE----EGVGKALKAASVAREELFITTKLWND-- 80
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEkevgEGVNRAIDEGLVKREELFLTSKLWNNfh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 DQKRPREALQESLKKLQLDYLDLYLMHWP-----VPAIDHY-------------------VDAWKGMIALQKEGLVKSIG 136
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfVPIEEKYppgfycgdgdnfvyedvpiLDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 137 VCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWS------------PLAQGGEGVFDQKVIRE 204
Cdd:cd19113 163 VSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSsfgpqsfvelnqGRALNTPTLFEHDTIKS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445935245 205 LADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRLGpDP 270
Cdd:cd19113 243 IAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFN-DP 307
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
7-260 |
5.93e-59 |
|
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: 189.63 E-value: 5.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVW--KASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAA----SVAREELFITTKLWND 80
Cdd:cd19119 4 FKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAiddgSIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 DQKRPREALQESLKKLQLDYLDLYLMHWPVP------------------------AIDHYVDAWKGMIALQKEGLVKSIG 136
Cdd:cd19119 84 FYDEVERSLDESLKALGLDYVDLLLVHWPVCfekdsddsgkpftpvnddgktryaASGDHITTYKQLEKIYLDGRAKAIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 137 VCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQKVIRELADKYGKTPAQI 216
Cdd:cd19119 164 VSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKYNVSTGDI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 445935245 217 VIRWHLDCGLVVIPKSVTPSRIAENFAVwdFRLDKDELGEIAKL 260
Cdd:cd19119 244 LISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
7-268 |
1.42e-57 |
|
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: 186.28 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVWKAsnEEV-----IAAIHKALEVGYRSIDTATAYQNEEGVGKAL----KAASVAREELFITTKL 77
Cdd:cd19108 3 VKLNDGHFIPVLGFGTYAP--EEVpkskaLEATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 78 WNDDQkRP---REALQESLKKLQLDYLDLYLMHWPVP---------------AIDHYVD---AWKGMIALQKEGLVKSIG 136
Cdd:cd19108 81 WCTFH-RPelvRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeelfpkdengkLIFDTVDlcaTWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 137 VCNFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPL-AQGGEGVFDQK--------VIREL 205
Cdd:cd19108 160 VSNFNRRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALgSQRDKEWVDQNspvlledpVLCAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445935245 206 ADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKRLGP 268
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-265 |
5.86e-57 |
|
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: 184.93 E-value: 5.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 2 ANPTIiRLQDGNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNE----EGVGKALKAASVAREELFITTKL 77
Cdd:cd19115 1 ASPTV-KLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEveagQGVARAIKEGIVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 78 WND--DQKRPREALQESLKKLQLDYLDLYLMHWPVPAidHYVD-------------------------AWKGMIALQKEG 130
Cdd:cd19115 80 WNTfhDGERVEPICRKQLADWGIDYFDLFLIHFPIAL--KYVDpavryppgwfydgkkvefsnapiqeTWTAMEKLVDKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 131 LVKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWS------------PLAQGGEGVFD 198
Cdd:cd19115 158 LARSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgpqsfleldlPGAKDTPPLFE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445935245 199 QKVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKR 265
Cdd:cd19115 238 HDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-260 |
3.51e-56 |
|
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: 181.95 E-value: 3.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKAL----KAASVAREELFITTKLWNDDQKRP--REAL 89
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFseifKDGGVKREDLFITSKLWPTMHQPEnvKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 90 QESLKKLQLDYLDLYLMHWPV---------PAIDHYV---------DAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDE 151
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLafdmdtdgdPRDDNQIqslskkpleDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 152 TGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL----AQGGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCGL- 226
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLggsyGDGNLTFLNDSELKALATKYNTTPPQVIIAWHLQKWPk 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 445935245 227 --VVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKL 260
Cdd:cd19128 242 nySVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-265 |
3.33e-51 |
|
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: 169.66 E-value: 3.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 12 GNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKAAS----VAREELFITTKLWND--DQKRP 85
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIqeglVKREDLFIVTKLWNNfhGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 REALQESLKKLQLDYLDLYLMHWPVPAidHYVD--------------------------AWKGMIALQKEGLVKSIGVCN 139
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPA--AYVDpaenypflwkdkelkkfpleqspmqeCWREMEKLVDAGLVRNIGIAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 140 FQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQK-----------VIRELADK 208
Cdd:cd19114 159 FNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHlkhftnllehpVVKKLADK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 445935245 209 YGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKR 265
Cdd:cd19114 239 HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-265 |
2.45e-49 |
|
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: 164.97 E-value: 2.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 12 GNVMPQLGLGVwKASNE-----EVIAAIHKALEVGYRSIDTATAYQNEEGVGKALKA----ASVAREELFITTKLWNDDQ 82
Cdd:cd19109 1 GNSIPIIGLGT-YSEPKttpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREkiaeGKVKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 KrP---REALQESLKKLQLDYLDLYLMHWPV---PAIDHY---------------VDAWKGMIALQKEGLVKSIGVCNFQ 141
Cdd:cd19109 80 P-PelvRPTLERTLKVLQLDYVDLYIIEMPMafkPGDEIYprdengkwlyhktnlCATWEALEACKDAGLVKSIGVSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 142 IHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGEG---------VFDQKVIRELADKYG 210
Cdd:cd19109 159 RRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPiwvnvssppLLEDPLLNSIGKKYN 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 445935245 211 KTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLDQGKR 265
Cdd:cd19109 239 KTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
18-261 |
2.87e-49 |
|
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: 164.41 E-value: 2.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 18 LGLGVWKASN-------EEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAASVAREELFITTKLWNDDQKRP-- 85
Cdd:pfam00248 1 IGLGTWQLGGgwgpiskEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWPsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 ------REALQESLKKLQLDYLDLYLMHWPVPAiDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVIN 159
Cdd:pfam00248 81 gskeniRKSLEESLKRLGTDYIDLYYLHWPDPD-TPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 160 QIELHPL--MQQRQLHAWNATHKIQTESWSPLAQG--------------GEGVFDQK-----------VIRELADKYGKT 212
Cdd:pfam00248 160 QVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpGERRRLLKkgtplnlealeALEEIAKEHGVS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 445935245 213 PAQIVIRWHL--DCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKLD 261
Cdd:pfam00248 240 PAQVALRWALskPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-242 |
4.11e-46 |
|
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: 156.24 E-value: 4.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 9 LQDGNVMPQLGLGVW--KASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALK-----AASVAREELFITTKLWNDd 81
Cdd:cd19122 3 LNNGVKIPAVGFGTFanEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRdflkeNPSVKREDLFICTKVWNH- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 82 QKRPREAL---QESLKKLQLDYLDLYLMHWPVPAIDH------------YV----------DAWKGMIALQKEGLVKSIG 136
Cdd:cd19122 82 LHEPEDVKwsiDNSLKNLKLDYIDLFLVHWPIAAEKNdqrspklgpdgkYVilkdltenpePTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 137 VCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQ------GGEGVFDQKVIRELADKYG 210
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvpsTGERVSENPTLNEVAEKGG 241
|
250 260 270
....*....|....*....|....*....|..
gi 445935245 211 KTPAQIVIRWHLDCGLVVIPKSVTPSRIAENF 242
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNF 273
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
7-257 |
1.17e-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: 154.33 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 7 IRLQDGNVMPQLGLGVW-----KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAsvaREELFITTKL- 77
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 78 -WNDDQKRPREALQESLKKLQLDYLDLYLMHWP--VPaIDHYVDAwkgMIALQKEGLVKSIGVCNFQIHHLQRLIDETGV 154
Cdd:cd19138 80 pSNASRQGTVRACERSLRRLGTDYLDLYLLHWRggVP-LAETVAA---MEELKKEGKIRAWGVSNFDTDDMEELWAVPGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 155 TP-VINQIELHplMQQR----QLHAWNATHKIQTESWSPLAQGGE---GVFDQKVIRELADKYGKTPAQIVIRWHLDCGL 226
Cdd:cd19138 156 GNcAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLlrrGLLENPTLKEIAARHGATPAQVALAWVLRDGN 233
|
250 260 270
....*....|....*....|....*....|..
gi 445935245 227 VV-IPKSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19138 234 VIaIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-254 |
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: 151.23 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWK--------ASN-EEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAasVAREELFITTKLWNDDQ 82
Cdd:cd19072 4 VPVLGLGTWGigggmskdYSDdKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG--FDREDLFITTKVSPDHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 KRP--REALQESLKKLQLDYLDLYLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPVI-N 159
Cdd:cd19072 82 KYDdvIKAAKESLKRLGTDYIDLYLIHWPNPSIP-IEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIVaN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 160 QIE-----------LHPLMQQrqlhawnatHKIQTESWSPLAQGG-EGVFDQKVIRELADKYGKTPAQIVIRWHL-DCGL 226
Cdd:cd19072 161 QVEynlfdreeesgLLPYCQK---------NGIAIIAYSPLEKGKlSNAKGSPLLDEIAKKYGKTPAQIALNWLIsKPNV 231
|
250 260
....*....|....*....|....*...
gi 445935245 227 VVIPKSVTPSRIAENFAVWDFRLDKDEL 254
Cdd:cd19072 232 IAIPKASNIEHLEENAGALGWELSEEDL 259
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
12-244 |
1.06e-43 |
|
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: 150.30 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 12 GNVMPQLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKA----LKAASVAREELFITTKLWNDDQK--RP 85
Cdd:cd19129 3 SGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAmqevFKAGKIRREDLFVTTKLWNTNHRpeRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 REALQESLKKLQLDYLDLYLMHWPV---PAIDH----------------YVDAWKGMIALQKEGLVKSIGVCNFQIHHLQ 146
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPFafqPGDEQdprdangnviyddgvtLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 147 RLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGE-GVFDQKVIRELADKYGKTPAQIVIRWHLDCG 225
Cdd:cd19129 163 EIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEpKLLEDPVITAIARRVNKTPAQVLLAWAIQRG 242
|
250
....*....|....*....
gi 445935245 226 LVVIPKSVTPSRIAENFAV 244
Cdd:cd19129 243 TALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-254 |
1.23e-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: 128.07 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 12 GNVMPQLGLGVWK---------ASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKaaSVAREELFITTKLWN 79
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIK--DFPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 80 DDQKRP--REALQESLKKLQLDYLDLYLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPV 157
Cdd:cd19137 79 TNLRYDdlLRSLQNSLRRLDTDYIDLYLIHWPNPNIP-LEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 158 INQIELHPL---MQQRQLHAWNATHKIQTESWSPLAQGGEGVFDQkvIRELADKYGKTPAQIVIRWHL-DCGLVVIPKSV 233
Cdd:cd19137 158 CNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRT--LEEIAKNYGKTIAQIALAWLIqKPNVVAIPKAG 235
|
250 260
....*....|....*....|.
gi 445935245 234 TPSRIAENFAVWDFRLDKDEL 254
Cdd:cd19137 236 RVEHLKENLKATEIKLSEEEM 256
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-257 |
4.41e-33 |
|
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: 122.25 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 18 LGLGVW--------KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAsvaREELFITTK---LWNDDQK 83
Cdd:cd19084 7 IGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKcglRWDGGKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RP--------REALQESLKKLQLDYLDLYLMHWPvpaiDHYV---DAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDET 152
Cdd:cd19084 84 VTkdlspesiRKEVEQSLRRLQTDYIDLYQIHWP----DPNTpieETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 153 GVtpVINQIELHPLMQQ--RQLHAWNATHKIQTESWSPLAQG-------GEGVFDQ----------------------KV 201
Cdd:cd19084 160 PI--VSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQGlltgkykKEPTFPPddrrsrfpffrgenfeknleivDK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 445935245 202 IRELADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19084 238 LKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
16-261 |
1.28e-31 |
|
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: 118.48 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGVWKASN-----------EEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAaSVAREELFITTKLWNDD 81
Cdd:cd19093 3 SPLGLGTWQWGDrlwwgygeygdEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKE-LGDRDEVVIATKFAPLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 82 QKRPRE----ALQESLKKLQLDYLDLYLMHWP---VPAIDHYvdaWKGMIALQKEGLVKSIGVCNFQIHHLQR---LIDE 151
Cdd:cd19093 82 WRLTRRsvvkALKASLERLGLDSIDLYQLHWPgpwYSQIEAL---MDGLADAVEEGLVRAVGVSNYSADQLRRahkALKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 152 TGVTPVINQIE---LHPLMQQRQLHAWNATHKIQTESWSPLAQG--------------------GEGVFDQ-----KVIR 203
Cdd:cd19093 159 RGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGlltgkyspenpppggrrrlfGRKNLEKvqpllDALE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 445935245 204 ELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDelgEIAKLD 261
Cdd:cd19093 239 EIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEE---EVAELD 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-257 |
2.99e-31 |
|
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: 117.30 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGVW---------KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAsvaREELFITTKLWNDDQK 83
Cdd:cd19085 2 SRLGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR---RDDVVIATKVSPDNLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RP--REALQESLKKLQLDYLDLYLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETgvTPVINQI 161
Cdd:cd19085 79 PEdvRKSCERSLKRLGTDYIDLYQIHWPSSDVP-LEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG--RIDSNQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 162 ELHPLmqQRQLHA----WNATHKIQTESWSPLAQG------------------------GEGVFDQKV------IRELAD 207
Cdd:cd19085 156 PYNLL--WRAIEYeilpFCREHGIGVLAYSPLAQGlltgkfssaedfppgdartrlfrhFEPGAEEETfealekLKEIAD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 445935245 208 KYGKTPAQIVIRW-----HLDCGLVvipKSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19085 234 ELGVTMAQLALAWvlqqpGVTSVIV---GARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-260 |
4.38e-30 |
|
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: 114.89 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 17 QLGLGVWKASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAasVAREELFITTKLWNDDQKRP-------- 85
Cdd:COG0667 22 TFGGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKG--RPRDDVVIATKVGRRMGPGPngrglsre 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 --REALQESLKklqldyldlyLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDET-GVTP-VINQI 161
Cdd:COG0667 100 hiRRAVEASLRrlgtdyidlyQLHRPDPDTP-IEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAeGLPPiVAVQN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 162 ELHPLMQQ--RQLHAWNATHKIQTESWSPLAQG-----------------GEGVFDQ-----------KVIRELADKYGK 211
Cdd:COG0667 179 EYSLLDRSaeEELLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdrAATNFVQgylternlalvDALRAIAAEHGV 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 445935245 212 TPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFAVWDFRLDKDELGEIAKL 260
Cdd:COG0667 259 TPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-260 |
4.69e-29 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 112.00 E-value: 4.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 18 LGLGVWKA------------SNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAAsvaREELFITTK---LWN 79
Cdd:cd19102 4 IGLGTWAIggggwgggwgpqDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 80 DDQK-----RP---REALQESLKKLQLDYLDLYLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDE 151
Cdd:cd19102 81 EEGRirrslKPasiRAECEASLRRLGVDVIDLYQIHWPDPDEP-IEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 152 TGVTPVinQIELHPLMQ--QRQLHAWNATHKIQTESWSPLAQGG-EGVFDQKVI-------------------------- 202
Cdd:cd19102 160 HPIASL--QPPYSLLRRgiEAEILPFCAEHGIGVIVYSPMQSGLlTGKMTPERVaslpaddwrrrspffqepnlarnlal 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445935245 203 ----RELADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFAVWDFRLDKDELGEIAKL 260
Cdd:cd19102 238 vdalRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
19-253 |
7.08e-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: 105.72 E-value: 7.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 19 GLGVWKASNEEVIAAIHKALEVGYRSIDTA---TAYQNEEGVGKALKAASVAREELFITTK--LWNDDQKRP-------- 85
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALALNPGLREKIEIQTKcgIRLGDDPRPgrikhydt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 -----REALQESLKKLQLDYLDLYLMHWPvpaiDHYVDAW---KGMIALQKEGLVKSIGVCNF---QIHHLQRLIDETGV 154
Cdd:cd19092 95 skehiLASVEGSLKRLGTDYLDLLLLHRP----DPLMDPEevaEAFDELVKSGKVRYFGVSNFtpsQIELLQSYLDQPLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 155 TpviNQIELHPLMQQrqlHAWNAT------HKIQTESWSPLAQGG-EGVFDQK------VIRELADKYGKTPAQIVIRWH 221
Cdd:cd19092 171 T---NQIELSLLHTE---AIDDGTldycqlLDITPMAWSPLGGGRlFGGFDERfqrlraALEELAEEYGVTIEAIALAWL 244
|
250 260 270
....*....|....*....|....*....|....
gi 445935245 222 LD--CGLVVIPKSVTPSRIAENFAVWDFRLDKDE 253
Cdd:cd19092 245 LRhpARIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-243 |
4.79e-26 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 102.21 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGVW----KASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAaSVAREELFITTKLWNDDQKRP--- 85
Cdd:cd06660 1 SRLGLGTMtfggDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKG-RGNRDDVVIATKGGHPPGGDPsrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 -------REALQESLKKLQLDYLDLYLMHW--PVPAIDHYVDAwkgMIALQKEGLVKSIGVCNF---QIHHLQRLIDETG 153
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHRddPSTPVEETLEA---LNELVREGKIRYIGVSNWsaeRLAEALAYAKAHG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 154 VTP-VINQIE---LHPLMQQRQLHAWNATHKIQTESWSPLAQGgegvfdqkvireladkygktPAQIVIRWHLDCGLV-- 227
Cdd:cd06660 157 LPGfAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------PAQLALAWLLSQPFVtv 216
|
250
....*....|....*.
gi 445935245 228 VIPKSVTPSRIAENFA 243
Cdd:cd06660 217 PIVGARSPEQLEENLA 232
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-250 |
2.08e-21 |
|
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: 90.35 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKAS--NEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAASvarEELFITTKL---------WND 80
Cdd:cd19088 9 MRLTGPGIWGPPadREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvrtgpgwWGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 DQkRP---REALQESLKKLQLDYLDLYLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPV 157
Cdd:cd19088 86 DG-SPeylRQAVEASLRRLGLDRIDLYQLHRIDPKVP-FEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIVSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 158 INQielHPLMQQRQLH--AWNATHKIQTESWSPLAqGGEGVFDQKVIRELADKYGKTPAQIVIRWHLDCG--LVVIPKSV 233
Cdd:cd19088 164 QNR---YNLANRDDEGvlDYCEAAGIAFIPWFPLG-GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTS 239
|
250
....*....|....*..
gi 445935245 234 TPSRIAENFAVWDFRLD 250
Cdd:cd19088 240 SVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-257 |
6.08e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 87.26 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 5 TIIRLQDGnvMPQLGLGVWKASNE-EVIAAIHKALEVGYRSIDTATAYQN-EEGVG---KALKAASVAREELFITTKLWN 79
Cdd:cd19101 1 TISRVING--MWQLSGGHGGIRDEdAAVRAMAAYVDAGLTTFDCADIYGPaEELIGefrKRLRRERDAADDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 80 DDQKRP------REALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDEtG 153
Cdd:cd19101 79 DPGELTmtrayvEAAIDRSLKRLGVDRLDLVQFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDA-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 154 VTPVINQIElHPLMQQRQLH---AWNATHKIQ------------TESW----SPLAQ-----------------GGEGVF 197
Cdd:cd19101 158 VPIVSNQVQ-YSLLDRRPENgmaALCEDHGIKllaygtlaggllSEKYlgvpEPTGPaletrslqkyklmidewGGWDLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445935245 198 DQ--KVIRELADKYGKTPAQIVIRWHLD--CGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19101 237 QEllRTLKAIADKHGVSIANVAVRWVLDqpGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
25-259 |
7.71e-19 |
|
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: 84.21 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 25 ASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAasvAREELFITTKL---WNDDQKRP----------REA 88
Cdd:cd19078 22 PDKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKFgfkIDGGKPGPlgldsrpehiRKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 89 LQESLKKLQldyldlylmhwpVPAID----HYVD--------AwKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTP 156
Cdd:cd19078 99 VEGSLKRLQ------------TDYIDlyyqHRVDpnvpieevA-GTMKELIKEGKIRHWGLSEAGVETIRRAHAVCPVTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 157 VINQI---------ELHPLMQQRqlhawnathKIQTESWSPLAQG------GEGV-FDQK-------------------- 200
Cdd:cd19078 166 VQSEYsmmwrepekEVLPTLEEL---------GIGFVPFSPLGKGfltgkiDENTkFDEGddraslprftpealeanqal 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445935245 201 --VIRELADKYGKTPAQIVIRWHLDCG--LVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAK 259
Cdd:cd19078 237 vdLLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
10-257 |
6.94e-18 |
|
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: 81.49 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 10 QDGNVMPQLGLGVW-------KASNEEVIAAIHKALEVGYRSIDTATAYQ---NEEGVGKALKAAsvaREELFITTK--- 76
Cdd:cd19076 7 TQGLEVSALGLGCMgmsafygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR---RDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 77 LWNDDQK------RP---REALQESLKKLQldyldlylmhwpVPAID----HYVDA-------WKGMIALQKEGLVKSIG 136
Cdd:cd19076 84 VRDPGSGfrgvdgRPeyvRAACEASLKRLG------------TDVIDlyyqHRVDPnvpieetVGAMAELVEEGKVRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 137 VCNfqihhlqrlidetgVTPviNQIelhplmqqRQLHAwnaTHKI---QTE------------------------SWSPL 189
Cdd:cd19076 152 LSE--------------ASA--DTI--------RRAHA---VHPItavQSEyslwtrdiedevlptcrelgigfvAYSPL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 190 AQG-------------------------GEgVFDQ-----KVIRELADKYGKTPAQIVIRWHLDCG--LVVIPKSVTPSR 237
Cdd:cd19076 205 GRGfltgaikspedlpeddfrrnnprfqGE-NFDKnlklvEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKY 283
|
330 340
....*....|....*....|
gi 445935245 238 IAENFAVWDFRLDKDELGEI 257
Cdd:cd19076 284 LEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
18-259 |
6.89e-17 |
|
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: 78.85 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 18 LGLGVW---------KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAsvaREELFITTK--LWNDDQK 83
Cdd:cd19149 14 IGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcgLRWDREG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 ----------------RP---REALQESLKKLQLDYLDLYLMHWPVPA--IDhyvDAWKGMIALQKEGLVKSIGVCNFQI 142
Cdd:cd19149 91 gsfffvrdgvtvyknlSPesiREEVEQSLKRLGTDYIDLYQTHWQDVEtpIE---ETMEALEELKRQGKIRAIGASNVSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 143 HHLQRLidETGVTPVINQIE---LHPLMQQRQLHAWNaTHKIQTESWSPLAQG-------GEGVFD-------------- 198
Cdd:cd19149 168 EQIKEY--VKAGQLDIIQEKysmLDRGIEKELLPYCK-KNNIAFQAYSPLEQGlltgkitPDREFDagdarsgipwfspe 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445935245 199 --QKV------IRELADKYGKTPAQIVIRWHLDCG--LVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAK 259
Cdd:cd19149 245 nrEKVlallekWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
19-257 |
3.22e-16 |
|
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: 76.96 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 19 GLGVWK--------ASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAASVaREELFITTKL---WNDDQKR 84
Cdd:cd19148 8 ALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYGK-RDRVVIATKVgleWDEGGEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 85 PREA--------LQESLKKLQLDYLDLYLMHWPVP--AIDHYVDAwkgMIALQKEGLVKSIGVCNF---QIHHLQRLIDE 151
Cdd:cd19148 87 VRNSsparirkeVEDSLRRLQTDYIDLYQVHWPDPlvPIEETAEA---LKELLDEGKIRAIGVSNFspeQMETFRKVAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 152 TGVTPVIN----QIELHPLMQQRQlhawnatHKIQTESWSPLAQG------------------------GEGVFDQ--KV 201
Cdd:cd19148 164 HTVQPPYNlferEIEKDVLPYARK-------HNIVTLAYGALCRGllsgkmtkdtkfegddlrrtdpkfQEPRFSQylAA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445935245 202 IREL----ADKYGKTPAQIVIRWHLDCGLVVIP--KSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19148 237 VEELdklaQERYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEI 298
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
27-260 |
5.71e-16 |
|
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: 76.30 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 27 NEEV-IAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAASvaREELFITTK----------LWNDDQKRPREALQES 92
Cdd:cd19083 31 DEEEgKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEYN--RNEVVIATKgahkfggdgsVLNNSPEFLRSAVEKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 93 LKKLQLDYLDLYLMHWPvpaiDHYV---DAWKGMIALQKEGLVKSIGVCNFQIHHLQRlIDETGVTPVInQIElHPLMQQ 169
Cdd:cd19083 109 LKRLNTDYIDLYYIHFP----DGETpkaEAVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGYVDVL-QGE-YNLLQR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 170 RQLHA---WNATHKIQTESWSPLAQG------------GEGVFDQKV-----------------IRELADKYGKTPAQIV 217
Cdd:cd19083 182 EAEEDilpYCVENNISFIPYFPLASGllagkytkdtkfPDNDLRNDKplfkgerfsenldkvdkLKSIADEKGVTVAHLA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 445935245 218 IRWHL--DCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKL 260
Cdd:cd19083 262 LAWYLtrPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-244 |
7.54e-16 |
|
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: 74.82 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 18 LGLGVW--------KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAsvaREELFITTKLWNDDQKRP- 85
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR---RDKVVIATKFGNRFDGGPe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 ----------REALQESLKKLQLDYLDLYLMH-WPVPAIDHYvDAWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGV 154
Cdd:cd19086 83 rpqdfspeyiREAVEASLKRLGTDYIDLYQLHnPPDEVLDND-ELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 155 TPVinQIELHPLMQQ--RQLHAWNATHKIQTESWSPLAQGGegvfdqkvireLADKygktPAQIVIRWHLDCGLV--VIP 230
Cdd:cd19086 162 DVV--QVIYNLLDQRpeEELFPLAEEHGVGVIARVPLASGL-----------LTGK----LAQAALRFILSHPAVstVIP 224
|
250
....*....|....
gi 445935245 231 KSVTPSRIAENFAV 244
Cdd:cd19086 225 GARSPEQVEENAAA 238
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
23-257 |
4.16e-15 |
|
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: 73.77 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 23 WKASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKaaSVA-REELFITTKL---WNDD-------QKRPREA 88
Cdd:cd19079 30 WVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALK--EFApRDEVVIATKVyfpMGDGpngrglsRKHIMAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 89 LQESLKKLQLDYLDLYLMHWpvpaIDHYVDAWKGMIALQ---KEGLVKSIGVCNF---QIHHLQRLIDETGVTPVINQIE 162
Cdd:cd19079 108 VDASLKRLGTDYIDLYQIHR----WDYETPIEETLEALHdvvKSGKVRYIGASSMyawQFAKALHLAEKNGWTKFVSMQN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 163 LHPLMQQ---RQLHAWNATHKIQTESWSPLAQG-------------------------GEGVFDQKVI---RELADKYGK 211
Cdd:cd19079 184 HYNLLYReeeREMIPLCEEEGIGVIPWSPLARGrlarpwgdtterrrsttdtaklkydYFTEADKEIVdrvEEVAKERGV 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 445935245 212 TPAQIVIRWHLDCGLVVIP--KSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19079 264 SMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-172 |
5.12e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 69.43 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLG---VWKASNEEVIAAIHKALEVGYRSIDTATAYQN-EEGVGKALKAAsvaREELFITTKLWNDDQKRPREALQE 91
Cdd:cd19100 12 SRLGFGggpLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR---RDKVFLATKTGARDYEGAKRDLER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 92 SLKKLQLDYLDLYLMHwpvpAIDHYVD---------AWKGMIALQKEGLVKSIGVCNfqiHHLQRLID--ETG----VTP 156
Cdd:cd19100 89 SLKRLGTDYIDLYQLH----AVDTEEDldqvfgpggALEALLEAKEEGKIRFIGISG---HSPEVLLRalETGefdvVLF 161
|
170
....*....|....*.
gi 445935245 157 VINQIELHPLMQQRQL 172
Cdd:cd19100 162 PINPAGDHIDSFREEL 177
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-252 |
5.86e-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: 70.31 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 17 QLGLGVW-----KASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAasVAREELFITTKL-W------ND- 80
Cdd:cd19074 6 ELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG--WPRESYVISTKVfWptgpgpNDr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 --DQKRPREALQESLKKLQLDYLDLYLMHWPVP--AIDHYVDAwkgMIALQKEGLVKSIGVCNF---QIHHLQRLIDETG 153
Cdd:cd19074 84 glSRKHIFESIHASLKRLQLDYVDIYYCHRYDPetPLEETVRA---MDDLIRQGKILYWGTSEWsaeQIAEAHDLARQFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 154 -VTPVINQIELHPLMQQR--QLHAWNATHKIQTESWSPLAQG---------------------------GEGVFDQKV-- 201
Cdd:cd19074 161 lIPPVVEQPQYNMLWREIeeEVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkRRLLTDENLek 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 445935245 202 ---IRELADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFAVWDFRLDKD 252
Cdd:cd19074 241 vkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
16-244 |
6.98e-14 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 69.57 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGVWK-------ASNEEVIAAIHKALEVGYRSIDTATAYQN-EEGVGKALkaASVAREELFITTKLW--NDDQKRP 85
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGthGEGGRDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 86 --------REALQESLKKLQLDYLDLYLMHWPVPAiDHYVDAWKGMIALQKEGLVKSIGVCNFQiHHLQRLIdETGVTPV 157
Cdd:cd19095 79 kdfspaaiRASIERSLRRLGTDYIDLLQLHGPSDD-ELTGEVLETLEDLKAAGKVRYIGVSGDG-EELEAAI-ASGVFDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 158 InQIELHPLMQ-QRQLHAWNATHKIQTESWSPLAQG--GEGVFDQKVIRELADKY-------GKTPAQIVIRWHLDCGLV 227
Cdd:cd19095 156 V-QLPYNVLDReEEELLPLAAEAGLGVIVNRPLANGrlRRRVRRRPLYADYARRPefaaeigGATWAQAALRFVLSHPGV 234
|
250
....*....|....*....
gi 445935245 228 --VIPKSVTPSRIAENFAV 244
Cdd:cd19095 235 ssAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
16-151 |
2.54e-13 |
|
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: 68.35 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLG------VWKA-SNEEVIAAIHKALEVGYRSIDTATAYQN-EEGVGKALKAasVAREELFITTKLWNDDQKRP-- 85
Cdd:cd19090 1 SALGLGtaglggVFGGvDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE--LPREPLVLSTKVGRLPEDTAdy 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445935245 86 -----REALQESLKKLQLDYLDLYLMH---WPVPAIDHYVD-AWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDE 151
Cdd:cd19090 79 sadrvRRSVEESLERLGRDRIDLLMIHdpeRVPWVDILAPGgALEALLELKEEGLIKHIGLGGGPPDLLRRAIET 153
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
28-220 |
2.39e-12 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 65.28 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 28 EEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAasVAREELFITTKL-WNDDQKRP--REALQESLKKLQLDYL 101
Cdd:cd19096 21 EKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKE--GPREKFYLATKLpPWSVKSAEdfRRILEESLKRLGVDYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 102 DLYLMHWPV-PAIDHYV---DAWKGMIALQKEGLVKSIGvcnFQIH----HLQRLIDETGVTPVinQIELHPLMQQRQ-- 171
Cdd:cd19096 99 DFYLLHGLNsPEWLEKArkgGLLEFLEKAKKEGLIRHIG---FSFHdspeLLKEILDSYDFDFV--QLQYNYLDQENQag 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445935245 172 --LHAWNATHKIQTESWSPLAQGGEGvFDQKVIRELADKYGKTPAQIVIRW 220
Cdd:cd19096 174 rpGIEYAAKKGMGVIIMEPLKGGGLA-NNPPEALAILCGAPLSPAEWALRF 223
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
17-257 |
4.42e-12 |
|
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: 64.95 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 17 QLGLG----VWKA---SNEEVIAAIHKALEVGYRSIDTATAY------QNEEGVGKALKAASVAREELFITTKL-WNDDQ 82
Cdd:cd19077 7 PIGLGlmglTWRPnptPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKGgLDPDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 83 KRP---REALQESLKKLQLDYLdlylmhwPVPAIDHYVDA-----------WKGMIALQKEGLVKSIGVCNFQIHHLQRL 148
Cdd:cd19077 87 LRPdgsPEAVRKSIENILRALG-------GTKKIDIFEPArvdpnvpieetIKALKELVKEGKIRGIGLSEVSAETIRRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 149 IDetgVTPV-INQIELHPLMQ---QRQLHAWNATHKIQTESWSPLAQG------------------------GEGVFDQ- 199
Cdd:cd19077 160 HA---VHPIaAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRGlltgriksladipegdfrrhldrfNGENFEKn 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445935245 200 ----KVIRELADKYGKTPAQIVIRW--HLDCGLVV-IPKSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19077 237 lklvDALQELAEKKGCTPAQLALAWilAQSGPKIIpIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-244 |
5.99e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 64.14 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVWKASNEEvIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAasVAREELFITTK-LWNDDQKRP---RE 87
Cdd:cd19105 13 VSRLGFGGGGLPRES-PELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG--LRRDKVFLATKaSPRLDKKDKaelLK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 88 ALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAW--KGMIALQKEGLVKSIGV-CNFQIHH-LQRLIDeTGVTPVInQIEL 163
Cdd:cd19105 90 SVEESLKRLQTDYIDIYQLHGVDTPEERLLNEEllEALEKLKKEGKVRFIGFsTHDNMAEvLQAAIE-SGWFDVI-MVAY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 164 HPLMQQRQL-HAWNATHK--IQTESWSPLAQGGEGVFDQKVIRELadkyGKTPAQIVIRW-----HLDcglVVIPKSVTP 235
Cdd:cd19105 168 NFLNQPAELeEALAAAAEkgIGVVAMKTLAGGYLQPALLSVLKAK----GFSLPQAALKWvlsnpRVD---TVVPGMRNF 240
|
....*....
gi 445935245 236 SRIAENFAV 244
Cdd:cd19105 241 AELEENLAA 249
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
4-260 |
1.40e-11 |
|
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: 63.62 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 4 PTIIRLQDGNVMPQLGLGVWKAS--------NEEVIAAIHKALEVGYRSIDTATAYQ-NEEGVGKALKAASVAREELFIT 74
Cdd:cd19144 2 PTRTLGRNGPSVPALGFGAMGLSafygppkpDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 75 TK-----------LW-NDDQKRPREALQESLKKLQLDYLDLYLMHW--PVPAIDHYVdawKGMIALQKEGLVKSIGVCNF 140
Cdd:cd19144 82 TKfgieknvetgeYSvDGSPEYVKKACETSLKRLGVDYIDLYYQHRvdGKTPIEKTV---AAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 141 QIHHLQRLIDETGVTPVinQIELHPL---MQQRQLHAWNATHK--IQTESWSPLAQG------------GEGVFDQKV-- 201
Cdd:cd19144 159 SAETLRRAHAVHPIAAV--QIEYSPFsldIERPEIGVLDTCRElgVAIVAYSPLGRGfltgairspddfEEGDFRRMApr 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445935245 202 ---------------IRELADKYGKTPAQIVIRWHL--DCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKL 260
Cdd:cd19144 237 fqaenfpknlelvdkIKAIAKKKNVTAGQLTLAWLLaqGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREI 312
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-262 |
3.28e-11 |
|
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: 62.63 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 12 GNVMPQLGLG-------------VWKASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAAsvaREELFITT 75
Cdd:cd19091 10 GLKVSELALGtmtfgggggffgaWGGVDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKGR---RDDVLIAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 76 KLW-------NDD---QKRPREALQESLKKLQLDYLDLYLMHW-----PVP----AIDHYVdawkgmialqKEGLVKSIG 136
Cdd:cd19091 87 KVRgrmgegpNDVglsRHHIIRAVEASLKRLGTDYIDLYQLHGfdaltPLEetlrALDDLV----------RQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 137 VCNF---QIHHLQRLIDETGVT-PVINQI-----------ELHPLMQQrqlhawnatHKIQTESWSPLAQG--------- 192
Cdd:cd19091 157 VSNFsawQIMKALGISERRGLArFVALQAyysllgrdlehELMPLALD---------QGVGLLVWSPLAGGllsgkyrrg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 193 ---GEG------------VFDQK------VIRELADKYGKTPAQIVIRW--HLDCGLVVIPKSVTPSRIAENFAVWDFRL 249
Cdd:cd19091 228 qpaPEGsrlrrtgfdfppVDRERgydvvdALREIAKETGATPAQVALAWllSRPTVSSVIIGARNEEQLEDNLGAAGLSL 307
|
330
....*....|...
gi 445935245 250 DKDelgEIAKLDQ 262
Cdd:cd19091 308 TPE---EIARLDK 317
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-150 |
4.30e-11 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 62.53 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVW---KASNEEVIAAIHKALEVGYRSIDTATAY-QNEEGVGKALKAAsvaREELFITTKL--WNDDQKRPREA 88
Cdd:COG1453 13 VSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP---RDKVILATKLppWVRDPEDMRKD 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445935245 89 LQESLKKLQLDYLDLYLMHWpVPAIDHY------VDAWKGMIALQKEGLVKSIGvcnFQIHH----LQRLID 150
Cdd:COG1453 90 LEESLKRLQTDYIDLYLIHG-LNTEEDLekvlkpGGALEALEKAKAEGKIRHIG---FSTHGslevIKEAID 157
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
16-240 |
2.72e-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: 59.49 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGV----WKASNEEVIAAIHKALEVGYRSIDTATAYQNEEGVGKALK------AASVAREELFITTK-----LWND 80
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGASERvigewlKSRGNRDKVVIATKgghpdLEDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 81 DQKR--P---REALQESLKKLQLDYLDLYLMHW-----PVPAIdhyVDAwkgMIALQKEGLVKSIGVCNFQIHHLQRLID 150
Cdd:cd19082 81 SRSRlsPediRADLEESLERLGTDYIDLYFLHRddpsvPVGEI---VDT---LNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 151 ---ETGVTP-VINQIEL---HPLMQQ----------RQLHAWNATHKIQTESWSPLAQG-------GEGVFDQKV----- 201
Cdd:cd19082 155 yakAHGLPGfAASSPQWslaRPNEPPwpgptlvamdEEMRAWHEENQLPVFAYSSQARGffskraaGGAEDDSELrrvyy 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 445935245 202 ----------IRELADKYGKTPAQIVIRWHLDCGLVVIPkSVTPSRIAE 240
Cdd:cd19082 235 seenferlerAKELAEEKGVSPTQIALAYVLNQPFPTVP-IIGPRTPEQ 282
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-137 |
1.06e-09 |
|
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: 57.54 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 17 QLGL--GV----WKASNEEVIAAIHKALEVGYRSIDTATAYQN-EEGVGKALKAASvareELFITTKL------WNDDQK 83
Cdd:cd19097 9 QFGLdyGIanksGKPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRLD----KFKIITKLpplkedKKEDEA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 445935245 84 RPREALQESLKKLQLDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIGV 137
Cdd:cd19097 85 AIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGV 138
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
25-220 |
2.78e-09 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 56.81 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 25 ASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAsvaREELFITTKL------WNDDQ----KRPREALQE 91
Cdd:cd19087 27 TDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKVfgpmgdDPNDRglsrRHIRRAVEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 92 SLKKLQLDYLDLYLMHwpvpAIDHYVD---AWKGMIALQKEGLVKSIGVCNF---QI---------HHLQRLIDEtgvTP 156
Cdd:cd19087 104 SLRRLQTDYIDLYQMH----HFDRDTPleeTLRALDDLVRQGKIRYIGVSNFaawQIakaqgiaarRGLLRFVSE---QP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 157 VIN----QIELH--PLMQqrqlhawnaTHKIQTESWSPLAQG---------GEGVFDQKVIRE----------------- 204
Cdd:cd19087 177 MYNllkrQAELEilPAAR---------AYGLGVIPYSPLAGGlltgkygkgKRPESGRLVERAryqarygleeyrdiaer 247
|
250
....*....|....*....
gi 445935245 205 ---LADKYGKTPAQIVIRW 220
Cdd:cd19087 248 feaLAAEAGLTPASLALAW 266
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-260 |
8.54e-09 |
|
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: 55.42 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGVW---------------KASNEEVIAAIHKALEVGYRSIDTATAYqneeGVGKALKA-----ASVAREELFIT 74
Cdd:cd19103 4 LPKIALGTWswgsggaggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVY----GMGASEKIlgeflKRYPREDYIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 75 TK----LWNDDQKRPREALQESLKKLQLDYLDLYLMHWPVPaidhyVDAW-KGMIALQKEGLVKSIGVCNF---QIHHLQ 146
Cdd:cd19103 80 TKftpqIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPAD-----VERWtPELIPLLKSGKVKHVGVSNHnlaEIKRAN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 147 RLIDETGV--TPVINQIEL-HPLMQQRQLHAWNATHKIQTESWSPLAQGG---------------------EGVFDQ--- 199
Cdd:cd19103 155 EILAKAGVslSAVQNHYSLlYRSSEEAGILDYCKENGITFFAYMVLEQGAlsgkydtkhplpegsgraetyNPLLPQlee 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445935245 200 --KVIRELADKYGKTPAQIVIRWHLDCGLVVIPKSVTPSRIAENFAVWDFRLDKDELGEIAKL 260
Cdd:cd19103 235 ltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-136 |
1.40e-08 |
|
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: 54.58 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 21 GVW-KASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAASvarEELFITTKLWNDDQKRP------REALQ 90
Cdd:cd19104 24 GLMgRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGLP---AGPYITTKVRLDPDDLGdiggqiERSVE 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 91 ESLKKLQ--------------LDYLDLYLMHWPVPAIDHYVDAWKGMIALQKEGLVKSIG 136
Cdd:cd19104 101 KSLKRLKrdsvdllqlhnrigDERDKPVGGTLSTTDVLGLGGVADAFERLRSEGKIRFIG 160
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
16-137 |
1.98e-08 |
|
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: 53.90 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLG------VWKASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALkaASVAREELFITTKL--------- 77
Cdd:cd19162 1 PRLGLGaaslgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAAL--ARHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 78 ---------WNDDQKRPREALQESLKKLQLDYLDLYLMHWPVPAIDHYV-DAWKGMIALQKEGLVKSIGV 137
Cdd:cd19162 79 grpagadrrFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALtDAFPALEELRAEGVVGAIGV 148
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
14-261 |
7.96e-08 |
|
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: 52.22 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 14 VMPqLGLGVW---KASNEEVIAAIHKA-LEVGYRSIDTATAY----------QNEEGVGKALKAaSVAREELFITTKL-W 78
Cdd:cd19081 9 VSP-LCLGTMvfgWTADEETSFALLDAfVDAGGNFIDTADVYsawvpgnaggESETIIGRWLKS-RGKRDRVVIATKVgF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 79 NDDQKRP-------REALQESLKKLQLDYLDLYLMHWPVPA--IDHYVDAWKGMIalqKEGLVKSIGVCNFQIHHLQRLI 149
Cdd:cd19081 87 PMGPNGPglsrkhiRRAVEASLRRLQTDYIDLYQAHWDDPAtpLEETLGALNDLI---RQGKVRYIGASNYSAWRLQEAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 150 D---ETGVTPVIN-------------QIELHPLMQQRQLHAWNathkiqtesWSPLAQG-----------------GEGV 196
Cdd:cd19081 164 ElsrQHGLPRYVSlqpeynlvdresfEGELLPLCREEGIGVIP---------YSPLAGGfltgkyrseadlpgstrRGEA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445935245 197 FDQ----------KVIRELADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFAVWDFRLDKDelgEIAKLD 261
Cdd:cd19081 235 AKRylnerglrilDALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDE---EVARLD 308
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
29-157 |
1.47e-07 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 51.38 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 29 EVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAASVAREELFITTKL-------WNDDQKRPREALQESLKKLQL 98
Cdd:cd19153 34 EAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVgryrdseFDYSAERVRASVATSLERLHT 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445935245 99 DYLDLYLMHwPVPAIDHYVD---AWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDETGVTPV 157
Cdd:cd19153 114 TYLDVVYLH-DIEFVDYDTLvdeALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSL 174
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-95 |
2.15e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 51.16 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 17 QLGLGVW-----KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAS----VAREELFITTK-----LWN 79
Cdd:cd19099 5 SLGLGTYrgdsdDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIekggIKRDEVVIVTKagyipGDG 84
|
90
....*....|....*.
gi 445935245 80 DDQKRPREALQESLKK 95
Cdd:cd19099 85 DEPLRPLKYLEEKLGR 100
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
28-257 |
5.19e-07 |
|
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: 49.74 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 28 EEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKaaSVAREELFITTKL---WNDDQKRP--------REALQESL 93
Cdd:cd19145 33 EEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQLATKFgihEIGGSGVEvrgdpayvRAACEASL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 94 KKLQLDYLDLYLMHwpvpAIDHYVDAWKGMIALQK---EGLVKSIGvcnfqihhlqrlIDETGVTPVINQIELHPLMQ-Q 169
Cdd:cd19145 111 KRLDVDYIDLYYQH----RIDTTVPIEITMGELKKlveEGKIKYIG------------LSEASADTIRRAHAVHPITAvQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 170 RQLHAWnaTHKIQTE-------------SWSPLAQG-------------------------GEGVFDQKVIRE----LAD 207
Cdd:cd19145 175 LEWSLW--TRDIEEEiiptcrelgigivPYSPLGRGffagkakleellensdvrkshprfqGENLEKNKVLYErveaLAK 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 445935245 208 KYGKTPAQIVIRWHLDCG--LVVIPKSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19145 253 KKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
17-257 |
5.44e-07 |
|
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: 49.90 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 17 QLGLGVW-----KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAASVAREELFITTKL-WNDDQKRPR- 86
Cdd:cd19143 15 ALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGGGGPPPNd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 87 ---------EALQESLKKLQLDYLDLYLMHWPVPA--IDHYVDAwkgMIALQKEGLVKSIGV---CNFQIHHLQRLIDET 152
Cdd:cd19143 95 rglsrkhivEGTKASLKRLQLDYVDLVFCHRPDPAtpIEETVRA---MNDLIDQGKAFYWGTsewSAQQIEEAHEIADRL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 153 GVTPvinqielhPLMQQRQLHAWN------------ATHKIQTESWSPLAQG---------------------------- 192
Cdd:cd19143 172 GLIP--------PVMEQPQYNLFHrerveveyaplyEKYGLGTTTWSPLASGlltgkynngipegsrlalpgyewlkdrk 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445935245 193 ---GEGVFDQ-KVIRELADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFAVWDF--RLDKDELGEI 257
Cdd:cd19143 244 eelGQEKIEKvRKLKPIAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEENLKALEVlpKLTPEVMEKI 316
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
15-155 |
1.65e-06 |
|
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: 48.32 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 15 MPQLGLGV-------WKASNEEVIAAIHKALEVGYRSIDTATAY---QNEEGVGKALKAasVAREELFITTKL------- 77
Cdd:cd19163 13 VSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALKG--IPRDSYYLATKVgrygldp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 78 ---WNDDQKRPREALQESLKKLQLDYLDLYLMHWP--VPAIDHYVD-AWKGMIALQKEGLVKSIGVCNFQIHHLQRLIDE 151
Cdd:cd19163 91 dkmFDFSAERITKSVEESLKRLGLDYIDIIQVHDIefAPSLDQILNeTLPALQKLKEEGKVRFIGITGYPLDVLKEVLER 170
|
....
gi 445935245 152 TGVT 155
Cdd:cd19163 171 SPVK 174
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
24-220 |
1.43e-05 |
|
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: 45.62 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 24 KASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAASvareELFITTKL--WNDDQKRP---REALQESLKK 95
Cdd:cd19075 16 FTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELGLGER----GFKIDTKAnpGVGGGLSPenvRKQLETSLKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 96 LQLDYLDLYLMHWPVPAIDhYVDAWKGMIALQKEGLVKSIGVCNF---QIHHLQRLIDETG-VTPVINQ----------- 160
Cdd:cd19075 92 LKVDKVDVFYLHAPDRSTP-LEETLAAIDELYKEGKFKEFGLSNYsawEVAEIVEICKENGwVLPTVYQgmynaitrqve 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 161 IELHPLMQQrqlhawnatHKIQTESWSPLAQG-------------GEGVFDQ---------------------KVIRELA 206
Cdd:cd19075 171 TELFPCLRK---------LGIRFYAYSPLAGGfltgkykysedkaGGGRFDPnnalgklyrdrywkpsyfealEKVEEAA 241
|
250
....*....|....
gi 445935245 207 DKYGKTPAQIVIRW 220
Cdd:cd19075 242 EKEGISLAEAALRW 255
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
23-257 |
2.64e-05 |
|
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: 44.90 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 23 WKASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAAsvaREELFITTKL-WNDDQKRP----------REA 88
Cdd:cd19080 26 WGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYtMNRRPGDPnaggnhrknlRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 89 LQESLKKLQLDYLDLYLMHW-----PVP----AIDHYVDAwkgmialqkeGLVKSIGVCNF---QIHHLQRLIDETGVTP 156
Cdd:cd19080 103 VEASLRRLQTDYIDLLYVHAwdfttPVEevmrALDDLVRA----------GKVLYVGISDTpawVVARANTLAELRGWSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 157 VIN-QI-----------ELHPLMQQrqlhawnatHKIQTESWSPLAQG----------------------GEGVFD---- 198
Cdd:cd19080 173 FVAlQIeysllertperELLPMARA---------LGLGVTPWSPLGGGlltgkyqrgeegrageakgvtvGFGKLTernw 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445935245 199 --QKVIRELADKYGKTPAQIVIRWHLDCGLVVIP--KSVTPSRIAENFAVWDFRLDKDELGEI 257
Cdd:cd19080 244 aiVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
28-260 |
8.04e-05 |
|
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: 43.32 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 28 EEVIAAIHKALEVGYRSIDTATAY----------QNEEGVGKALKAaSVAREELFITTKL--------WND------DQK 83
Cdd:cd19094 18 AEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKK-KGNRDKVVLATKVagpgegitWPRgggtrlDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 84 RPREALQESLKKLQLDYLDLYLMHWPvpaiDHYVDAW---------------------KGMIALQKEGLVKSIGVCN--- 139
Cdd:cd19094 97 NIREAVEGSLKRLGTDYIDLYQLHWP----DRYTPLFgggyytepseeedsvsfeeqlEALGELVKAGKIRHIGLSNetp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 140 FQIHHLQRLIDETGVTPVIN-QIELHPLMQQRQLHAWNATHKIQTE--SWSPLAQG---G-------------------- 193
Cdd:cd19094 173 WGVMKFLELAEQLGLPRIVSiQNPYSLLNRNFEEGLAEACHRENVGllAYSPLAGGvltGkyldgaarpeggrlnlfpgy 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445935245 194 ----EGVFDQKVIRE---LADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFAVWDFRLDKDELGEIAKL 260
Cdd:cd19094 253 maryRSPQALEAVAEyvkLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
16-243 |
1.05e-04 |
|
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: 42.98 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLG-------VWKASNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKaaSVAREELFITTKL-------- 77
Cdd:cd19152 1 PKLGFGtaplgnlYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR--ELGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 78 ----------WNDDQKRP---------REALQESLKKLQLDYLDLYLMHWPVPaiDHYVDAWK---------GMIALQK- 128
Cdd:cd19152 79 eveptfepgfWNPLPFDAvfdysydgiLRSIEDSLQRLGLSRIDLLSIHDPDE--DLAGAESDehfaqaikgAFRALEEl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 129 --EGLVKSIGV-CNF-QIhhLQRLIDETGVTPV--------INQIELHPLMQQRqlhawnATHKIQTESWSPLAQG---- 192
Cdd:cd19152 157 reEGVIKAIGLgVNDwEV--ILRILEEADLDWVmlagrytlLDHSAARELLPEC------EKRGVKVVNAGPFNSGflag 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445935245 193 ------------GEGVFDQKV-IRELADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENFA 243
Cdd:cd19152 229 gdnfdyyeygpaPPELIARRDrIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVA 294
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
26-97 |
2.91e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 41.69 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 26 SNEEVIAAIHKALEVGYRSIDTATAYQN---EEGVGKALKAASVAREELFITTKL------WNDDQKRPREALQESLKKL 96
Cdd:PLN02587 29 SEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCgrygegFDFSAERVTKSVDESLARL 108
|
.
gi 445935245 97 Q 97
Cdd:PLN02587 109 Q 109
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
16-255 |
4.36e-04 |
|
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: 41.09 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGVWK-----ASNEEVIAAIHKALEVGYRSIDTATAYQNEEG-----VGKALKAASVA-REELFITTK----LW-- 78
Cdd:cd19089 12 PAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPPPGsaeenFGRILKRDLRPyRDELVISTKagygMWpg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 79 -NDD---QKRPREALQESLKKLQldyldlylmhwpvpaIDhYVDAW------------KGMIALqkEGLVKS-----IGV 137
Cdd:cd19089 92 pYGDggsRKYLLASLDQSLKRMG---------------LD-YVDIFyhhrydpdtpleETMTAL--ADAVRSgkalyVGI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 138 CNFQIHHLQRLID---ETGVTPVINQIELHplMQQRQ--------LHAWNathkIQTESWSPLAQG-------------- 192
Cdd:cd19089 154 SNYPGAKARRAIAllrELGVPLIIHQPRYS--LLDRWaedgllevLEEAG----IGFIAFSPLAQGlltdkylngippds 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 193 ---GEGVF---------DQKVIREL---ADKYGKTPAQIVIRWHLD----CGLVVIPKSvtPSRIAENFAVWD-FRLDKD 252
Cdd:cd19089 228 rraAESKFlteealtpeKLEQLRKLnkiAAKRGQSLAQLALSWVLRdprvTSVLIGASS--PSQLEDNVAALKnLDFSEE 305
|
...
gi 445935245 253 ELG 255
Cdd:cd19089 306 ELA 308
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-243 |
1.58e-03 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 39.24 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 16 PQLGLGVW----KASNEEVIAAIHKALEVGYRSIDTATAY----------QNEEGVGKALKAASVaREELFITTKL---- 77
Cdd:cd19752 1 SELCLGTMyfgtRTDEETSFAILDRYVAAGGNFLDTANNYafwteggvggESERLIGRWLKDRGN-RDDVVIATKVgagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 78 -----WNDD-----QKRPREALQESLKKLQLDYLDLYLMHW--PVPAIDHYVDAWKgmiALQKEGLVKSIGVCNFQIHHL 145
Cdd:cd19752 80 rdpdgGPESpeglsAETIEQEIDKSLRRLGTDYIDLYYAHVddRDTPLEETLEAFN---ELVKAGKVRAIGASNFAAWRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 146 QRlidetgvtpvINQI------ELHPLMQQRQLHAW---NATHKIQ----TE--------------SWSPLAQGGEGVFD 198
Cdd:cd19752 157 ER----------ARQIarqqgwAEFSAIQQRHSYLRprpGADFGVQrivtDElldyassrpdltllAYSPLLSGAYTRPD 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445935245 199 QK---------------VIRELADKYGKTPAQIVIRWHLDCGLVVIP--KSVTPSRIAENFA 243
Cdd:cd19752 227 RPlpeqydgpdsdarlaVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
17-109 |
5.12e-03 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 37.91 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 17 QLGLGVW----KASNEEVIAAIHKALEVGYRSIDTATAYQ----------NEEGVGKALKAASvAREELFITTKLW---- 78
Cdd:PRK10625 15 TLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSgpsr 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 445935245 79 -ND---------DQKRPREALQESLKKLQLDYLDLYLMHWP 109
Cdd:PRK10625 94 nNDkgirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWP 134
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
10-259 |
7.11e-03 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 37.28 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 10 QDGNVMPQLGLGVWKASN-----EEVIAAIHKALEVGYRSIDTATAY-----QNEEGVGKALKAASVA-REELFITTK-- 76
Cdd:PRK09912 20 KSGLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKag 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 77 --LW------NDDQKRPREALQESLKKLQLD---------YLDLYLMHWPVPAIDHYVDAWK----GMIALQKEGLVKSI 135
Cdd:PRK09912 100 ydMWpgpygsGGSRKYLLASLDQSLKRMGLEyvdifyshrVDENTPMEETASALAHAVQSGKalyvGISSYSPERTQKMV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935245 136 GVCN-----FQIHH-----LQRLIDETGVTPVINQ-----IELHPLMQ----QRQLHAWNATHKIQTEswsplAQGGEGV 196
Cdd:PRK09912 180 ELLRewkipLLIHQpsynlLNRWVDKSGLLDTLQNngvgcIAFTPLAQglltGKYLNGIPQDSRMHRE-----GNKVRGL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445935245 197 FDQ----------KVIRELADKYGKTPAQIVIRWHLDCGLV--VIPKSVTPSRIAENF-AVWDFRLDKDELGEIAK 259
Cdd:PRK09912 255 TPKmlteanlnslRLLNEMAQQRGQSMAQMALSWLLKDERVtsVLIGASRAEQLEENVqALNNLTFSTEELAQIDQ 330
|
|
| |
