|
Name |
Accession |
Description |
Interval |
E-value |
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
1-258 |
5.88e-172 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 474.54 E-value: 5.88e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:COG0656 5 IPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAAFEES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPskGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:COG0656 85 LERLGLDYLDLYLIHWPGP--GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQREL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTED 240
Cdd:COG0656 163 LAFCREHGIVVEAYSPLGRGK-LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDED 241
|
250
....*....|....*...
gi 2748858100 241 IAAISALNEDRRLGPDPA 258
Cdd:COG0656 242 MAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
1-248 |
4.79e-163 |
|
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: 451.83 E-value: 4.79e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19131 10 IPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDSTLRAFDES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:cd19131 90 LRKLGLDYVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIELHPRFQQREL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQGkGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTED 240
Cdd:cd19131 170 RAFHAKHGIQTESWSPLGQG-GLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADD 248
|
....*...
gi 2748858100 241 IAAISALN 248
Cdd:cd19131 249 MQAIAGLD 256
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
1-244 |
8.70e-142 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 398.01 E-value: 8.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSK-----GTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHL 155
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPGKeggskEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 156 QQRAAREFHAEQGIATEAWSPLGQG-KGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDF 234
Cdd:cd19071 161 QQKELVEFCKEHGIVVQAYSPLGRGrRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDF 240
|
250
....*....|
gi 2748858100 235 SLDTEDIAAI 244
Cdd:cd19071 241 ELSEEDMAAI 250
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
1-257 |
2.20e-140 |
|
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: 394.84 E-value: 2.20e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDD-EAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDT 79
Cdd:cd19157 10 MPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYDSTLKAFEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 80 SLDKLGLDYVDLYLIHWPTPSKgtYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRA 159
Cdd:cd19157 90 SLERLGLDYLDLYLIHWPVKGK--YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFHPRLTQKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 160 AREFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:cd19157 168 LRDYCKKQGIQLEAWSPLMQGQ-LLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQE 246
|
250
....*....|....*...
gi 2748858100 240 DIAAISALNEDRRLGPDP 257
Cdd:cd19157 247 DMDKIDALNENLRVGPDP 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-260 |
1.51e-139 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 393.28 E-value: 1.51e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHdsALRAFDTS 80
Cdd:PRK11565 15 MPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKR--PREALEES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:PRK11565 93 LKKLQLDYVDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQ-GKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:PRK11565 173 HAWNATHKIQTESWSPLAQgGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKD 252
|
250 260
....*....|....*....|.
gi 2748858100 240 DIAAISALNEDRRLGPDPATF 260
Cdd:PRK11565 253 ELGEIAKLDQGKRLGPDPDQF 273
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
1-260 |
1.30e-138 |
|
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: 390.34 E-value: 1.30e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPD-DEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDT 79
Cdd:cd19156 9 MPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYESTLAAFEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 80 SLDKLGLDYVDLYLIHWPTpsKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRA 159
Cdd:cd19156 89 SLEKLGLDYVDLYLIHWPV--KGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHPLLTQEP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 160 AREFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:cd19156 167 LRKFCKEKNIAVEAWSPLGQGK-LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAE 245
|
250 260
....*....|....*....|.
gi 2748858100 240 DIAAISALNEDRRLGPDPATF 260
Cdd:cd19156 246 EIRQIDGLNTDHRYGPDPDNF 266
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
1-248 |
1.15e-136 |
|
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: 385.25 E-value: 1.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPD-DEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDT 79
Cdd:cd19126 9 MPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARRTEDAFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 80 SLDKLGLDYVDLYLIHWPTPSKgtYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRA 159
Cdd:cd19126 89 SLDRLGLDYVDLYLIHWPGKDK--FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPYLTQKE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 160 AREFHAEQGIATEAWSPLGQGkGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:cd19126 167 LRGYCKSKGIVVEAWSPLGQG-GLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSED 245
|
....*....
gi 2748858100 240 DIAAISALN 248
Cdd:cd19126 246 DMTAIDALN 254
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
1-248 |
1.62e-134 |
|
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: 379.69 E-value: 1.62e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19132 7 IPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEALRTIEES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:cd19132 87 LYRLGLDYVDLYLIHWPNPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHPYFPQAEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTED 240
Cdd:cd19132 167 RAYHREHGIVTQSWSPLGRGSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDED 246
|
....*...
gi 2748858100 241 IAAISALN 248
Cdd:cd19132 247 MAAIAALD 254
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
1-248 |
1.66e-131 |
|
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: 372.51 E-value: 1.66e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19127 9 MPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKALRGFDAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSK-GTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRA 159
Cdd:cd19127 89 LRRLGLDYVDLYLLHWPVPNDfDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVELHPYFSQKD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 160 AREFHAEQGIATEAWSPLG-----------QGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKEN 228
Cdd:cd19127 169 LRAFHRRLGIVTQAWSPIGgvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAEN 248
|
250 260
....*....|....*....|
gi 2748858100 229 IDVFDFSLDTEDIAAISALN 248
Cdd:cd19127 249 IDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
1-248 |
2.17e-129 |
|
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: 366.93 E-value: 2.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEPAAAFAES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:cd19130 90 LAKLGLDQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHPAYQQRTI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTED 240
Cdd:cd19130 170 RDWAQAHDVKIEAWSPLGQGK-LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTE 248
|
....*...
gi 2748858100 241 IAAISALN 248
Cdd:cd19130 249 IAAIDALD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
1-248 |
5.68e-128 |
|
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: 363.05 E-value: 5.68e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDD-EAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDT 79
Cdd:cd19133 9 MPILGFGVFQIPDPeECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEKAKKAFER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 80 SLDKLGLDYVDLYLIHWPTpskGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRA 159
Cdd:cd19133 89 SLKRLGLDYLDLYLIHQPF---GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHPFNQQIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 160 AREFHAEQGIATEAWSPLGQGK-GLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDT 238
Cdd:cd19133 166 AVEFLKKYGVQIEAWGPFAEGRnNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSD 245
|
250
....*....|
gi 2748858100 239 EDIAAISALN 248
Cdd:cd19133 246 EDMEAIAALD 255
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
1-254 |
9.01e-126 |
|
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: 358.01 E-value: 9.01e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19134 11 MPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTASQAACRAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:cd19134 91 LERLGLDYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIELHPLLNQAEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTED 240
Cdd:cd19134 171 RKVNAQHGIVTQAYSPLGVGR-LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADH 249
|
250
....*....|....
gi 2748858100 241 IAAISALNEDRRLG 254
Cdd:cd19134 250 MDALDGLDDGTRFR 263
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
1-247 |
1.57e-108 |
|
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: 314.18 E-value: 1.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPD-DEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNAS----GIAREELFVTTKLWNSDQGHDSALR 75
Cdd:cd19136 1 MPILGLGTFRLRGeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 76 AFDTSLDKLGLDYVDLYLIHWPTPSKGTYVD---------TFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAV 146
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSDprnaelrreSWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 147 NQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKG-LLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRI 225
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLrLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 2748858100 226 KENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
1-252 |
6.05e-105 |
|
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: 306.13 E-value: 6.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQ-VPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAV----NASGIAREELFVTTKLWNSDQGHDSALR 75
Cdd:cd19116 11 IPAIALGTWKlKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIrekiAEGVVKREDLFITTKLWNSYHEREQVEP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 76 AFDTSLDKLGLDYVDLYLIHWP---------------TPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEET 140
Cdd:cd19116 91 ALRESLKRLGLDYVDLYLIHWPvafkenndsesngdgSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 141 SVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKG--------LLEVPAIVAIAQKHGRTPAQIVLRWHLQLG 212
Cdd:cd19116 171 NIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgqtnpppRLDDPTLVAIAKKYGKTTAQIVLRYLIDRG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2748858100 213 NVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRR 252
Cdd:cd19116 251 VVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQR 290
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-247 |
1.64e-100 |
|
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: 293.85 E-value: 1.64e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAErAVATAL-ESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDT 79
Cdd:cd19135 13 MPILGLGTSHSGGYSHE-AVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYESTKQAFEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 80 SLDKLGLDYVDLYLIHWPTP------SKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHP 153
Cdd:cd19135 92 SLKRLGVDYLDLYLLHWPDCpssgknVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHVNQVEFHP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 154 HLQQRAAREFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFD 233
Cdd:cd19135 172 FQNPVELIEYCRDNNIVFEGYCPLAKGK-ALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFD 250
|
250
....*....|....
gi 2748858100 234 FSLDTEDIAAISAL 247
Cdd:cd19135 251 FSLSEEDMATLDSL 264
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
1-253 |
3.16e-99 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 291.56 E-value: 3.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASG----IAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19125 11 IPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDHAPEDVPPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWP--------TPSKGTYV-----DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVI 143
Cdd:cd19125 91 LEKTLKDLQLDYLDLYLIHWPvrlkkgahMPEPEEVLppdipSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARVP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 144 PAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG-QGKG-----LLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIP 217
Cdd:cd19125 171 PAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGsPGTTwvkknVLKDPIVTKVAEKLGKTPAQVALRWGLQRGTSVLP 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 2748858100 218 KSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRL 253
Cdd:cd19125 251 KSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
1-244 |
6.26e-99 |
|
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: 289.17 E-value: 6.26e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKgTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNPTV-PLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTED 240
Cdd:cd19073 160 LEYCRENDIVITAYSPLARGE-VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSED 238
|
....
gi 2748858100 241 IAAI 244
Cdd:cd19073 239 VAKI 242
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
1-247 |
5.14e-98 |
|
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: 287.23 E-value: 5.14e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19140 8 IPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASVEES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPtPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHPHLQQRAA 160
Cdd:cd19140 88 LRKLRTDYVDLLLLHWP-NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYLDQRKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 REFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNV-VIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:cd19140 167 LDAAREHGIALTAYSPLARGE-VLKDPVLQEIGRKHGKTPAQVALRWLLQQEGVaAIPKATNPERLEENLDIFDFTLSDE 245
|
....*...
gi 2748858100 240 DIAAISAL 247
Cdd:cd19140 246 EMARIAAL 253
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
1-247 |
3.57e-97 |
|
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: 286.32 E-value: 3.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSAlrAFDTS 80
Cdd:cd19117 14 IPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRRVEE--ALDQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKG--------------------TYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLI--E 138
Cdd:cd19117 92 LKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIGVSNFSIKNLEKLLasP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKG-LLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIP 217
Cdd:cd19117 172 SAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNApLLKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLP 251
|
250 260 270
....*....|....*....|....*....|
gi 2748858100 218 KSVTPSRIKENIDVfdFSLDTEDIAAISAL 247
Cdd:cd19117 252 KSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
1-253 |
1.26e-92 |
|
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: 275.42 E-value: 1.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNAS-----GIAREELFVTTKLWNSDQGHDSALR 75
Cdd:cd19106 7 MPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHHPEDVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 76 AFDTSLDKLGLDYVDLYLIHWPTPSK-----------GT-------YVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLI 137
Cdd:cd19106 87 ALRKTLKDLQLDYLDLYLIHWPYAFErgdnpfpknpdGTirydsthYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 138 EETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKG---------LLEVPAIVAIAQKHGRTPAQIVLRWH 208
Cdd:cd19106 167 SVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRpwakpdepvLLEEPKVKALAKKYNKSPAQILLRWQ 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2748858100 209 LQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRL 253
Cdd:cd19106 247 VQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-253 |
1.04e-90 |
|
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: 270.05 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAV----NASGIAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNNSHAPEDVLPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWPTP---------SKGTYV--------DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEE 139
Cdd:cd19123 92 LEKTLADLQLDYLDLYLMHWPVAlkkgvgfpeSGEDLLslspipleDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 140 TSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGK-----------GLLEVPAIVAIAQKHGRTPAQIVLRWH 208
Cdd:cd19123 172 ARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepVLLEDPVINKIAEKHGASPAQVLIAWA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2748858100 209 LQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRL 253
Cdd:cd19123 252 IQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
1-253 |
2.03e-88 |
|
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: 264.66 E-value: 2.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVN---ASGI-AREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19154 12 MPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAellEEGVvKREDLFITTKLWTHEHAPEDVEEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWPTPSKGT------------------YVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE 138
Cdd:cd19154 92 LRESLKKLQLEYVDLYLIHAPAAFKDDegesgtmengmsihdavdVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQ--------------GKGLLEVPAIVAIAQKHGRTPAQIV 204
Cdd:cd19154 172 NARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspAPNLLQDPIVKAIAEKHGKTPAQVL 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2748858100 205 LRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRL 253
Cdd:cd19154 252 LRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
1-247 |
4.73e-86 |
|
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: 257.72 E-value: 4.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAV-----NASGIAREELFVTTKLWNSDQGHDSALR 75
Cdd:cd19118 7 IPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALkellkEEPGVKREDLFITSKLWNNSHRPEYVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 76 AFDTSLDKLGLDYVDLYLIHWPTPSKGT-----------------------YVDTFKAFEKIYADGRAKAIGTSNFLPEH 132
Cdd:cd19118 87 ALDDTLKELGLDYLDLYLIHWPVAFKPTgdlnpltavptnggevdldlsvsLVDTWKAMVELKKTGKVKSIGVSNFSIDH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 133 LAKLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG---QGKGLL-EVPAIVAIAQKHGRTPAQIVLRWH 208
Cdd:cd19118 167 LQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGnnlAGLPLLvQHPEVKAIAAKLGKTPAQVLIAWG 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 2748858100 209 LQLGNVVIPKSVTPSRIKENIDvfDFSLDTEDIAAISAL 247
Cdd:cd19118 247 IQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
1-246 |
3.18e-85 |
|
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: 255.23 E-value: 3.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGV----WQVPDDEAER----AVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNsdqGHDS 72
Cdd:cd19120 4 IPAIAFGTgtawYKSGDDDIQRdlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSP---GIKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 73 ALRAFDTSLDKLGLDYVDLYLIHWP---TPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQI 149
Cdd:cd19120 81 PREALRKSLAKLGVDYVDLYLIHSPffaKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAVNQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 150 ELHPHL--QQRAAREFHAEQGIATEAWSPL---GQGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSR 224
Cdd:cd19120 161 EFHPYLypQQPALLEYCREHGIVVSAYSPLsplTRDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEER 240
|
250 260
....*....|....*....|..
gi 2748858100 225 IKENIDVFDFSLDTEDIAAISA 246
Cdd:cd19120 241 MKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-244 |
2.83e-84 |
|
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: 253.22 E-value: 2.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTG---KAVNASGIAREELFVTTKLWNSDqgHDSALRAF 77
Cdd:cd19121 12 IPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGegiKEAIAGGVKREDLFVTTKLWSTY--HRRVELCL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 78 DTSLDKLGLDYVDLYLIHWPTPSKG---------------------TYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKL 136
Cdd:cd19121 90 DRSLKSLGLDYVDLYLVHWPVLLNPngnhdlfptlpdgsrdldwdwNHVDTWKQMEKVLKTGKTKAIGVSNYSIPYLEEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 137 IEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQ-GKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVV 215
Cdd:cd19121 170 LKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGStGSPLISDEPVVEIAKKHNVGPGTVLISYQVARGAVV 249
|
250 260
....*....|....*....|....*....
gi 2748858100 216 IPKSVTPSRIKENIDVFDFslDTEDIAAI 244
Cdd:cd19121 250 LPKSVTPDRIKSNLEIIDL--DDEDMNKL 276
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
1-247 |
1.41e-81 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 246.41 E-value: 1.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFG--VWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVN---ASG--IAREELFVTTKLWNSDQGHDSA 73
Cdd:cd19124 5 MPVIGMGtaSDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGlvKSRDELFVTSKLWCSDAHPDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 74 LRAFDTSLDKLGLDYVDLYLIHWPTPSK-GTYV--------------DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE 138
Cdd:cd19124 85 LPALKKSLRNLQLEYVDLYLIHWPVSLKpGKFSfpieeedflpfdikGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQG------KGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLG 212
Cdd:cd19124 165 FATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPgtkwgsNAVMESDVLKEIAAAKGKTVAQVSLRWVYEQG 244
|
250 260 270
....*....|....*....|....*....|....*
gi 2748858100 213 NVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19124 245 VSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
1-252 |
1.46e-80 |
|
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: 244.64 E-value: 1.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNA----SGIAREELFVTTKLWNSDqgHDSAL-- 74
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEkikeQVVKREDLFIVSKLWCTF--HEKGLvk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 75 RAFDTSLDKLGLDYVDLYLIHWPT------------------PSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKL 136
Cdd:cd19107 82 GACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnviPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 137 IEETSVI--PAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG---------QGKGLLEVPAIVAIAQKHGRTPAQIVL 205
Cdd:cd19107 162 LNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwakpEDPSLLEDPKIKEIAAKHNKTTAQVLI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2748858100 206 RWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRR 252
Cdd:cd19107 242 RFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
1-247 |
2.65e-80 |
|
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: 241.87 E-value: 2.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKGTYV-DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIP-AVNQIELHPHLQQR 158
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDEVPVeEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAiATNQIELSPYLQNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 159 AAREFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDT 238
Cdd:cd19139 161 KLVAHCKQHGIHVTSYMTLAYGK-VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDA 239
|
....*....
gi 2748858100 239 EDIAAISAL 247
Cdd:cd19139 240 DDMAAIAAL 248
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
1-253 |
2.00e-77 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 235.30 E-value: 2.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRAFDTS 80
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWPTPSKGTYVDTF-KAFEKIYADGRAKAIGTSNFLPEHLAKLIEE--TSVIpAVNQIELHPHLQQ 157
Cdd:PRK11172 83 LQKLRTDYVDLTLIHWPSPNDEVSVEEFmQALLEAKKQGLTREIGISNFTIALMKQAIAAvgAENI-ATNQIELSPYLQN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 158 RAAREFHAEQGIATEAWSPLGQGKGLLEvPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLD 237
Cdd:PRK11172 162 RKVVAFAKEHGIHVTSYMTLAYGKVLKD-PVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLD 240
|
250
....*....|....*.
gi 2748858100 238 TEDIAAISALNEDRRL 253
Cdd:PRK11172 241 AEDMAAIAALDRNGRL 256
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
1-253 |
3.35e-77 |
|
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: 235.47 E-value: 3.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVN---ASG-IAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19111 4 MPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDTEKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWPT----PSKGTY--------VDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIP 144
Cdd:cd19111 84 LEKSLENLKLPYVDLYLIHHPCgfvnKKDKGErelassdvTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAKVKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 145 AVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQ-GKG----------LLEVPAIVAIAQKHGRTPAQIVLRWHLQLGN 213
Cdd:cd19111 164 SNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRAnqslwpdqpdLLEDPTVLAIAKELDKTPAQVLLRFVLQRGT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2748858100 214 VVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRL 253
Cdd:cd19111 244 GVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-260 |
5.00e-76 |
|
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: 233.47 E-value: 5.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNE----EGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19115 13 MPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEveagQGVARAIKEGIVKREDLFIVSKLWNTFHDGERVEPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWP-----------------------TPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHL 133
Cdd:cd19115 93 CRKQLADWGIDYFDLFLIHFPialkyvdpavryppgwfydgkkvEFSNAPIQETWTAMEKLVDKGLARSIGVSNFSAQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 134 AKLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG----------QGKG---LLEVPAIVAIAQKHGRTP 200
Cdd:cd19115 173 MDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldlpGAKDtppLFEHDVIKSIAEKHGKTP 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 201 AQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRLGpDPATF 260
Cdd:cd19115 253 AQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFN-NPLNY 311
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
1-253 |
1.17e-75 |
|
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: 232.42 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVN---ASG-IAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19155 12 MPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwiDSGkVKREELFIVTKLPPGGNRREKVEKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWPTPSKGT--------------------YVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKL 136
Cdd:cd19155 92 LLKSLEKLQLDYVDLYLIHFPVGSLSKeddsgkldptgehkqdyttdLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 137 IEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQ--------GKG--------LLEVPAIVAIAQKHGRTP 200
Cdd:cd19155 172 LKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfspGTGspsgsspdLLQDPVVKAIAERHGKSP 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2748858100 201 AQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRL 253
Cdd:cd19155 252 AQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
1-252 |
4.27e-75 |
|
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: 230.84 E-value: 4.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAV----NASGIAREELFVTTKLWNSDQGHdsALRA 76
Cdd:cd19112 11 MPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALaeafKTGLVKREDLFITTKLWNSDHGH--VIEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWPTPSKGTYV----------------------DTFKAFEKIYADGRAKAIGTSNFLPEHLA 134
Cdd:cd19112 89 CKDSLKKLQLDYLDLYLVHFPVATKHTGVgttgsalgedgvldidvtisleTTWHAMEKLVSAGLVRSIGISNYDIFLTR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 135 KLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQG---------KGLLEVPAIVAIAQKHGRTPAQIVL 205
Cdd:cd19112 169 DCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsVSPLDDPVLKDLAKKYGKSAAQIVL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2748858100 206 RWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRR 252
Cdd:cd19112 249 RWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
1-241 |
4.40e-73 |
|
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: 225.07 E-value: 4.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWqVPDD---EAERAVATALESGYRSIDTAAIYGNEEGTGKAVN---ASG-IAREELFVTTKLWNSdqGHDSA 73
Cdd:cd19119 12 IPALGLGTA-SPHEdraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraiDDGsIKREELFITTKVWPT--FYDEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 74 LRAFDTSLDKLGLDYVDLYLIHWPTPSK------------------------GTYVDTFKAFEKIYADGRAKAIGTSNFL 129
Cdd:cd19119 89 ERSLDESLKALGLDYVDLLLVHWPVCFEkdsddsgkpftpvnddgktryaasGDHITTYKQLEKIYLDGRAKAIGVSNYS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 130 PEHLAKLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG-QGKGLLEVPAIVAIAQKHGRTPAQIVLRWH 208
Cdd:cd19119 169 IVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGsHGAPNLKNPLVKKIAEKYNVSTGDILISYH 248
|
250 260 270
....*....|....*....|....*....|...
gi 2748858100 209 LQLGNVVIPKSVTPSRIKENIDVfdFSLDTEDI 241
Cdd:cd19119 249 VRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDL 279
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
1-260 |
1.59e-71 |
|
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: 221.66 E-value: 1.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTG----KAVNASGIAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19114 4 MPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGKDHVREA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWPTPSKgtYVD--------------------------TFKAFEKIYADGRAKAIGTSNFLP 130
Cdd:cd19114 84 FDRQLKDYGLDYIDLYLIHFPIPAA--YVDpaenypflwkdkelkkfpleqspmqeCWREMEKLVDAGLVRNIGIANFNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 131 EHLAKLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG---------QGK---GLLEVPAIVAIAQKHGR 198
Cdd:cd19114 162 QLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtkHLKhftNLLEHPVVKKLADKHKR 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2748858100 199 TPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRLGpDPATF 260
Cdd:cd19114 242 DTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFN-DPVVY 302
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
1-259 |
5.20e-71 |
|
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: 220.22 E-value: 5.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNAS----GIAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKikegVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWP------------------TPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE 138
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPmgfkpgepdlpldrsgmvIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETS--VIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG---QGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGN 213
Cdd:cd19110 164 KPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGgscEGVDLIDDPVIQRIAKKHGKSPAQILIRFQIQRNV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2748858100 214 VVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRLGPDPAT 259
Cdd:cd19110 244 IVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPIT 289
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
1-260 |
4.30e-70 |
|
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: 218.08 E-value: 4.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNE----EGTGKAVNASGIAREELFVTTKLWNSDQGHDSALRA 76
Cdd:cd19113 11 MPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEkevgEGVNRAIDEGLVKREELFLTSKLWNNFHDPKNVETA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWPTPSK----------GTY--------------VDTFKAFEKIYADGRAKAIGTSNFLPEH 132
Cdd:cd19113 91 LNKTLSDLKLDYVDLFLIHFPIAFKfvpieekyppGFYcgdgdnfvyedvpiLDTWKALEKLVDAGKIKSIGVSNFPGAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 133 LAKLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG--------QGKG-----LLEVPAIVAIAQKHGRT 199
Cdd:cd19113 171 ILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvelnQGRAlntptLFEHDTIKSIAAKHNKT 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2748858100 200 PAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRLGpDPATF 260
Cdd:cd19113 251 PAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFN-DPWDW 310
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
1-255 |
1.11e-69 |
|
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: 216.71 E-value: 1.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVW---QVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVNaSGIA-----REELFVTTKLWNSDQGHDS 72
Cdd:cd19108 11 IPVLGFGTYapeEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIR-SKIAdgtvkREDIFYTSKLWCTFHRPEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 73 ALRAFDTSLDKLGLDYVDLYLIHWPTPSKG---------------TYVD---TFKAFEKIYADGRAKAIGTSNFLPEHLA 134
Cdd:cd19108 90 VRPALEKSLKKLQLDYVDLYLIHFPVALKPgeelfpkdengklifDTVDlcaTWEAMEKCKDAGLAKSIGVSNFNRRQLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 135 KLIEETSVI--PAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKG----------LLEVPAIVAIAQKHGRTPAQ 202
Cdd:cd19108 170 MILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDkewvdqnspvLLEDPVLCALAKKHKRTPAL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2748858100 203 IVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRRLGP 255
Cdd:cd19108 250 IALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
2-247 |
2.91e-68 |
|
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: 212.38 E-value: 2.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAV----NASGIAREELFVTTKLWNSDQGHDSALRAF 77
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFseifKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 78 DTSLDKLGLDYVDLYLIHWPTP------------------SKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEE 139
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAfdmdtdgdprddnqiqslSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 140 TSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKG-----LLEVPAIVAIAQKHGRTPAQIVLRWHLQ--LG 212
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGdgnltFLNDSELKALATKYNTTPPQVIIAWHLQkwPK 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 2748858100 213 N-VVIPKSVTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19128 242 NySVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
1-250 |
3.82e-64 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 202.30 E-value: 3.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWqVPDDEAER-AVATALESGYRSIDTAAIYGNEEGTGKAVN----ASGIAREELFVTTKLWNSDQGHDSALR 75
Cdd:cd19129 6 IPALGFGTL-IPDPSATRnAVKAALEAGFRHFDCAERYRNEAEVGEAMQevfkAGKIRREDLFVTTKLWNTNHRPERVKP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 76 AFDTSLDKLGLDYVDLYLIHWPTPSKG-------------------TYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKL 136
Cdd:cd19129 85 AFEASLKRLQLDYLDLYLIHTPFAFQPgdeqdprdangnviyddgvTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 137 IEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQG--KGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNV 214
Cdd:cd19129 165 FEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmePKLLEDPVITAIARRVNKTPAQVLLAWAIQRGTA 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 2748858100 215 VIPKSVTPSRIKENidvFDFSLDTEDiaAISALNED 250
Cdd:cd19129 245 LLTTSKTPSRIREN---FDISTLPED--AMREINEG 275
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
3-248 |
3.39e-63 |
|
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: 199.85 E-value: 3.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVNASGIAREELFVTTKLWNSDQGHDS------A 73
Cdd:pfam00248 7 QLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVPDGDGPWPSggskenI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 74 LRAFDTSLDKLGLDYVDLYLIHWPTPSKgTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQIELHP 153
Cdd:pfam00248 87 RKSLEESLKRLGTDYIDLYYLHWPDPDT-PIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 154 --HLQQRAAREFHAEQGIATEAWSPLGQG--------------------------KGLLEVPAIVAIAQKHGRTPAQIVL 205
Cdd:pfam00248 166 lrRRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkgtpLNLEALEALEEIAKEHGVSPAQVAL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2748858100 206 RWHLQ--LGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALN 248
Cdd:pfam00248 246 RWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
1-252 |
1.09e-61 |
|
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: 196.56 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVW----QVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKAVN---ASG-IAREELFVTTKLWNSDQGHDS 72
Cdd:cd19109 4 IPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIRekiAEGkVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 73 ALRAFDTSLDKLGLDYVDLYLIHWPTPSK-----------GTYV-------DTFKAFEKIYADGRAKAIGTSNFLPEHLA 134
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiyprdenGKWLyhktnlcATWEALEACKDAGLVKSIGVSNFNRRQLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 135 KLIEETSVI--PAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKG----------LLEVPAIVAIAQKHGRTPAQ 202
Cdd:cd19109 164 LILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpiwvnvssppLLEDPLLNSIGKKYNKTAAQ 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2748858100 203 IVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNEDRR 252
Cdd:cd19109 244 VVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
1-249 |
1.65e-61 |
|
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: 195.53 E-value: 1.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAE--RAVATALESGYRSIDTAAIYGNEEGTGKAVN-----ASGIAREELFVTTKLWNSDQGHDSA 73
Cdd:cd19122 9 IPAVGFGTFANEGAKGEtyAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRdflkeNPSVKREDLFICTKVWNHLHEPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 74 LRAFDTSLDKLGLDYVDLYLIHWPTPS------------KGTYV----------DTFKAFEKIYADGRAKAIGTSNFLPE 131
Cdd:cd19122 89 KWSIDNSLKNLKLDYIDLFLVHWPIAAekndqrspklgpDGKYVilkdltenpePTWRAMEEIYESGKAKAIGVSNWTIP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 132 HLAKLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQ-------GKGLLEVPAIVAIAQKHGRTPAQIV 204
Cdd:cd19122 169 GLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvpstGERVSENPTLNEVAEKGGYSLAQVL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2748858100 205 LRWHLQLGNVVIPKSVTPSRIKENIDVFDFSldTEDIAAISALNE 249
Cdd:cd19122 249 IAWGLRRGYVVLPKSSTPSRIESNFKSIELS--DEDFEAINQVAK 291
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
1-245 |
1.88e-60 |
|
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: 191.67 E-value: 1.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVP---------DDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVnaSGIAREELFVTTKLWNSDQ 68
Cdd:cd19072 4 VPVLGLGTWGIGggmskdysdDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI--KGFDREDLFITTKVSPDHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 69 GHDSALRAFDTSLDKLGLDYVDLYLIHWPTPSkGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIP-AVN 147
Cdd:cd19072 82 KYDDVIKAAKESLKRLGTDYIDLYLIHWPNPS-IPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPiVAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 148 QIELhpHLQQRAAR----EFHAEQGIATEAWSPLGQGK--GLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVV-IPKSV 220
Cdd:cd19072 161 QVEY--NLFDREEEsgllPYCQKNGIAIIAYSPLEKGKlsNAKGSPLLDEIAKKYGKTPAQIALNWLISKPNVIaIPKAS 238
|
250 260
....*....|....*....|....*
gi 2748858100 221 TPSRIKENIDVFDFSLDTEDIAAIS 245
Cdd:cd19072 239 NIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
1-244 |
1.72e-58 |
|
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: 187.07 E-value: 1.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDDEAER-----AVATALESGYRSIDTAAIYGN---EEGTGKAVNASgiaREELFVTTKLWNSDQGHDS 72
Cdd:cd19138 11 VPALGQGTWYMGEDPAKRaqeieALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLPSNASRQG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 73 ALRAFDTSLDKLGLDYVDLYLIHWPtpskGTY--VDTFKAFEKIYADGRAKAIGTSNFLPehlaKLIEETSVIP-----A 145
Cdd:cd19138 88 TVRACERSLRRLGTDYLDLYLLHWR----GGVplAETVAAMEELKKEGKIRAWGVSNFDT----DDMEELWAVPgggncA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 146 VNQIeLHpHLQQRAArEF-----HAEQGIATEAWSPLGQG----KGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVV- 215
Cdd:cd19138 160 ANQV-LY-NLGSRGI-EYdllpwCREHGVPVMAYSPLAQGgllrRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIa 236
|
250 260
....*....|....*....|....*....
gi 2748858100 216 IPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19138 237 IPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
3-247 |
1.23e-51 |
|
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: 170.74 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVnaSGIAREELFVTTKL-WNSDQGH-------D 71
Cdd:COG0667 22 TFGGPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEAL--KGRPRDDVVIATKVgRRMGPGPngrglsrE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 72 SALRAFDTSLDKLGLDYVDLYLIHWPTPSkgTYV-DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIP--AVNQ 148
Cdd:COG0667 100 HIRRAVEASLRRLGTDYIDLYQLHRPDPD--TPIeETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPpiVAVQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 149 IELHPhLQQRAAREFH---AEQGIATEAWSPLGQG-----------------------------KGLLEVPAIVAIAQKH 196
Cdd:COG0667 178 NEYSL-LDRSAEEELLpaaRELGVGVLAYSPLAGGlltgkyrrgatfpegdraatnfvqgylteRNLALVDALRAIAAEH 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2748858100 197 GRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:COG0667 257 GVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
1-244 |
1.59e-47 |
|
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: 158.50 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQV---------PDDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVnaSGIAREELFVTTKLWNSDQ 68
Cdd:cd19137 4 IPALGLGTWGIggfltpdysRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAI--KDFPREDLFIVTKVWPTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 69 GHDSALRAFDTSLDKLGLDYVDLYLIHWPTPSKgTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVNQ 148
Cdd:cd19137 82 RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNI-PLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVCNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 149 IE--LHPH-LQQRAAREFHAEQGIATEAWSPLGQGkGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVV-IPKSVTPSR 224
Cdd:cd19137 161 VKynLEDRdPERDGLLEYCQKNGITVVAYSPLRRG-LEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVaIPKAGRVEH 239
|
250 260
....*....|....*....|
gi 2748858100 225 IKENIDVFDFSLDTEDIAAI 244
Cdd:cd19137 240 LKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
4-244 |
3.01e-45 |
|
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: 153.84 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVWQ--------VPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVnaSGIaREELFVTTK---LWNSDQG 69
Cdd:cd19084 7 IGLGTWAiggtwwgeVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKAL--KGR-RDDVVIATKcglRWDGGKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 70 H------DSALRAFDTSLDKLGLDYVDLYLIHWPTPSkgTYV-DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSV 142
Cdd:cd19084 84 VtkdlspESIRKEVEQSLRRLQTDYIDLYQIHWPDPN--TPIeETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 143 ipAVNQIELHPhLQQRAARE---FHAEQGIATEAWSPLGQG--------------------------KGLLEVPAIVA-- 191
Cdd:cd19084 162 --VSLQPPYSM-LEREIEEEllpYCRENGIGVLPYGPLAQGlltgkykkeptfppddrrsrfpffrgENFEKNLEIVDkl 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2748858100 192 --IAQKHGRTPAQIVLRWHLQ--LGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19084 239 keIAEKYGKSLAQLAIAWTLAqpGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
2-230 |
1.45e-44 |
|
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: 149.98 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQ----VPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASGIaREELFVTTKLWNSDQGHDSA- 73
Cdd:cd06660 1 SRLGLGTMTfggdGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 74 -------LRAFDTSLDKLGLDYVDLYLIHWPTPSkgTYVD-TFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE----ETS 141
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHRDDPS--TPVEeTLEALNELVREGKIRYIGVSNWSAERLAEALAyakaHGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 142 VIPAVNQIE---LHPHLQQRAAREFHAEQGIATEAWSPLGQGkgllevpaivaiaqkhgrtPAQIVLRWHLQLGNV--VI 216
Cdd:cd06660 158 PGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARG-------------------PAQLALAWLLSQPFVtvPI 218
|
250
....*....|....
gi 2748858100 217 PKSVTPSRIKENID 230
Cdd:cd06660 219 VGARSPEQLEENLA 232
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
2-250 |
1.75e-44 |
|
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: 151.59 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQ---------VPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASgiaREELFVTTKLWNSDQG 69
Cdd:cd19085 2 SRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR---RDDVVIATKVSPDNLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 70 HDSALRAFDTSLDKLGLDYVDLYLIHWPTPSKgTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIpaVNQI 149
Cdd:cd19085 79 PEDVRKSCERSLKRLGTDYIDLYQIHWPSSDV-PLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 150 ELhpHLQQRAA----REFHAEQGIATEAWSPLGQgkGLL--------EVP-------------------------AIVAI 192
Cdd:cd19085 156 PY--NLLWRAIeyeiLPFCREHGIGVLAYSPLAQ--GLLtgkfssaeDFPpgdartrlfrhfepgaeeetfealeKLKEI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 193 AQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTEDIAAISALNED 250
Cdd:cd19085 232 ADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
2-244 |
2.82e-44 |
|
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: 151.23 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQVPD-----------DEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASGiAREELFVTTKLWN-- 65
Cdd:cd19093 3 SPLGLGTWQWGDrlwwgygeygdEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAPlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 66 SDQGHDSALRAFDTSLDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHL---AKLIEETSV 142
Cdd:cd19093 82 WRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLrraHKALKERGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 143 IPAVNQIE---LHPHLQQRAAREFHAEQGIATEAWSPLGQG----------------------KGLLEVPAIV----AIA 193
Cdd:cd19093 162 PLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGlltgkyspenpppggrrrlfgrKNLEKVQPLLdaleEIA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2748858100 194 QKHGRTPAQIVLRWHLQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19093 242 EKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
5-240 |
1.28e-33 |
|
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: 123.05 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 5 GFGVWQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASGIAREELFVTTK----LWNSDQGHDSA---- 73
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgirLGDDPRPGRIKhydt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 74 -----LRAFDTSLDKLGLDYVDLYLIHWPTPskgtYVD---TFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPA 145
Cdd:cd19092 95 skehiLASVEGSLKRLGTDYLDLLLLHRPDP----LMDpeeVAEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 146 VNQIE---LHPHLQQRAAREFHAEQGIATEAWSPLGQGKgLLEVP---------AIVAIAQKHGRTPAQIVLRWHLQL-- 211
Cdd:cd19092 171 TNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGGGR-LFGGFderfqrlraALEELAEEYGVTIEAIALAWLLRHpa 249
|
250 260
....*....|....*....|....*....
gi 2748858100 212 GNVVIPKSVTPSRIKENIDVFDFSLDTED 240
Cdd:cd19092 250 RIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-247 |
1.22e-32 |
|
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: 120.86 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVWQV----------PDDEAE--RAVATALESGYRSIDTAAIYG---NEEGTGKAVNAsgiAREELFVTTK---LWN 65
Cdd:cd19102 4 IGLGTWAIggggwgggwgPQDDRDsiAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKG---LRDRPIVATKcglLWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 66 sDQGH-------DSALRAFDTSLDKLGLDYVDLYLIHWPTPSKGTyVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE 138
Cdd:cd19102 81 -EEGRirrslkpASIRAECEASLRRLGVDVIDLYQIHWPDPDEPI-EEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVipAVNQIE---LHPHLQQRAAReFHAEQGIATEAWSPLgqGKGLLE------------------------------ 185
Cdd:cd19102 159 IHPI--ASLQPPyslLRRGIEAEILP-FCAEHGIGVIVYSPM--QSGLLTgkmtpervaslpaddwrrrspffqepnlar 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2748858100 186 ----VPAIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19102 234 nlalVDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-247 |
6.57e-31 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 117.61 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVW--QVPD-DEAERAVATALESGYRSIDTAAIYGN-EEGTGKAVnaSGIaREELFVTTKL--WNSDqgHDSAL 74
Cdd:COG1453 13 VSVLGFGGMrlPRKDeEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKAL--KGP-RDKVILATKLppWVRD--PEDMR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 75 RAFDTSLDKLGLDYVDLYLIH-------WPTPSKGTyvDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIPAVn 147
Cdd:COG1453 88 KDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPG--GALEALEKAKAEGKIRHIGFSTHGSLEVIKEAIDTGDFDFV- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 148 QIELHPHLQQRAAR----EFHAEQGIATEAWSPLGQGKgLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVVIPKS--VT 221
Cdd:COG1453 165 QLQYNYLDQDNQAGeealEAAAEKGIGVIIMKPLKGGR-LANPPEKLVELLCPPLSPAEWALRFLLSHPEVTTVLSgmST 243
|
250 260
....*....|....*....|....*...
gi 2748858100 222 PSRIKENIDVFD--FSLDTEDIAAISAL 247
Cdd:COG1453 244 PEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
2-231 |
3.10e-30 |
|
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: 113.48 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQ-------VPDDEAERAVATALESGYRSIDTAAIYGN-EEGTGKAVnaSGIAREELFVTTKLWNSDQGH--- 70
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGTHGEGGrdr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 71 -----DSALRAFDTSLDKLGLDYVDLYLIHWPTPSKGTyVDTFKAFEKIYADGRAKAIGTSNFLPEhLAKLIeETSVIPA 145
Cdd:cd19095 79 kdfspAAIRASIERSLRRLGTDYIDLLQLHGPSDDELT-GEVLETLEDLKAAGKVRYIGVSGDGEE-LEAAI-ASGVFDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 146 VnQIELHPHLQQRAAR-EFHAEQGIATEAWSPLGQGKGLLEVPAIVAIAQKH----------GRTPAQIVLRWHLQ--LG 212
Cdd:cd19095 156 V-QLPYNVLDREEEELlPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYArrpefaaeigGATWAQAALRFVLShpGV 234
|
250
....*....|....*....
gi 2748858100 213 NVVIPKSVTPSRIKENIDV 231
Cdd:cd19095 235 SSAIVGTTNPEHLEENLAA 253
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
9-244 |
1.71e-29 |
|
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: 112.68 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 9 WQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVnASGIAREELFVTTKLWN--SDQGHDSAL------RAF 77
Cdd:cd19079 30 WVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRAL-KEFAPRDEVVIATKVYFpmGDGPNGRGLsrkhimAEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 78 DTSLDKLGLDYVDLYLIHWP---TPSKgtyvDTFKAFEKIYADGRAKAIGTSNFLPEHLAKL--IEE----TSVIPAVNQ 148
Cdd:cd19079 109 DASLKRLGTDYIDLYQIHRWdyeTPIE----ETLEALHDVVKSGKVRYIGASSMYAWQFAKAlhLAEkngwTKFVSMQNH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 149 IELhphLQQRAARE---FHAEQGIATEAWSPLGQG-----------------------------KGLLEVPAIVAIAQKH 196
Cdd:cd19079 185 YNL---LYREEEREmipLCEEEGIGVIPWSPLARGrlarpwgdtterrrsttdtaklkydyfteADKEIVDRVEEVAKER 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2748858100 197 GRTPAQIVLRWHLQLGNVVIP--KSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19079 262 GVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
2-237 |
1.07e-28 |
|
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: 109.61 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFG--------VWQVPDDEAErAVAT---ALESGYRSIDTAAIYG---NEEGTGKAVNAsgiAREELFVTTKL---- 63
Cdd:cd19088 2 SRLGYGamrltgpgIWGPPADREE-AIAVlrrALELGVNFIDTADSYGpdvNERLIAEALHP---YPDDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 64 -----WNSDQGHDSALRAFDTSLDKLGLDYVDLYLIHWPTPsKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE 138
Cdd:cd19088 78 tgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDP-KVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIPAVNQIELHpHLQQRAAREFHAEQGIATEAWSPLGQGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNVV--I 216
Cdd:cd19088 157 IVRIVSVQNRYNLA-NRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMlpI 235
|
250 260
....*....|....*....|.
gi 2748858100 217 PKSVTPSRIKENIDVFDFSLD 237
Cdd:cd19088 236 PGTSSVEHLEENLAAAGLRLS 256
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
3-239 |
4.60e-28 |
|
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: 108.83 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFGVW-----QVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVnaSGIAREELFVTTKL-WN-SDQGHDS 72
Cdd:cd19074 6 ELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKAL--KGWPRESYVISTKVfWPtGPGPNDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 73 AL------RAFDTSLDKLGLDYVDLYLIHWPTPSkgTYVD-TFKAFEKIYADGRAKAIGTSNFLPEHLAK---LIEETSV 142
Cdd:cd19074 84 GLsrkhifESIHASLKRLQLDYVDIYYCHRYDPE--TPLEeTVRAMDDLIRQGKILYWGTSEWSAEQIAEahdLARQFGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 143 I-PAVNQIELhpHLQQRAA----REFHAEQGIATEAWSPLGQG-------KGLLE------------------------- 185
Cdd:cd19074 162 IpPVVEQPQY--NMLWREIeeevIPLCEKNGIGLVVWSPLAQGlltgkyrDGIPPpsrsratdednrdkkrrlltdenle 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2748858100 186 -VPAIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:cd19074 240 kVKKLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-231 |
1.19e-27 |
|
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: 106.51 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVwQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVnaSGIAREELFVTTKLWNSDQGHDSA--LR 75
Cdd:cd19105 13 VSRLGFGG-GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEAL--KGLRRDKVFLATKASPRLDKKDKAelLK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 76 AFDTSLDKLGLDYVDLYLIHWPTPSKGTYVD--TFKAFEKIYADGRAKAIGTS--NFLPEHLAKLIEE---TSVIPAVNq 148
Cdd:cd19105 90 SVEESLKRLQTDYIDIYQLHGVDTPEERLLNeeLLEALEKLKKEGKVRFIGFSthDNMAEVLQAAIESgwfDVIMVAYN- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 149 ielhpHLQQRAARE----FHAEQGIATEAWSPLGqgkGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTP 222
Cdd:cd19105 169 -----FLNQPAELEealaAAAEKGIGVVAMKTLA---GGYLQPALLSVLKAKGFSLPQAALKWVLSNPRVdtVVPGMRNF 240
|
....*....
gi 2748858100 223 SRIKENIDV 231
Cdd:cd19105 241 AELEENLAA 249
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
4-246 |
1.37e-27 |
|
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: 107.74 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVWQV---------PDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASgiaREELFVTTK---LWNSDQ 68
Cdd:cd19149 14 IGLGTWAIgggpwwggsDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcglRWDREG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 69 GH----------------DSALRAFDTSLDKLGLDYVDLYLIHWP---TPSKgtyvDTFKAFEKIYADGRAKAIGTSNFL 129
Cdd:cd19149 91 GSfffvrdgvtvyknlspESIREEVEQSLKRLGTDYIDLYQTHWQdveTPIE----ETMEALEELKRQGKIRAIGASNVS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 130 PEHLAKLIEETSVipAVNQiELHPHLQQRAAREFH---AEQGIATEAWSPLGQG-------------KG----------- 182
Cdd:cd19149 167 VEQIKEYVKAGQL--DIIQ-EKYSMLDRGIEKELLpycKKNNIAFQAYSPLEQGlltgkitpdrefdAGdarsgipwfsp 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2748858100 183 --------LLEvpAIVAIAQKHGRTPAQIVLRWHLQLGN--VVIPKSVTPSRIKENIDVFDFSLDTEDIAAISA 246
Cdd:cd19149 244 enrekvlaLLE--KWKPLCEKYGCTLAQLVIAWTLAQPGitSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
2-233 |
1.56e-27 |
|
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: 106.49 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFG------VWQVPDDEaERAVAT---ALESGYRSIDTAAIYGN---EEGTGKAVnaSGIAREELFVTTKL-WNSDQ 68
Cdd:cd19096 1 SVLGFGtmrlpeSDDDSIDE-EKAIEMiryAIDAGINYFDTAYGYGGgksEEILGEAL--KEGPREKFYLATKLpPWSVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 69 GHDSALRAFDTSLDKLGLDYVDLYLIHWptPSKGTYVDT------FKAFEKIYADGRAKAIG-TSNFLPEHLAKLIEETS 141
Cdd:cd19096 78 SAEDFRRILEESLKRLGVDYIDFYLLHG--LNSPEWLEKarkgglLEFLEKAKKEGLIRHIGfSFHDSPELLKEILDSYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 142 VipAVNQIELH----PHLQQRAAREFHAEQGIATEAWSPLGQGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGNV--V 215
Cdd:cd19096 156 F--DFVQLQYNyldqENQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGAPLSPAEWALRFLLSHPEVttV 233
|
250
....*....|....*...
gi 2748858100 216 IPKSVTPSRIKENIDVFD 233
Cdd:cd19096 234 LSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
13-247 |
2.36e-27 |
|
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: 107.12 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 13 DDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVnaSGIAREELFVTTKLWNSDQGHDSAL--------RAFDTSL 81
Cdd:cd19083 32 EEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVL--KEYNRNEVVIATKGAHKFGGDGSVLnnspeflrSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 82 DKLGLDYVDLYLIHWP---TPSKgtyvDTFKAFEKIYADGRAKAIGTSNFLPEHLakliEETSVIPAVNQIELHPHLQQR 158
Cdd:cd19083 110 KRLNTDYIDLYYIHFPdgeTPKA----EAVGALQELKDEGKIRAIGVSNFSLEQL----KEANKDGYVDVLQGEYNLLQR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 159 AAREFH----AEQGIATEAWSPLGQG------------------------------KGLLEVPAIVAIAQKHGRTPAQIV 204
Cdd:cd19083 182 EAEEDIlpycVENNISFIPYFPLASGllagkytkdtkfpdndlrndkplfkgerfsENLDKVDKLKSIADEKGVTVAHLA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2748858100 205 LRWHLQ--LGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19083 262 LAWYLTrpAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
2-247 |
2.79e-27 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 106.93 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFG-------------VWQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNAsgiAREELFVTTK--L 63
Cdd:cd19091 14 SELALGtmtfgggggffgaWGGVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKG---RRDDVLIATKvrG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 64 WNSDQGHDSAL------RAFDTSLDKLGLDYVDLYLIHWPTPskGTYVD-TFKAFEKIYADGRAKAIGTSNFLPEHLAKL 136
Cdd:cd19091 91 RMGEGPNDVGLsrhhiiRAVEASLKRLGTDYIDLYQLHGFDA--LTPLEeTLRALDDLVRQGKVRYIGVSNFSAWQIMKA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 137 --IEETSVIPAVNQIELHPHLqqrAAREFHAE-------QGIATEAWSPLGQG--------------------------- 180
Cdd:cd19091 169 lgISERRGLARFVALQAYYSL---LGRDLEHElmplaldQGVGLLVWSPLAGGllsgkyrrgqpapegsrlrrtgfdfpp 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2748858100 181 ----KGLLEVPAIVAIAQKHGRTPAQIVLRWHLQ---LGNVVIPKSvTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19091 246 vdreRGYDVVDALREIAKETGATPAQVALAWLLSrptVSSVIIGAR-NEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
2-244 |
1.50e-26 |
|
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: 105.22 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQV--------PDDEAERAVATALESGYRSIDTAAIYG-NEEGTGKAVNASGIAREELFVTTKLWNSDQGHDS 72
Cdd:cd19144 14 PALGFGAMGLsafygppkPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFGIEKNVETG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 73 AL----------RAFDTSLDKLGLDYVDLYLIHWPTPSkgTYVD-TFKAFEKIYADGRAKAIGTSNFLPEHL--AKLIEE 139
Cdd:cd19144 94 EYsvdgspeyvkKACETSLKRLGVDYIDLYYQHRVDGK--TPIEkTVAAMAELVQEGKIKHIGLSECSAETLrrAHAVHP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 140 tsvIPAVnQIELHPHL-----QQRAAREFHAEQGIATEAWSPLGQG------------------------------KGLL 184
Cdd:cd19144 172 ---IAAV-QIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGfltgairspddfeegdfrrmaprfqaenfpKNLE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2748858100 185 EVPAIVAIAQKHGRTPAQIVLRWHLQLGN--VVIPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19144 248 LVDKIKAIAKKKNVTAGQLTLAWLLAQGDdiIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
4-231 |
5.89e-26 |
|
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: 101.79 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVWQ--------VPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASgiaREELFVTTKLWNSDQGH-- 70
Cdd:cd19086 6 IGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR---RDKVVIATKFGNRFDGGpe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 71 -------DSALRAFDTSLDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVi 143
Cdd:cd19086 83 rpqdfspEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 144 pAVNQIELHPhLQQRAAREFH---AEQGIATEAWSPLgqGKGLLEvpaivaiaqkhGRtPAQIVLRWHLQLGNV--VIPK 218
Cdd:cd19086 162 -DVVQVIYNL-LDQRPEEELFplaEEHGVGVIARVPL--ASGLLT-----------GK-LAQAALRFILSHPAVstVIPG 225
|
250
....*....|...
gi 2748858100 219 SVTPSRIKENIDV 231
Cdd:cd19086 226 ARSPEQVEENAAA 238
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
12-244 |
1.11e-25 |
|
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: 102.29 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 12 PDDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVNAsgiAREELFVTTK---LWNSDQGH-------DSALRAFD 78
Cdd:cd19076 30 DEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVIATKfgiVRDPGSGFrgvdgrpEYVRAACE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 79 TSLDKLGLDYVDLYLIHWPTPSkgTYV-DTFKAFEKIYADGRAKAIGTSNFLPEHLAKlieETSVIP--AVnQIELhpHL 155
Cdd:cd19076 107 ASLKRLGTDVIDLYYQHRVDPN--VPIeETVGAMAELVEEGKVRYIGLSEASADTIRR---AHAVHPitAV-QSEY--SL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 156 QQR--------AAREFhaeqGIATEAWSPLGQG------------------------------KGLLEVPAIVAIAQKHG 197
Cdd:cd19076 179 WTRdiedevlpTCREL----GIGFVAYSPLGRGfltgaikspedlpeddfrrnnprfqgenfdKNLKLVEKLEAIAAEKG 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2748858100 198 RTPAQIVLRWHLQLGNVVIP----KSVTpsRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19076 255 CTPAQLALAWVLAQGDDIVPipgtKRIK--YLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-230 |
2.16e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 97.55 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFG---VWQVPDDEAERAVATALESGYRSIDTAAIYGN-EEGTGKAVnaSGIaREELFVTTKLWNSDQghDSALRAF 77
Cdd:cd19100 12 SRLGFGggpLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKAL--KGR-RDKVFLATKTGARDY--EGAKRDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 78 DTSLDKLGLDYVDLYLIHwptpskgtYVDTFKAFEKIYADGRA-------------KAIGTSNFLPEHLAKLIEET---S 141
Cdd:cd19100 87 ERSLKRLGTDYIDLYQLH--------AVDTEEDLDQVFGPGGAlealleakeegkiRFIGISGHSPEVLLRALETGefdV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 142 VIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLGQGKGLLEVPAIVAIAqkhgrtpaqivLRWHLQLGNV--VIPKS 219
Cdd:cd19100 159 VLFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQA-----------LRYALSLPPVdvVIVGM 227
|
250
....*....|.
gi 2748858100 220 VTPSRIKENID 230
Cdd:cd19100 228 DSPEELDENLA 238
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-244 |
3.03e-23 |
|
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: 96.13 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 6 FGvWQVPDDEAERAVATALESGYRSIDTAAIY-----GNEEGT-----GKAVNASGiAREELFVTTKL-WNSDQGH---- 70
Cdd:cd19081 19 FG-WTADEETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGEsetiiGRWLKSRG-KRDRVVIATKVgFPMGPNGpgls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 71 -DSALRAFDTSLDKLGLDYVDLYLIHWPTPSKgTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKlIEETSVIPAVNQI 149
Cdd:cd19081 97 rKHIRRAVEASLRRLQTDYIDLYQAHWDDPAT-PLEETLGALNDLIRQGKVRYIGASNYSAWRLQE-ALELSRQHGLPRY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 150 E-LHPH--LQQRAAREFH-----AEQGIATEAWSPLGQG----------------------------KGLLEVPAIVAIA 193
Cdd:cd19081 175 VsLQPEynLVDRESFEGEllplcREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakrylneRGLRILDALDEVA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2748858100 194 QKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19081 255 AEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-246 |
4.77e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 92.66 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQV--------PDDEAERAVATALESGYRSIDTAAIYGN-EEGTGKAVN---ASGIAREELFVTTKlWNSDQ 68
Cdd:cd19101 2 ISRVINGMWQLsgghggirDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKrlrRERDAADDVQIHTK-WVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 69 GHDSALRAF-----DTSLDKLGLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEEtsVI 143
Cdd:cd19101 81 GELTMTRAYveaaiDRSLKRLGVDRLDLVQFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDA--GV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 144 PAV-NQIElHPHLQQRAARE---FHAEQGIA------------TEAWspLGQGKG------------------------- 182
Cdd:cd19101 159 PIVsNQVQ-YSLLDRRPENGmaaLCEDHGIKllaygtlaggllSEKY--LGVPEPtgpaletrslqkyklmidewggwdl 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2748858100 183 ---LLEVPAivAIAQKHGRTPAQIVLRWHLQ---LGNVVIpkSVTPSR-IKENIDVFDFSLDTEDIAAISA 246
Cdd:cd19101 236 fqeLLRTLK--AIADKHGVSIANVAVRWVLDqpgVAGVIV--GARNSEhIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
3-180 |
1.23e-21 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 91.08 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFGVWQVPDDEAERAVATALESGYRSIDTAAIYGN-EEGTGKAVNasGIAREELFVTTKL-----WNSDQGHDSALRA 76
Cdd:cd19090 9 GLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKVgrlpeDTADYSADRVRRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIH---WPTPSKGTYVD-TFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEET--SVIPAVNQIE 150
Cdd:cd19090 87 VEESLERLGRDRIDLLMIHdpeRVPWVDILAPGgALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGdfDVVLTANRYT 166
|
170 180 190
....*....|....*....|....*....|...
gi 2748858100 151 LhphLQQRAAREF--HAEQ-GIATEAWSPLGQG 180
Cdd:cd19090 167 L---LDQSAADELlpAAARhGVGVINASPLGMG 196
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
9-247 |
3.41e-21 |
|
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: 90.44 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 9 WQVPDDEAerAVAT---ALESGYRSIDTAAIYG---NEEGTGKAVNASGIaREELFVTTKL---WNSDQG---HDSALRA 76
Cdd:cd19148 19 WGGTDEKE--AIETihkALDLGINLIDTAPVYGfglSEEIVGKALKEYGK-RDRVVIATKVgleWDEGGEvvrNSSPARI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 F---DTSLDKLGLDYVDLYLIHWPTPsKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLaklieET--SVIP-AVNQIE 150
Cdd:cd19148 96 RkevEDSLRRLQTDYIDLYQVHWPDP-LVPIEETAEALKELLDEGKIRAIGVSNFSPEQM-----ETfrKVAPlHTVQPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 151 LhpHLQQRAARE----FHAEQGIATEAWSPLGQG------------------------------KGLLEVPAIVAIAQKH 196
Cdd:cd19148 170 Y--NLFEREIEKdvlpYARKHNIVTLAYGALCRGllsgkmtkdtkfegddlrrtdpkfqeprfsQYLAAVEELDKLAQER 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2748858100 197 -GRTPAQIVLRWHLQLGNVVIP--KSVTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19148 248 yGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
2-233 |
5.64e-21 |
|
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: 89.53 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGV----WQVPDDEAERAVATALESGYRSIDTAAIYGNEEGTGKA-------VNASGIaREELFVTTK-------- 62
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServigewLKSRGN-RDKVVIATKgghpdled 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 63 LWNSDQGHDSALRAFDTSLDKLGLDYVDLYLIHWPTPSK--GTYVDTfkaFEKIYADGRAKAIGTSNFLPEHLAKLIE-- 138
Cdd:cd19082 80 MSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVpvGEIVDT---LNELVRAGKIRAFGASNWSTERIAEANAya 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIP--AVNQIEL------HPHL-------QQRAAREFHAEQGIATEAWSPLGQG------KGLLEVP---------- 187
Cdd:cd19082 157 KAHGLPgfAASSPQWslarpnEPPWpgptlvaMDEEMRAWHEENQLPVFAYSSQARGffskraAGGAEDDselrrvyyse 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2748858100 188 -------AIVAIAQKHGRTPAQIVLRWHLQLGNVVIP--KSVTPSRIKENIDVFD 233
Cdd:cd19082 237 enferleRAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-207 |
2.45e-19 |
|
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: 85.45 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFGVWQVP-----DDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAV----NASGIAREELFVTTK-------- 62
Cdd:cd19099 5 SLGLGTYRGDsddetDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALreliEKGGIKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 63 -------------------LWNSDQGHDSAL------RAFDTSLDKLGLDYVDLYLIHWP------TPSKGTY---VDTF 108
Cdd:cd19099 85 deplrplkyleeklgrgliDVADSAGLRHCIspayleDQIERSLKRLGLDTIDLYLLHNPeeqlleLGEEEFYdrlEEAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 109 KAFEKIYADGRAKAIGTSNF-----LPEHLAKLIEETSVIPAVNQIELHPHLQ----------QRAAREFH--------- 164
Cdd:cd19099 165 EALEEAVAEGKIRYYGISTWdgfraPPALPGHLSLEKLVAAAEEVGGDNHHFKviqlplnllePEALTEKNtvkgealsl 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2748858100 165 ----AEQGIATEAWSPLGQGKGLLEVPAIVAIAQKHGRTPAQIVLRW 207
Cdd:cd19099 245 leaaKELGLGVIASRPLNQGQLLGELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
6-247 |
5.08e-19 |
|
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: 84.55 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 6 FGVwQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAvnasgIA--REELFVTTKL------WNSDQG----H 70
Cdd:cd19087 23 FGG-RTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRW-----IAgrRDDIVLATKVfgpmgdDPNDRGlsrrH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 71 dsALRAFDTSLDKLGLDYVDLYLIHWPTPSkgTYVD-TFKAFEKIYADGRAKAIGTSNFLP------------EHLAKLI 137
Cdd:cd19087 97 --IRRAVEASLRRLQTDYIDLYQMHHFDRD--TPLEeTLRALDDLVRQGKIRYIGVSNFAAwqiakaqgiaarRGLLRFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 138 EETSVIPAVN-QIELH--PhlqqrAAREFhaeqGIATEAWSPLGQG------------------------------KGLL 184
Cdd:cd19087 173 SEQPMYNLLKrQAELEilP-----AARAY----GLGVIPYSPLAGGlltgkygkgkrpesgrlveraryqarygleEYRD 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2748858100 185 EVPAIVAIAQKHGRTPAQIVLRWhlQLGNVVIPKSV----TPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19087 244 IAERFEALAAEAGLTPASLALAW--VLSHPAVTSPIigprTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
9-244 |
5.62e-19 |
|
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: 84.19 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 9 WQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASgiaREELFVTTKLWNSDQGHDSA---------LRA 76
Cdd:cd19080 26 WGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYTMNRRPGDPNaggnhrknlRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIHWP---TPSKgtyvDTFKAFEKIYADGRAKAIGTSNFlP-------EHLAKLIEETSVIpav 146
Cdd:cd19080 103 VEASLRRLQTDYIDLLYVHAWdftTPVE----EVMRALDDLVRAGKVLYVGISDT-PawvvaraNTLAELRGWSPFV--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 147 nQIELHPHLQQRAA-REFHA---EQGIATEAWSPLGQGK-----------------------GLLE------VPAIVAIA 193
Cdd:cd19080 175 -ALQIEYSLLERTPeRELLPmarALGLGVTPWSPLGGGLltgkyqrgeegrageakgvtvgfGKLTernwaiVDVVAAVA 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2748858100 194 QKHGRTPAQIVLRWHLQLGNVVIP--KSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19080 254 EELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
3-228 |
2.62e-18 |
|
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: 82.64 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFGVW-----QVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASGIAREELFVTTKL---WNSDQGHD 71
Cdd:cd19143 15 ALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfwgGGGPPPND 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 72 SAL------RAFDTSLDKLGLDYVDLYLIHWPTPSkgTYV-DTFKAFEKIYADGRAKAIGTSnflpEHLAKLIEETSVI- 143
Cdd:cd19143 95 RGLsrkhivEGTKASLKRLQLDYVDLVFCHRPDPA--TPIeETVRAMNDLIDQGKAFYWGTS----EWSAQQIEEAHEIa 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 144 -------PAVNQIELHPHLQQRAAREF---HAEQGIATEAWSPLGQG-------KGLLE--------------------- 185
Cdd:cd19143 169 drlglipPVMEQPQYNLFHRERVEVEYaplYEKYGLGTTTWSPLASGlltgkynNGIPEgsrlalpgyewlkdrkeelgq 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2748858100 186 -----VPAIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKEN 228
Cdd:cd19143 249 ekiekVRKLKPIAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEEN 298
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
4-244 |
7.54e-18 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 81.13 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVWQVPD-DEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVNAsgiAREELFVTTKL---WNSDQGHDSAL-- 74
Cdd:cd19078 14 MSHGYGPPPDkEEMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKP---FRDQVVIATKFgfkIDGGKPGPLGLds 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 75 ------RAFDTSLDKLGLDYVDLYLIHWPTPSkgtyV---DTFKAFEKIYADGRAKAIGTSnflpEHLAKLIEETSVIPA 145
Cdd:cd19078 91 rpehirKAVEGSLKRLQTDYIDLYYQHRVDPN----VpieEVAGTMKELIKEGKIRHWGLS----EAGVETIRRAHAVCP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 146 VNQIELHPHLQQRAARE----FHAEQGIATEAWSPLGQG--------------------------------KGLLEVpaI 189
Cdd:cd19078 163 VTAVQSEYSMMWREPEKevlpTLEELGIGFVPFSPLGKGfltgkidentkfdegddraslprftpealeanQALVDL--L 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2748858100 190 VAIAQKHGRTPAQIVLRWHL-QLGNVV-IPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19078 241 KEFAEEKGATPAQIALAWLLaKKPWIVpIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-233 |
3.87e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 78.72 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 10 QVPDDEAERAVATALESGYRSIDTAAIYGN-EEGTGKAvnasGIAREELFVTTKL----WNSDQGHDSALRAFDTSLDKL 84
Cdd:cd19097 22 KPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKF----LKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 85 GLDYVDLYLIHWPTPSKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSV----IP--AVNQ-IELHPHLQQ 157
Cdd:cd19097 98 KVDSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIdiiqLPfnILDQrFLKSGLLAK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 158 RAAR--EFHAE----QGI----ATEAWSPLGQGKGLLEvpAIVAIAQKHGRTPAQIVLRWHLQLGNvvIPKSV----TPS 223
Cdd:cd19097 178 LKKKgiEIHARsvflQGLllmePDKLPAKFAPAKPLLK--KLHELAKKLGLSPLELALGFVLSLPE--IDKIVvgvdSLE 253
|
250
....*....|
gi 2748858100 224 RIKENIDVFD 233
Cdd:cd19097 254 QLKEIIAAFK 263
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
14-230 |
4.16e-17 |
|
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: 79.14 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 14 DEAERAVATALESGYRSIDTAAIYGN---EEGTGKAvnasGIAREELFVTTKlWNSDQG----HDSALRAFDTSLDKLGL 86
Cdd:cd19075 20 EAAAELLDAFLERGHTEIDTARVYPDgtsEELLGEL----GLGERGFKIDTK-ANPGVGgglsPENVRKQLETSLKRLKV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 87 DYVDLYLIHwpTPSKGTYV-DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLI----EETSVIPAVNQ-----------IE 150
Cdd:cd19075 95 DKVDVFYLH--APDRSTPLeETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVeickENGWVLPTVYQgmynaitrqveTE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 151 LHPHLqqraaREFhaeqGIATEAWSPLGQG------KGLLEVPA-----------------------------IVAIAQK 195
Cdd:cd19075 173 LFPCL-----RKL----GIRFYAYSPLAGGfltgkyKYSEDKAGggrfdpnnalgklyrdrywkpsyfealekVEEAAEK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2748858100 196 HGRTPAQIVLRW---HLQL----GNVVIPKSVTPSRIKENID 230
Cdd:cd19075 244 EGISLAEAALRWlyhHSALdgekGDGVILGASSLEQLEENLA 285
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
11-244 |
4.96e-17 |
|
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: 79.01 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 11 VPDDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVnaSGIAREELFVTTKLWNSD-QGHDSALR--------AFD 78
Cdd:cd19145 30 KPEEEGIALIHHAFNSGVTFLDTSDIYGpntNEVLLGKAL--KDGPREKVQLATKFGIHEiGGSGVEVRgdpayvraACE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 79 TSLDKLGLDYVDLYLIHwptpSKGTYV---DTFKAFEKIYADGRAKAIGtsnfLPEHLAKLIEETSVIPAVNQIELHPHL 155
Cdd:cd19145 108 ASLKRLDVDYIDLYYQH----RIDTTVpieITMGELKKLVEEGKIKYIG----LSEASADTIRRAHAVHPITAVQLEWSL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 156 QQRAARE----FHAEQGIATEAWSPLGQG-----KGLLEVPA-------------------------IVAIAQKHGRTPA 201
Cdd:cd19145 180 WTRDIEEeiipTCRELGIGIVPYSPLGRGffagkAKLEELLEnsdvrkshprfqgenleknkvlyerVEALAKKKGCTPA 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2748858100 202 QIVLRWHLQLGNVV--IPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19145 260 QLALAWVLHQGEDVvpIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
2-233 |
5.90e-17 |
|
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: 78.84 E-value: 5.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQVPDDEAERAVA-----TALESGYRSIDTAAIYGNEEGT-----GKAVNASGIA-REELFVTTK----LWNS 66
Cdd:cd19089 12 PAISLGLWHNFGDYTSPEEArellrTAFDLGITHFDLANNYGPPPGSaeenfGRILKRDLRPyRDELVISTKagygMWPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 67 DQGHDSA----LRAFDTSLDKLGLDYVDLYLIHWPTPSkgTYVD-TFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE--- 138
Cdd:cd19089 92 PYGDGGSrkylLASLDQSLKRMGLDYVDIFYHHRYDPD--TPLEeTMTALADAVRSGKALYVGISNYPGAKARRAIAllr 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIPAVNQIELhpHLQQRAAR----EFHAEQGIATEAWSPLGQG----KGLLEVP----------------------- 187
Cdd:cd19089 170 ELGVPLIIHQPRY--SLLDRWAEdgllEVLEEAGIGFIAFSPLAQGlltdKYLNGIPpdsrraaeskflteealtpekle 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2748858100 188 ---AIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFD 233
Cdd:cd19089 248 qlrKLNKIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDNVAALK 298
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
23-247 |
1.98e-16 |
|
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: 77.22 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 23 ALESGYRSIDTAAIY---------G-NEEGTGKAVNASGiAREELFVTTK----------LWNSDQGHDSA--LRAFDTS 80
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqGrTEEIIGSWLKKKG-NRDKVVLATKvagpgegitwPRGGGTRLDREniREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 81 LDKLGLDYVDLYLIHWP---TP--SKGTYV------------DTFKAFEKIYADGRAKAIGTSNFLPEHLAKLIE--ETS 141
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPdryTPlfGGGYYTepseeedsvsfeEQLEALGELVKAGKIRHIGLSNETPWGVMKFLElaEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 142 VIPAVNQIELHPHLQQRAAREFHAE----QGIATEAWSPLGQG-------------------------------KGLLEV 186
Cdd:cd19094 186 GLPRIVSIQNPYSLLNRNFEEGLAEachrENVGLLAYSPLAGGvltgkyldgaarpeggrlnlfpgymaryrspQALEAV 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2748858100 187 PAIVAIAQKHGRTPAQIVLRWHLQ---LGNVVIPKSvTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19094 266 AEYVKLARKHGLSPAQLALAWVRSrpfVTSTIIGAT-TLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-230 |
2.38e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 76.60 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 6 FGVwQVPDDEAERAVATALESGYRSIDTAAIYG----------NEEGTGKAVNASGiAREELFVTTKL---------WNS 66
Cdd:cd19752 10 FGT-RTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvggeSERLIGRWLKDRG-NRDDVVIATKVgagprdpdgGPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 67 D---QGHDSALRAFDTSLDKLGLDYVDLYLIH---WPTPSKgtyvDTFKAFEKIYADGRAKAIGTSNFLPEHL--AKLIE 138
Cdd:cd19752 88 SpegLSAETIEQEIDKSLRRLGTDYIDLYYAHvddRDTPLE----ETLEAFNELVKAGKVRAIGASNFAAWRLerARQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIPAVNQIEL-HPHLQQRAAREFHAEQGIATE--------------AWSPLGQG------KGLLE----------VP 187
Cdd:cd19752 164 RQQGWAEFSAIQQrHSYLRPRPGADFGVQRIVTDElldyassrpdltllAYSPLLSGaytrpdRPLPEqydgpdsdarLA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2748858100 188 AIVAIAQKHGRTPAQIVLRWHLQLGNVVIP--KSVTPSRIKENID 230
Cdd:cd19752 244 VLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-239 |
3.50e-16 |
|
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: 76.44 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGV-------WQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVnaSGIAREELFVTTK------LW 64
Cdd:cd19163 13 VSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL--KGIPRDSYYLATKvgryglDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 65 NS--DQGHDSALRAFDTSLDKLGLDYVDLYLIHwpTPSKGTYVD-----TFKAFEKIYADGRAKAIGTSNFLPEHLAKLI 137
Cdd:cd19163 91 DKmfDFSAERITKSVEESLKRLGLDYIDIIQVH--DIEFAPSLDqilneTLPALQKLKEEGKVRFIGITGYPLDVLKEVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 138 EETSVipAVNQIELHPH--LQQRAARE---FHAEQGIATEAWSPLGQgkGLL-------------EVPAI----VAIAQK 195
Cdd:cd19163 169 ERSPV--KIDTVLSYCHytLNDTSLLEllpFFKEKGVGVINASPLSM--GLLtergppdwhpaspEIKEAcakaAAYCKS 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2748858100 196 HGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:cd19163 245 RGVDISKLALQFALSNPDIatTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
2-180 |
1.74e-15 |
|
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: 74.32 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFG------VWQVPDDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVnaSGIAREELFVTTKL-----WNSD 67
Cdd:cd19162 1 PRLGLGaaslgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAAL--ARHPRAEYVVSTKVgrllePGAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 68 QGHDSALRAFD-----------TSLDKLGLDYVDLYLIHWPTPSKGTYV-DTFKAFEKIYADGRAKAIGTSNFLPEHLAK 135
Cdd:cd19162 79 GRPAGADRRFDfsadgirrsieASLERLGLDRLDLVFLHDPDRHLLQALtDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2748858100 136 LIEEtSVIPAVNQIELHPHLQQRAAREFH---AEQGIATEAWSPLGQG 180
Cdd:cd19162 159 AARR-ADVDVVMVAGRYTLLDRRAATELLplcAAKGVAVVAAGVFNSG 205
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
3-244 |
7.99e-15 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 72.66 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFG----VW---QVPDDEAERAVATALESGYRSIDTAAIYGNEEGT------GKAVNASGIAREELFVTTKL-WNS-- 66
Cdd:cd19077 7 PIGLGlmglTWrpnPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHanlkllARFFRKYPEYADKVVLSVKGgLDPdt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 67 ---DQGHDSALRAFDTSLDKLG-LDYVDLYlihwpTPS---KGTYV-DTFKAFEKIYADGRAKAIGTSnflpEHLAKLIE 138
Cdd:cd19077 87 lrpDGSPEAVRKSIENILRALGgTKKIDIF-----EPArvdPNVPIeETIKALKELVKEGKIRGIGLS----EVSAETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETS-VIP-AVNQIELHP---HLQQRAAREFHAEQGIATEAWSPLGQG------KGLLEVP-------------------- 187
Cdd:cd19077 158 RAHaVHPiAAVEVEYSLfsrEIEENGVLETCAELGIPIIAYSPLGRGlltgriKSLADIPegdfrrhldrfngenfeknl 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2748858100 188 ----AIVAIAQKHGRTPAQIVLRWHLQLGN---VVIPKSVTPSRIKENIDVFDFSLDTEDIAAI 244
Cdd:cd19077 238 klvdALQELAEKKGCTPAQLALAWILAQSGpkiIPIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
3-249 |
1.96e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 71.81 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFGVW----QVPDDEAERAVATALESGYRSIDTAAIYG----------NEEGTGKAVNASGiAREELFVTTKLWNSDQ 68
Cdd:PRK10625 15 TLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSGPSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 69 GHDSALR------------AFDTSLDKLGLDYVDLYLIHWP---TPSKG-------------TYVDTFKAFEKIYADGRA 120
Cdd:PRK10625 94 NNDKGIRpnqaldrknireALHDSLKRLQTDYLDLYQVHWPqrpTNCFGklgyswtdsapavSLLETLDALAEQQRAGKI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 121 KAIGTSNFLP------EHLAKLIEETSVIPAVNQIELHPHLQQRAAREFHAEQGIATEAWSPLG----QGKGL------- 183
Cdd:PRK10625 174 RYIGVSNETAfgvmryLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAfgtlTGKYLngakpag 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 184 ------------------LEVPAIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTEDIAA 243
Cdd:PRK10625 254 arntlfsrftrysgeqtqKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLSEEVLAE 333
|
....*.
gi 2748858100 244 ISALNE 249
Cdd:PRK10625 334 IEAVHQ 339
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-253 |
3.15e-14 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 71.17 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQ----VPDDEAERAV-ATALESGYRSIDTAAIYG-----NEEGTGKAVNASGIA-REELFVTTK----LWN 65
Cdd:PRK09912 25 LPALSLGLWHnfghVNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagydMWP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 66 SDQGHDSA----LRAFDTSLDKLGLDYVDLYLIHW---PTPSKgtyvDTFKAFEKIYADGRAKAIGTSNFLPEH---LAK 135
Cdd:PRK09912 105 GPYGSGGSrkylLASLDQSLKRMGLEYVDIFYSHRvdeNTPME----ETASALAHAVQSGKALYVGISSYSPERtqkMVE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 136 LIEETSVIPAVNQIE---LHPHLQQRAAREFHAEQGIATEAWSPLGQG-----------------------KGLLEVPAI 189
Cdd:PRK09912 181 LLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvRGLTPKMLT 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2748858100 190 VA----------IAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVF-DFSLDTEDIAAISALNEDRRL 253
Cdd:PRK09912 261 EAnlnslrllneMAQQRGQSMAQMALSWLLKDERVtsVLIGASRAEQLEENVQALnNLTFSTEELAQIDQHIADGEL 337
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
4-180 |
9.17e-14 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 69.78 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVW-----QVPDDEAERAVATALESGYRSIDTAAIY--GNEEGT-GKAVNASGIAREELFVTTKL-W----NSDQG- 69
Cdd:cd19141 15 LGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYaaGKAEIVlGKILKKKGWRRSSYVITTKIfWggkaETERGl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 70 -HDSALRAFDTSLDKLGLDYVDLYLIHWPTPSKgTYVDTFKAFEKIYADGRAKAIGTSNFLPehlAKLIEETSVI----- 143
Cdd:cd19141 95 sRKHIIEGLKASLERLQLEYVDIVFANRPDPNT-PMEEIVRAFTHVINQGMAMYWGTSRWSA---MEIMEAYSVArqfnl 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2748858100 144 --PAVNQIELhpHLQQRAAREFHAEQ-----GIATEAWSPLGQG 180
Cdd:cd19141 171 ipPIVEQAEY--HLFQREKVEMQLPElfhkiGVGAMTWSPLACG 212
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-247 |
9.06e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 66.59 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 13 DDEAERAVATALESGYRSIDTAAIYGneegTGKAVNASG-----IAREELFVTTKL--WNSDQGHDSALRAFDTSLDKLG 85
Cdd:cd19103 31 EDTLKAVFDKAMAAGLNLWDTAAVYG----MGASEKILGeflkrYPREDYIISTKFtpQIAGQSADPVADMLEGSLARLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 86 LDYVDLYLIHWPTpskgtyvDTFKAFEKI---YADGRAKAIGTSNF-LPE-HLAKLIEETSVIPaVNQIELHPHLQQRAA 160
Cdd:cd19103 107 TDYIDIYWIHNPA-------DVERWTPELiplLKSGKVKHVGVSNHnLAEiKRANEILAKAGVS-LSAVQNHYSLLYRSS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 161 RE-------------FHA----EQGIATEAWS---PLGQGKGLLE------------VPAIVAIAQKHGRTPAQIVLRWH 208
Cdd:cd19103 179 EEagildyckengitFFAymvlEQGALSGKYDtkhPLPEGSGRAEtynpllpqleelTAVMAEIGAKHGASIAQVAIAWA 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 2748858100 209 LQLGNVVIPKSVTPSRIKENIDVFDFSLDTEDIAAISAL 247
Cdd:cd19103 259 IAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
2-239 |
1.05e-12 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 66.48 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFG-------VWQVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVnaSGIAREELFVTTKL-------- 63
Cdd:cd19152 1 PKLGFGtaplgnlYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAAL--RELGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 64 ---------WNSDQGH--------DSALRAFDTSLDKLGLDYVDLYLIHWPTP------SKGTY----VDTFKAFEKIYA 116
Cdd:cd19152 79 eveptfepgFWNPLPFdavfdysyDGILRSIEDSLQRLGLSRIDLLSIHDPDEdlagaeSDEHFaqaiKGAFRALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 117 DGRAKAIGTSNFLPEHLAKLIEET--SVIPAVNQIELhphLQQRAAREFH---AEQGIATEAWSPLGQgkGLL------- 184
Cdd:cd19152 159 EGVIKAIGLGVNDWEVILRILEEAdlDWVMLAGRYTL---LDHSAARELLpecEKRGVKVVNAGPFNS--GFLaggdnfd 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 185 -----EVP--------AIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENIDVFDFSLDTE 239
Cdd:cd19152 234 yyeygPAPpeliarrdRIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
7-144 |
2.70e-12 |
|
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: 65.25 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 7 GVWQVP--DDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASGIAREELFVTTKLWN-SDQGHD---SALRA- 76
Cdd:cd19153 24 GVYGDGleQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVGRyRDSEFDysaERVRAs 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 77 FDTSLDKLGLDYVDLYLIH-WPTPSKGTYVD-TFKAFEKIYADGRAKAIGTSNFLPEHLAKLIEETSVIP 144
Cdd:cd19153 104 VATSLERLHTTYLDVVYLHdIEFVDYDTLVDeALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS 173
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
1-237 |
7.67e-12 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 63.96 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQ----VPDDEAERA-VATALESGYRSIDTAAIYG-----NEEGTGKaVNASGIA--REELFVTTK----LW 64
Cdd:cd19151 12 LPAISLGLWHnfgdVDRYENSRAmLRRAFDLGITHFDLANNYGpppgsAEENFGR-ILKEDLKpyRDELIISTKagytMW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 65 NS---DQGHDSALRA-FDTSLDKLGLDYVDLYLIHWP---TPSKgtyvDTFKAFEKIYADGRAKAIGTSNFLPEHL---A 134
Cdd:cd19151 91 PGpygDWGSKKYLIAsLDQSLKRMGLDYVDIFYHHRPdpeTPLE----ETMGALDQIVRQGKALYVGISNYPPEEAreaA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 135 KLIEETSVIPAVNQielhPH--LQQRAARE----FHAEQGIATEAWSPLGQG-------KGLLE---------------- 185
Cdd:cd19151 167 AILKDLGTPCLIHQ----PKysMFNRWVEEglldVLEEEGIGCIAFSPLAQGlltdrylNGIPEdsraakgssflkpeqi 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2748858100 186 -------VPAIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKENI---DVFDFSLD 237
Cdd:cd19151 243 teeklakVRRLNEIAQARGQKLAQMALAWVLRNKRVtsVLIGASKPSQIEDAVgalDNREFSEE 306
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-124 |
2.56e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 62.67 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QLGFG------VW-QVPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNAsgiAREELFVTTK----LWNSDQ 68
Cdd:cd19104 14 ELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKG---LPAGPYITTKvrldPDDLGD 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 69 GHDSALRAFDTSLDKLGLDYVDLYLIH--------WPTPSKGT------YVDTFKAFEKIYADGRAKAIG 124
Cdd:cd19104 91 IGGQIERSVEKSLKRLKRDSVDLLQLHnrigderdKPVGGTLSttdvlgLGGVADAFERLRSEGKIRFIG 160
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
4-180 |
3.06e-11 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 62.31 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVW-----QVPDDEAERAVATALESGYRSIDTAAIY--GNEEGT-GKAVNASGIAREELFVTTKLWNSDQGHDS--- 72
Cdd:cd19160 18 LGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYaaGKAERTlGNILKSKGWRRSSYVVTTKIYWGGQAETErgl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 73 ----ALRAFDTSLDKLGLDYVDLYLIHWPTPSkGTYVDTFKAFEKIYADGRAKAIGTSNFlpeHLAKLIEETSV------ 142
Cdd:cd19160 98 srkhIIEGLRGSLDRLQLEYVDIVFANRSDPN-SPMEEIVRAMTYVINQGMAMYWGTSRW---SAMEIMEAYSVarqfnl 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2748858100 143 IPAVNQIELHpHLQQRAARE------FHaEQGIATEAWSPLGQG 180
Cdd:cd19160 174 IPPVCEQAEY-HLFQREKVEmqlpelYH-KIGVGSVTWSPLACG 215
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
1-237 |
4.33e-11 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 62.09 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 1 MPQLGFGVWQVPDD----EAERAVA-TALESGYRSIDTAAIYG-----NEEGTGKAVNASGIA-REELFVTTK----LWN 65
Cdd:cd19150 12 LPALSLGLWHNFGDdtplETQRAILrTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAGyRDELIISTKagydMWP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 66 SDQGHDSA----LRAFDTSLDKLGLDYVDLYLIHWPTPsKGTYVDTFKAFEKIYADGRAKAIGTSNFLPE---HLAKLIE 138
Cdd:cd19150 92 GPYGEWGSrkylLASLDQSLKRMGLDYVDIFYSHRFDP-DTPLEETMGALDHAVRSGKALYVGISSYSPErtrEAAAILR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 139 ETSVIPAVNQIE---LHPHLQQRAAREFHAEQGIATEAWSPLGQG-------------------KGLLE----------V 186
Cdd:cd19150 171 ELGTPLLIHQPSynmLNRWVEESGLLDTLQELGVGCIAFTPLAQGlltdkylngipegsraskeRSLSPkmlteanlnsI 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2748858100 187 PAIVAIAQKHGRTPAQIVLRWHLQLGNV--VIPKSVTPSRIKEN---IDVFDFSLD 237
Cdd:cd19150 251 RALNEIAQKRGQSLAQMALAWVLRDGRVtsALIGASRPEQLEENvgaLDNLTFSAD 306
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
4-180 |
6.32e-11 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 61.60 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVW-----QVPDDEAERAVATALESGYRSIDTAAIYGNEEGT---GKAVNASGIAREELFVTTKLW-----NSDQG- 69
Cdd:cd19159 16 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEvilGSIIKKKGWRRSSLVITTKLYwggkaETERGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 70 -HDSALRAFDTSLDKLGLDYVDLYLIHWP---TPSKgtyvDTFKAFEKIYADGRAKAIGTSNFlpeHLAKLIEETSVIPA 145
Cdd:cd19159 96 sRKHIIEGLKGSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRW---SAMEIMEAYSVARQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2748858100 146 VNQI-----ELHPHLQQRAA-----REFHAEQGIATEAWSPLGQG 180
Cdd:cd19159 169 FNMIppvceQAEYHLFQREKvevqlPELYHKIGVGAMTWSPLACG 213
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
11-126 |
1.81e-10 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 60.18 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 11 VPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASGIAREELFVTTKLWNSDQGHD-SA---LRAFDTSLDK 83
Cdd:PLN02587 28 VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCGRYGEGFDfSAervTKSVDESLAR 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2748858100 84 LGLDYVDLYLIHwptPSKGTYVD-----TFKAFEKIYADGRAKAIGTS 126
Cdd:PLN02587 108 LQLDYVDILHCH---DIEFGSLDqivneTIPALQKLKESGKVRFIGIT 152
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
4-180 |
2.49e-10 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 59.71 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 4 LGFGVW-----QVPDDEAERAVATALESGYRSIDTAAIYG---NEEGTGKAVNASGIAREELFVTTKL-WNSDQGHDSAL 74
Cdd:cd19158 16 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAagkAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 75 ------RAFDTSLDKLGLDYVDLYLIHWPTPSKgTYVDTFKAFEKIYADGRAKAIGTSNFlpeHLAKLIEETSVIPAVNQ 148
Cdd:cd19158 96 srkhiiEGLKASLERLQLEYVDVVFANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRW---SSMEIMEAYSVARQFNL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2748858100 149 I-----ELHPHLQQRAARE------FHaEQGIATEAWSPLGQG 180
Cdd:cd19158 172 IppiceQAEYHMFQREKVEvqlpelFH-KIGVGAMTWSPLACG 213
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
2-214 |
1.19e-09 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 57.86 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 2 PQLGFGVWQ-----VPDDEAERAVATALESGYRSIDTAAIYGN---EEGTGKAVNASGIAREELFVTTKLWNSDQGHDSA 73
Cdd:cd19142 14 SNVGLGTWStfstaISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIYWSYGSEERG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 74 L------RAFDTSLDKLGLDYVDLYLIHWPTPsKGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHLAKLI----EETSVI 143
Cdd:cd19142 94 LsrkhiiESVRASLRRLQLDYIDIVIIHKADP-MCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFsiarQFNCPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 144 PAVNQIELHPHLQQRAA---REFHAEQGIATEAWSPLGQG-------------------KGLLEVPA------------- 188
Cdd:cd19142 173 PICEQSEYHMFCREKMElymPELYNKVGVGLITWSPLSLGldpgiseetrrlvtklsfkSSKYKVGSdgngiheetrras 252
|
250 260 270
....*....|....*....|....*....|.
gi 2748858100 189 -----IVAIAQKHGRTPAQIVLRWHLQLGNV 214
Cdd:cd19142 253 hklreLSLIAERLGCDLTQLLIAWSLKNENV 283
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
3-248 |
2.17e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 56.90 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 3 QL-GFGVWQVPDD-EAERAVA-TALESGYRSIDTAAIYG----NEegtgkavnasgIAREELF-------VTTKL----- 63
Cdd:PRK10376 26 QLaGPGVFGPPKDrDAAIAVLrEAVALGVNHIDTSDFYGphvtNQ-----------LIREALHpypddltIVTKVgarrg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 64 ----WNSDQGHDSALRAFDTSLDKLGLDYVDL------YLIHWPTPskGTYVDTFKAFEKIYADGRAKAIGTSNFLPEHl 133
Cdd:PRK10376 95 edgsWLPAFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAE--GSIEEPLTVLAELQRQGLVRHIGLSNVTPTQ- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 134 aklIEETSVIPAVNQIELHPHLQQRAAREF---HAEQGIATEAWSPLGqGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQ 210
Cdd:PRK10376 172 ---VAEARKIAEIVCVQNHYNLAHRADDALidaLARDGIAYVPFFPLG-GFTPLQSSTLSDVAASLGATPMQVALAWLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2748858100 211 LG-NV-VIPKSVTPSRIKENIDVFDFSLDTEDIAAISALN 248
Cdd:PRK10376 248 RSpNIlLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
11-124 |
4.02e-07 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 50.02 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 11 VPDDEAERAVATALESGYRSIDTAAIYGNeegtGKAVNASGIA-----REELFVTTKL-----------------W---- 64
Cdd:cd19161 17 VSNADADATLDAAWDSGIRYFDTAPMYGH----GLAEHRLGDFlrekpRDEFVLSTKVgrllkparegsvpdpngFvdpl 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2748858100 65 ----NSDQGHDSALRAFDTSLDKLGLDYVDLYLIH---------------WPTPSKGtyvdTFKAFEKIYADGRAKAIG 124
Cdd:cd19161 93 pfeiVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHdigvythgdrkerhhFAQLMSG----GFKALEELKKAGVIKAFG 167
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-250 |
2.64e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 47.72 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 23 ALESGYRSIDTAAIYGN-EEGTGKAVNASGIAREELFVTTKL-------WNSD--------QGHDSALRAFDTSLDKLGl 86
Cdd:cd19098 44 AWAAGVRYFDAARSYGRaEEFLGSWLRSRNIAPDAVFVGSKWgytytadWQVDaavhevkdHSLARLLKQWEETRSLLG- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 87 DYVDLYLIHWPTPSKGTYVDT--FKAFEKIYADGRAKAIGTSNflpehlaklIEETSVIPAVNQIELHPH---------- 154
Cdd:cd19098 123 KHLDLYQIHSATLESGVLEDAdvLAALAELKAEGVKIGLSLSG---------PQQAETLRRALEIEIDGArlfdsvqatw 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 155 --LQQRAAREFHA--EQG---IATEAwspLGQG---------KGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLG--NVVI 216
Cdd:cd19098 194 nlLEQSAGEALEEahEAGmgvIVKEA---LANGrltdrnpspELAPLMAVLKAVADRLGVTPDALALAAVLAQPfvDVVL 270
|
250 260 270
....*....|....*....|....*....|....
gi 2748858100 217 PKSVTPSRIKENIDVFDFSLDTEDIAAISALNED 250
Cdd:cd19098 271 SGAATPEQLRSNLRALDVSLDLELLAALADLAEP 304
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
17-239 |
1.44e-04 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 42.26 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 17 ERAVATALESGYRSIDTAAIYGN-EEGTGKAVNA--SGIAREELFVTTKL---------WNSDQGHDSALRafdtSLDKL 84
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGPsEIILGRALKAlrDEFPRDTYFIITKVgrygpddfdYSPEWIRASVER----SLRRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 85 GLDYVDLYLIHwptpskgtyvDT-FKAFEKIYA----------DGRAKAIGTSNF-LP--EHLAKLIEETSVIP--AV-- 146
Cdd:cd19164 113 HTDYLDLVYLH----------DVeFVADEEVLEalkelfklkdEGKIRNVGISGYpLPvlLRLAELARTTAGRPldAVls 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2748858100 147 -NQIELH--------PHLQQRAAREFhaeqgIATEawSPLGQG--------------KGLLEVPA-IVAIAQKHGRTPAQ 202
Cdd:cd19164 183 yCHYTLQnttllayiPKFLAAAGVKV-----VLNA--SPLSMGllrsqgppewhpasPELRAAAAkAAEYCQAKGTDLAD 255
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2748858100 203 IVLRWHLQ----LGNVVIPKSvTPSRIKENIDVFDFSLDTE 239
Cdd:cd19164 256 VALRYALRewggEGPTVVGCS-NVDELEEAVEAYWSVLAGA 295
|
|
| |
