|
Name |
Accession |
Description |
Interval |
E-value |
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-270 |
4.08e-177 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 488.03 E-value: 4.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGVYKAkEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEETLE 89
Cdd:COG0656 1 NGVEIPALGLGTWQL-PGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 90 AFEKSLKKLQMDYVDLYLIHWPIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPMLTQ 169
Cdd:COG0656 80 AFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 170 FELRNFCQGEQIQMEAWSPLMRGGeVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLT 249
Cdd:COG0656 160 RELLAFCREHGIVVEAYSPLGRGK-LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELS 238
|
250 260
....*....|....*....|.
gi 446470145 250 EEEMTQINTLNRNLHVGTNPD 270
Cdd:COG0656 239 DEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
5-270 |
9.81e-169 |
|
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: 467.25 E-value: 9.81e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 5 TTTLHNGVKMPMIGLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGY 84
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 85 EETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELH 164
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 165 PMLTQFELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIF 244
Cdd:cd19157 161 PRLTQKELRDYCKKQGIQLEAWSPLMQ-GQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVF 239
|
250 260
....*....|....*....|....*.
gi 446470145 245 DFSLTEEEMTQINTLNRNLHVGTNPD 270
Cdd:cd19157 240 DFELSQEDMDKIDALNENLRVGPDPD 265
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
7-260 |
1.71e-151 |
|
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: 423.00 E-value: 1.71e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEE 86
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 87 TLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPM 166
Cdd:cd19126 82 TEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 167 LTQFELRNFCQGEQIQMEAWSPLMRGGeVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDF 246
Cdd:cd19126 162 LTQKELRGYCKSKGIVVEAWSPLGQGG-LLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDF 240
|
250
....*....|....
gi 446470145 247 SLTEEEMTQINTLN 260
Cdd:cd19126 241 ELSEDDMTAIDALN 254
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
7-272 |
2.11e-150 |
|
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: 420.77 E-value: 2.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEE 86
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 87 TLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPM 166
Cdd:cd19156 82 TLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 167 LTQFELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDF 246
Cdd:cd19156 162 LTQEPLRKFCKEKNIAVEAWSPLGQ-GKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDF 240
|
250 260
....*....|....*....|....*.
gi 446470145 247 SLTEEEMTQINTLNRNLHVGTNPDKY 272
Cdd:cd19156 241 ELTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-257 |
3.08e-150 |
|
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: 419.58 E-value: 3.08e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 14 MPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEETLEAFEK 93
Cdd:cd19071 1 MPLIGLGTYKLK-PEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 94 SLKKLQMDYVDLYLIHWPIRGK-------YVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPM 166
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVPGKeggskeaRLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 167 LTQFELRNFCQGEQIQMEAWSPLMRGGE-VFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFD 245
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGRGRRpLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|..
gi 446470145 246 FSLTEEEMTQIN 257
Cdd:cd19071 240 FELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-260 |
7.90e-144 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 403.68 E-value: 7.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 5 TTTLHNGVKMPMIGLGVYKAkEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGY 84
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQV-SNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 85 EETLEAFEKSLKKLQMDYVDLYLIHWPI--RGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVE 162
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPVpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 163 LHPMLTQFELRNFCQGEQIQMEAWSPLMRGGeVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFS 242
Cdd:cd19131 160 LHPRFQQRELRAFHAKHGIQTESWSPLGQGG-LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFD 238
|
250
....*....|....*...
gi 446470145 243 IFDFSLTEEEMTQINTLN 260
Cdd:cd19131 239 VFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
6-260 |
1.89e-140 |
|
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: 395.02 E-value: 1.89e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 6 TTLHNGVKMPMIGLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYE 85
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 86 ETLEAFEKSLKKLQMDYVDLYLIHWPIrGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHP 165
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPF-GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 166 MLTQFELRNFCQGEQIQMEAWSPLMRG-GEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIF 244
Cdd:cd19133 160 FNQQIEAVEFLKKYGVQIEAWGPFAEGrNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIF 239
|
250
....*....|....*.
gi 446470145 245 DFSLTEEEMTQINTLN 260
Cdd:cd19133 240 DFELSDEDMEAIAALD 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
4-272 |
1.60e-128 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 365.93 E-value: 1.60e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHNGVKMPMIGLGVYKAKEgDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQG 83
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 YEEtlEAFEKSLKKLQMDYVDLYLIHWPI--RGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQV 161
Cdd:PRK11565 84 RPR--EALEESLKKLQLDYVDLYLMHWPVpaIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 162 ELHPMLTQFELRNFCQGEQIQMEAWSPLMRGGE-VFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQEN 240
Cdd:PRK11565 162 ELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKgVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAEN 241
|
250 260 270
....*....|....*....|....*....|..
gi 446470145 241 FSIFDFSLTEEEMTQINTLNRNLHVGTNPDKY 272
Cdd:PRK11565 242 FDVFDFRLDKDELGEIAKLDQGKRLGPDPDQF 273
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-260 |
1.19e-123 |
|
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: 353.25 E-value: 1.19e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 6 TTLHNGVKMPMIGLGVYKAKEgDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYE 85
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPP-EETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 86 ETLEAFEKSLKKLQMDYVDLYLIHWPIRGKY---VDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVE 162
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPVPNDFdrtIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 163 LHPMLTQFELRNFCQGEQIQMEAWSPL---MR--------GGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKS 231
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIggvMRygasgptgPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKS 239
|
250 260
....*....|....*....|....*....
gi 446470145 232 VTPSRIQENFSIFDFSLTEEEMTQINTLN 260
Cdd:cd19127 240 VHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-261 |
2.77e-123 |
|
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: 351.57 E-value: 2.77e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 8 LHNGVKMPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEET 87
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLK-GDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 88 LEAFEKSLKKLQMDYVDLYLIHWPI--RGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHP 165
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHWPNpsRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 166 MLTQFELRNFCQGEQIQMEAWSPLMRGGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFD 245
Cdd:cd19132 160 YFPQAEQRAYHREHGIVTQSWSPLGRGSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFD 239
|
250
....*....|....*.
gi 446470145 246 FSLTEEEMTQINTLNR 261
Cdd:cd19132 240 FELSDEDMAAIAALDR 255
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-259 |
5.36e-122 |
|
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: 348.85 E-value: 5.36e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 14 MPMIGLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRES----GIPREDIFITTKVWNDDQGYEETLE 89
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 90 AFEKSLKKLQMDYVDLYLIHWPIRGKY-----------VDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMV 158
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLkpsdprnaelrRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 159 NQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGGEVF-QHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRI 237
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLlEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 446470145 238 QENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
3-259 |
1.67e-117 |
|
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: 337.37 E-value: 1.67e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 3 IPTTTLHNGVKMPMIGLGVykAKEGDEVKQAVKTAL-EVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDD 81
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGT--SHSGGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 82 QGYEETLEAFEKSLKKLQMDYVDLYLIHWP--------IRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCK 153
Cdd:cd19135 80 YGYESTKQAFEASLKRLGVDYLDLYLLHWPdcpssgknVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 154 IKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVT 233
Cdd:cd19135 160 VVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAK-GKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTK 238
|
250 260
....*....|....*....|....*.
gi 446470145 234 PSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19135 239 EERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-265 |
4.29e-117 |
|
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: 337.33 E-value: 4.29e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHNGVKMPMIGLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRE----SGIPREDIFITTKVWN 79
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREkiaeGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 DDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGK-----------------YVDTYRALEKLYEEGKVRAIGVSNFHK 142
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKenndsesngdgslsdidYLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 143 HHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL----MRGGE----VFQHPIIQAIATKYEKTPAQ 214
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvPRGQTnpppRLDDPTLVAIAKKYGKTTAQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446470145 215 VILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNLHV 265
Cdd:cd19116 241 IVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-262 |
1.97e-115 |
|
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: 333.58 E-value: 1.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 8 LHNGVKMPMIGLGVYKAKEGdEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRES-----GIPREDIFITTKVWNDDQ 82
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPG-QVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 83 GYEETLEAFEKSLKKLQMDYVDLYLIHWPI---RG-----------------KYVDTYRALEKLYEEGKVRAIGVSNFHK 142
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYafeRGdnpfpknpdgtirydstHYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 143 HHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL-------MRGGE--VFQHPIIQAIATKYEKTPA 213
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwAKPDEpvLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446470145 214 QVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRN 262
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRN 288
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-257 |
1.46e-111 |
|
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: 321.53 E-value: 1.46e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 14 MPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEETLEAFEK 93
Cdd:cd19073 1 IPALGLGTWQLR-GDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 94 SLKKLQMDYVDLYLIHWPIRGKYV-DTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPMLTQFEL 172
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWPNPTVPLeETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 173 RNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEE 252
Cdd:cd19073 160 LEYCRENDIVITAYSPLAR-GEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSED 238
|
....*
gi 446470145 253 MTQIN 257
Cdd:cd19073 239 VAKID 243
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
7-265 |
2.02e-109 |
|
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: 318.59 E-value: 2.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRE---SGI-PREDIFITTKVWNDDQ 82
Cdd:cd19154 5 TLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 83 GYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGK--------------------YVDTYRALEKLYEEGKVRAIGVSNFHK 142
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPAAFKddegesgtmengmsihdavdVEDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 143 HHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGGEV--------------FQHPIIQAIATKY 208
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRAnftkstgvspapnlLQDPIVKAIAEKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446470145 209 EKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNLHV 265
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-260 |
1.49e-106 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 309.86 E-value: 1.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHNGVKMPMIGLGVYKAKEgDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQG 83
Cdd:cd19134 1 PTVTLNDDNTMPVIGLGVGELSD-DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 YEETLEAFEKSLKKLQMDYVDLYLIHWPI--RGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQV 161
Cdd:cd19134 80 FTASQAACRASLERLGLDYVDLYLIHWPAgrEGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 162 ELHPMLTQFELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENF 241
Cdd:cd19134 160 ELHPLLNQAELRKVNAQHGIVTQAYSPLGV-GRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNL 238
|
250
....*....|....*....
gi 446470145 242 SIFDFSLTEEEMTQINTLN 260
Cdd:cd19134 239 DVFDFELTADHMDALDGLD 257
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
7-259 |
7.27e-106 |
|
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: 308.89 E-value: 7.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYKAKEGDeVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESG----IPREDIFITTKVWNDDQ 82
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADPGV-VGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 83 GYEETLEAFEKSLKKLQMDYVDLYLIHWPIR----------GKYV-----DTYRALEKLYEEGKVRAIGVSNFHKHHLEL 147
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpepEEVLppdipSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 148 LLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGG------EVFQHPIIQAIATKYEKTPAQVILRWDI 221
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGttwvkkNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 446470145 222 QSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
5-263 |
2.93e-102 |
|
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: 300.10 E-value: 2.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 5 TTTLHNGVKMPMIGLGVYKAKEGdEVKQAVKTALEVGYRSIDTATVYENESGVGEAV----RESGIPREDIFITTKVWND 80
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKPG-EVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 81 DQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGK-------------------YVDTYRALEKLYEEGKVRAIGVSNFH 141
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKkgvgfpesgedllslspipLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 142 KHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGGE-----------VFQHPIIQAIATKYEK 210
Cdd:cd19123 162 VKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRpaamkaegepvLLEDPVINKIAEKHGA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446470145 211 TPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNL 263
Cdd:cd19123 242 SPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHH 294
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-259 |
2.42e-101 |
|
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: 296.09 E-value: 2.42e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLGVYKAkEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEETL 88
Cdd:cd19140 3 VNGVRIPALGLGTYPL-TGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 89 EAFEKSLKKLQMDYVDLYLIHWPIR-GKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPML 167
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWPNKdVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 168 TQFELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDI-QSGIVTIPKSVTPSRIQENFSIFDF 246
Cdd:cd19140 162 DQRKLLDAAREHGIALTAYSPLAR-GEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIFDF 240
|
250
....*....|...
gi 446470145 247 SLTEEEMTQINTL 259
Cdd:cd19140 241 TLSDEEMARIAAL 253
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-260 |
5.96e-101 |
|
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: 295.28 E-value: 5.96e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYKAKEGDeVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEE 86
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPAD-TQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 87 TLEAFEKSLKKLQMDYVDLYLIHWPI--RGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELH 164
Cdd:cd19130 82 PAAAFAESLAKLGLDQVDLYLVHWPTpaAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 165 PMLTQFELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIF 244
Cdd:cd19130 162 PAYQQRTIRDWAQAHDVKIEAWSPLGQ-GKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVF 240
|
250
....*....|....*.
gi 446470145 245 DFSLTEEEMTQINTLN 260
Cdd:cd19130 241 DFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-261 |
4.88e-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: 4.88e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 5 TTTLHNGVKMPMIGLGVYKAKEGdEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGY 84
Cdd:cd19117 5 TFKLNTGAEIPAVGLGTWQSKPN-EVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 85 EEtlEAFEKSLKKLQMDYVDLYLIHWPIRGK----------------------YVDTYRALEKLYEEGKVRAIGVSNFHK 142
Cdd:cd19117 84 VE--EALDQSLKKLGLDYVDLYLMHWPVPLDpdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 143 HHLELLL--PNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL-MRGGEVFQHPIIQAIATKYEKTPAQVILRW 219
Cdd:cd19117 162 KNLEKLLasPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgSTNAPLLKEPVIIKIAKKHGKTPAQVIISW 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446470145 220 DIQSGIVTIPKSVTPSRIQENFSIfdFSLTEEEMTQINTLNR 261
Cdd:cd19117 242 GLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-262 |
1.08e-93 |
|
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: 278.53 E-value: 1.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYKAKEGdEVKQAVKTALEVGYRSIDTATVYENESGVGEAV----RESGIPREDIFITTKVWNDDqgYEE 86
Cdd:cd19107 1 GAKMPILGLGTWKSPPG-QVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTF--HEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 87 TL--EAFEKSLKKLQMDYVDLYLIHWPI--------------------RGKYVDTYRALEKLYEEGKVRAIGVSNFHKHH 144
Cdd:cd19107 78 GLvkGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 145 LELLL--PNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL-------MRGGE--VFQHPIIQAIATKYEKTPA 213
Cdd:cd19107 158 IERILnkPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwAKPEDpsLLEDPKIKEIAAKHNKTTA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446470145 214 QVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRN 262
Cdd:cd19107 238 QVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRN 286
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-264 |
1.36e-89 |
|
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: 266.79 E-value: 1.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGV----YKAKEGD---EVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQg 83
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 yeETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVDT-----YRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMV 158
Cdd:cd19120 80 --DPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPtlaeaWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 159 NQVELHPMLT--QFELRNFCQGEQIQMEAWSPLM-----RGGEVfqHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKS 231
Cdd:cd19120 158 NQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSpltrdAGGPL--DPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTS 235
|
250 260 270
....*....|....*....|....*....|...
gi 446470145 232 VTPSRIQENFSIFDFSLTEEEMTQINTLNRNLH 264
Cdd:cd19120 236 SKEERMKEYLEAFDFELTEEEVEEIDKAGKQKH 268
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-259 |
1.21e-88 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 265.04 E-value: 1.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 8 LHNGVKMPMIGLGVYKAKEGdEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRES-----GIPREDIFITTKVWNDDQ 82
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPG-EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 83 GYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKY-------------------------VDTYRALEKLYEEGKVRAIGV 137
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPtgdlnpltavptnggevdldlsvslVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 138 SNFHKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL----MRGGEVFQHPIIQAIATKYEKTPA 213
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnlAGLPLLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446470145 214 QVILRWDIQSGIVTIPKSVTPSRIQENFSifDFSLTEEEMTQINTL 259
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
7-259 |
1.78e-88 |
|
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: 264.39 E-value: 1.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYKAKEGdEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRES---GIPREDIFITTKVWNDdqg 83
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAG-EVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWST--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 YEETLE-AFEKSLKKLQMDYVDLYLIHWPIR---------------GK--------YVDTYRALEKLYEEGKVRAIGVSN 139
Cdd:cd19121 81 YHRRVElCLDRSLKSLGLDYVDLYLVHWPVLlnpngnhdlfptlpdGSrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 140 FHKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL-MRGGEVFQHPIIQAIATKYEKTPAQVILR 218
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgSTGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446470145 219 WDIQSGIVTIPKSVTPSRIQENFSIFDFslTEEEMTQINTL 259
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
10-259 |
3.75e-88 |
|
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: 263.74 E-value: 3.75e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGVY-KAKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRE---SG--IPREDIFITTKVWNDDQG 83
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGlvKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 YEETLEAFEKSLKKLQMDYVDLYLIHWPIR---GKYV--------------DTYRALEKLYEEGKVRAIGVSNFHKHHLE 146
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSlkpGKFSfpieeedflpfdikGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 147 LLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGG------EVFQHPIIQAIATKYEKTPAQVILRWD 220
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGtkwgsnAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 446470145 221 IQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-269 |
9.25e-88 |
|
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: 263.58 E-value: 9.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHNGVKMPMIGLGVYKAkEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESG----IPREDIFITTKVWN 79
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 DDQGYeeTLEAFEKSLKKLQMDYVDLYLIHWPIRGKY------------------------VDTYRALEKLYEEGKVRAI 135
Cdd:cd19112 80 SDHGH--VIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvgttgsalgedgvldidvtislETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 136 GVSNFHKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLmrGG-----EVF------QHPIIQAI 204
Cdd:cd19112 158 GISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPL--GGaaanaEWFgsvsplDDPVLKDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446470145 205 ATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNLHVGTNP 269
Cdd:cd19112 236 AKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-262 |
2.76e-87 |
|
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: 262.46 E-value: 2.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYKAkEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRE---SG-IPREDIFITTKVWNDDQ 82
Cdd:cd19155 5 TFNNGEKMPVVGLGTWQS-SPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 83 GYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKY----------------------VDTYRALEKLYEEGKVRAIGVSNF 140
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSkeddsgkldptgehkqdyttdlLDIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 141 HKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGG----------------EVFQHPIIQAI 204
Cdd:cd19155 164 NREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGaahfspgtgspsgsspDLLQDPVVKAI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446470145 205 ATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRN 262
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKN 301
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-262 |
3.05e-87 |
|
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: 261.66 E-value: 3.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVR---ESG-IPREDIFITTKVWNDDQGYEE 86
Cdd:cd19111 1 GFPMPVIGLGTYQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 87 TLEAFEKSLKKLQMDYVDLYLIHWPIRGKY--------------VDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNC 152
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVNkkdkgerelassdvTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 153 KIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGGEV-----------FQHPIIQAIATKYEKTPAQVILRWDI 221
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqslwpdqpdlLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446470145 222 QSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRN 262
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRN 280
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
11-263 |
9.49e-86 |
|
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: 258.58 E-value: 9.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYKAKEG---DEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRES----GIPREDIFITTKVWNDDQG 83
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTtpkGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 YEETLEAFEKSLKKLQMDYVDLYLIHWPI-------------RGKYV-------DTYRALEKLYEEGKVRAIGVSNFHKH 143
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMafkpgdeiyprdeNGKWLyhktnlcATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 144 HLELLL--PNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL----------MRGGEVFQHPIIQAIATKYEKT 211
Cdd:cd19109 161 QLELILnkPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLgtcrdpiwvnVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446470145 212 PAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNL 263
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNV 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
13-269 |
1.15e-85 |
|
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: 257.97 E-value: 1.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 13 KMPMIGLGVYKAKEGdEVKQAVKTALEVGYRSIDTATVYENESGVG----EAVRESGIPREDIFITTKVWNDDQGYEETL 88
Cdd:cd19110 3 DIPAVGLGTWKASPG-EVTEAVKVAIDAGYRHFDCAYLYHNESEVGagirEKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 89 EAFEKSLKKLQMDYVDLYLIHWPIRGK--------------------YVDTYRALEKLYEEGKVRAIGVSNFHKHHLELL 148
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 149 L--PNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGGE---VFQHPIIQAIATKYEKTPAQVILRWDIQS 223
Cdd:cd19110 162 LnkPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEgvdLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446470145 224 GIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNLHVGTNP 269
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-264 |
4.46e-85 |
|
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: 256.39 E-value: 4.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 8 LHNGVKMPMIGLGVYKAKE--GDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVR---ESG-IPREDIFITTKVWNDD 81
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRskiADGtVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 82 QGYEETLEAFEKSLKKLQMDYVDLYLIHWPI-------------RGKYV-------DTYRALEKLYEEGKVRAIGVSNFH 141
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPValkpgeelfpkdeNGKLIfdtvdlcATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 142 KHHLELLL--PNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL--MRGGE--------VFQHPIIQAIATKYE 209
Cdd:cd19108 165 RRQLEMILnkPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALgsQRDKEwvdqnspvLLEDPVLCALAKKHK 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446470145 210 KTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNLH 264
Cdd:cd19108 245 RTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-263 |
1.22e-79 |
|
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: 243.12 E-value: 1.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHNGVKMPMIGLGVYK---AKEGDEVKQAVKtaleVGYRSIDTATVYENESGVGE----AVRESGIPREDIFITTK 76
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKldnATAADQIYQAIK----AGYRLFDGAEDYGNEKEVGEgvnrAIDEGLVKREELFLTSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 VWNDDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYV--------------------------DTYRALEKLYEEG 130
Cdd:cd19113 77 LWNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVpieekyppgfycgdgdnfvyedvpilDTWKALEKLVDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 131 KVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL-------MRGGEV------FQ 197
Cdd:cd19113 157 KIKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFgpqsfveLNQGRAlntptlFE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470145 198 HPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNL 263
Cdd:cd19113 237 HDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGL 302
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-259 |
7.29e-79 |
|
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: 238.79 E-value: 7.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 14 MPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEETLEAFEK 93
Cdd:cd19139 1 IPAFGLGTFRLK-DDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 94 SLKKLQMDYVDLYLIHWPIRGKYV---DTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMV-NQVELHPMLTQ 169
Cdd:cd19139 80 SLEKLRTDYVDLTLIHWPSPNDEVpveEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAtNQIELSPYLQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 170 FELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLT 249
Cdd:cd19139 160 RKLVAHCKQHGIHVTSYMTLAY-GKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLD 238
|
250
....*....|
gi 446470145 250 EEEMTQINTL 259
Cdd:cd19139 239 ADDMAAIAAL 248
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
4-272 |
2.17e-77 |
|
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: 237.32 E-value: 2.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHNGVKMPMIGLGVYKAKE---GDEVKQAVKTalevGYRSIDTATVYENE----SGVGEAVRESGIPREDIFITTK 76
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLWKVNNdtcADQVYNAIKA----GYRLFDGACDYGNEveagQGVARAIKEGIVKREDLFIVSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 VWNDDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVD-------------------------TYRALEKLYEEGK 131
Cdd:cd19115 79 LWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDpavryppgwfydgkkvefsnapiqeTWTAMEKLVDKGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 132 VRAIGVSNFHKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWS---PL------MRGGE----VFQH 198
Cdd:cd19115 159 ARSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgPQsfleldLPGAKdtppLFEH 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446470145 199 PIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNLHVgTNPDKY 272
Cdd:cd19115 239 DVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF-NNPLNY 311
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-257 |
2.48e-76 |
|
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: 233.89 E-value: 2.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLGVYKAKEGDeVKQAVKTALEVGYRSIDTATVYENESGVGEAVRE----SGIPREDIFITTKVWNDDQGY 84
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSA-TRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 85 EETLEAFEKSLKKLQMDYVDLYLIHWP-------------IRG--------KYVDTYRALEKLYEEGKVRAIGVSNFHKH 143
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdANGnviyddgvTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 144 HLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMRGGE--VFQHPIIQAIATKYEKTPAQVILRWDI 221
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEpkLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 446470145 222 QSGIVTIPKSVTPSRIQENFSIfdFSLTEEEMTQIN 257
Cdd:cd19129 240 QRGTALLTTSKTPSRIRENFDI--STLPEDAMREIN 273
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-270 |
7.16e-76 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 231.84 E-value: 7.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 13 KMPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRESGIPREDIFITTKVWNDDQGYEETLEAFE 92
Cdd:PRK11172 2 SIPAFGLGTFRLK-DQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 93 KSLKKLQMDYVDLYLIHWPIRGKYVDTYRALEKLYE---EGKVRAIGVSNFHKHHLELLLPNCKIKPM-VNQVELHPMLT 168
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEakkQGLTREIGISNFTIALMKQAIAAVGAENIaTNQIELSPYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 169 QFELRNFCQGEQIQMEAWSPLMRgGEVFQHPIIQAIATKYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSL 248
Cdd:PRK11172 161 NRKVVAFAKEHGIHVTSYMTLAY-GKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQL 239
|
250 260
....*....|....*....|..
gi 446470145 249 TEEEMTQINTLNRNlHVGTNPD 270
Cdd:PRK11172 240 DAEDMAAIAALDRN-GRLVSPE 260
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-257 |
8.48e-76 |
|
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: 232.51 E-value: 8.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 7 TLHNGVKMPMIGLGVYkAKEGD--EVKQAVKTALEVGYRSIDTATVYENESGVGEAVRE-----SGIPREDIFITTKVWN 79
Cdd:cd19122 2 TLNNGVKIPAVGFGTF-ANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 DDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPI--------------RGKYV----------DTYRALEKLYEEGKVRAI 135
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaekndqrspklgpDGKYVilkdltenpePTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 136 GVSNFHKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL-------MRGGEVFQHPIIQAIATKY 208
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgsqnqvpSTGERVSENPTLNEVAEKG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446470145 209 EKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDfsLTEEEMTQIN 257
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAIN 287
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-261 |
2.01e-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: 226.61 E-value: 2.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 8 LHNGVKMPMIGLGVYKAKEG-DEVKQAVKTALEVGYRSIDTATVYENESGVGEAVR----ESGIPREDIFITTKVWndDQ 82
Cdd:cd19119 6 LNTGASIPALGLGTASPHEDrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKVW--PT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 83 GYEETLEAFEKSLKKLQMDYVDLYLIHWPI--------------------------RGKYVDTYRALEKLYEEGKVRAIG 136
Cdd:cd19119 84 FYDEVERSLDESLKALGLDYVDLLLVHWPVcfekdsddsgkpftpvnddgktryaaSGDHITTYKQLEKIYLDGRAKAIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 137 VSNFHKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPL-MRGGEVFQHPIIQAIATKYEKTPAQV 215
Cdd:cd19119 164 VSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLgSHGAPNLKNPLVKKIAEKYNVSTGDI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446470145 216 ILRWDIQSGIVTIPKSVTPSRIQENFSIfdFSLTEEEMTQINTLNR 261
Cdd:cd19119 244 LISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-259 |
6.83e-70 |
|
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: 217.01 E-value: 6.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 15 PMIGLGVYKAKEgDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVRE----SGIPREDIFITTKVWNDDQGYEETLEA 90
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 91 FEKSLKKLQMDYVDLYLIHWPIR------------------GKYV--DTYRALEKLYEEGKVRAIGVSNFHKHHLELLLP 150
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAfdmdtdgdprddnqiqslSKKPleDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 151 NCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLMR----GGEVFQH-PIIQAIATKYEKTPAQVILRWDIQ--- 222
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGsygdGNLTFLNdSELKALATKYNTTPPQVIIAWHLQkwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 446470145 223 SGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19128 241 KNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-262 |
1.41e-69 |
|
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: 217.04 E-value: 1.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYKAKeGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAVR----ESGIPREDIFITTKVWNDDQGYEE 86
Cdd:cd19114 1 GDKMPLVGFGTAKIK-ANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRkaiqEGLVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 87 TLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVD--------------------------TYRALEKLYEEGKVRAIGVSNF 140
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaenypflwkdkelkkfpleqspmqeCWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 141 HKHHLELLLPNCKIKPMVNQVELHPMLTQFELRNFCQGEQIQMEAWSPLmrGGEVF--------------QHPIIQAIAT 206
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSF--GNAVYtkvtkhlkhftnllEHPVVKKLAD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446470145 207 KYEKTPAQVILRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRN 262
Cdd:cd19114 238 KHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEAN 293
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-257 |
4.80e-67 |
|
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: 209.01 E-value: 4.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYKAKEG------DEVKQ--AVKTALEVGYRSIDTATVY---ENESGVGEAVResGIPREDIFITTKVWN 79
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGmskdysDDKKAieALRYAIELGINLIDTAEMYgggHAEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 DDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPirGKYVD---TYRALEKLYEEGKVRAIGVSNFHKHHLELLLpNC--KI 154
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP--NPSIPieeTLRAMEELVEEGKIRYIGVSNFSLEELEEAQ-SYlkKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 155 KPMVNQVELHpMLTQFELRN---FCQGEQIQMEAWSPLMRGG--EVFQHPIIQAIATKYEKTPAQVILRWDI-QSGIVTI 228
Cdd:cd19072 156 PIVANQVEYN-LFDREEESGllpYCQKNGIAIIAYSPLEKGKlsNAKGSPLLDEIAKKYGKTPAQIALNWLIsKPNVIAI 234
|
250 260
....*....|....*....|....*....
gi 446470145 229 PKSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19072 235 PKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
4-257 |
5.97e-61 |
|
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: 193.62 E-value: 5.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHNGVKMPMIGLGVY-----KAKEGDEVKqAVKTALEVGYRSIDTATVYEN---ESGVGEAVRESgipREDIFITT 75
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWymgedPAKRAQEIE-ALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 76 KVWNDDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELL--LPNcK 153
Cdd:cd19138 77 KVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELwaVPG-G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 154 IKPMVNQVELHpmLTQ----FELRNFCQGEQIQMEAWSPLMRGGE----VFQHPIIQAIATKYEKTPAQVILRWDI-QSG 224
Cdd:cd19138 156 GNCAANQVLYN--LGSrgieYDLLPWCREHGVPVMAYSPLAQGGLlrrgLLENPTLKEIAARHGATPAQVALAWVLrDGN 233
|
250 260 270
....*....|....*....|....*....|...
gi 446470145 225 IVTIPKSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19138 234 VIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-257 |
1.30e-57 |
|
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: 185.08 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYKA--------KEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVREsgIPREDIFITTKVWN 79
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 DDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVD-TYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMV 158
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEeTLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 159 NQVELHPMLTQFELRN---FCQGEQIQMEAWSPLMRGGEVFQHpIIQAIATKYEKTPAQVILRWDIQS-GIVTIPKSVTP 234
Cdd:cd19137 159 NQVKYNLEDRDPERDGlleYCQKNGITVVAYSPLRRGLEKTNR-TLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRV 237
|
250 260
....*....|....*....|...
gi 446470145 235 SRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19137 238 EHLKENLKATEIKLSEEEMKLLD 260
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-260 |
7.09e-57 |
|
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: 184.05 E-value: 7.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 17 IGLG------VYKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESGIPREDIFITTKVWNDDQGY--- 84
Cdd:pfam00248 1 IGLGtwqlggGWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWpsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 85 ---EETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYV-DTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQ 160
Cdd:pfam00248 81 gskENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIeETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 161 VELHPM--LTQFELRNFCQGEQIQMEAWSPLMRG------------------------GEVFQH--PIIQAIATKYEKTP 212
Cdd:pfam00248 161 VEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkgTPLNLEalEALEEIAKEHGVSP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446470145 213 AQVILRWDIQS--GIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLN 260
Cdd:pfam00248 241 AQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
11-257 |
1.93e-51 |
|
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: 170.01 E-value: 1.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG-------VYKAKEGDEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVRESgipREDIFITTKV--- 77
Cdd:cd19084 1 DLKVSRIGLGtwaiggtWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKCglr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 WNDDQGYEETL------EAFEKSLKKLQMDYVDLYLIHW-----PIRgkyvDTYRALEKLYEEGKVRAIGVSNFHKHHLE 146
Cdd:cd19084 78 WDGGKGVTKDLspesirKEVEQSLRRLQTDYIDLYQIHWpdpntPIE----ETAEALEKLKKEGKIRYIGVSNFSVEQLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 147 LLLPNCKIkpMVNQVELHpMLTQF---ELRNFCQGEQIQMEAWSPLMRG-------------------------GEVFQH 198
Cdd:cd19084 154 EARKYGPI--VSLQPPYS-MLEREieeELLPYCRENGIGVLPYGPLAQGlltgkykkeptfppddrrsrfpffrGENFEK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446470145 199 PI-----IQAIATKYEKTPAQVILRWDI-QSGIVTI---PKsvTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19084 231 NLeivdkLKEIAEKYGKSLAQLAIAWTLaQPGVTSAivgAK--NPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
28-263 |
1.12e-47 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 160.44 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVREsgiPREDIFITTKVWNDDQGYEETLEAFEKSLKKLQMDYVD 104
Cdd:cd19085 23 EESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNLTPEDVRKSCERSLKRLGTDYID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 105 LYLIHWPIRGKYVD-TYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKpmVNQVELHPMLTQ--FELRNFCQGEQI 181
Cdd:cd19085 100 LYQIHWPSSDVPLEeTMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQLPYNLLWRAieYEILPFCREHGI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 182 QMEAWSPLMRG--------GEVFQ--------------------HPIIQA---IATKYEKTPAQVILRW-----DIQSGI 225
Cdd:cd19085 178 GVLAYSPLAQGlltgkfssAEDFPpgdartrlfrhfepgaeeetFEALEKlkeIADELGVTMAQLALAWvlqqpGVTSVI 257
|
250 260 270
....*....|....*....|....*....|....*...
gi 446470145 226 VtipKSVTPSRIQENFSIFDFSLTEEEMTQINTLNRNL 263
Cdd:cd19085 258 V---GARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
19-257 |
1.31e-45 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 155.08 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 19 LGVYKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESGiPREDIFITTKVWND--DQGYEETLEAFEK 93
Cdd:cd19093 17 WWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKFAPLpwRLTRRSVVKALKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 94 SLKKLQMDYVDLYLIHWPI-RGKYVDTY-RALEKLYEEGKVRAIGVSNFHKHHLE---LLLPNCKIKPMVNQVE---LHP 165
Cdd:cd19093 96 SLERLGLDSIDLYQLHWPGpWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRrahKALKERGVPLASNQVEyslLYR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 166 MLTQFELRNFCQGEQIQMEAWSPLMRG----------------GEVFQH-------PIIQA---IATKYEKTPAQVILRW 219
Cdd:cd19093 176 DPEQNGLLPACDELGITLIAYSPLAQGlltgkyspenpppggrRRLFGRknlekvqPLLDAleeIAEKYGKTPAQVALNW 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 446470145 220 DIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19093 256 LIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-242 |
2.17e-43 |
|
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: 147.28 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 15 PMIGLGVYK---AKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESGIpREDIFITTKVWNDDQGYEET- 87
Cdd:cd06660 1 SRLGLGTMTfggDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 88 -------LEAFEKSLKKLQMDYVDLYLIHWPIRGKYVD-TYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCK----IK 155
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEeTLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 156 PMVNQVE---LHPMLTQFELRNFCQGEQIQMEAWSPLMRGgevfqhpiiqaiatkyektPAQVILRWDIQSGIVT--IPK 230
Cdd:cd06660 160 FAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARG-------------------PAQLALAWLLSQPFVTvpIVG 220
|
250
....*....|..
gi 446470145 231 SVTPSRIQENFS 242
Cdd:cd06660 221 ARSPEQLEENLA 232
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
11-259 |
4.10e-43 |
|
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: 149.17 E-value: 4.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG------VYKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVResGIPREDIFITTKV---- 77
Cdd:COG0667 10 GLKVSRLGLGtmtfggPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVVIATKVgrrm 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 ----WNDDQGYEETLEAFEKSLKKLQMDYVDLYLIHWP-IRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNC 152
Cdd:COG0667 88 gpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPdPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 153 KIKPMV--NQVELHpMLTQ---FELRNFCQGEQIQMEAWSPLMRG------------------GEVFQHPI--------- 200
Cdd:COG0667 168 EGLPPIvaVQNEYS-LLDRsaeEELLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdraATNFVQGYlternlalv 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446470145 201 --IQAIATKYEKTPAQVILRWDIQSGIVT--IPKSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:COG0667 247 daLRAIAAEHGVTPAQLALAWLLAQPGVTsvIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
9-252 |
1.59e-42 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 147.22 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLGVYKAKEGD----EVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESGIPREDIFITTKV---- 77
Cdd:COG4989 8 ASGLSVSRIVLGCMRLGEWDlspaEAAALIEAALELGITTFDHADIYggyTCEALFGEALKLSPSLREKIELQTKCgirl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 -----WND----DQGYEETLEAFEKSLKKLQMDYVDLYLIHWPirgkyvD-------TYRALEKLYEEGKVRAIGVSNFH 141
Cdd:COG4989 88 psearDNRvkhyDTSKEHIIASVEGSLRRLGTDYLDLLLLHRP------DplmdpeeVAEAFDELKASGKVRHFGVSNFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 142 KHHLELLLPNCKIKPMVNQVELHPMLTQF---ELRNFCQGEQIQMEAWSPLmRGGEVFQ---------HPIIQAIATKYE 209
Cdd:COG4989 162 PSQFELLQSALDQPLVTNQIELSLLHTDAfddGTLDYCQLNGITPMAWSPL-AGGRLFGgfdeqfprlRAALDELAEKYG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446470145 210 KTPAQVILRWDIQ--SGIVTIPKSVTPSRIQENFSIFDFSLTEEE 252
Cdd:COG4989 241 VSPEAIALAWLLRhpAGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
28-256 |
8.75e-40 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 139.61 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESGIPREDIFITTK----VWNDDQG---------YEETLEAF 91
Cdd:cd19092 24 EELLSLIEAALELGITTFDHADIYgggKCEELFGEALALNPGLREKIEIQTKcgirLGDDPRPgrikhydtsKEHILASV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 92 EKSLKKLQMDYVDLYLIHWPirgkyvD-------TYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKPMVNQVELH 164
Cdd:cd19092 104 EGSLKRLGTDYLDLLLLHRP------DplmdpeeVAEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIELS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 165 PMLTQF---ELRNFCQGEQIQMEAWSPLMRG------GEVFQ--HPIIQAIATKYEKTPAQVILRWDIQ--SGIVTIPKS 231
Cdd:cd19092 178 LLHTEAiddGTLDYCQLLDITPMAWSPLGGGrlfggfDERFQrlRAALEELAEEYGVTIEAIALAWLLRhpARIQPILGT 257
|
250 260
....*....|....*....|....*
gi 446470145 232 VTPSRIQENFSIFDFSLTEEEMTQI 256
Cdd:cd19092 258 TNPERIRSAVKALDIELTREEWYEI 282
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
27-259 |
1.09e-34 |
|
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: 126.65 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 27 GDEVKQAVKT---ALEVGYRSIDTATVY---ENESGVGEAVRESGiPREDIFITTKV---WNDDQGY------EETLEAF 91
Cdd:cd19148 21 GTDEKEAIETihkALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGEVvrnsspARIRKEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 92 EKSLKKLQMDYVDLYLIHWPIRGKYVD-TYRALEKLYEEGKVRAIGVSNFHKHHLELLLpncKIKPM-VNQvelhPMLTQ 169
Cdd:cd19148 100 EDSLRRLQTDYIDLYQVHWPDPLVPIEeTAEALKELLDEGKIRAIGVSNFSPEQMETFR---KVAPLhTVQ----PPYNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 170 FE------LRNFCQGEQIQMEAWSPLMRG---GEV-----------------FQHP----IIQAI-------ATKYEKTP 212
Cdd:cd19148 173 FEreiekdVLPYARKHNIVTLAYGALCRGllsGKMtkdtkfegddlrrtdpkFQEPrfsqYLAAVeeldklaQERYGKSV 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446470145 213 AQVILRWDIQSGIVTIP--KSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19148 253 IHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
9-257 |
2.54e-34 |
|
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: 126.16 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLGVY---KAKEG------DEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVRESgIPREDIFITTK 76
Cdd:cd19079 7 NSGLKVSRLCLGCMsfgDPKWRpwvldeEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEF-APRDEVVIATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 VWN------DDQGY--EETLEAFEKSLKKLQMDYVDLYLIHW-----PIRgkyvDTYRALEKLYEEGKVRAIGVSNFHKH 143
Cdd:cd19079 86 VYFpmgdgpNGRGLsrKHIMAEVDASLKRLGTDYIDLYQIHRwdyetPIE----ETLEALHDVVKSGKVRYIGASSMYAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 144 HLELLLPNCKIK---PMVNQVELHPMLTQFELRN---FCQGEQIQMEAWSPLMRG------------------------- 192
Cdd:cd19079 162 QFAKALHLAEKNgwtKFVSMQNHYNLLYREEEREmipLCEEEGIGVIPWSPLARGrlarpwgdtterrrsttdtaklkyd 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446470145 193 -GEVFQHPII---QAIATKYEKTPAQVILRWDIQSGIVTIP--KSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19079 242 yFTEADKEIVdrvEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-138 |
1.87e-33 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 122.31 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 3 IPTTTLHN-GVKMPMIGLGVYKAkeGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVResGIPREDIFITTKVW 78
Cdd:cd19105 1 MPYRTLGKtGLKVSRLGFGGGGL--PRESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALK--GLRRDKVFLATKAS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470145 79 N--DDQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYV----DTYRALEKLYEEGKVRAIGVS 138
Cdd:cd19105 77 PrlDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllneELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
9-259 |
4.62e-31 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 117.71 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLG--------VYKAKEG----DEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESgipREDIFI 73
Cdd:cd19091 8 RSGLKVSELALGtmtfggggGFFGAWGgvdqEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKGR---RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 74 TTKVW-------NDD-QGYEETLEAFEKSLKKLQMDYVDLYLIH-WPIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHH 144
Cdd:cd19091 85 ATKVRgrmgegpNDVgLSRHHIIRAVEASLKRLGTDYIDLYQLHgFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 145 LELLLPNCK----IKPMVNQV-------ELhpmltQFELRNFCQGEQIQMEAWSPL--------------------MRGG 193
Cdd:cd19091 165 IMKALGISErrglARFVALQAyysllgrDL-----EHELMPLALDQGVGLLVWSPLaggllsgkyrrgqpapegsrLRRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 194 EVFQHPI-----------IQAIATKYEKTPAQVILRWDIQSGIVTipkSV-----TPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19091 240 GFDFPPVdrergydvvdaLREIAKETGATPAQVALAWLLSRPTVS---SViigarNEEQLEDNLGAAGLSLTPEEIARLD 316
|
..
gi 446470145 258 TL 259
Cdd:cd19091 317 KV 318
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-264 |
5.71e-31 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 118.38 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLGV--YKAKEGDEVKQAVKTALEVGYRSIDTATVYEN-ESGVGEAVREsgiPREDIFITTK--VWNDDqg 83
Cdd:COG1453 8 KTGLEVSVLGFGGmrLPRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKlpPWVRD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 YEETLEAFEKSLKKLQMDYVDLYLIH-------WPIRGKYVDTYRALEKLYEEGKVRAIGVSnFHkHHLELllpnckIKP 156
Cdd:COG1453 83 PEDMRKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPGGALEALEKAKAEGKIRHIGFS-TH-GSLEV------IKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 157 MVN-------QVELHPMLTQFELRNfcqgEQIQ-----------MEawsPLmRGGEVFQHPI-IQAIATKyEKTPAQVIL 217
Cdd:COG1453 155 AIDtgdfdfvQLQYNYLDQDNQAGE----EALEaaaekgigviiMK---PL-KGGRLANPPEkLVELLCP-PLSPAEWAL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446470145 218 RWdIQS--GIVTIpkSV---TPSRIQENFSIFD--FSLTEEEMTQINTLNRNLH 264
Cdd:COG1453 226 RF-LLShpEVTTV--LSgmsTPEQLDENLKTADnlEPLTEEELAILERLAEELG 276
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
10-256 |
2.50e-30 |
|
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: 115.39 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGV------YKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVREsgiPREDIFITTK---V 77
Cdd:cd19076 8 QGLEVSALGLGCmgmsafYGPADEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIATKfgiV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 WNDDQGY-------EETLEAFEKSLKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVSNF----- 140
Cdd:cd19076 85 RDPGSGFrgvdgrpEYVRAACEASLKRLGTDVIDLYYQHrvdpnVPIE----ETVGAMAELVEEGKVRYIGLSEAsadti 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 141 ---HKHH------LELLLpnckikpMVNQVELHPMLTQFELrnfcqGeqIQMEAWSPLMRG------------------- 192
Cdd:cd19076 161 rraHAVHpitavqSEYSL-------WTRDIEDEVLPTCREL-----G--IGFVAYSPLGRGfltgaikspedlpeddfrr 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446470145 193 ------GEVFQHPI-----IQAIATKYEKTPAQVILRWDIQSG--IVTIPKSVTPSRIQENFSIFDFSLTEEEMTQI 256
Cdd:cd19076 227 nnprfqGENFDKNLklvekLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-256 |
2.03e-29 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 113.14 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLG--------VYKAKEGDEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVRESgipREDIFITTK- 76
Cdd:cd19149 6 KSGIEASVIGLGtwaigggpWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 --VWNDDQGY----------------EETLEAFEKSLKKLQMDYVDLYLIHW-----PIRgkyvDTYRALEKLYEEGKVR 133
Cdd:cd19149 83 glRWDREGGSfffvrdgvtvyknlspESIREEVEQSLKRLGTDYIDLYQTHWqdvetPIE----ETMEALEELKRQGKIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 134 AIGVSNFHKHHLELLLPNCKIKpmVNQvELHPMLTQF---ELRNFCQGEQIQMEAWSPLMRG---GEVFQ---------- 197
Cdd:cd19149 159 AIGASNVSVEQIKEYVKAGQLD--IIQ-EKYSMLDRGiekELLPYCKKNNIAFQAYSPLEQGlltGKITPdrefdagdar 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446470145 198 --HP---------------IIQAIATKYEKTPAQVILRWDI-QSGIVT-IPKSVTPSRIQENFSIFDFSLTEEEMTQI 256
Cdd:cd19149 236 sgIPwfspenrekvlalleKWKPLCEKYGCTLAQLVIAWTLaQPGITSaLCGARKPEQAEENAKAGDIRLSAEDIATM 313
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-259 |
2.49e-29 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 112.38 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 17 IGLGVYKAKEGD-----------EVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESgipREDIFITTK---VWN 79
Cdd:cd19102 4 IGLGTWAIGGGGwgggwgpqddrDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 DD----QGY--EETLEAFEKSLKKLQMDYVDLYLIHWPIRGK-YVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLpnc 152
Cdd:cd19102 81 EEgrirRSLkpASIRAECEASLRRLGVDVIDLYQIHWPDPDEpIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQ--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 153 KIKPMVNqveLHPMLT------QFELRNFCQGEQIQMEAWSPLMRG---GEV-------------------FQHP----- 199
Cdd:cd19102 158 AIHPIAS---LQPPYSllrrgiEAEILPFCAEHGIGVIVYSPMQSGlltGKMtpervaslpaddwrrrspfFQEPnlarn 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446470145 200 -----IIQAIATKYEKTPAQVILRWDIQSGIVT--IPKSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19102 235 lalvdALRPIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
11-259 |
6.43e-29 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 111.74 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG--------VYKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESGipREDIFITTKVWN 79
Cdd:cd19083 8 DIDVNPIGLGtnavgghnLYPNLDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEYN--RNEVVIATKGAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 DDQGYEETL--------EAFEKSLKKLQMDYVDLYLIHWPIRGKYVD-TYRALEKLYEEGKVRAIGVSNFHKHHLElllp 150
Cdd:cd19083 86 KFGGDGSVLnnspeflrSAVEKSLKRLNTDYIDLYYIHFPDGETPKAeAVGALQELKDEGKIRAIGVSNFSLEQLK---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 151 NCKIKPMVNQVELHPMLTQFELRN----FCQGEQIQMEAWSPLMRG-------------------------GEVFQHPI- 200
Cdd:cd19083 162 EANKDGYVDVLQGEYNLLQREAEEdilpYCVENNISFIPYFPLASGllagkytkdtkfpdndlrndkplfkGERFSENLd 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446470145 201 ----IQAIATKYEKTPAQVILRWDI-QSGI-VTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19083 242 kvdkLKSIADEKGVTVAHLALAWYLtRPAIdVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-149 |
4.45e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 107.57 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG--VYKAKEGDEVKQAVKTALEVGYRSIDTATVYEN-ESGVGEAVREsgiPREDIFITTKVWNDDqgYEET 87
Cdd:cd19100 8 GLKVSRLGFGggPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARD--YEGA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446470145 88 LEAFEKSLKKLQMDYVDLYLIHwpirgkYVDT-------------YRALEKLYEEGKVRAIGVSNfhkHHLELLL 149
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLH------AVDTeedldqvfgpggaLEALLEAKEEGKIRFIGISG---HSPEVLL 148
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
3-256 |
1.85e-27 |
|
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: 107.91 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 3 IPTTTL-HNGVKMPMIGLGV------YKAKEGDEVKQAVKT-ALEVGYRSIDTATVY-ENESGVGEAVRESGIPREDIFI 73
Cdd:cd19144 1 IPTRTLgRNGPSVPALGFGAmglsafYGPPKPDEERFAVLDaAFELGCTFWDTADIYgDSEELIGRWFKQNPGKREKIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 74 TTKVWNDDQGY----------EETLEAFEKSLKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVS 138
Cdd:cd19144 81 ATKFGIEKNVEtgeysvdgspEYVKKACETSLKRLGVDYIDLYYQHrvdgkTPIE----KTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 139 NFHKhhlELLLPNCKIKPMVN-QVELHPMLT-----QFELRNFCQGEQIQMEAWSPLMRG-------------------- 192
Cdd:cd19144 157 ECSA---ETLRRAHAVHPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGRGfltgairspddfeegdfrrm 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470145 193 -----GEVFQHPI-----IQAIATKYEKTPAQVILRWDIQSG--IVTIPKSVTPSRIQENFSIFDFSLTEEEMTQI 256
Cdd:cd19144 234 aprfqAENFPKNLelvdkIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-251 |
3.42e-27 |
|
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: 106.91 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG---VYKAKEGDEVKQA-VKTALEVGYRSIDTATVYEN---ESGVGEAVResGIPREDIFITTKV-WN-DD 81
Cdd:cd19074 1 GLKVSELSLGtwlTFGGQVDDEDAKAcVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWPtGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 82 QGYEETL------EAFEKSLKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLP 150
Cdd:cd19074 79 GPNDRGLsrkhifESIHASLKRLQLDYVDIYYCHrydpeTPLE----ETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 151 NCK----IKPMVNQVELHpMLTQF---ELRNFCQGEQIQMEAWSPLMRG--------------GEVFQHPII-------- 201
Cdd:cd19074 155 LARqfglIPPVVEQPQYN-MLWREieeEVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsRSRATDEDNrdkkrrll 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470145 202 -----------QAIATKYEKTPAQVILRWDIQSGIVTipkSV-----TPSRIQENFSIFDFSLTEE 251
Cdd:cd19074 234 tdenlekvkklKPIADELGLTLAQLALAWCLRNPAVS---SAiigasRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-138 |
8.14e-27 |
|
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: 104.48 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 17 IGLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVREsgiPREDIFITTKVWNDDQGYEET------ 87
Cdd:cd19086 13 LGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKG---RRDKVVIATKFGNRFDGGPERpqdfsp 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446470145 88 ---LEAFEKSLKKLQMDYVDLYLIH-WPIRGKYVD-TYRALEKLYEEGKVRAIGVS 138
Cdd:cd19086 90 eyiREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDeLFEALEKLKQEGKIRAYGVS 145
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
17-258 |
8.61e-27 |
|
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: 105.78 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 17 IGLGVY-------KAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVREsgiPREDIFITTK---VWNDDQG 83
Cdd:cd19078 7 IGLGCMgmshgygPPPDKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKfgfKIDGGKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 84 YEETL--------EAFEKSLKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVSN-----FHKHHl 145
Cdd:cd19078 84 GPLGLdsrpehirKAVEGSLKRLQTDYIDLYYQHrvdpnVPIE----EVAGTMKELIKEGKIRHWGLSEagvetIRRAH- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 146 elllpncKIKPMVN-QVELHPMLTQFE--LRNFCQGEQIQMEAWSPLMRG---GEV-----------------FQHP--- 199
Cdd:cd19078 159 -------AVCPVTAvQSEYSMMWREPEkeVLPTLEELGIGFVPFSPLGKGfltGKIdentkfdegddraslprFTPEale 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446470145 200 -------IIQAIATKYEKTPAQVILRWDI--QSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINT 258
Cdd:cd19078 232 anqalvdLLKEFAEEKGATPAQIALAWLLakKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
39-257 |
2.01e-26 |
|
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: 104.99 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 39 EVGYRSIDTATVY----------ENESGVGEAVRESGiPREDIFITTKV--WNDDQGY----EETLEAFEKSLKKLQMDY 102
Cdd:cd19081 37 DAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgfPMGPNGPglsrKHIRRAVEASLRRLQTDY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 103 VDLYLIHW-----PIRgkyvDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCK----IKPMVNQVE---LHPMLTQF 170
Cdd:cd19081 116 IDLYQAHWddpatPLE----ETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEynlVDRESFEG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 171 ELRNFCQGEQIQMEAWSPL------------------MRGGEVFQ-------HPIIQA---IATKYEKTPAQVILRWDIQ 222
Cdd:cd19081 192 ELLPLCREEGIGVIPYSPLaggfltgkyrseadlpgsTRRGEAAKrylnergLRILDAldeVAAEHGATPAQVALAWLLA 271
|
250 260 270
....*....|....*....|....*....|....*..
gi 446470145 223 SGIVTIP--KSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19081 272 RPGVTAPiaGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-249 |
1.87e-25 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 101.14 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 14 MPMIGLGVYKA-KEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESGiprEDIFITTKV---------WND 80
Cdd:cd19088 9 MRLTGPGIWGPpADREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvrtgpgwWGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 81 DQGYEETLEAFEKSLKKLQMDYVDLYLIHWP-IRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLpncKIKPMVN 159
Cdd:cd19088 86 DGSPEYLRQAVEASLRRLGLDRIDLYQLHRIdPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEAR---AIVRIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 160 -QVELHPMLTQ-FELRNFCQGEQIQMEAWSPLMRGGEVFQHPIIQAIATKYEKTPAQVILRWDIQSG--IVTIPKSVTPS 235
Cdd:cd19088 163 vQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVE 242
|
250
....*....|....
gi 446470145 236 RIQENFSIFDFSLT 249
Cdd:cd19088 243 HLEENLAAAGLRLS 256
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
28-259 |
1.47e-24 |
|
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: 99.95 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESgipREDIFITTKV------WNDDQGYE--ETLEAFEKSLK 96
Cdd:cd19087 30 ETSFAIMDRALDAGINFFDTADVYgggRSEEIIGRWIAGR---RDDIVLATKVfgpmgdDPNDRGLSrrHIRRAVEASLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 97 KLQMDYVDLYLIHWPIRGKYVD-TYRALEKLYEEGKVRAIGVSNF------------HKHHlelLLPNCKIKPMVN---- 159
Cdd:cd19087 107 RLQTDYIDLYQMHHFDRDTPLEeTLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaARRG---LLRFVSEQPMYNllkr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 160 --QVELHPMltqfelrnfCQGEQIQMEAWSPLMRG-----------------------GEVFQHPIIQAIATKYEK---- 210
Cdd:cd19087 184 qaELEILPA---------ARAYGLGVIPYSPLAGGlltgkygkgkrpesgrlveraryQARYGLEEYRDIAERFEAlaae 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446470145 211 ---TPAQVILRWDIQSGIVTIP--KSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19087 255 aglTPASLALAWVLSHPAVTSPiiGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
28-141 |
1.54e-23 |
|
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: 96.09 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVREsgIPREDIFITTKV-WNDDQGYEETLEAFEKSLKKLQMDYV 103
Cdd:cd19096 21 EKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKE--GPREKFYLATKLpPWSVKSAEDFRRILEESLKRLGVDYI 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446470145 104 DLYLIHWPIRGKYVDTYR------ALEKLYEEGKVRAIGVSnFH 141
Cdd:cd19096 99 DFYLLHGLNSPEWLEKARkgglleFLEKAKKEGLIRHIGFS-FH 141
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
15-148 |
8.33e-22 |
|
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: 91.85 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 15 PMIGLG---VYKAKEG---DEVKQAVKTALEVGYRSIDTATVY-ENESGVGEAVREsgIPREDIFITTKV-----WNDDQ 82
Cdd:cd19090 1 SALGLGtagLGGVFGGvddDEAVATIRAALDLGINYIDTAPAYgDSEERLGLALAE--LPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446470145 83 GYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVD------TYRALEKLYEEGKVRAIGVS-NFHKHHLELL 148
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDilapggALEALLELKEEGLIKHIGLGgGPPDLLRRAI 151
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
37-257 |
2.21e-21 |
|
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: 91.47 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 37 ALEVGYRSIDTATVY----------ENESGVGEAVRESGiPREDIFITTKV--------WNDDQG----YEETLEAFEKS 94
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRGGGtrldRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 95 LKKLQMDYVDLYLIHWPIR-------GKYV------------DTYRALEKLYEEGKVRAIGVSN--------FHKHHLEL 147
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPDRytplfggGYYTepseeedsvsfeEQLEALGELVKAGKIRHIGLSNetpwgvmkFLELAEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 148 LLPnckiKPMVNQVElhpmltqFEL--RNF-------CQGEQIQMEAWSPL------------------------MRGGE 194
Cdd:cd19094 186 GLP----RIVSIQNP-------YSLlnRNFeeglaeaCHRENVGLLAYSPLaggvltgkyldgaarpeggrlnlfPGYMA 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446470145 195 VFQHPIIQA-------IATKYEKTPAQVILRWDIQSGIV--TIPKSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19094 255 RYRSPQALEavaeyvkLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEID 326
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
28-240 |
9.52e-21 |
|
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: 88.45 E-value: 9.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVYEN-ESGVGEAVreSGIPREDIFITTKVW--------NDDQGYEETLEAFEKSLKKL 98
Cdd:cd19095 20 AEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGthgeggrdRKDFSPAAIRASIERSLRRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 99 QMDYVDLYLIH----WPIRGkyvDTYRALEKLYEEGKVRAIGVSNFHKHHLELL---------LPNCkikpmVNQVELHP 165
Cdd:cd19095 98 GTDYIDLLQLHgpsdDELTG---EVLETLEDLKAAGKVRYIGVSGDGEELEAAIasgvfdvvqLPYN-----VLDREEEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 166 MLTQFELRN--------FCQGEQIQMEAWSPLMRGGEVFQHPIIQAIATkyekTPAQVILRWDIQSGIVT--IPKSVTPS 235
Cdd:cd19095 170 LLPLAAEAGlgvivnrpLANGRLRRRVRRRPLYADYARRPEFAAEIGGA----TWAQAALRFVLSHPGVSsaIVGTTNPE 245
|
....*
gi 446470145 236 RIQEN 240
Cdd:cd19095 246 HLEEN 250
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
11-138 |
1.36e-20 |
|
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: 88.76 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG------VYKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVResGIPREDIFITTKV---- 77
Cdd:cd19163 10 GLKVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYYLATKVgryg 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 --WND--DQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKYVD-----TYRALEKLYEEGKVRAIGVS 138
Cdd:cd19163 88 ldPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDqilneTLPALQKLKEEGKVRFIGIT 157
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-240 |
1.52e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 88.54 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 38 LEVGYRSIDTATVY----------ENESGVGEAVRESGIpREDIFITTKV---WNDDQGYEETLE---------AFEKSL 95
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDRGN-RDDVVIATKVgagPRDPDGGPESPEglsaetieqEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 96 KKLQMDYVDLYLIHWPIRGKYV-DTYRALEKLYEEGKVRAIGVSNFH------------KHHLE----------LLLPNc 152
Cdd:cd19752 106 RRLGTDYIDLYYAHVDDRDTPLeETLEAFNELVKAGKVRAIGASNFAawrlerarqiarQQGWAefsaiqqrhsYLRPR- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 153 KIKPMVNQVELHPmltqfELRNFCQGE-QIQMEAWSPLMRGG---------EVFQHP-------IIQAIATKYEKTPAQV 215
Cdd:cd19752 185 PGADFGVQRIVTD-----ELLDYASSRpDLTLLAYSPLLSGAytrpdrplpEQYDGPdsdarlaVLEEVAGELGATPNQV 259
|
250 260
....*....|....*....|....*..
gi 446470145 216 ILRWDIQSGIVTIP--KSVTPSRIQEN 240
Cdd:cd19752 260 VLAWLLHRTPAIIPllGASTVEQLEEN 286
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
28-219 |
3.67e-20 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 87.61 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAvresGIPREDIFITTKV---WNDDQGYEETLEAFEKSLKKLQMD 101
Cdd:cd19075 20 EAAAELLDAFLERGHTEIDTARVYpdgTSEELLGEL----GLGERGFKIDTKAnpgVGGGLSPENVRKQLETSLKRLKVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 102 YVDLYLIHWPIRGKYV-DTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCK----IKPMVNQ-----------VELHP 165
Cdd:cd19075 96 KVDVFYLHAPDRSTPLeETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVYQgmynaitrqveTELFP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 166 MLTQFELR--------------NFCQGEQIQMEA-WSPLMRGGEVFQ----HP-------IIQAIATKYEKTPAQVILRW 219
Cdd:cd19075 176 CLRKLGIRfyaysplaggfltgKYKYSEDKAGGGrFDPNNALGKLYRdrywKPsyfealeKVEEAAEKEGISLAEAALRW 255
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-259 |
1.15e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 86.23 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVREsgIPREDIFITTKVWND--DQGYEETLEAFEKSLKKLQMDY 102
Cdd:cd19103 32 DTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKFTPQiaGQSADPVADMLEGSLARLGTDY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 103 VDLYLIHWPirgkyVDTYRALEK---LYEEGKVRAIGVSNfhkHHLElllpncKIKpMVNQ------VELHPMLTQFELR 173
Cdd:cd19103 110 IDIYWIHNP-----ADVERWTPElipLLKSGKVKHVGVSN---HNLA------EIK-RANEilakagVSLSAVQNHYSLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 174 N----------FCQGEQIQMEAWSPL----MRGGEVFQHPI-----------------------IQAIATKYEKTPAQVI 216
Cdd:cd19103 175 YrsseeagildYCKENGITFFAYMVLeqgaLSGKYDTKHPLpegsgraetynpllpqleeltavMAEIGAKHGASIAQVA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446470145 217 LRWDIQSGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTL 259
Cdd:cd19103 255 IAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-257 |
2.26e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 85.72 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 23 KAKEGDEVKQAVKTALEVGYRSIDTATVYEN-ESGVGEAVRE---SGIPREDIFITTKVWNDDQ----GYEETLEAFEKS 94
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRlrrERDAADDVQIHTKWVPDPGeltmTRAYVEAAIDRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 95 LKKLQMDYVDLYLIHW--PIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLpNCKIKPMVNQVelhpmltQF-- 170
Cdd:cd19101 98 LKRLGVDRLDLVQFHWwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL-DAGVPIVSNQV-------QYsl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 171 -------ELRNFCQGEQIQMEAWSPLMRG-------------GEVFQHP-------II----------------QAIATK 207
Cdd:cd19101 170 ldrrpenGMAALCEDHGIKLLAYGTLAGGllsekylgvpeptGPALETRslqkyklMIdewggwdlfqellrtlKAIADK 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446470145 208 YEKTPAQVILRWDI-QSGIVTIPKSVTPSR-IQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19101 250 HGVSIANVAVRWVLdQPGVAGVIVGARNSEhIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
28-257 |
3.85e-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: 84.96 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVRESgipREDIFITTK-VWNDDQG--------YEETLEAFEKSL 95
Cdd:cd19080 31 EEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKyTMNRRPGdpnaggnhRKNLRRSVEASL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 96 KKLQMDYVDLYLIHWPIRGKYVD-TYRALEKLYEEGKVRAIGVSNF------------HKHHLElllpnckikPMVN-QV 161
Cdd:cd19080 108 RRLQTDYIDLLYVHAWDFTTPVEeVMRALDDLVRAGKVLYVGISDTpawvvarantlaELRGWS---------PFVAlQI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 162 -----------ELHPMLTQFELrnfcqgeqiQMEAWSPL------------------MRGGEVFQHPII----------- 201
Cdd:cd19080 179 eysllertperELLPMARALGL---------GVTPWSPLggglltgkyqrgeegragEAKGVTVGFGKLternwaivdvv 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446470145 202 QAIATKYEKTPAQVILRWDIQSGIVTIP--KSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19080 250 AAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
10-257 |
5.43e-18 |
|
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: 81.90 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGV------YKAKEGDEVKQAVKTALEVGYRSIDTATVY------ENESGVGEAVRESGIPREDIFITTK- 76
Cdd:cd19077 1 NGKLVGPIGLGLmgltwrPNPTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 -VWNDDQGYEETLEAFEKSLKKL-----QMDYVDLYLI-----HWPIRgkyvDTYRALEKLYEEGKVRAIGVS-----NF 140
Cdd:cd19077 81 gLDPDTLRPDGSPEAVRKSIENIlralgGTKKIDIFEParvdpNVPIE----ETIKALKELVKEGKIRGIGLSevsaeTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 141 HKHHlelllpncKIKPMV-NQVELHPMLTQFELRN---FCQGEQIQMEAWSPLMRG------------------------ 192
Cdd:cd19077 157 RRAH--------AVHPIAaVEVEYSLFSREIEENGvleTCAELGIPIIAYSPLGRGlltgriksladipegdfrrhldrf 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446470145 193 -GEVFQHPI-----IQAIATKYEKTPAQVILRWDI-QSG--IVTIPKSVTPSRIQENFSIFDFSLTEEEMTQIN 257
Cdd:cd19077 229 nGENFEKNLklvdaLQELAEKKGCTPAQLALAWILaQSGpkIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-138 |
1.93e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 80.44 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 17 IGLGVYKAKEGD----EVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRES----GIPREDIFITTKV-------- 77
Cdd:cd19099 6 LGLGTYRGDSDDetdeEYREALKAALDSGINVIDTAINYrggRSERLIGKALRELiekgGIKRDEVVIVTKAgyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 -------W--------NDDQGYEETL----------EAFEKSLKKLQMDYVDLYLIHWPIRG-----------KYVDTYR 121
Cdd:cd19099 86 eplrplkYleeklgrgLIDVADSAGLrhcispayleDQIERSLKRLGLDTIDLYLLHNPEEQllelgeeefydRLEEAFE 165
|
170
....*....|....*..
gi 446470145 122 ALEKLYEEGKVRAIGVS 138
Cdd:cd19099 166 ALEEAVAEGKIRYYGIS 182
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-218 |
3.72e-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: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVYEN-ESGVGEAVRESgiprEDIFITTKV----WNDDQGYEETLEAFEKSLKKLQMDY 102
Cdd:cd19097 26 KEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL----DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 103 VDLYLIHWP----IRGKYVdtYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCKIKpMVnQV---------ELHPMLTQ 169
Cdd:cd19097 102 LDGLLLHNPddllKHGGKL--VEALLELKKEGLIRKIGVSVYSPEELEKALESFKID-II-QLpfnildqrfLKSGLLAK 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446470145 170 FELRN--------FCQG------EQIQ--MEAWSPLMRggevfqhpIIQAIATKYEKTPAQVILR 218
Cdd:cd19097 178 LKKKGieiharsvFLQGlllmepDKLPakFAPAKPLLK--------KLHELAKKLGLSPLELALG 234
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
36-242 |
6.47e-17 |
|
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: 78.75 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 36 TALEVGYRSIDTATVY-------ENESGVGEAVRESGIpREDIFITTK-----VWNDDQGY---EETLEAFEKSLKKLQM 100
Cdd:cd19082 25 AFVELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-RDKVVIATKgghpdLEDMSRSRlspEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 101 DYVDLYLIHwpiR-------GKYVDTyraLEKLYEEGKVRAIGVSNFH------------KHHLElllpnckiKPMVNQV 161
Cdd:cd19082 104 DYIDLYFLH---RddpsvpvGEIVDT---LNELVRAGKIRAFGASNWSteriaeanayakAHGLP--------GFAASSP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 162 EL------HPML-------TQFELRNFCQGEQIQMEAWSPLMRG----------------GEVFQHPI-------IQAIA 205
Cdd:cd19082 170 QWslarpnEPPWpgptlvaMDEEMRAWHEENQLPVFAYSSQARGffskraaggaeddselRRVYYSEEnferlerAKELA 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 446470145 206 TKYEKTPAQVILRWDIQSGIVTIP--KSVTPSRIQENFS 242
Cdd:cd19082 250 EEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLA 288
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
11-256 |
1.90e-16 |
|
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: 77.47 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG-------VYKAKEGDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVResGIPREDIFITTKV--- 77
Cdd:cd19145 9 GLEVSAQGLGcmglsgdYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQLATKFgih 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 WNDDQGYEET------LEAFEKSLKKLQMDYVDLYLIHW-----PIRgkyvDTYRALEKLYEEGKVRAIGVS-----NFH 141
Cdd:cd19145 87 EIGGSGVEVRgdpayvRAACEASLKRLDVDYIDLYYQHRidttvPIE----ITMGELKKLVEEGKIKYIGLSeasadTIR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 142 KHHlelllpncKIKPmVNQVELHPML----TQFELRNFCQGEQIQMEAWSPLMRG----GEVF-----------QHPIIQ 202
Cdd:cd19145 163 RAH--------AVHP-ITAVQLEWSLwtrdIEEEIIPTCRELGIGIVPYSPLGRGffagKAKLeellensdvrkSHPRFQ 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446470145 203 ---------------AIATKYEKTPAQVILRWDIQSG--IVTIPKSVTPSRIQENFSIFDFSLTEEEMTQI 256
Cdd:cd19145 234 genleknkvlyerveALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-138 |
4.36e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 76.54 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 28 DEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVRESgipREDIFITTKV----WNDDQGYEETLEAFEKSLKKLQM 100
Cdd:cd19104 32 EEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL---PAGPYITTKVrldpDDLGDIGGQIERSVEKSLKRLKR 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446470145 101 DYVDLYLIHWPI---RGKYVDTYR-------------ALEKLYEEGKVRAIGVS 138
Cdd:cd19104 109 DSVDLLQLHNRIgdeRDKPVGGTLsttdvlglggvadAFERLRSEGKIRFIGIT 162
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
27-256 |
5.16e-15 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 73.40 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 27 GDEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVRESGIPREDIFITTKV-WNDDQGYEET--------LEAFEKS 94
Cdd:cd19143 30 VDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGGGGPPPNDrglsrkhiVEGTKAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 95 LKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVSNF------------HKHHLelllpnckIKPM 157
Cdd:cd19143 110 LKRLQLDYVDLVFCHrpdpaTPIE----ETVRAMNDLIDQGKAFYWGTSEWsaqqieeaheiaDRLGL--------IPPV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 158 VNQVELHpMLT--QFE------LRNFCQGEQIqmeaWSPLMRG----------------------------GEVFQHPI- 200
Cdd:cd19143 178 MEQPQYN-LFHreRVEveyaplYEKYGLGTTT----WSPLASGlltgkynngipegsrlalpgyewlkdrkEELGQEKIe 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446470145 201 ----IQAIATKYEKTPAQVILRWDIQSGIV--TIPKSVTPSRIQENFSIFDF--SLTEEEMTQI 256
Cdd:cd19143 253 kvrkLKPIAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEENLKALEVlpKLTPEVMEKI 316
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-261 |
1.06e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 72.96 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 1 MH---IPtttlHNGVKMPMIGLGVY----KAKEGDEVKQaVKTALEVGYRSIDTATVYE----------NESGVGEAVRE 63
Cdd:PRK10625 1 MQyhrIP----HSSLEVSTLGLGTMtfgeQNSEADAHAQ-LDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 64 SGiPREDIFITTKV----WNDDQGY--EETL------EAFEKSLKKLQMDYVDLYLIHWPIR-----GK----------- 115
Cdd:PRK10625 76 RG-SREKLIIASKVsgpsRNNDKGIrpNQALdrknirEALHDSLKRLQTDYLDLYQVHWPQRptncfGKlgyswtdsapa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 116 --YVDTYRALEKLYEEGKVRAIGVSN---------FH---KHHLElllpncKIKPMVNQVELHPMLTQFELRNFCQGEQI 181
Cdd:PRK10625 155 vsLLETLDALAEQQRAGKIRYIGVSNetafgvmryLHlaeKHDLP------RIVTIQNPYSLLNRSFEVGLAEVSQYEGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 182 QMEAWSPLMRG---------------------------GEVFQHPIIQ--AIATKYEKTPAQVILRWDIQSGIV--TIPK 230
Cdd:PRK10625 229 ELLAYSCLAFGtltgkylngakpagarntlfsrftrysGEQTQKAVAAyvDIAKRHGLDPAQMALAFVRRQPFVasTLLG 308
|
330 340 350
....*....|....*....|....*....|.
gi 446470145 231 SVTPSRIQENFSIFDFSLTEEEMTQINTLNR 261
Cdd:PRK10625 309 ATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-137 |
5.67e-14 |
|
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: 70.33 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 15 PMIGLG------VYKAKEGDEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVREsgIPREDIFITTKV-------- 77
Cdd:cd19152 1 PKLGFGtaplgnLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE--LGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 ----------WND-------DQGYEETLEAFEKSLKKLQMDYVDLYLIHWPIRGKY------------VDTYRALEKLYE 128
Cdd:cd19152 79 eveptfepgfWNPlpfdavfDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaiKGAFRALEELRE 158
|
....*....
gi 446470145 129 EGKVRAIGV 137
Cdd:cd19152 159 EGVIKAIGL 167
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-157 |
7.74e-14 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 69.87 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 4 PTTTLHN-GVKMPMIGLG------VYKAK-EGDEVKQAVKTALEVGYRSIDTATVYENESG---VGEAVRESGIPREDIF 72
Cdd:cd19153 1 FGETLEIaLGNVSPVGLGtaalggVYGDGlEQDEAVAIVAEAFAAGINHFDTSPYYGAESSeavLGKALAALQVPRSSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 73 ITTKVWN-DDQGYEETLEAFEK----SLKKLQMDYVDLYLIHWPIRGKY----VDTYRALEKLYEEGKVRAIGVSNFHKH 143
Cdd:cd19153 81 VATKVGRyRDSEFDYSAERVRAsvatSLERLHTTYLDVVYLHDIEFVDYdtlvDEALPALRTLKDEGVIKRIGIAGYPLD 160
|
170
....*....|....
gi 446470145 144 HLELLLPNCKIKPM 157
Cdd:cd19153 161 TLTRATRRCSPGSL 174
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
11-138 |
1.75e-13 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 69.04 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLG------VYKAKEGDEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVRESGIPREDIFITTKVWNDD 81
Cdd:PLN02587 8 GLKVSSVGFGasplgsVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCGRYG 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470145 82 QGY----EETLEAFEKSLKKLQMDYVDLYLIHwPIRGKYVD-----TYRALEKLYEEGKVRAIGVS 138
Cdd:PLN02587 88 EGFdfsaERVTKSVDESLARLQLDYVDILHCH-DIEFGSLDqivneTIPALQKLKESGKVRFIGIT 152
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
15-138 |
2.20e-13 |
|
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: 68.54 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 15 PMIGLG------VYKAKEgDEVKQAVKTALEVGYRSIDTATVY---ENESGVGEAVResGIPREDIFITTKV-------- 77
Cdd:cd19162 1 PRLGLGaaslgnLARAGE-DEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepga 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446470145 78 ------WNDDQGYEE--TLEAFEKSLKKLQMDYVDLYLIHWPIRGKYV---DTYRALEKLYEEGKVRAIGVS 138
Cdd:cd19162 78 agrpagADRRFDFSAdgIRRSIEASLERLGLDRLDLVFLHDPDRHLLQaltDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-149 |
2.35e-13 |
|
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: 68.46 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 18 GLGVYKAKEGDEVKQAVKTALEVGYRSIDTATVY-ENESGVGEAVR--ESGIPREDIFITTKVW---NDDQGY-EETLEA 90
Cdd:cd19164 24 SYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYgPSEIILGRALKalRDEFPRDTYFIITKVGrygPDDFDYsPEWIRA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446470145 91 -FEKSLKKLQMDYVDLYLIH---WPIRGKYVDTYRALEKLYEEGKVRAIGVSNFhkhHLELLL 149
Cdd:cd19164 104 sVERSLRRLHTDYLDLVYLHdveFVADEEVLEALKELFKLKDEGKIRNVGISGY---PLPVLL 163
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
10-189 |
2.57e-12 |
|
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: 65.95 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLG---VYKAKEGDEVKQA-VKTALEVGYRSIDTATVYEN---ESGVGEAVRESGIPREDIFITTKV-WN-- 79
Cdd:cd19142 9 SGLRVSNVGLGtwsTFSTAISEEQAEEiVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIyWSyg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 80 -DDQGY--EETLEAFEKSLKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPN 151
Cdd:cd19142 89 sEERGLsrKHIIESVRASLRRLQLDYIDIVIIHkadpmCPME----EVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446470145 152 CK----IKPMVNQVELHPmltqfelrnFCQGE-QIQME-----------AWSPL 189
Cdd:cd19142 165 ARqfncPTPICEQSEYHM---------FCREKmELYMPelynkvgvgliTWSPL 209
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-136 |
9.41e-10 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 58.11 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 15 PMIGLG------VYKAKEGDEVKQAVKTALEVGYRSIDTATVYEN---ESGVGEAVREsgIPREDIFITTKV-------- 77
Cdd:cd19161 1 SELGLGtaglgnLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkpar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 78 ---------WND--------DQGYEETLEAFEKSLKKLQMDYVDLYLIHwPIrGKYV--DT-------------YRALEK 125
Cdd:cd19161 79 egsvpdpngFVDplpfeivyDYSYDGIMRSFEDSLQRLGLNRIDILYVH-DI-GVYThgDRkerhhfaqlmsggFKALEE 156
|
170
....*....|.
gi 446470145 126 LYEEGKVRAIG 136
Cdd:cd19161 157 LKKAGVIKAFG 167
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-254 |
7.41e-09 |
|
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: 55.49 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLGVYKAKEG----DEVKQAVKTALEVGYRSIDTATVY-----ENESGVGEAVRESGIP-REDIFITTK-- 76
Cdd:cd19151 7 RSGLKLPAISLGLWHNFGDvdryENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 --VWND---DQGYEETLEA-FEKSLKKLQMDYVDLYLIHWPIRGKYV-DTYRALEKLYEEGKVRAIGVSNFHKHHLEL-- 147
Cdd:cd19151 87 ytMWPGpygDWGSKKYLIAsLDQSLKRMGLDYVDIFYHHRPDPETPLeETMGALDQIVRQGKALYVGISNYPPEEAREaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 148 -LLPNCKIKPMVNQvelhPMLTQFE------LRNFCQGEQIQMEAWSPLMRG------------------GEVFQHP--- 199
Cdd:cd19151 167 aILKDLGTPCLIHQ----PKYSMFNrwveegLLDVLEEEGIGCIAFSPLAQGlltdrylngipedsraakGSSFLKPeqi 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446470145 200 ---------IIQAIATKYEKTPAQVILRWDIQSGIVT---IPKSvTPSRIQENFSIFD-FSLTEEEMT 254
Cdd:cd19151 243 teeklakvrRLNEIAQARGQKLAQMALAWVLRNKRVTsvlIGAS-KPSQIEDAVGALDnREFSEEELA 309
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
11-161 |
1.45e-08 |
|
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: 54.57 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYK----AKEGDEVKQAVKTALEVGYRSIDTATVYENESGVGEAV------RESGIPREDIFITTKVwnd 80
Cdd:cd19089 8 GLHLPAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENfgrilkRDLRPYRDELVISTKA--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 81 dqGYE-------------ETLEAFEKSLKKLQMDYVDLYLIHWPirgkyvD-------TYRALEKLYEEGKVRAIGVSNF 140
Cdd:cd19089 85 --GYGmwpgpygdggsrkYLLASLDQSLKRMGLDYVDIFYHHRY------DpdtpleeTMTALADAVRSGKALYVGISNY 156
|
170 180
....*....|....*....|....
gi 446470145 141 HKHHLELLLPNC---KIKPMVNQV 161
Cdd:cd19089 157 PGAKARRAIALLrelGVPLIIHQP 180
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-253 |
2.79e-08 |
|
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: 53.61 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 9 HNGVKMPMIGLGVYKAKEGD---EVKQAV-KTALEVGYRSIDTATVY-----ENESGVGEAVRESGIP-REDIFITTK-- 76
Cdd:cd19150 7 KSGLKLPALSLGLWHNFGDDtplETQRAIlRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 --VWNDDQG----YEETLEAFEKSLKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVSNFHKHHL 145
Cdd:cd19150 87 ydMWPGPYGewgsRKYLLASLDQSLKRMGLDYVDIFYSHrfdpdTPLE----ETMGALDHAVRSGKALYVGISSYSPERT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 146 E---LLLPNCKIKPMVNQVElHPMLTQF----ELRNFCQGEQIQMEAWSPLMRG------------------GEVFQHPI 200
Cdd:cd19150 163 ReaaAILRELGTPLLIHQPS-YNMLNRWveesGLLDTLQELGVGCIAFTPLAQGlltdkylngipegsraskERSLSPKM 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446470145 201 I-----------QAIATKYEKTPAQVILRWDIQSGIVT---IPKSvTPSRIQENFSIFD-FSLTEEEM 253
Cdd:cd19150 242 LteanlnsiralNEIAQKRGQSLAQMALAWVLRDGRVTsalIGAS-RPEQLEENVGALDnLTFSADEL 308
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
39-139 |
1.08e-07 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 52.13 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 39 EVGYRSIDTATVYENESG---VGEAVRESGIpREDIFITTKVWNDDQGYEE---------------TLEAFEKSLKKLQM 100
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDYKAYEVgkgkavnycgnhkrsLHVSVRDSLRKLQT 123
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446470145 101 DYVDLYLIH-WPIRGKYVDTYRALEKLYEEGKVRAIGVSN 139
Cdd:cd19147 124 DWIDILYVHwWDYTTSIEEVMDSLHILVQQGKVLYLGVSD 163
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
11-192 |
2.81e-07 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 50.91 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 11 GVKMPMIGLGVYKAKEG---DEVKQAVKT-ALEVGYRSIDTATVY---ENESGVGEAVRESGIPREDIFITTKV-WNddq 82
Cdd:cd19141 9 GLRVSCLGLGTWVTFGSqisDEVAEELVTlAYENGINLFDTAEVYaagKAEIVLGKILKKKGWRRSSYVITTKIfWG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 83 GYEET---------LEAFEKSLKKLQMDYVDLYLIHWP-IRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNC 152
Cdd:cd19141 86 GKAETerglsrkhiIEGLKASLERLQLEYVDIVFANRPdPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446470145 153 K----IKPMVNQVELHpmltqfelrnFCQGEQIQME-------------AWSPLMRG 192
Cdd:cd19141 166 RqfnlIPPIVEQAEYH----------LFQREKVEMQlpelfhkigvgamTWSPLACG 212
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
10-192 |
4.48e-07 |
|
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: 50.04 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGVYKAKEG---DEVKQAVKT-ALEVGYRSIDTATVY---ENESGVGEAVRESGIPREDIFITTKV-WNDD 81
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGqisDEVAERLMTiAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 82 QGYEETL------EAFEKSLKKLQMDYVDLYLIHWPIRGKYV-DTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCK- 153
Cdd:cd19159 89 AETERGLsrkhiiEGLKGSLQRLQLEYVDVVFANRPDSNTPMeEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446470145 154 ---IKPMVNQVELHPML---TQFELRNFCQGEQIQMEAWSPLMRG 192
Cdd:cd19159 169 fnmIPPVCEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLACG 213
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
45-139 |
9.69e-07 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 49.34 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 45 IDTATVY---ENESGVGEAVRESGIpREDIFITTKVwndDQGYEETLE-----------------AFEKSLKKLQMDYVD 104
Cdd:cd19146 52 IDTANNYqgeESERWVGEWMASRGN-RDEMVLATKY---TTGYRRGGPikiksnyqgnhakslrlSVEASLKKLQTSYID 127
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446470145 105 LYLIHW-----PIRgkyvDTYRALEKLYEEGKVRAIGVSN 139
Cdd:cd19146 128 ILYVHWwdyttSIP----ELMQSLNHLVAAGKVLYLGVSD 163
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
10-105 |
9.82e-07 |
|
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: 49.21 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGV---YKAKEGDEVKQAVKT-ALEVGYRSIDTATVY---ENESGVGEAVRESGIPREDIFITTKVWNDDQ 82
Cdd:cd19160 11 SGLRVSCLGLGTwvtFGSQISDETAEDLLTvAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVVTTKIYWGGQ 90
|
90 100 110
....*....|....*....|....*....|
gi 446470145 83 GYEE-------TLEAFEKSLKKLQMDYVDL 105
Cdd:cd19160 91 AETErglsrkhIIEGLRGSLDRLQLEYVDI 120
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
14-261 |
2.08e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.04 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 14 MPMIGLGVYKAKEGDEVKQAV-KTALEVGYRSIDTATVY----ENEsgvgeAVRESGIP-REDIFITTKV---------W 78
Cdd:PRK10376 25 MQLAGPGVFGPPKDRDAAIAVlREAVALGVNHIDTSDFYgphvTNQ-----LIREALHPyPDDLTIVTKVgarrgedgsW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 79 NDDQGYEETLEAFEKSLKKLQMDYVDL------YLIHWPIRGKYVDTYRALEKLYEEGKVRAIGVSNFHKHHLElllPNC 152
Cdd:PRK10376 100 LPAFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVA---EAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 153 KIKPMV---NQVEL-H-------PMLTQ--------FELRNFcqgeqiqmeawSPLmrggevfQHPIIQAIATKYEKTPA 213
Cdd:PRK10376 177 KIAEIVcvqNHYNLaHraddaliDALARdgiayvpfFPLGGF-----------TPL-------QSSTLSDVAASLGATPM 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446470145 214 QVILRWDIQ--SGIVTIPKSVTPSRIQENFSIFDFSLTEEEMTQINTLNR 261
Cdd:PRK10376 239 QVALAWLLQrsPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIAR 288
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
10-257 |
2.45e-06 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 48.06 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGVYKA----KEGDEVKQAVKTALEVGYRSIDTATVY-----ENESGVGEAVRESGIP-REDIFITTK--- 76
Cdd:PRK09912 21 SGLRLPALSLGLWHNfghvNALESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 77 -VWNDDQGYEET----LEAFEKSLKKLQMDYVDLYLIH-----WPIRgkyvDTYRALEKLYEEGKVRAIGVSNF---HKH 143
Cdd:PRK09912 101 dMWPGPYGSGGSrkylLASLDQSLKRMGLEYVDIFYSHrvdenTPME----ETASALAHAVQSGKALYVGISSYspeRTQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 144 HLELLLPNCKIKPMVNQVE---LHPMLTQFELRNFCQGEQIQMEAWSPLMRG------------GEVFQHP--------- 199
Cdd:PRK09912 177 KMVELLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqDSRMHREgnkvrgltp 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446470145 200 ------------IIQAIATKYEKTPAQVILRWDIQSGIVT--IPKSVTPSRIQENF-SIFDFSLTEEEMTQIN 257
Cdd:PRK09912 257 kmlteanlnslrLLNEMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVqALNNLTFSTEELAQID 329
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
10-192 |
2.94e-06 |
|
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: 47.77 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 10 NGVKMPMIGLGVYKAKEG---DEVKQAVKT-ALEVGYRSIDTATVY---ENESGVGEAVRESGIPREDIFITTKV-WNDD 81
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGqitDEMAEHLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470145 82 QGYEETL------EAFEKSLKKLQMDYVDLYLIHWPIRGKYV-DTYRALEKLYEEGKVRAIGVSNFHKHHLELLLPNCK- 153
Cdd:cd19158 89 AETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPDPNTPMeETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446470145 154 ---IKPMVNQVELHPML---TQFELRNFCQGEQIQMEAWSPLMRG 192
Cdd:cd19158 169 fnlIPPICEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLACG 213
|
|
| |
