|
Name |
Accession |
Description |
Interval |
E-value |
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-271 |
5.66e-154 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 429.86 E-value: 5.66e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTFEY 89
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 90 FNKSIENLQTDYLDLFLIHWPceADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPYFN 169
Cdd:COG0656 81 FEESLERLGLDYLDLYLIHWP--GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 170 QQELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNL 249
Cdd:COG0656 159 QRELLAFCREHGIVVEAYSPLGRGK-LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFEL 237
|
250 260
....*....|....*....|..
gi 757676546 250 ELTEVAEIDALNRNARQGKNPD 271
Cdd:COG0656 238 SDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-258 |
1.08e-139 |
|
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: 393.39 E-value: 1.08e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 14 MPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTFEYFNKS 93
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 94 IENLQTDYLDLFLIHWPC-----EADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPYF 168
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 169 NQQELQEFCDRHDIKVTAWMPLMRN-RGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDF 247
Cdd:cd19071 161 QQKELVEFCKEHGIVVQAYSPLGRGrRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDF 240
|
250
....*....|.
gi 757676546 248 NLELTEVAEID 258
Cdd:cd19071 241 ELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-261 |
2.04e-129 |
|
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: 367.47 E-value: 2.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTF 87
Cdd:cd19131 4 LNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 88 EYFNKSIENLQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPY 167
Cdd:cd19131 84 RAFDESLRKLGLDYVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIELHPR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 168 FNQQELQEFCDRHDIKVTAWMPLMRNrGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDF 247
Cdd:cd19131 164 FQQRELRAFHAKHGIQTESWSPLGQG-GLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDF 242
|
250
....*....|....
gi 757676546 248 NLELTEVAEIDALN 261
Cdd:cd19131 243 ELDADDMQAIAGLD 256
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-271 |
8.70e-124 |
|
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: 353.62 E-value: 8.70e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISD-EDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKT 86
Cdd:cd19157 4 LNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYDST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPCEadGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHP 166
Cdd:cd19157 84 LKAFEASLERLGLDYLDLYLIHWPVK--GKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQQELQEFCDRHDIKVTAWMPLMRNrGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILD 246
Cdd:cd19157 162 RLTQKELRDYCKKQGIQLEAWSPLMQG-QLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFD 240
|
250 260
....*....|....*....|....*
gi 757676546 247 FNLELTEVAEIDALNRNARQGKNPD 271
Cdd:cd19157 241 FELSQEDMDKIDALNENLRVGPDPD 265
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-261 |
1.09e-119 |
|
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: 342.88 E-value: 1.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMT-KVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKT 86
Cdd:cd19126 3 LNNGTRMPWLGLGVFQTPDGDETeRAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARRT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPceADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHP 166
Cdd:cd19126 83 EDAFQESLDRLGLDYVDLYLIHWP--GKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQQELQEFCDRHDIKVTAWMPLMRNrGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILD 246
Cdd:cd19126 161 YLTQKELRGYCKSKGIVVEAWSPLGQG-GLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFD 239
|
250
....*....|....*
gi 757676546 247 FNLELTEVAEIDALN 261
Cdd:cd19126 240 FELSEDDMTAIDALN 254
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-272 |
1.92e-117 |
|
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: 337.57 E-value: 1.92e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISD-EDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKT 86
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYEST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPCEadGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHP 166
Cdd:cd19156 83 LAAFEESLEKLGLDYVDLYLIHWPVK--GKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQQELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILD 246
Cdd:cd19156 161 LLTQEPLRKFCKEKNIAVEAWSPLGQGK-LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFD 239
|
250 260
....*....|....*....|....*.
gi 757676546 247 FNLELTEVAEIDALNRNARQGKNPDD 272
Cdd:cd19156 240 FELTAEEIRQIDGLNTDHRYGPDPDN 265
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-261 |
4.99e-114 |
|
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: 328.98 E-value: 4.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWN-DYqGYEKT 86
Cdd:cd19127 3 LNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWIsDY-GYDKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPCEADglF---LETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIE 163
Cdd:cd19127 82 LRGFDASLRRLGLDYVDLYLLHWPVPND--FdrtIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 164 VHPYFNQQELQEFCDRHDIKVTAWMPL---MRNRG--------LLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKS 232
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIggvMRYGAsgptgpgdVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKS 239
|
250 260
....*....|....*....|....*....
gi 757676546 233 QTPKRIQENIDILDFNLELTEVAEIDALN 261
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 ... |
8-262 |
2.46e-113 |
|
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: 326.53 E-value: 2.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTF 87
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 88 EYFNKSIENLQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPY 167
Cdd:cd19132 81 RTIEESLYRLGLDYVDLYLIHWPNPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 168 FNQQELQEFCDRHDIKVTAWMPLMRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDF 247
Cdd:cd19132 161 FPQAEQRAYHREHGIVTQSWSPLGRGSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDF 240
|
250
....*....|....*
gi 757676546 248 NLELTEVAEIDALNR 262
Cdd:cd19132 241 ELSDEDMAAIAALDR 255
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
7-261 |
1.49e-108 |
|
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: 314.51 E-value: 1.49e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 7 ILNNGYPMPSVGLGVYKISDEDMT-KVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEK 85
Cdd:cd19133 2 TLNNGVEMPILGFGVFQIPDPEECeRAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 86 TFEYFNKSIENLQTDYLDLFLIHWPCeadGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVH 165
Cdd:cd19133 82 AKKAFERSLKRLGLDYLDLYLIHQPF---GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 166 PYFNQQELQEFCDRHDIKVTAWMPLMRNR-GLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDI 244
Cdd:cd19133 159 PFNQQIEAVEFLKKYGVQIEAWGPFAEGRnNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDI 238
|
250
....*....|....*..
gi 757676546 245 LDFNLELTEVAEIDALN 261
Cdd:cd19133 239 FDFELSDEDMEAIAALD 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-271 |
2.52e-108 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 314.70 E-value: 2.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKtf 87
Cdd:PRK11565 9 LQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKRPR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 88 EYFNKSIENLQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPY 167
Cdd:PRK11565 87 EALEESLKKLQLDYVDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 168 FNQQELQEFCDRHDIKVTAWMPLMR-NRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILD 246
Cdd:PRK11565 167 MQQRQLHAWNATHKIQTESWSPLAQgGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFD 246
|
250 260
....*....|....*....|....*
gi 757676546 247 FNLELTEVAEIDALNRNARQGKNPD 271
Cdd:PRK11565 247 FRLDKDELGEIAKLDQGKRLGPDPD 271
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-266 |
9.47e-105 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 306.13 E-value: 9.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYK-ISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRAL----KDNGVDREDLFITTKLWNDYQG 82
Cdd:cd19116 5 LNDGNEIPAIALGTWKlKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIrekiAEGVVKREDLFITTKLWNSYHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 83 YEKTFEYFNKSIENLQTDYLDLFLIHWP--------CEADGL-------FLETYKAMEELYEQGKVKAIGVCNFNVHHLE 147
Cdd:cd19116 85 REQVEPALRESLKRLGLDYVDLYLIHWPvafkenndSESNGDgslsdidYLETWRGMEDLVKLGLTRSIGVSNFNSEQIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 148 KLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL----MRNRGL----LDDPVIVKIAEKYHKTPAQVVLR 219
Cdd:cd19116 165 RLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvPRGQTNppprLDDPTLVAIAKKYGKTTAQIVLR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 757676546 220 WHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNARQ 266
Cdd:cd19116 245 YLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-260 |
1.76e-104 |
|
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: 304.55 E-value: 1.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 14 MPSVGLGVYKISDEDMT-KVVNVAIDAGYRAFDTAYFYVNEASLGRALKD----NGVDREDLFITTKLWNDYQGYEKTFE 88
Cdd:cd19136 1 MPILGLGTFRLRGEEEVrQAVDAALKAGYRLIDTASVYRNEADIGKALRDllpkYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 89 YFNKSIENLQTDYLDLFLIHWP----CEAD-----GLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMV 159
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgvqgLKPSdprnaELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 160 NQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRG-LLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRI 238
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLrLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 757676546 239 QENIDILDFNLELTEVAEIDAL 260
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-258 |
5.76e-103 |
|
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: 299.96 E-value: 5.76e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 14 MPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTFEYFNKS 93
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 94 IENLQTDYLDLFLIHWPCEADGLfLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPYFNQQEL 173
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNPTVPL-EETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 174 QEFCDRHDIKVTAWMPLMRnRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTE 253
Cdd:cd19073 160 LEYCRENDIVITAYSPLAR-GEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSED 238
|
....*
gi 757676546 254 VAEID 258
Cdd:cd19073 239 VAKID 243
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-261 |
3.31e-98 |
|
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: 288.35 E-value: 3.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 7 ILNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKT 86
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHP 166
Cdd:cd19130 83 AAAFAESLAKLGLDQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQQELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILD 246
Cdd:cd19130 163 AYQQRTIRDWAQAHDVKIEAWSPLGQGK-LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFD 241
|
250
....*....|....*
gi 757676546 247 FNLELTEVAEIDALN 261
Cdd:cd19130 242 FDLTDTEIAAIDALD 256
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-260 |
8.49e-96 |
|
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: 282.68 E-value: 8.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTF 87
Cdd:cd19135 7 LSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYESTK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 88 EYFNKSIENLQTDYLDLFLIHWP-CEADG-----LFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQ 161
Cdd:cd19135 87 QAFEASLKRLGVDYLDLYLLHWPdCPSSGknvkeTRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHVNQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 162 IEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQEN 241
Cdd:cd19135 167 VEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-ALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKEN 245
|
250
....*....|....*....
gi 757676546 242 IDILDFNLELTEVAEIDAL 260
Cdd:cd19135 246 CQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-265 |
3.01e-95 |
|
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: 282.74 E-value: 3.01e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALK-----DNGVDREDLFITTKLWNDYQG 82
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKekvgpGKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 83 YEKTFEYFNKSIENLQTDYLDLFLIHWPC-----------EADGL-------FLETYKAMEELYEQGKVKAIGVCNFNVH 144
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYafergdnpfpkNPDGTirydsthYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 145 HLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL------MRNRG---LLDDPVIVKIAEKYHKTPAQ 215
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpWAKPDepvLLEEPKVKALAKKYNKSPAQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 757676546 216 VVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19106 241 ILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWR 290
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
6-265 |
6.25e-94 |
|
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: 278.91 E-value: 6.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 6 QILNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRAL----KDNGVDREDLFITTKLWNDYQ 81
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 GYEKTFEYFNKSIENLQTDYLDLFLIHWPC-----------EADGLFL------ETYKAMEELYEQGKVKAIGVCNFNVH 144
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPValkkgvgfpesGEDLLSLspipleDTWRAMEELVDKGLCRHIGVSNFSVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 145 HLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL---MRNRG--------LLDDPVIVKIAEKYHKTP 213
Cdd:cd19123 164 KLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLgsgDRPAAmkaegepvLLEDPVINKIAEKHGASP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 757676546 214 AQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19123 244 AQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-265 |
1.23e-93 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 278.53 E-value: 1.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKD---NGV-DREDLFITTKLWNDYQGY 83
Cdd:cd19154 6 LSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHEHAP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 84 EKTFEYFNKSIENLQTDYLDLFLIHWP-----------------CEADGL-FLETYKAMEELYEQGKVKAIGVCNFNVHH 145
Cdd:cd19154 86 EDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmSIHDAVdVEDVWRGMEKVYDEGLTKAIGVSNFNNDQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 146 LEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMR--------------NRGLLDDPVIVKIAEKYHK 211
Cdd:cd19154 166 IQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspAPNLLQDPIVKAIAEKHGK 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 757676546 212 TPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19154 246 TPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-260 |
8.26e-92 |
|
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: 271.82 E-value: 8.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLW-NDYQGY--EKT 86
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWpDNYSPDdfLAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEyfnKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHP 166
Cdd:cd19140 84 VE---ESLRKLRTDYVDLLLLHWP-NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQQELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRII-IPKSQTPKRIQENIDIL 245
Cdd:cd19140 160 YLDQRKLLDAAREHGIALTAYSPLARGE-VLKDPVLQEIGRKHGKTPAQVALRWLLQQEGVAaIPKATNPERLEENLDIF 238
|
250
....*....|....*
gi 757676546 246 DFNLELTEVAEIDAL 260
Cdd:cd19140 239 DFTLSDEEMARIAAL 253
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-265 |
1.85e-91 |
|
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: 271.73 E-value: 1.85e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 7 ILNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKT 86
Cdd:cd19134 4 TLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHP 166
Cdd:cd19134 84 QAACRASLERLGLDYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIELHP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQQELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILD 246
Cdd:cd19134 164 LLNQAELRKVNAQHGIVTQAYSPLGVGR-LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFD 242
|
250
....*....|....*....
gi 757676546 247 FNLELTEVAEIDALNRNAR 265
Cdd:cd19134 243 FELTADHMDALDGLDDGTR 261
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-257 |
6.08e-91 |
|
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: 271.14 E-value: 6.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALK----DNGVDREDLFITTKLWNDYQGY 83
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKklfeDGVVKREDLFITSKLWCTDHAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 84 EKTFEYFNKSIENLQTDYLDLFLIHWPCE--------ADGLFLE-----TYKAMEELYEQGKVKAIGVCNFNVHHLEKLM 150
Cdd:cd19125 85 EDVPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpEPEEVLPpdipsTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 151 AQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL------MRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAH 224
Cdd:cd19125 165 AVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgttWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQR 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 757676546 225 NRIIIPKSQTPKRIQENIDILDFNL---ELTEVAEI 257
Cdd:cd19125 245 GTSVLPKSTNEERIKENIDVFDWSIpeeDFAKFSSI 280
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-265 |
1.34e-85 |
|
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: 258.12 E-value: 1.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 11 GYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRA----LKDNGVDREDLFITTKLWNDYqgYEKT 86
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAiqekIKEQVVKREDLFIVSKLWCTF--HEKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 F--EYFNKSIENLQTDYLDLFLIHWP------------------CEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHL 146
Cdd:cd19107 79 LvkGACQKTLSDLKLDYLDLYLIHWPtgfkpgkelfpldesgnvIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 147 EKLMAQSSIK--PMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMR-NR--------GLLDDPVIVKIAEKYHKTPAQ 215
Cdd:cd19107 159 ERILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpDRpwakpedpSLLEDPKIKEIAAKHNKTTAQ 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 757676546 216 VVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19107 239 VLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-265 |
9.18e-85 |
|
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: 255.50 E-value: 9.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 11 GYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALK---DNG-VDREDLFITTKLWNDYQGYEKT 86
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPC----EADGLFLE--------TYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSS 154
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCgfvnKKDKGERElassdvtsVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 155 IKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL-----------MRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLA 223
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgspgranqslwPDQPDLLEDPTVLAIAKELDKTPAQVLLRFVLQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 757676546 224 HNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19111 241 RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-270 |
1.03e-84 |
|
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: 255.87 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALK---DNG-VDREDLFITTKLWNDYQGY 83
Cdd:cd19112 5 LNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAeafKTGlVKREDLFITTKLWNSDHGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 84 EKtfEYFNKSIENLQTDYLDLFLIHWP--------------CEADGLF-------LE-TYKAMEELYEQGKVKAIGVCNF 141
Cdd:cd19112 85 VI--EACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsaLGEDGVLdidvtisLEtTWHAMEKLVSAGLVRSIGISNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 142 NVHHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL---------MRNRGLLDDPVIVKIAEKYHKT 212
Cdd:cd19112 163 DIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLggaaanaewFGSVSPLDDPVLKDLAKKYGKS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 757676546 213 PAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNARQGKNP 270
Cdd:cd19112 243 AAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-265 |
2.02e-84 |
|
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: 255.14 E-value: 2.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALK---DNG-VDREDLFITTKLWNDYQGY 83
Cdd:cd19155 6 FNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwiDSGkVKREELFIVTKLPPGGNRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 84 EKTFEYFNKSIENLQTDYLDLFLIHWP------------CEADGLF--------LETYKAMEELYEQGKVKAIGVCNFNV 143
Cdd:cd19155 86 EKVEKFLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkLDPTGEHkqdyttdlLDIWKAMEAQVDQGLTRSIGLSNFNR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 144 HHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL--------MRNRG--------LLDDPVIVKIAE 207
Cdd:cd19155 166 EQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfSPGTGspsgsspdLLQDPVVKAIAE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 757676546 208 KYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19155 246 RHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
14-259 |
3.93e-84 |
|
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: 252.92 E-value: 3.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 14 MPSVGLGV----YKIS----DEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEK 85
Cdd:cd19120 4 IPAIAFGTgtawYKSGdddiQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIKDPRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 86 TFEyfnKSIENLQTDYLDLFLIHWPCEADGL---FLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQI 162
Cdd:cd19120 84 ALR---KSLAKLGVDYVDLYLIHSPFFAKEGgptLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAVNQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 163 EVHPYFN--QQELQEFCDRHDIKVTAW---MPLMRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKR 237
Cdd:cd19120 161 EFHPYLYpqQPALLEYCREHGIVVSAYsplSPLTRDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEER 240
|
250 260
....*....|....*....|..
gi 757676546 238 IQENIDILDFNLELTEVAEIDA 259
Cdd:cd19120 241 MKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-262 |
6.48e-83 |
|
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: 250.49 E-value: 6.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 2 LNEIQILNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQ 81
Cdd:cd19117 2 SSKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 gyEKTFEYFNKSIENLQTDYLDLFLIHWPC------------EADGL--------FLETYKAMEELYEQGKVKAIGVCNF 141
Cdd:cd19117 82 --RRVEEALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkKDDGTkdhepdwdFIKTWELMQKLPATGKVKAIGVSNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 142 NVHHLEKLMAQSSIK--PMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL-MRNRGLLDDPVIVKIAEKYHKTPAQVVL 218
Cdd:cd19117 160 SIKNLEKLLASPSAKivPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgSTNAPLLKEPVIIKIAKKHGKTPAQVII 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 757676546 219 RWHLAHNRIIIPKSQTPKRIQENIDIldFNLELTEVAEIDALNR 262
Cdd:cd19117 240 SWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-260 |
1.41e-82 |
|
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: 248.42 E-value: 1.41e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 14 MPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTFEYFNKS 93
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 94 IENLQTDYLDLFLIHWPCEADGLFLETY-KAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMV-NQIEVHPYFNQQ 171
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDEVPVEEYiGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAtNQIELSPYLQNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 172 ELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLEL 251
Cdd:cd19139 161 KLVAHCKQHGIHVTSYMTLAYGK-VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDA 239
|
....*....
gi 757676546 252 TEVAEIDAL 260
Cdd:cd19139 240 DDMAAIAAL 248
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
14-270 |
1.41e-82 |
|
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: 250.26 E-value: 1.41e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 14 MPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRAL----KDNGVDREDLFITTKLWNDYQGYEKTFEY 89
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIrekiKEGVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 90 FNKSIENLQTDYLDLFLIHWP------------------CEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMA 151
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPmgfkpgepdlpldrsgmvIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 152 QSS--IKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRG---LLDDPVIVKIAEKYHKTPAQVVLRWHLAHNR 226
Cdd:cd19110 164 KPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEgvdLIDDPVIQRIAKKHGKSPAQILIRFQIQRNV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 757676546 227 IIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNARQGKNP 270
Cdd:cd19110 244 IVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-260 |
3.41e-78 |
|
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: 238.46 E-value: 3.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKD-----NGVDREDLFITTKLWNDYQG 82
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKEllkeePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 83 YEKTFEYFNKSIENLQTDYLDLFLIHWPC------EADGLF-----------------LETYKAMEELYEQGKVKAIGVC 139
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVafkptgDLNPLTavptnggevdldlsvslVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 140 NFNVHHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRG----LLDDPVIVKIAEKYHKTPAQ 215
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAglplLVQHPEVKAIAAKLGKTPAQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 757676546 216 VVLRWHLAHNRIIIPKSQTPKRIQENIDilDFNLELTEVAEIDAL 260
Cdd:cd19118 241 VLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-265 |
8.00e-78 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 238.47 E-value: 8.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLG----RALKDNGVDREDLFITTKLWNDYQGY 83
Cdd:cd19115 7 LNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGqgvaRAIKEGIVKREDLFIVSKLWNTFHDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 84 EKTFEYFNKSIENLQTDYLDLFLIHWPC---------------EADGLFL--------ETYKAMEELYEQGKVKAIGVCN 140
Cdd:cd19115 87 ERVEPICRKQLADWGIDYFDLFLIHFPIalkyvdpavryppgwFYDGKKVefsnapiqETWTAMEKLVDKGLARSIGVSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 141 FNVHHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAW------------MPLMRNRG-LLDDPVIVKIAE 207
Cdd:cd19115 167 FSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYssfgpqsfleldLPGAKDTPpLFEHDVIKSIAE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 757676546 208 KYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19115 247 KHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-262 |
3.72e-76 |
|
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: 233.18 E-value: 3.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 15 PSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRAL----KDNGVDREDLFITTKLWNDYQGYEKTFEYF 90
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFseifKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 91 NKSIENLQTDYLDLFLIHWPCE----ADGLFL--------------ETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQ 152
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAfdmdTDGDPRddnqiqslskkpleDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 153 SSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMR-----NRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAH--- 224
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGsygdgNLTFLNDSELKALATKYNTTPPQVIIAWHLQKwpk 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 757676546 225 NRIIIPKSQTPKRIQENIDILDFNLElTEvaEIDALNR 262
Cdd:cd19128 242 NYSVIPKSANKSRCQQNFDINDLALT-KE--DMDAINT 276
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
10-253 |
7.59e-76 |
|
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: 232.54 E-value: 7.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLG--VYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALK---DNGV--DREDLFITTKLWNDYQG 82
Cdd:cd19124 1 SGQTMPVIGMGtaSDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGLvkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 83 YEKTFEYFNKSIENLQTDYLDLFLIHWPCE----------ADGLFL-----ETYKAMEELYEQGKVKAIGVCNFNVHHLE 147
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSlkpgkfsfpiEEEDFLpfdikGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 148 KLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNR------GLLDDPVIVKIAEKYHKTPAQVVLRWH 221
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGtkwgsnAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270
....*....|....*....|....*....|..
gi 757676546 222 LAHNRIIIPKSQTPKRIQENIDILDFnlELTE 253
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDW--ELTE 270
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-265 |
8.19e-75 |
|
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: 230.58 E-value: 8.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYK---ISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRAL----KDNGVDREDLFITTKLWNDY 80
Cdd:cd19108 5 LNDGHFIPVLGFGTYApeeVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 81 QGYEKTFEYFNKSIENLQTDYLDLFLIHWPC-----------EADGLFL-------ETYKAMEELYEQGKVKAIGVCNFN 142
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPValkpgeelfpkDENGKLIfdtvdlcATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 143 VHHLEKLMAQSSIK--PMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRG----------LLDDPVIVKIAEKYH 210
Cdd:cd19108 165 RRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDkewvdqnspvLLEDPVLCALAKKHK 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 757676546 211 KTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
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 ... |
8-265 |
2.03e-73 |
|
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: 227.33 E-value: 2.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLG----RALKDNGVDREDLFITTKLWNDYQGY 83
Cdd:cd19113 5 LNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGegvnRAIDEGLVKREELFLTSKLWNNFHDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 84 EKTFEYFNKSIENLQTDYLDLFLIHWP-----------------C-------EADGLFLETYKAMEELYEQGKVKAIGVC 139
Cdd:cd19113 85 KNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfyCgdgdnfvYEDVPILDTWKALEKLVDAGKIKSIGVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 140 NFNVHHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL-------MRNRGLLDDP------VIVKIA 206
Cdd:cd19113 165 NFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFgpqsfveLNQGRALNTPtlfehdTIKSIA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 757676546 207 EKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19113 245 AKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-271 |
1.18e-72 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 223.75 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 13 PMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTFEYFNK 92
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 93 SIENLQTDYLDLFLIHWPCEADGLFLETYkaMEELYE---QGKVKAIGVCNFNVHHLEKLMA---QSSIKpmVNQIEVHP 166
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWPSPNDEVSVEEF--MQALLEakkQGLTREIGISNFTIALMKQAIAavgAENIA--TNQIELSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQQELQEFCDRHDIKVTAWMPLMRNRgLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILD 246
Cdd:PRK11172 158 YLQNRKVVAFAKEHGIHVTSYMTLAYGK-VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQD 236
|
250 260
....*....|....*....|....*
gi 757676546 247 FNLELTEVAEIDALNRNARQgKNPD 271
Cdd:PRK11172 237 LQLDAEDMAAIAALDRNGRL-VSPE 260
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-250 |
1.63e-72 |
|
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: 223.95 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKD---NGVDREDLFITTKLWNDYqgYE 84
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEaiaGGVKREDLFVTTKLWSTY--HR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 85 KTFEYFNKSIENLQTDYLDLFLIHWPC-------------EADGL--------FLETYKAMEELYEQGKVKAIGVCNFNV 143
Cdd:cd19121 84 RVELCLDRSLKSLGLDYVDLYLVHWPVllnpngnhdlfptLPDGSrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSNYSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 144 HHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRG-LLDDPVIVKIAEKYHKTPAQVVLRWHL 222
Cdd:cd19121 164 PYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSpLISDEPVVEIAKKHNVGPGTVLISYQV 243
|
250 260
....*....|....*....|....*...
gi 757676546 223 AHNRIIIPKSQTPKRIQENIDILDFNLE 250
Cdd:cd19121 244 ARGAVVLPKSVTPDRIKSNLEIIDLDDE 271
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
11-265 |
4.86e-71 |
|
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: 221.21 E-value: 4.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 11 GYPMPSVGLGVY---KISDEDMTK-VVNVAIDAGYRAFDTAYFYVNEASLGRALK----DNGVDREDLFITTKLWNDYQG 82
Cdd:cd19109 1 GNSIPIIGLGTYsepKTTPKGACAeAVKVAIDTGYRHIDGAYIYQNEHEVGQAIRekiaEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 83 YEKTFEYFNKSIENLQTDYLDLFLIH-----------WPCEADGLFL-------ETYKAMEELYEQGKVKAIGVCNFNVH 144
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEmpmafkpgdeiYPRDENGKWLyhktnlcATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 145 HLEKLMAQSSIK--PMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRG----------LLDDPVIVKIAEKYHKT 212
Cdd:cd19109 161 QLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 757676546 213 PAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-266 |
1.22e-70 |
|
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: 219.68 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVYKISD--EDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALK----DNGVDREDLFITTKLWNDYq 81
Cdd:cd19119 6 LNTGASIPALGLGTASPHEdrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKVWPTF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 gYEKTFEYFNKSIENLQTDYLDLFLIHWP----CEAD--------------------GLFLETYKAMEELYEQGKVKAIG 137
Cdd:cd19119 85 -YDEVERSLDESLKALGLDYVDLLLVHWPvcfeKDSDdsgkpftpvnddgktryaasGDHITTYKQLEKIYLDGRAKAIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 138 VCNFNVHHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRG-LLDDPVIVKIAEKYHKTPAQV 216
Cdd:cd19119 164 VSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGApNLKNPLVKKIAEKYNVSTGDI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 757676546 217 VLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLEltevaEIDALNRNARQ 266
Cdd:cd19119 244 LISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKE-----DLQKLDDIGEK 288
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
14-258 |
9.80e-68 |
|
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: 210.93 E-value: 9.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 14 MPSVGLGVYKIS---------DEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKdnGVDREDLFITTKLWNDYQ 81
Cdd:cd19072 4 VPVLGLGTWGIGggmskdysdDKKAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIK--GFDREDLFITTKVSPDHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 GYEKTFEYFNKSIENLQTDYLDLFLIHWPCEADGLFlETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSS-IKPMVN 160
Cdd:cd19072 82 KYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIE-ETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKkGPIVAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 161 QIEVHpYFNQQE---LQEFCDRHDIKVTAWMPLmrNRGLL----DDPVIVKIAEKYHKTPAQVVLRWHLAHNRII-IPKS 232
Cdd:cd19072 161 QVEYN-LFDREEesgLLPYCQKNGIAIIAYSPL--EKGKLsnakGSPLLDEIAKKYGKTPAQIALNWLISKPNVIaIPKA 237
|
250 260
....*....|....*....|....*.
gi 757676546 233 QTPKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19072 238 SNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-244 |
5.05e-65 |
|
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: 205.38 E-value: 5.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 9 NNGYPMPSVGLGVYkISDEDMTK-VVNVAIDAGYRAFDTAYFYVNEASLGRALKD----NGVDREDLFITTKLWNDYQGY 83
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRnAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 84 EKTFEYFNKSIENLQTDYLDLFLIHWPC-----------EADG--------LFLETYKAMEELYEQGKVKAIGVCNFNVH 144
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFafqpgdeqdprDANGnviyddgvTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 145 HLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNR--GLLDDPVIVKIAEKYHKTPAQVVLRWHL 222
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMepKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260
....*....|....*....|..
gi 757676546 223 AHNRIIIPKSQTPKRIQENIDI 244
Cdd:cd19129 240 QRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-265 |
1.03e-64 |
|
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: 204.39 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 8 LNNGYPMPSVGLGVY--KISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGRALKD-----NGVDREDLFITTKLWNDY 80
Cdd:cd19122 3 LNNGVKIPAVGFGTFanEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 81 QGYEKTFEYFNKSIENLQTDYLDLFLIHWPCEA------------DGLFL----------ETYKAMEELYEQGKVKAIGV 138
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAekndqrspklgpDGKYVilkdltenpePTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 139 CNFNVHHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMPL-------MRNRGLLDDPVIVKIAEKYHK 211
Cdd:cd19122 163 SNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgsqnqvpSTGERVSENPTLNEVAEKGGY 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 757676546 212 TPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDIldfnLELTEvAEIDALNRNAR 265
Cdd:cd19122 243 SLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS----IELSD-EDFEAINQVAK 291
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-261 |
4.73e-63 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 199.85 E-value: 4.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 16 SVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYV---NEASLGRALKDNGVDREDLFITTKLWNDYQGYEKTFEY--- 89
Cdd:pfam00248 7 QLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVPDGDGPWPSGGSKeni 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 90 ---FNKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHP 166
Cdd:pfam00248 87 rksLEESLKRLGTDYIDLYYLHWP-DPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YF--NQQELQEFCDRHDIKVTAWMPLMrnRGLLD----------------------------DPVIVKIAEKYHKTPAQV 216
Cdd:pfam00248 166 LRrrQEEELLEYCKKNGIPLIAYSPLG--GGLLTgkytrdpdkgpgerrrllkkgtplnleaLEALEEIAKEHGVSPAQV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 757676546 217 VLRWHLAHNR--IIIPKSQTPKRIQENIDILDFNLELTEVAEIDALN 261
Cdd:pfam00248 244 ALRWALSKPGvtIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-265 |
9.40e-63 |
|
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: 199.71 E-value: 9.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 11 GYPMPSVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEASLGR----ALKDNGVDREDLFITTKLWNDYQGYEKT 86
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRgirkAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPC------------------EADGLFLE------TYKAMEELYEQGKVKAIGVCNFN 142
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIpaayvdpaenypflwkdkELKKFPLEqspmqeCWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 143 VHHLEKLMAQSSIKPMVNQIEVHPYFNQQELQEFCDRHDIKVTAWMP------------LMRNRGLLDDPVIVKIAEKYH 210
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSfgnavytkvtkhLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 757676546 211 KTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRNAR 265
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
7-258 |
1.55e-54 |
|
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: 177.44 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 7 ILNNGYPMPSVGLGVYKISD-----EDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDngvDREDLFITTKLWN 78
Cdd:cd19138 4 TLPDGTKVPALGQGTWYMGEdpakrAQEIEALRAGIDLGMTLIDTAEMYGDGGSeelVGEAIRG---RRDKVFLVSKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 79 DYQGYEKTFEYFNKSIENLQTDYLDLFLIHWPCEADglFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPM 158
Cdd:cd19138 81 SNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVP--LAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 159 V-NQIEVH-----PYFnqqELQEFCDRHDIKVTAWMPL----MRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRII 228
Cdd:cd19138 159 AaNQVLYNlgsrgIEY---DLLPWCREHGVPVMAYSPLaqggLLRRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVI 235
|
250 260 270
....*....|....*....|....*....|.
gi 757676546 229 -IPKSQTPKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19138 236 aIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
23-263 |
1.67e-49 |
|
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: 165.07 E-value: 1.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNgvdREDLFITTKLWNDYQGYEKTFEYFNKSIENLQT 99
Cdd:cd19085 19 DQDDEESIATIHAALDAGINFFDTAEAYgdgHSEEVLGKALKGR---RDDVVIATKVSPDNLTPEDVRKSCERSLKRLGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 100 DYLDLFLIHWP-CEADglFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKpmVNQIevhPYfN------QQE 172
Cdd:cd19085 96 DYIDLYQIHWPsSDVP--LEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQL---PY-NllwraiEYE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 173 LQEFCDRHDIKVTAWMPLMrnRGLL--------DDPV-------------------------IVKIAEKYHKTPAQVVLR 219
Cdd:cd19085 168 ILPFCREHGIGVLAYSPLA--QGLLtgkfssaeDFPPgdartrlfrhfepgaeeetfealekLKEIADELGVTMAQLALA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 757676546 220 WHLAHNRI--IIPKSQTPKRIQENIDILDFNLELTEVAEIDALNRN 263
Cdd:cd19085 246 WVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
18-270 |
1.50e-48 |
|
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: 163.43 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 18 GLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDngVDREDLFITTKLWNDYQG--------YEKT 86
Cdd:COG0667 24 GGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKG--RPRDDVVIATKVGRRMGPgpngrglsREHI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQS-SIKPMV-NQIEv 164
Cdd:COG0667 102 RRAVEASLRRLGTDYIDLYQLHRP-DPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAeGLPPIVaVQNE- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 165 hpY--FNQ---QELQEFCDRHDIKVTAWMPLmrNRGLL------------DD-------------------PVIVKIAEK 208
Cdd:COG0667 180 --YslLDRsaeEELLPAARELGVGVLAYSPL--AGGLLtgkyrrgatfpeGDraatnfvqgylternlalvDALRAIAAE 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757676546 209 YHKTPAQVVLRWHLAHNRII--IPKSQTPKRIQENIDILDFNLELTEVAEIDALnrnARQGKNP 270
Cdd:COG0667 256 HGVTPAQLALAWLLAQPGVTsvIPGARSPEQLEENLAAADLELSAEDLAALDAA---LAAVPAP 316
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-258 |
4.97e-48 |
|
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: 160.43 E-value: 4.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 11 GYPMPSVGLGVYKIS---------DEDMTKVVNVAIDAGYRAFDTAYFYV---NEASLGRALKDngVDREDLFITTKLWN 78
Cdd:cd19137 1 GEKIPALGLGTWGIGgfltpdysrDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 79 DYQGYEKTFEYFNKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPM 158
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP-NPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 159 VNQIEVHPY---FNQQELQEFCDRHDIKVTAWMPLMRNRGLLDDpVIVKIAEKYHKTPAQVVLRWHLAH-NRIIIPKSQT 234
Cdd:cd19137 158 CNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLEKTNR-TLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGR 236
|
250 260
....*....|....*....|....
gi 757676546 235 PKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19137 237 VEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
23-258 |
1.94e-47 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 160.00 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNgvdREDLFITTK---LWNDYQGYEK--TFEYFNKSI 94
Cdd:cd19084 21 EVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKcglRWDGGKGVTKdlSPESIRKEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 95 E----NLQTDYLDLFLIHWPCEaDGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKlmAQSSIKPMVNQIevhPY--F 168
Cdd:cd19084 98 EqslrRLQTDYIDLYQIHWPDP-NTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEE--ARKYGPIVSLQP---PYsmL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 169 NQQ---ELQEFCDRHDIKVTAWMPLMrnRGLL------------DD--------------------PVIVKIAEKYHKTP 213
Cdd:cd19084 172 EREieeELLPYCRENGIGVLPYGPLA--QGLLtgkykkeptfppDDrrsrfpffrgenfeknleivDKLKEIAEKYGKSL 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 757676546 214 AQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19084 250 AQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
5-253 |
9.47e-46 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 155.69 E-value: 9.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 5 IQILNNGYPMPSVGLGVYKISDEDMT-----KVVNVAIDAGYRAFDTA--Y-FYVNEASLGRALKDNGVDREDLFITTK- 75
Cdd:COG4989 4 IKLGASGLSVSRIVLGCMRLGEWDLSpaeaaALIEAALELGITTFDHAdiYgGYTCEALFGEALKLSPSLREKIELQTKc 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 76 ---LWNDyqGYEKTFEYFN-----------KSIENLQTDYLDLFLIHWP---CEADglflETYKAMEELYEQGKVKAIGV 138
Cdd:COG4989 84 girLPSE--ARDNRVKHYDtskehiiasveGSLRRLGTDYLDLLLLHRPdplMDPE----EVAEAFDELKASGKVRHFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 139 CNFNVHHLEKLmaQSSIK-PMV-NQIEVHPY----FNQQELqEFCDRHDIKVTAWMPLmrNRGLL---DDP-------VI 202
Cdd:COG4989 158 SNFTPSQFELL--QSALDqPLVtNQIELSLLhtdaFDDGTL-DYCQLNGITPMAWSPL--AGGRLfggFDEqfprlraAL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 757676546 203 VKIAEKYHKTPAQVVLRWHLAHNRIIIP--KSQTPKRIQENIDILDFNLELTE 253
Cdd:COG4989 233 DELAEKYGVSPEAIALAWLLRHPAGIQPviGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
24-258 |
1.63e-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: 154.69 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 24 ISDEDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNGvDREDLFITTKLW-----NDYQGYEKTFEyfnKSIE 95
Cdd:cd19093 23 YGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSerlLGRFLKELG-DRDEVVIATKFAplpwrLTRRSVVKALK---ASLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 96 NLQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEK---LMAQSSIKPMVNQIE---VHPYFN 169
Cdd:cd19093 99 RLGLDSIDLYQLHWPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRahkALKERGVPLASNQVEyslLYRDPE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 170 QQELQEFCDRHDIKVTAWMPLM---------------RNRGLL--------DDPVIV---KIAEKYHKTPAQVVLRWHLA 223
Cdd:cd19093 179 QNGLLPACDELGITLIAYSPLAqglltgkyspenpppGGRRRLfgrknlekVQPLLDaleEIAEKYGKTPAQVALNWLIA 258
|
250 260 270
....*....|....*....|....*....|....*
gi 757676546 224 HNRIIIPKSQTPKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19093 259 KGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-243 |
4.27e-42 |
|
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: 144.20 E-value: 4.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 15 PSVGLGVY----KISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNGVdREDLFITTKLWNDYQGYEKTF 87
Cdd:cd06660 1 SRLGLGTMtfggDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 88 EY--------FNKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMA----QSSI 155
Cdd:cd06660 80 RLspehirrdLEESLRRLGTDYIDLYYLHRD-DPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAyakaHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 156 KPMVNQIE---VHPYFNQQELQEFCDRHDIKVTAWMPLmrNRGllddpvivkiaekyhktPAQVVLRWHLAHNR--IIIP 230
Cdd:cd06660 159 GFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPL--ARG-----------------PAQLALAWLLSQPFvtVPIV 219
|
250
....*....|...
gi 757676546 231 KSQTPKRIQENID 243
Cdd:cd06660 220 GARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-253 |
1.67e-39 |
|
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: 139.23 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 9 NNGYPMPSVGLGVYKISDEDMT-----KVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNGVDREDLFITTK--LWN 78
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESaeellSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 79 DYQGYEKTFEYFN-----------KSIENLQTDYLDLFLIHWPC---EADglflETYKAMEELYEQGKVKAIGVCNFNVH 144
Cdd:cd19092 81 GDDPRPGRIKHYDtskehilasveGSLKRLGTDYLDLLLLHRPDplmDPE----EVAEAFDELVKSGKVRYFGVSNFTPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 145 HLEKLMAQSSIKPMVNQIE---VHPYFNQQELQEFCDRHDIKVTAWMPLmrNRGLLDDP----------VIVKIAEKYHK 211
Cdd:cd19092 157 QIELLQSYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPL--GGGRLFGGfderfqrlraALEELAEEYGV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 757676546 212 TPAQVVLRWHLAHNRIIIP--KSQTPKRIQENIDILDFNLELTE 253
Cdd:cd19092 235 TIEAIALAWLLRHPARIQPilGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-243 |
2.32e-34 |
|
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: 124.13 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 17 VGLGVY--------KISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNgvdREDLFITTKLWNDYQGYEK 85
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR---RDKVVIATKFGNRFDGGPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 86 TFEYFNK---------SIENLQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIK 156
Cdd:cd19086 83 RPQDFSPeyireaveaSLKRLGTDYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 157 PMvnQIEVHPyFNQ---QELQEFCDRHDIKVTAWMPLmrNRGLLDDpvivkiaekyhkTPAQVVLRWHLAHNRI--IIPK 231
Cdd:cd19086 163 VV--QVIYNL-LDQrpeEELFPLAEEHGVGVIARVPL--ASGLLTG------------KLAQAALRFILSHPAVstVIPG 225
|
250
....*....|..
gi 757676546 232 SQTPKRIQENID 243
Cdd:cd19086 226 ARSPEQVEENAA 237
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-245 |
5.09e-34 |
|
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: 123.85 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 9 NNGYPMPSVGLGVYKISDEDmTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKdnGVDREDLFITTKLW-----NDY 80
Cdd:cd19105 8 KTGLKVSRLGFGGGGLPRES-PELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASprldkKDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 81 QGYEKTFEyfnKSIENLQTDYLDLFLIHWPCEADGLFL--ETYKAMEELYEQGKVKAIGV-CNFNVHhlEKLMAQSSIKP 157
Cdd:cd19105 85 AELLKSVE---ESLKRLQTDYIDIYQLHGVDTPEERLLneELLEALEKLKKEGKVRFIGFsTHDNMA--EVLQAAIESGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 158 ----MVNQIEVHPYFNQQELQEFCDRHDIKVTAwMPLMRNRGLLDDPVIVKIAEKYhkTPAQVVLRWHLAHNRI--IIPK 231
Cdd:cd19105 160 fdviMVAYNFLNQPAELEEALAAAAEKGIGVVA-MKTLAGGYLQPALLSVLKAKGF--SLPQAALKWVLSNPRVdtVVPG 236
|
250
....*....|....
gi 757676546 232 SQTPKRIQENIDIL 245
Cdd:cd19105 237 MRNFAELEENLAAA 250
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-266 |
9.22e-33 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 123.01 E-value: 9.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 9 NNGYPMPSVGLGV--YKISDED-MTKVVNVAIDAGYRAFDTAYFYVN-EASLGRALKDngvDREDLFITTKL---WNDYQ 81
Cdd:COG1453 8 KTGLEVSVLGFGGmrLPRKDEEeAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKLppwVRDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 GYEKtfeYFNKSIENLQTDYLDLFLIHWPCEADGLF-----LETYKAMEELYEQGKVKAIGvcnFNVHHLEKLmaqssIK 156
Cdd:COG1453 85 DMRK---DLEESLKRLQTDYIDLYLIHGLNTEEDLEkvlkpGGALEALEKAKAEGKIRHIG---FSTHGSLEV-----IK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 157 PMVN-------QIEVHpYFNQ-----QELQEFCDRHDIKVTAwM-PLmrnRG--LLDDPVIVKIAEKYHKTPAQVVLRWH 221
Cdd:COG1453 154 EAIDtgdfdfvQLQYN-YLDQdnqagEEALEAAAEKGIGVII-MkPL---KGgrLANPPEKLVELLCPPLSPAEWALRFL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 757676546 222 LAHNRI--IIPKSQTPKRIQENIDILDFNLELTEvAEIDALNRNARQ 266
Cdd:COG1453 229 LSHPEVttVLSGMSTPEQLDENLKTADNLEPLTE-EELAILERLAEE 274
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-260 |
1.80e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 120.86 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 17 VGLGVYKI------------SDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNgvdREDLFITTK---LWN 78
Cdd:cd19102 4 IGLGTWAIggggwgggwgpqDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 79 D----YQGYEKtfEYFNKSIEN----LQTDYLDLFLIHWPCEADGLfLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLM 150
Cdd:cd19102 81 EegriRRSLKP--ASIRAECEAslrrLGVDVIDLYQIHWPDPDEPI-EEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 151 AQSSI---KPMVNQIEVHpyfNQQELQEFCDRHDIKVTAWMPLmrNRGLL--------------DDP------------- 200
Cdd:cd19102 158 AIHPIaslQPPYSLLRRG---IEAEILPFCAEHGIGVIVYSPM--QSGLLtgkmtpervaslpaDDWrrrspffqepnla 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757676546 201 -------VIVKIAEKYHKTPAQVVLRWHLAHNRII--IPKSQTPKRIQENIDILDFNLELTEVAEIDAL 260
Cdd:cd19102 233 rnlalvdALRPIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
21-260 |
3.95e-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: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 21 VYKISDEDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNgvdREDLFITTKLW-------NDY-QGYEKTFEY 89
Cdd:cd19091 33 WGGVDQEEADRLVDIALDAGINFFDTADVYSEGESeeiLGKALKGR---RDDVLIATKVRgrmgegpNDVgLSRHHIIRA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 90 FNKSIENLQTDYLDLFLIHWPceaDGL--FLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSS----IKPMVNQIe 163
Cdd:cd19091 110 VEASLKRLGTDYIDLYQLHGF---DALtpLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQA- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 164 vhpYFN------QQELQEFCDRHDIKVTAWMPL--------------------MRNRGL----LDDP-------VIVKIA 206
Cdd:cd19091 186 ---YYSllgrdlEHELMPLALDQGVGLLVWSPLaggllsgkyrrgqpapegsrLRRTGFdfppVDRErgydvvdALREIA 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 757676546 207 EKYHKTPAQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILDFNLELTEVAEIDAL 260
Cdd:cd19091 263 KETGATPAQVALAWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-243 |
1.02e-29 |
|
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: 112.33 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 17 VGLGVYKI-------SDEDMTKVVNVAIDAGYRAFDTAYFYVN-EASLGRALKdnGVDREDLFITTKLWNDYQGYEKTFE 88
Cdd:cd19095 3 LGLGTSGIgrvwgvpSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA--GLRRDDLFIATKVGTHGEGGRDRKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 89 YFNK--------SIENLQTDYLDLFLIHWPCEADgLFLETYKAMEELYEQGKVKAIGVCNFNvHHLEKLMAQSSIKpmVN 160
Cdd:cd19095 81 FSPAairasierSLRRLGTDYIDLLQLHGPSDDE-LTGEVLETLEDLKAAGKVRYIGVSGDG-EELEAAIASGVFD--VV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 161 QIEVHPyFNQQELQ--EFCDRHDIKVTAWMPLmrNRGLLDDPVIVKIAEKYHK------------TPAQVVLRWHLAHNR 226
Cdd:cd19095 157 QLPYNV-LDREEEEllPLAAEAGLGVIVNRPL--ANGRLRRRVRRRPLYADYArrpefaaeiggaTWAQAALRFVLSHPG 233
|
250
....*....|....*....
gi 757676546 227 I--IIPKSQTPKRIQENID 243
Cdd:cd19095 234 VssAIVGTTNPEHLEENLA 252
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
23-246 |
6.21e-29 |
|
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: 110.34 E-value: 6.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNgvDREDLFITTKL-WNDYQGYEKTFEYFNKSIENLQ 98
Cdd:cd19096 17 SIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSeeiLGEALKEG--PREKFYLATKLpPWSVKSAEDFRRILEESLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 99 TDYLDLFLIHWPCEADGLF----LETYKAMEELYEQGKVKAIGvcnFNVHhleklMAQSSIKPMVN-------QIEVHpY 167
Cdd:cd19096 95 VDYIDFYLLHGLNSPEWLEkarkGGLLEFLEKAKKEGLIRHIG---FSFH-----DSPELLKEILDsydfdfvQLQYN-Y 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 168 FNQQELQ-----EFCDRHDIKVTAWMPLMRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKS--QTPKRIQE 240
Cdd:cd19096 166 LDQENQAgrpgiEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSgmSTPEQLDE 245
|
....*.
gi 757676546 241 NIDILD 246
Cdd:cd19096 246 NIAAAD 251
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
24-260 |
2.31e-28 |
|
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: 110.20 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 24 ISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKdnGVDREDLFITTKLWNDYQGYEKTF----EYFNKSIEN 96
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLK--EYNRNEVVIATKGAHKFGGDGSVLnnspEFLRSAVEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 97 ----LQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPYFNQQE 172
Cdd:cd19083 108 slkrLNTDYIDLYYIHFP-DGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQREAEED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 173 LQEFCDRHDIKVTAWMPL-------------------MRNR-GLLDDPVIVK----------IAEKYHKTPAQVVLRWHL 222
Cdd:cd19083 187 ILPYCVENNISFIPYFPLasgllagkytkdtkfpdndLRNDkPLFKGERFSEnldkvdklksIADEKGVTVAHLALAWYL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 757676546 223 AHNRI--IIPKSQTPKRIQENIDILDFNLELTEVAEIDAL 260
Cdd:cd19083 267 TRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
5-259 |
2.78e-28 |
|
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: 110.05 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 5 IQILNNGYPMPSVGLGVYKI---------SDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNgvdREDLFI 72
Cdd:cd19149 2 RKLGKSGIEASVIGLGTWAIgggpwwggsDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGR---RDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 73 TTK---LWNDyqgyEKTFEYF--------------------NKSIENLQTDYLDLFLIHWPCEADGLfLETYKAMEELYE 129
Cdd:cd19149 79 ATKcglRWDR----EGGSFFFvrdgvtvyknlspesireevEQSLKRLGTDYIDLYQTHWQDVETPI-EETMEALEELKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 130 QGKVKAIGVCNFNVHHLEKLMAQ---SSIKP---MVN-QIEvhpyfnqQELQEFCDRHDIKVTAWMPLmrNRGLLDDPV- 201
Cdd:cd19149 154 QGKIRAIGASNVSVEQIKEYVKAgqlDIIQEkysMLDrGIE-------KELLPYCKKNNIAFQAYSPL--EQGLLTGKIt 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 202 -------------------------------IVKIAEKYHKTPAQVVLRWHLAH--NRIIIPKSQTPKRIQENIDILDFN 248
Cdd:cd19149 225 pdrefdagdarsgipwfspenrekvlallekWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARKPEQAEENAKAGDIR 304
|
330
....*....|.
gi 757676546 249 LELTEVAEIDA 259
Cdd:cd19149 305 LSAEDIATMRS 315
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
26-261 |
6.40e-28 |
|
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: 109.21 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 26 DEDMT-KVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNGvDREDLFITTKLwndyqgYEKTFEYFN---------- 91
Cdd:cd19079 33 DEEESrPIIKRALDLGINFFDTANVYSGGASeeiLGRALKEFA-PRDEVVIATKV------YFPMGDGPNgrglsrkhim 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 92 ----KSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEVHPY 167
Cdd:cd19079 106 aevdASLKRLGTDYIDLYQIHRW-DYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 168 FN------QQELQEFCDRHDIKVTAWMPLMrnRGLL----------------------------DDPVI---VKIAEKYH 210
Cdd:cd19079 185 YNllyreeEREMIPLCEEEGIGVIPWSPLA--RGRLarpwgdtterrrsttdtaklkydyfteaDKEIVdrvEEVAKERG 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 757676546 211 KTPAQVVLRWHLAHNRIIIP--KSQTPKRIQENIDILDfnLELTEVaEIDALN 261
Cdd:cd19079 263 VSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALD--IKLSEE-EIKYLE 312
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
23-249 |
5.56e-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: 106.14 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKdnGVDREDLFITTKL-W------NDyQGYEKT--FEYF 90
Cdd:cd19074 18 QVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWptgpgpND-RGLSRKhiFESI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 91 NKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSS----IKPMVNQIEVHp 166
Cdd:cd19074 95 HASLKRLQLDYVDIYYCHRY-DPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYN- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFNQ---QELQEFCDRHDIKVTAWMPLmrNRGLLD---DPVIV--------------------------------KIAEK 208
Cdd:cd19074 173 MLWReieEEVIPLCEKNGIGLVVWSPL--AQGLLTgkyRDGIPppsrsratdednrdkkrrlltdenlekvkklkPIADE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 757676546 209 YHKTPAQVVLRWHLAHNRI---IIPKSqTPKRIQENIDILDFNL 249
Cdd:cd19074 251 LGLTLAQLALAWCLRNPAVssaIIGAS-RPEQLEENVKASGVKL 293
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
16-258 |
3.61e-26 |
|
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: 104.24 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 16 SVGLGVYKIS--------DEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNgvdREDLFITTKLWNDYQGYE 84
Cdd:cd19078 6 AIGLGCMGMShgygpppdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF---RDQVVIATKFGFKIDGGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 85 KTFEYFN-----------KSIENLQTDYLDLFLIH-----WPCEadglflETYKAMEELYEQGKVKAIGVCNFNV----- 143
Cdd:cd19078 83 PGPLGLDsrpehirkaveGSLKRLQTDYIDLYYQHrvdpnVPIE------EVAGTMKELIKEGKIRHWGLSEAGVetirr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 144 -HHLEKLMAQSSIKPMVnqiEVHPyfnQQELQEFCDRHDIKVTAWMPLMR------------------------------ 192
Cdd:cd19078 157 aHAVCPVTAVQSEYSMM---WREP---EKEVLPTLEELGIGFVPFSPLGKgfltgkidentkfdegddraslprftpeal 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 193 --NRGLLDdpVIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPK--RIQENIDILDFNLELTEVAEID 258
Cdd:cd19078 231 eaNQALVD--LLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKlsRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
17-197 |
9.01e-26 |
|
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: 103.16 E-value: 9.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 17 VGLGVYKI-------SDEDMT-KVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNGVdREDLFITTKL---WNDYQG 82
Cdd:cd19148 7 IALGTWAIggwmwggTDEKEAiETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYGK-RDRVVIATKVgleWDEGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 83 Y------EKTFEYFNKSIENLQTDYLDLFLIHWPceaDGL--FLETYKAMEELYEQGKVKAIGVCNFNVHHLE---KLMA 151
Cdd:cd19148 86 VvrnsspARIRKEVEDSLRRLQTDYIDLYQVHWP---DPLvpIEETAEALKELLDEGKIRAIGVSNFSPEQMEtfrKVAP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757676546 152 QSSIKPMVN----QIE--VHPYfnqqelqefCDRHDIKVTAWMPLMrnRGLL 197
Cdd:cd19148 163 LHTVQPPYNlferEIEkdVLPY---------ARKHNIVTLAYGALC--RGLL 203
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-243 |
2.41e-25 |
|
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: 100.63 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 17 VGLG---VYKISDEDMTKVVNVAIDAGYRAFDTAYFY-VNEASLGRALKDngvDREDLFITTKLWN-DYQGYEKTFEyfn 91
Cdd:cd19100 14 LGFGggpLGRLSQEEAAAIIRRALDLGINYFDTAPSYgDSEEKIGKALKG---RRDKVFLATKTGArDYEGAKRDLE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 92 KSIENLQTDYLDLFLIHWPCEADGLFLET-----YKAMEELYEQGKVKAIGVCNfnvHHLE--KLMAQS----SIKPMVN 160
Cdd:cd19100 88 RSLKRLGTDYIDLYQLHAVDTEEDLDQVFgpggaLEALLEAKEEGKIRFIGISG---HSPEvlLRALETgefdVVLFPIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 161 QIEVHPYFNQQELQEFCDRHDIKVTAWMPLMRNRGLLDDPVIVKIAekyhktpaqvvLRWHLAHNRI--IIPKSQTPKRI 238
Cdd:cd19100 165 PAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQA-----------LRYALSLPPVdvVIVGMDSPEEL 233
|
....*
gi 757676546 239 QENID 243
Cdd:cd19100 234 DENLA 238
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
37-258 |
4.04e-25 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 101.52 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 37 IDAGYRAFDTAYFY----------VNEASLGRALKDNGvDREDLFITTKL--WNDYQGYEKTFEYFNKSIEN----LQTD 100
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgfPMGPNGPGLSRKHIRRAVEAslrrLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 101 YLDLFLIHWPCEADGLFlETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQS---------SIKPMVNQIEVHPYfnQQ 171
Cdd:cd19081 115 YIDLYQAHWDDPATPLE-ETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSrqhglpryvSLQPEYNLVDRESF--EG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 172 ELQEFCDRHDIKVTAWMPLM------------------------------RNRGLLDdpVIVKIAEKYHKTPAQVVLRWH 221
Cdd:cd19081 192 ELLPLCREEGIGVIPYSPLAggfltgkyrseadlpgstrrgeaakrylneRGLRILD--ALDEVAAEHGATPAQVALAWL 269
|
250 260 270
....*....|....*....|....*....|....*....
gi 757676546 222 LAHNRI--IIPKSQTPKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19081 270 LARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
9-257 |
6.87e-25 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 100.75 E-value: 6.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 9 NNGYPMPSVGLGV-------YKISDEDMTKVVNVAIDAGYRAFDTAYFYV---NEASLGRALKDNgvdREDLFITTK--- 75
Cdd:cd19076 7 TQGLEVSALGLGCmgmsafyGPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR---RDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 76 LWNDYQGYEK---TFEYFNK----SIENLQTDYLDLFLIH-----WPCEadglflETYKAMEELYEQGKVKAIGV--CNF 141
Cdd:cd19076 84 VRDPGSGFRGvdgRPEYVRAaceaSLKRLGTDVIDLYYQHrvdpnVPIE------ETVGAMAELVEEGKVRYIGLseASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 142 N-------VHHLEKLmaQSSIKPMVNQIEvhpyfnqQELQEFCDRHDIKVTAWMPLmrNRGLLDDPV------------- 201
Cdd:cd19076 158 DtirrahaVHPITAV--QSEYSLWTRDIE-------DEVLPTCRELGIGFVAYSPL--GRGFLTGAIkspedlpeddfrr 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757676546 202 -------------------IVKIAEKYHKTPAQVVLRWHLA-HNRII-IPKSQTPKRIQENIDILDFNLELTEVAEI 257
Cdd:cd19076 227 nnprfqgenfdknlklvekLEAIAAEKGCTPAQLALAWVLAqGDDIVpIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
32-250 |
8.22e-24 |
|
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: 96.90 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 32 VVNVAIDAGYRAFDTAYFY---VNEASLGRALKDngvDREDLFITTKL---------WNDYQGYEKTFEYFNKSIENLQT 99
Cdd:cd19088 29 VLRRALELGVNFIDTADSYgpdVNERLIAEALHP---YPDDVVIATKGglvrtgpgwWGPDGSPEYLRQAVEASLRRLGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 100 DYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEklmAQSSIKPMV---NQIEVhpyFNQQ--ELQ 174
Cdd:cd19088 106 DRIDLYQLHRI-DPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIE---EARAIVRIVsvqNRYNL---ANRDdeGVL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757676546 175 EFCDRHDIKVTAWMPLMRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAH--NRIIIPKSQTPKRIQENIDILDFNLE 250
Cdd:cd19088 179 DYCEAAGIAFIPWFPLGGGDLAQPGGLLAEVAARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-264 |
1.04e-22 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 95.20 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 6 QILNNGYPMPSVGLGVYKIS--------DEDMTKVVNVAIDAGYRAFDTAYFYV-NEASLGRALKDNGVDREDLFITTKL 76
Cdd:cd19144 5 TLGRNGPSVPALGFGAMGLSafygppkpDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 77 WNDYQGYEKTF------EYFNKSIE----NLQTDYLDLFLIH-----WPCEadglflETYKAMEELYEQGKVKAIGVCNF 141
Cdd:cd19144 85 GIEKNVETGEYsvdgspEYVKKACEtslkRLGVDYIDLYYQHrvdgkTPIE------KTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 142 NVHHLEKLMAQSSIKPMvnQIEVHPYF-----NQQELQEFCDRHDIKVTAWMPLmrNRGLL-------DD---------- 199
Cdd:cd19144 159 SAETLRRAHAVHPIAAV--QIEYSPFSldierPEIGVLDTCRELGVAIVAYSPL--GRGFLtgairspDDfeegdfrrma 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 200 P---------------VIVKIAEKYHKTPAQVVLRWHLAHNR--IIIPKSQTPKRIQENIDILDFNLELTEVAEIDALNR 262
Cdd:cd19144 235 PrfqaenfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGDdiIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAE 314
|
..
gi 757676546 263 NA 264
Cdd:cd19144 315 EA 316
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
20-255 |
1.32e-22 |
|
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: 94.54 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 20 GVYK-ISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKdnGVDREDLFITTK------LWN---DYQgYEKT 86
Cdd:cd19163 25 GVFGpVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYYLATKvgryglDPDkmfDFS-AERI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 87 FEYFNKSIENLQTDYLDLFLIHWPCEADGL---FLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKpmvnqIE 163
Cdd:cd19163 102 TKSVEESLKRLGLDYIDIIQVHDIEFAPSLdqiLNETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSPVK-----ID 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 164 V-----HPYFNQQELQE---FCDRHDIKV-----TAwMPLMRNRGLLD----DPVI-------VKIAEKYHKTPAQVVLR 219
Cdd:cd19163 177 TvlsycHYTLNDTSLLEllpFFKEKGVGVinaspLS-MGLLTERGPPDwhpaSPEIkeacakaAAYCKSRGVDISKLALQ 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 757676546 220 WHLAHNRII--IPKSQTPKRIQENIDILDFNLELTEVA 255
Cdd:cd19163 256 FALSNPDIAttLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
25-260 |
6.82e-21 |
|
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: 89.94 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 25 SDEDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNgvdREDLFITTKL------WNDYQGYE--KTFEYFNKS 93
Cdd:cd19087 28 DEETSFAIMDRALDAGINFFDTADVYGGGRSeeiIGRWIAGR---RDDIVLATKVfgpmgdDPNDRGLSrrHIRRAVEAS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 94 IENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEK---------LMAQSSIKPMVN---- 160
Cdd:cd19087 105 LRRLQTDYIDLYQMHHF-DRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKaqgiaarrgLLRFVSEQPMYNllkr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 161 QIEVhpyfnqqELQEFCDRHDIKVTAWMPLmrNRGLL----------DDPVIVK---------------IAEKYHK---- 211
Cdd:cd19087 184 QAEL-------EILPAARAYGLGVIPYSPL--AGGLLtgkygkgkrpESGRLVEraryqarygleeyrdIAERFEAlaae 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 757676546 212 ---TPAQVVLRWHLAH----NRIIIPKsqTPKRIQENIDILDFNLELTEVAEIDAL 260
Cdd:cd19087 255 aglTPASLALAWVLSHpavtSPIIGPR--TLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
10-258 |
1.52e-20 |
|
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: 88.84 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLGV-------YKISDEDMTKVVNVAIDAGYRAFDTAYFY------VNEASLGRALKDNGVDREDLFITTK- 75
Cdd:cd19077 1 NGKLVGPIGLGLmgltwrpNPTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 76 -LWNDYQGYEKTFEYFNKSIENL-----QTDYLDLFLI-----HWPCEadglflETYKAMEELYEQGKVKAIGVCNFNVh 144
Cdd:cd19077 81 gLDPDTLRPDGSPEAVRKSIENIlralgGTKKIDIFEParvdpNVPIE------ETIKALKELVKEGKIRGIGLSEVSA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 145 hlEKLMAQSSIKPMV-NQIEVHPYFN---QQELQEFCDRHDIKVTAWMPLmrNRGLL------------DDP-------- 200
Cdd:cd19077 154 --ETIRRAHAVHPIAaVEVEYSLFSReieENGVLETCAELGIPIIAYSPL--GRGLLtgriksladipeGDFrrhldrfn 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757676546 201 ------------VIVKIAEKYHKTPAQVVLRWHLA--HNRII-IPKSQTPKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19077 230 genfeknlklvdALQELAEKKGCTPAQLALAWILAqsGPKIIpIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
15-242 |
1.62e-20 |
|
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: 88.38 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 15 PSVGLGVY-------KISDEDMTKVVNVAIDAGYRAFDTAYFYVN-EASLGRALKdnGVDREDLFITTKL-----WNDYQ 81
Cdd:cd19090 1 SALGLGTAglggvfgGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 GYEKTFEYFNKSIENLQTDYLDLFLIHWPcEADGLFLETYK-----AMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIk 156
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHDP-ERVPWVDILAPggaleALLELKEEGLIKHIGLGGGPPDLLRRAIETGDF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 157 pmvNQIEVHPYFN---QQELQEFCD---RHDIKVTAWMPLMrnRGLL-------------------DDPV--IVKIAEKY 209
Cdd:cd19090 157 ---DVVLTANRYTlldQSAADELLPaaaRHGVGVINASPLG--MGLLagrppervrytyrwlspelLDRAkrLYELCDEH 231
|
250 260 270
....*....|....*....|....*....|....*
gi 757676546 210 HKTPAQVVLRWHLAHNRI--IIPKSQTPKRIQENI 242
Cdd:cd19090 232 GVPLPALALRFLLRDPRIstVLVGASSPEELEQNV 266
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-259 |
2.61e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 88.42 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 24 ISDEDMTKVVNVAIDAGYRAFDTAYFYVN-EASLGRALK---DNGVDREDLFITTKLWNDYQGYEKTFEYFNKSIEN--- 96
Cdd:cd19101 20 RDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKrlrRERDAADDVQIHTKWVPDPGELTMTRAYVEAAIDRslk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 97 -LQTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMaQSSIKPMVNQ-----IEVHPyfnQ 170
Cdd:cd19101 100 rLGVDRLDLVQFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL-DAGVPIVSNQvqyslLDRRP---E 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 171 QELQEFCDRHDIKVTAWMPLMrnRGLL-------DDP-------------------------------VIVKIAEKYHKT 212
Cdd:cd19101 176 NGMAALCEDHGIKLLAYGTLA--GGLLsekylgvPEPtgpaletrslqkyklmidewggwdlfqellrTLKAIADKHGVS 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 757676546 213 PAQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILDFNLELTEVAEIDA 259
Cdd:cd19101 254 IANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
23-260 |
3.80e-20 |
|
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: 88.01 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFY----------VNEASLGRALKDNGvDREDLFITTKL--------WNDYQG-- 82
Cdd:cd19094 14 QNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRGGGtr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 83 --YEKTFEYFNKSIENLQTDYLDLFLIHWP----------------CEADGL-FLETYKAMEELYEQGKVKAIGVCN--- 140
Cdd:cd19094 93 ldRENIREAVEGSLKRLGTDYIDLYQLHWPdrytplfgggyytepsEEEDSVsFEEQLEALGELVKAGKIRHIGLSNetp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 141 FNVHHLEKLMAQSSIKPMVN-QievHPY--FNQQ---ELQEFCDRHDIKVTAWMPL------------------------ 190
Cdd:cd19094 173 WGVMKFLELAEQLGLPRIVSiQ---NPYslLNRNfeeGLAEACHRENVGLLAYSPLaggvltgkyldgaarpeggrlnlf 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 191 MRNRGLLDDP-------VIVKIAEKYHKTPAQVVLRWhlAHNR-----IIIPKSqTPKRIQENIDilDFNLELTE--VAE 256
Cdd:cd19094 250 PGYMARYRSPqaleavaEYVKLARKHGLSPAQLALAW--VRSRpfvtsTIIGAT-TLEQLKENID--AFDVPLSDelLAE 324
|
....
gi 757676546 257 IDAL 260
Cdd:cd19094 325 IDAV 328
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-260 |
1.97e-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: 85.85 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 13 PMPSVGLGVY---------------KISDEDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDngVDREDLFITT 74
Cdd:cd19103 3 KLPKIALGTWswgsggaggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASekiLGEFLKR--YPREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 75 KLWND--YQGYEKTFEYFNKSIENLQTDYLDLFLIHWPCEADGLFLEtykaMEELYEQGKVKAIGVCNFNVHHLEK---L 149
Cdd:cd19103 81 KFTPQiaGQSADPVADMLEGSLARLGTDYIDIYWIHNPADVERWTPE----LIPLLKSGKVKHVGVSNHNLAEIKRaneI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 150 MAQSSIKpmVNQIEVH---PYFNQQE--LQEFCDRHDIKVTAWMPLmrNRGLLDDP------------------------ 200
Cdd:cd19103 157 LAKAGVS--LSAVQNHyslLYRSSEEagILDYCKENGITFFAYMVL--EQGALSGKydtkhplpegsgraetynpllpql 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757676546 201 -----VIVKIAEKYHKTPAQVVLRWHLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEIDAL 260
Cdd:cd19103 233 eeltaVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
23-246 |
4.64e-18 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 81.83 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFY-------VNEASLGRALKDNGVdREDLFITTK-----LWNDYQG--YEKTFE 88
Cdd:cd19082 13 RIDEEEAFALLDAFVELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-RDKVVIATKgghpdLEDMSRSrlSPEDIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 89 Y-FNKSIENLQTDYLDLFLIHwpceAD------GLFLETykaMEELYEQGKVKAIGVCNFNV------------HHLEKL 149
Cdd:cd19082 92 AdLEESLERLGTDYIDLYFLH----RDdpsvpvGEIVDT---LNELVRAGKIRAFGASNWSTeriaeanayakaHGLPGF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 150 MA---QSSIKPMVNQIEVHP--YFNQQELQEFCDRHDIKVTAWMPL-------MRNRGLLDDPVIVK------------- 204
Cdd:cd19082 165 AAsspQWSLARPNEPPWPGPtlVAMDEEMRAWHEENQLPVFAYSSQargffskRAAGGAEDDSELRRvyyseenferler 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 757676546 205 ---IAEKYHKTPAQVVLRWhLAHNR-----IIIPksQTPKRIQENIDILD 246
Cdd:cd19082 245 akeLAEEKGVSPTQIALAY-VLNQPfptvpIIGP--RTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-246 |
6.49e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 81.61 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFYV----------NEASLGRALKDNGVdREDLFITTKLWNDYQGYEKTFEYF-- 90
Cdd:cd19752 13 RTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvggeSERLIGRWLKDRGN-RDDVVIATKVGAGPRDPDGGPESPeg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 91 ----------NKSIENLQTDYLDLFLIH-----WPCEadglflETYKAMEELYEQGKVKAIGVCNFNVHHLEK---LMAQ 152
Cdd:cd19752 92 lsaetieqeiDKSLRRLGTDYIDLYYAHvddrdTPLE------ETLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 153 SSIKPMVNQIEVHPYF---------NQ----QELQEFCDRH-DIKVTAWMPLMrnRGLLDDP------------------ 200
Cdd:cd19752 166 QGWAEFSAIQQRHSYLrprpgadfgVQrivtDELLDYASSRpDLTLLAYSPLL--SGAYTRPdrplpeqydgpdsdarla 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 757676546 201 VIVKIAEKYHKTPAQVVLRWHLAHNRIIIP--KSQTPKRIQENIDILD 246
Cdd:cd19752 244 VLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLAALD 291
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
16-248 |
6.82e-17 |
|
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: 78.81 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 16 SVGLGVYKISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDngVDREDLFITTKL---------------- 76
Cdd:cd19152 9 PLGNLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYgagLSEERLGAALRE--LGREDYVISTKVgrllvplqeveptfep 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 77 --WND----------YQGYEKTFEyfnKSIENLQTDYLDLFLIH----------WPCEADGLFLETYKAMEELYEQGKVK 134
Cdd:cd19152 87 gfWNPlpfdavfdysYDGILRSIE---DSLQRLGLSRIDLLSIHdpdedlagaeSDEHFAQAIKGAFRALEELREEGVIK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 135 AIGV-CNFnVHHLEKLMAQSSIKPMVNQIEVHPYfNQQELQEF---CDRHDIKVTAWMPLmrNRGLL------------- 197
Cdd:cd19152 164 AIGLgVND-WEVILRILEEADLDWVMLAGRYTLL-DHSAARELlpeCEKRGVKVVNAGPF--NSGFLaggdnfdyyeygp 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 198 -DDPVIVK------IAEKYHKTPAQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILDFN 248
Cdd:cd19152 240 aPPELIARrdrieaLCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALLATE 299
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-138 |
3.45e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 76.41 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFYVN-EASLGRALKDNgvdrEDLFITTKL---WNDYQGYEKTFE-YFNKSIENL 97
Cdd:cd19097 22 KPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL----DKFKIITKLpplKEDKKEDEAAIEaSVEASLKRL 97
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 757676546 98 QTDYLDLFLIHWPCEADGLFLETYKAMEELYEQGKVKAIGV 138
Cdd:cd19097 98 KVDSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGV 138
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
16-158 |
1.72e-15 |
|
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: 74.88 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 16 SVGLG-VYKISDE--DMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNGVDREDLFITTKLWndyQGYEKTFEY 89
Cdd:cd19153 19 TAALGgVYGDGLEqdEAVAIVAEAFAAGINHFDTSPYYGAESSeavLGKALAALQVPRSSYTVATKVG---RYRDSEFDY 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757676546 90 --------FNKSIENLQTDYLDLFLIH--WPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPM 158
Cdd:cd19153 96 saervrasVATSLERLHTTYLDVVYLHdiEFVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSL 174
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
25-258 |
1.73e-15 |
|
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: 74.95 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 25 SDEDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNgvdREDLFITTKL-WND------YQGYEKT--FEYFNK 92
Cdd:cd19080 29 DREEARAMFDAYVEAGGNFIDTANNYTNGTSerlLGEFIAGN---RDRIVLATKYtMNRrpgdpnAGGNHRKnlRRSVEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 93 SIENLQTDYLDLFLIHW-----PCEadglflETYKAMEELYEQGKVKAIGVCNF------------NVHHLEklmaqssi 155
Cdd:cd19080 106 SLRRLQTDYIDLLYVHAwdfttPVE------EVMRALDDLVRAGKVLYVGISDTpawvvarantlaELRGWS-------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 156 kPMVN-QIEvhpyFN------QQELQEFCDRHDIKVTAWMPLM-------------------------------RNRGLL 197
Cdd:cd19080 172 -PFVAlQIE----YSllertpERELLPMARALGLGVTPWSPLGgglltgkyqrgeegrageakgvtvgfgklteRNWAIV 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757676546 198 DdpVIVKIAEKYHKTPAQVVLRWHLAHNRIIIP--KSQTPKRIQENIDILDFNLELTEVAEID 258
Cdd:cd19080 247 D--VVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-229 |
1.96e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 74.66 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 16 SVGLGVYKIS-----DEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALK----DNGVDREDLFITTK-------- 75
Cdd:cd19099 5 SLGLGTYRGDsddetDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRelieKGGIKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 76 ---------LWNDYQGYEKTFEY----------------FNKSIENLQTDYLDLFLIHWP------CEADGLF---LETY 121
Cdd:cd19099 85 deplrplkyLEEKLGRGLIDVADsaglrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqlleLGEEEFYdrlEEAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 122 KAMEELYEQGKVKAIGV----------CNFNVHHLEKLMA---------------QSSIKPMVNQIEVHPYFNQQELQ-- 174
Cdd:cd19099 165 EALEEAVAEGKIRYYGIstwdgfrappALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLEPEALTEKNTVKGEALsl 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 757676546 175 -EFCDRHDIKVTAWMPLMRNRGLLDDPVIVKIAEKYHKTPAQVVLRWHLAHNRIII 229
Cdd:cd19099 245 lEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGATLAQRALQFARSTPGVDS 300
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
23-259 |
2.14e-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: 74.55 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 23 KISDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNGVDREDLFITTKL-WNDYQGYEKT--------FEYF 90
Cdd:cd19143 27 QVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGGGGPPPNDrglsrkhiVEGT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 91 NKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKV--------------KAIGVCnfNVHHLeklmaqssIK 156
Cdd:cd19143 107 KASLKRLQLDYVDLVFCHRP-DPATPIEETVRAMNDLIDQGKAfywgtsewsaqqieEAHEIA--DRLGL--------IP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 157 PMVNQievhPYFN-------QQELQEFCDRHDIKVTAWMPL--------------------------MRNRGLLDDPVIV 203
Cdd:cd19143 176 PVMEQ----PQYNlfhrervEVEYAPLYEKYGLGTTTWSPLasglltgkynngipegsrlalpgyewLKDRKEELGQEKI 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757676546 204 -------KIAEKYHKTPAQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILDFNLELTE--VAEIDA 259
Cdd:cd19143 252 ekvrklkPIAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEENLKALEVLPKLTPevMEKIEA 318
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-260 |
3.38e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 74.22 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 25 SDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNgvdREDLFITTK----LWNDYQGYEKTFEYFNKSIENL 97
Cdd:cd19104 30 TREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL---PAGPYITTKvrldPDDLGDIGGQIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 98 QTDYLDLFLIH--------WPCEA-----DGLFL-ETYKAMEELYEQGKVKAIG-VCNFNVHHLEKLMAQ---SSIKPMV 159
Cdd:cd19104 107 KRDSVDLLQLHnrigderdKPVGGtlsttDVLGLgGVADAFERLRSEGKIRFIGiTGLGNPPAIRELLDSgkfDAVQVYY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 160 N------QIEVHPYFNQQELQEFCDR---HDIKVTAWMPLMR-------NRGLLDDPVI--------------VKIAEKY 209
Cdd:cd19104 187 NllnpsaAEARPRGWSAQDYGGIIDAaaeHGVGVMGIRVLAAgalttslDRGREAPPTSdsdvaidfrraaafRALAREW 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 757676546 210 HKTPAQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILDFN-LELTEVAEIDAL 260
Cdd:cd19104 267 GETLAQLAHRFALSNPGVstVLVGVKNREELEEAVAAEAAGpLPAENLARLEAL 320
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
10-190 |
6.49e-14 |
|
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: 70.57 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLGVYK-----ISDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNGVDREDLFITTKLWNDYQ 81
Cdd:cd19142 9 SGLRVSNVGLGTWStfstaISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIYWSYG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 GYEKTF------EYFNKSIENLQTDYLDLFLIHwpcEADGL--FLETYKAMEELYEQGKVKAIGVCNFN-VHHLEKLMAQ 152
Cdd:cd19142 89 SEERGLsrkhiiESVRASLRRLQLDYIDIVIIH---KADPMcpMEEVVRAMSYLIDNGLIMYWGTSRWSpVEIMEAFSIA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 757676546 153 ---SSIKPMVNQIEVHPYFNQQ-ELQ--EFCDRHDIKVTAWMPL 190
Cdd:cd19142 166 rqfNCPTPICEQSEYHMFCREKmELYmpELYNKVGVGLITWSPL 209
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
27-260 |
1.34e-13 |
|
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: 69.51 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 27 EDMTKVVNVAIDAGYRAFDTAYFYVNEAS---LGRALKDNgvdrEDLFITTKlWNDYQG----YEKTFEYFNKSIENLQT 99
Cdd:cd19075 20 EAAAELLDAFLERGHTEIDTARVYPDGTSeelLGELGLGE----RGFKIDTK-ANPGVGgglsPENVRKQLETSLKRLKV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 100 DYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLEKLM----AQSSIKPMVNQ---------IEvhp 166
Cdd:cd19075 95 DKVDVFYLHAP-DRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVeickENGWVLPTVYQgmynaitrqVE--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 yfnqQELQEFCDRHDIK------------------------------VTAWMPLMRNR-------GLLDdpVIVKIAEKY 209
Cdd:cd19075 171 ----TELFPCLRKLGIRfyaysplaggfltgkykysedkagggrfdpNNALGKLYRDRywkpsyfEALE--KVEEAAEKE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757676546 210 HKTPAQVVLRWhLAHN---------RIIIPKSqTPKRIQENIDILDFN-LELTEVAEIDAL 260
Cdd:cd19075 245 GISLAEAALRW-LYHHsaldgekgdGVILGAS-SLEQLEENLAALEKGpLPEEVVKAIDEA 303
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
30-138 |
1.05e-12 |
|
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: 66.92 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 30 TKVVNVAIDAGYRAFDTAYFYVN-EASLGRALKD--NGVDREDLFITTKLwndyqGYE--KTFEY--------FNKSIEN 96
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGPsEIILGRALKAlrDEFPRDTYFIITKV-----GRYgpDDFDYspewirasVERSLRR 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 757676546 97 LQTDYLDLFLIHwPCE--ADGLFLETYKAMEELYEQGKVKAIGV 138
Cdd:cd19164 112 LHTDYLDLVYLH-DVEfvADEEVLEALKELFKLKDEGKIRNVGI 154
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
24-257 |
1.70e-12 |
|
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: 66.30 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 24 ISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDnGVdREDLFITTKLWNDYQGYEK-----TFEYF----N 91
Cdd:cd19145 30 KPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKD-GP-REKVQLATKFGIHEIGGSGvevrgDPAYVraacE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 92 KSIENLQTDYLDLFLIHW-----PCEadglflETYKAMEELYEQGKVKAIGVCNFNVHHLEKLMAQSSIKPMvnQIEVHP 166
Cdd:cd19145 108 ASLKRLDVDYIDLYYQHRidttvPIE------ITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVHPITAV--QLEWSL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 167 YFN--QQELQEFCDRHDIKVTAWMPLMRN---------RGLLDDPV---------------------IVKIAEKYHKTPA 214
Cdd:cd19145 180 WTRdiEEEIIPTCRELGIGIVPYSPLGRGffagkakleELLENSDVrkshprfqgenleknkvlyerVEALAKKKGCTPA 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 757676546 215 QVVLRW--HLAHNRIIIPKSQTPKRIQENIDILDFNLELTEVAEI 257
Cdd:cd19145 260 QLALAWvlHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
15-138 |
1.78e-12 |
|
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: 65.84 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 15 PSVGLG------VYKISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNgvDREDLFITTKL--------W 77
Cdd:cd19162 1 PRLGLGaaslgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH--PRAEYVVSTKVgrllepgaA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 78 NDYQGYEKTFEY--------FNKSIENLQTDYLDLFLIHWPCEADGLFL-ETYKAMEELYEQGKVKAIGV 138
Cdd:cd19162 79 GRPAGADRRFDFsadgirrsIEASLERLGLDRLDLVFLHDPDRHLLQALtDAFPALEELRAEGVVGAIGV 148
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
9-138 |
6.38e-12 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 64.80 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 9 NNGYPMPSVGLG------VY-KISDEDMTKVVNVAIDAGYRAFDTAYFY---VNEASLGRALKDNGVDREDLFITTKLWN 78
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFgPVSEEDAIASVREAFRLGINFFDTSPYYggtLSEKVLGKALKALGIPREKYVVSTKCGR 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757676546 79 DYQGY----EKTFEYFNKSIENLQTDYLDLFLIHwPCE---ADGLFLETYKAMEELYEQGKVKAIGV 138
Cdd:PLN02587 86 YGEGFdfsaERVTKSVDESLARLQLDYVDILHCH-DIEfgsLDQIVNETIPALQKLKESGKVRFIGI 151
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-246 |
7.93e-11 |
|
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: 61.57 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 15 PSVGLG------VYK-ISDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNgvDREDLFITTKL-------- 76
Cdd:cd19161 1 SELGLGtaglgnLYTaVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREK--PRDEFVLSTKVgrllkpar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 77 ---------WNDYQGYEKTFEY--------FNKSIENLQTDYLDLFLIH----------WPCEADGLFLET-YKAMEELY 128
Cdd:cd19161 79 egsvpdpngFVDPLPFEIVYDYsydgimrsFEDSLQRLGLNRIDILYVHdigvythgdrKERHHFAQLMSGgFKALEELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 129 EQGKVKAIGVCNFNVHHLEKLMAQSSIKPMVNQIEvHPYFNQQELQEF---CDRHDIKVTAWMPLmrNRGLLDDPV---- 201
Cdd:cd19161 159 KAGVIKAFGLGVNEVQICLEALDEADLDCFLLAGR-YSLLDQSAEEEFlprCEQRGTSLVIGGVF--NSGILATGTksga 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757676546 202 -----------------IVKIAEKYHKTPAQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILD 246
Cdd:cd19161 236 kfnygdapaeiisrvmeIEKICDAYNVPLAAAALQFPLRHPAVasVLTGARNPAQLRQNVEAFQ 299
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
10-263 |
4.10e-10 |
|
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: 59.29 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLGVY-----KISDEDMTKVVNVAIDAGYRAFDTAYFYV---NEASLGRALKDNGVDREDLFITTKL-WNDY 80
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAagkAEVILGSIIKKKGWRRSSLVITTKLyWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 81 QGYEK------TFEYFNKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVhhLEKLMAQSS 154
Cdd:cd19159 89 AETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA--MEIMEAYSV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 155 ------IKPMVNQIEVHPYFNQQ---ELQEFCDRHDIKVTAWMPL--------------------MRNRGLLDDPVI--- 202
Cdd:cd19159 166 arqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygngvpessrasLKCYQWLKERIVsee 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757676546 203 -----------VKIAEKYHKTPAQVVLRWHLAHNRI--IIPKSQTPKRIQENIDILDFNLELTE--VAEIDALNRN 263
Cdd:cd19159 246 grkqqnklkdlSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGAIQVLPKMTShvVNEIDNILRN 321
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
16-140 |
5.24e-10 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 59.10 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 16 SVGLGVYKI----SDEDMTKVVNVAIDAGYRAFDTAYFY----------VNEASLGRALKDNGvDREDLFITTKLWNDYQ 81
Cdd:PRK10625 15 TLGLGTMTFgeqnSEADAHAQLDYAVAQGINLIDVAEMYpvpprpetqgLTETYIGNWLAKRG-SREKLIIASKVSGPSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 82 GYEKTF------------EYFNKSIENLQTDYLDLFLIHWPCEADGLF----------------LETYKAMEELYEQGKV 133
Cdd:PRK10625 94 NNDKGIrpnqaldrknirEALHDSLKRLQTDYLDLYQVHWPQRPTNCFgklgyswtdsapavslLETLDALAEQQRAGKI 173
|
....*..
gi 757676546 134 KAIGVCN 140
Cdd:PRK10625 174 RYIGVSN 180
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
10-190 |
8.79e-10 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 58.56 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLGVY-----KISDEDMTKVVNVAIDAGYRAFDTAYFYV---NEASLGRALKDNGVDREDLFITTKL-WNDY 80
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAagkAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 81 QGYEK------TFEYFNKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVhhLEKLMAQSS 154
Cdd:cd19158 89 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRP-DPNTPMEETVRAMTHVINQGMAMYWGTSRWSS--MEIMEAYSV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 757676546 155 ------IKPMVNQIEVHPYFNQQ---ELQEFCDRHDIKVTAWMPL 190
Cdd:cd19158 166 arqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPL 210
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
17-191 |
1.69e-09 |
|
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: 57.46 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 17 VGLGVY-----KISDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNGVDREDLFITTKL-WNDYQGYEKTF 87
Cdd:cd19141 15 LGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYAAgkaEIVLGKILKKKGWRRSSYVITTKIfWGGKAETERGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 88 ------EYFNKSIENLQTDYLDLFLI-----HWPCEadglflETYKAMEELYEQGKVKAIGVCNFNVhhLEKLMAQSS-- 154
Cdd:cd19141 95 srkhiiEGLKASLERLQLEYVDIVFAnrpdpNTPME------EIVRAFTHVINQGMAMYWGTSRWSA--MEIMEAYSVar 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 757676546 155 ----IKPMVNQIEVHpyFNQQE-----LQEFCDRHDIKVTAWMPLM 191
Cdd:cd19141 167 qfnlIPPIVEQAEYH--LFQREkvemqLPELFHKIGVGAMTWSPLA 210
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
10-190 |
2.93e-09 |
|
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: 56.92 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 10 NGYPMPSVGLGVY-----KISDEDMTKVVNVAIDAGYRAFDTAYFYVN---EASLGRALKDNGVDREDLFITTKL-WNDY 80
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIyWGGQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 81 QGYEK------TFEYFNKSIENLQTDYLDLFLIHwPCEADGLFLETYKAMEELYEQGKVKAIGVCNFNVhhLEKLMAQSS 154
Cdd:cd19160 91 AETERglsrkhIIEGLRGSLDRLQLEYVDIVFAN-RSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSA--MEIMEAYSV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 757676546 155 ------IKPMVNQIEVHPYFNQQ---ELQEFCDRHDIKVTAWMPL 190
Cdd:cd19160 168 arqfnlIPPVCEQAEYHLFQREKvemQLPELYHKIGVGSVTWSPL 212
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
38-140 |
2.23e-08 |
|
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: 54.06 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 38 DAGYRAFDTAYFYVNEAS---LGRALKDNGvDREDLFITTKLWNDYQGYE----KTFEY-----------FNKSIENLQT 99
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGEWMKSRK-NRDQIVIATKFTTDYKAYEvgkgKAVNYcgnhkrslhvsVRDSLRKLQT 123
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 757676546 100 DYLDLFLIHWpCEADGLFLETYKAMEELYEQGKVKAIGVCN 140
Cdd:cd19147 124 DWIDILYVHW-WDYTTSIEEVMDSLHILVQQGKVLYLGVSD 163
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
13-257 |
3.10e-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: 53.80 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 13 PMPSVGL----GVYKiSDEDMTKVVNVAIDAGYRAFDTAYFY-----VNEASLGRALK-DNGVDREDLFITTK----LW- 77
Cdd:cd19089 12 PAISLGLwhnfGDYT-SPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKrDLRPYRDELVISTKagygMWp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 78 ---NDYQGYEKTFEYFNKSIENLQTDYLDLFLIH-----WPCEadglflETYKAMEELYEQGKVKAIGVCNFN---VHHL 146
Cdd:cd19089 91 gpyGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHrydpdTPLE------ETMTALADAVRSGKALYVGISNYPgakARRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 147 EKLMAQSSIKPMVNQIevhPY--FNQ---QELQEFCDRHDIKVTAWMPLmrNRGLLDDPVIV------------------ 203
Cdd:cd19089 165 IALLRELGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPL--AQGLLTDKYLNgippdsrraaeskfltee 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757676546 204 --------------KIAEKYHKTPAQVVLRWHLAHNRI---IIPKSQtPKRIQENIDILDfNLELTEvAEI 257
Cdd:cd19089 240 altpekleqlrklnKIAAKRGQSLAQLALSWVLRDPRVtsvLIGASS-PSQLEDNVAALK-NLDFSE-EEL 307
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-253 |
3.61e-08 |
|
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: 53.56 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 9 NNGYPMPSVGLGVY-KISD----EDMTKVVNVAIDAGYRAFDTAYFY-----VNEASLGRALKDNGVD-REDLFITTK-- 75
Cdd:cd19151 7 RSGLKLPAISLGLWhNFGDvdryENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 76 --LWNDYQGYEKTFEY----FNKSIENLQTDYLDLFLIHWPcEADGLFLETYKAMEELYEQGKVKAIGVCNFNVHHLE-- 147
Cdd:cd19151 87 ytMWPGPYGDWGSKKYliasLDQSLKRMGLDYVDIFYHHRP-DPETPLEETMGALDQIVRQGKALYVGISNYPPEEARea 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 148 -KLMAQSSIKPMVNQIEvHPYFN---QQELQEFCDRHDIKVTAWMPLMrnRGLLDD------PV---------------- 201
Cdd:cd19151 166 aAILKDLGTPCLIHQPK-YSMFNrwvEEGLLDVLEEEGIGCIAFSPLA--QGLLTDrylngiPEdsraakgssflkpeqi 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757676546 202 ----------IVKIAEKYHKTPAQVVLRWHLAHNRI---IIPKSQtPKRIQENIDILDfNLELTE 253
Cdd:cd19151 243 teeklakvrrLNEIAQARGQKLAQMALAWVLRNKRVtsvLIGASK-PSQIEDAVGALD-NREFSE 305
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
28-138 |
1.17e-04 |
|
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: 42.80 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 28 DMTKVVNVAI-DAGYRA----FDTAYFYVNEAS---LGRALKDNGvDREDLFITTKLWNDYQGYEKTFEYFN-------- 91
Cdd:cd19146 31 ECDKETAFKLlDAFYEQggnfIDTANNYQGEESerwVGEWMASRG-NRDEMVLATKYTTGYRRGGPIKIKSNyqgnhaks 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 757676546 92 ------KSIENLQTDYLDLFLIHW-----PCEadglflETYKAMEELYEQGKVKAIGV 138
Cdd:cd19146 110 lrlsveASLKKLQTSYIDILYVHWwdyttSIP------ELMQSLNHLVAAGKVLYLGV 161
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|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-131 |
5.32e-03 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 37.71 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757676546 31 KVVNVAIDAGYRAFDTAYFY-VNEASLGRALKDNGVDREDLFITTKlWndyqGYEKT---------FEYFNKSIENLQT- 99
Cdd:cd19098 39 AVLDAAWAAGVRYFDAARSYgRAEEFLGSWLRSRNIAPDAVFVGSK-W----GYTYTadwqvdaavHEVKDHSLARLLKq 113
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 757676546 100 ---------DYLDLFLIHWPCEADGLF--LETYKAMEELYEQG 131
Cdd:cd19098 114 weetrsllgKHLDLYQIHSATLESGVLedADVLAALAELKAEG 156
|
|
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