|
Name |
Accession |
Description |
Interval |
E-value |
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-270 |
1.44e-151 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 423.31 E-value: 1.44e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 10 DGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAESRRA 89
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 90 LEESLTKLGLDYVNLYLIHWPTPAqkNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD-TGIIPAVDQIELHPQFQ 168
Cdd:COG0656 81 FEESLERLGLDYLDLYLIHWPGPG--PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAeTGVKPAVNQVELHPYLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 169 QIDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTL 248
Cdd:COG0656 159 QRELLAFCREHGIVVEAYSPLGRGKL-LDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFEL 237
|
250 260
....*....|....*....|..
gi 1949187231 249 TDAEMASIDALENGGRVSADPA 270
Cdd:COG0656 238 SDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
6-260 |
4.17e-134 |
|
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: 379.02 E-value: 4.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAE 85
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 86 SRRALEESLTKLGLDYVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD-TGIIPAVDQIELH 164
Cdd:cd19131 82 TLRAFDESLRKLGLDYVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDeTGVVPVVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 165 PQFQQIDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVF 244
Cdd:cd19131 162 PRFQQRELRAFHAKHGIQTESWSPLGQGGL-LSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVF 240
|
250
....*....|....*.
gi 1949187231 245 DFTLTDAEMASIDALE 260
Cdd:cd19131 241 DFELDADDMQAIAGLD 256
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
6-260 |
1.10e-124 |
|
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: 355.37 E-value: 1.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAE 85
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 86 SRRALEESLTKLGLDYVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD-TGIIPAVDQIELH 164
Cdd:cd19130 82 PAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAaTGVVPAVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 165 PQFQQIDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVF 244
Cdd:cd19130 162 PAYQQRTIRDWAQAHDVKIEAWSPLGQGKL-LGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVF 240
|
250
....*....|....*.
gi 1949187231 245 DFTLTDAEMASIDALE 260
Cdd:cd19130 241 DFDLTDTEIAAIDALD 256
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-257 |
1.88e-124 |
|
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: 354.48 E-value: 1.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 14 IPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAESRRALEES 93
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 94 LTKLGLDYVNLYLIHWPTP-----AQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD-TGIIPAVDQIELHPQF 167
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPgkeggSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAaARIKPAVNQIELHPYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 168 QQIDTRPLLAENDIKIEAWGPLGQGNVDY-ASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDF 246
Cdd:cd19071 161 QQKELVEFCKEHGIVVQAYSPLGRGRRPLlDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDF 240
|
250
....*....|.
gi 1949187231 247 TLTDAEMASID 257
Cdd:cd19071 241 ELSEEDMAAID 251
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
6-259 |
3.78e-119 |
|
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: 341.09 E-value: 3.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKV-DPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAA 84
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIpDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 85 ESRRALEESLTKLGLDYVNLYLIHWPTpaqKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTG-IIPAVDQIEL 163
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPF---GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNeVKPAVNQIET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 164 HPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYAST-VIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFD 242
Cdd:cd19133 158 HPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENpVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFD 237
|
250
....*....|....*..
gi 1949187231 243 VFDFTLTDAEMASIDAL 259
Cdd:cd19133 238 IFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-261 |
3.02e-114 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 328.85 E-value: 3.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 8 LNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAESR 87
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 88 RALEESLTKLGLDYVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFdyryLPEILD-----TGIIPAVDQIE 162
Cdd:cd19132 81 RTIEESLYRLGLDYVDLYLIHWPNPSRDLYVEAWQALIEAREEGLVRSIGVSNF----LPEHLDrlideTGVTPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 163 LHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFD 242
Cdd:cd19132 157 LHPYFPQAEQRAYHREHGIVTQSWSPLGRGSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLA 236
|
250
....*....|....*....
gi 1949187231 243 VFDFTLTDAEMASIDALEN 261
Cdd:cd19132 237 IFDFELSDEDMAAIAALDR 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-270 |
6.44e-113 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 326.26 E-value: 6.44e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 1 MSVPDL-TLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWND 79
Cdd:PRK11565 1 MANPTViKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 80 RHGAAesRRALEESLTKLGLDYVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD-TGIIPAV 158
Cdd:PRK11565 81 DHKRP--REALEESLKKLQLDYVDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDeTGVTPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 159 DQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQG--NVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRER 236
Cdd:PRK11565 159 NQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGgkGV-FDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSR 237
|
250 260 270
....*....|....*....|....*....|....
gi 1949187231 237 MAQNFDVFDFTLTDAEMASIDALENGGRVSADPA 270
Cdd:PRK11565 238 IAENFDVFDFRLDKDELGEIAKLDQGKRLGPDPD 271
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-269 |
6.46e-112 |
|
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: 323.19 E-value: 6.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKV-DPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAA 84
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVeEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 85 ESRRALEESLTKLGLDYVNLYLIHWPTPAqKNaVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEIL-DTGIIPAVDQIEL 163
Cdd:cd19157 82 STLKAFEASLERLGLDYLDLYLIHWPVKG-KY-KETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLaDAEIVPMVNQVEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 164 HPQFQQIDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDV 243
Cdd:cd19157 160 HPRLTQKELRDYCKKQGIQLEAWSPLMQGQL-LDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADV 238
|
250 260
....*....|....*....|....*.
gi 1949187231 244 FDFTLTDAEMASIDALENGGRVSADP 269
Cdd:cd19157 239 FDFELSQEDMDKIDALNENLRVGPDP 264
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
6-269 |
3.17e-110 |
|
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: 319.08 E-value: 3.17e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKV-DPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAA 84
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVqDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 85 ESRRALEESLTKLGLDYVNLYLIHWptPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTG-IIPAVDQIEL 163
Cdd:cd19156 81 STLAAFEESLEKLGLDYVDLYLIHW--PVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCkVAPMVNQIEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 164 HPQFQQIDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDV 243
Cdd:cd19156 159 HPLLTQEPLRKFCKEKNIAVEAWSPLGQGKL-LSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDV 237
|
250 260
....*....|....*....|....*.
gi 1949187231 244 FDFTLTDAEMASIDALENGGRVSADP 269
Cdd:cd19156 238 FDFELTAEEIRQIDGLNTDHRYGPDP 263
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-260 |
1.24e-106 |
|
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: 309.37 E-value: 1.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKV-DPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAA 84
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTpDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 85 ESRRALEESLTKLGLDYVNLYLIHWPTPAQknAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEIL-DTGIIPAVDQIEL 163
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHWPGKDK--FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLaHADVVPAVNQVEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 164 HPQFQQIDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDV 243
Cdd:cd19126 159 HPYLTQKELRGYCKSKGIVVEAWSPLGQGGL-LSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADI 237
|
250
....*....|....*..
gi 1949187231 244 FDFTLTDAEMASIDALE 260
Cdd:cd19126 238 FDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-265 |
6.59e-106 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 307.94 E-value: 6.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 4 PDLTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGA 83
Cdd:cd19134 1 PTVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 84 AESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD-TGIIPAVDQIE 162
Cdd:cd19134 81 TASQAACRASLERLGLDYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDlTFFTPAVNQIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 163 LHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYASTVIgEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFD 242
Cdd:cd19134 161 LHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVT-AIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLD 239
|
250 260
....*....|....*....|...
gi 1949187231 243 VFDFTLTDAEMASIDALENGGRV 265
Cdd:cd19134 240 VFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-259 |
1.36e-105 |
|
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: 307.41 E-value: 1.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAE 85
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 86 SRRALEESLTKLGLDYVNLYLIHWPTPAQKNA-VETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD-TGIIPAVDQIEL 163
Cdd:cd19127 81 ALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRtIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDaTTVVPAVNQVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 164 HPQFQQIDTRPLLAENDIKIEAWGPLG----------QGNVDYAS-TVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSN 232
Cdd:cd19127 161 HPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygasgpTGPGDVLQdPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSV 240
|
250 260
....*....|....*....|....*..
gi 1949187231 233 NRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19127 241 HPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-265 |
1.32e-100 |
|
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: 295.73 E-value: 1.32e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 4 PDLTLNDGLTIPQLGFGVFK-VDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALA---ASG-IPRDELFITTKLWN 78
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKlKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIRekiAEGvVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNA---------------VETWEAFPGYRDEGLTRSIGVSNFDY 143
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNdsesngdgslsdidyLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 144 RYLPEILDTG-IIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQ--------GNVDYASTVIGEIAEAHGKSWAQ 214
Cdd:cd19116 161 EQINRLLSNCnIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRlvprgqtnPPPRLDDPTLVAIAKKYGKTTAQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1949187231 215 VIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRV 265
Cdd:cd19116 241 IVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-259 |
1.87e-93 |
|
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: 276.06 E-value: 1.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAESRRAL 90
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 91 EESLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIP-AVDQIELHPqfqQ 169
Cdd:cd19140 85 EESLRKLRTDYVDLLLLHWPNKDVPLA-ETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPlFTNQVEYHP---Y 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 170 IDTRPLLA---ENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQR-GHILFPKSNNRERMAQNFDVFD 245
Cdd:cd19140 161 LDQRKLLDaarEHGIALTAYSPLARGEV-LKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFD 239
|
250
....*....|....
gi 1949187231 246 FTLTDAEMASIDAL 259
Cdd:cd19140 240 FTLSDEEMARIAAL 253
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-259 |
1.54e-91 |
|
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: 271.43 E-value: 1.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 14 IPQLGFGVFKV-DPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAAS----GIPRDELFITTKLWNDRHGAAESRR 88
Cdd:cd19136 1 MPILGLGTFRLrGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 89 ALEESLTKLGLDYVNLYLIHWP--------TPAQK-NAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEIL-DTGIIPAV 158
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgvqglkpsDPRNAeLRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLkYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 159 DQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYAS-TVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERM 237
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEdPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 1949187231 238 AQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-257 |
9.69e-90 |
|
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: 266.06 E-value: 9.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 14 IPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAESRRALEES 93
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 94 LTKLGLDYVNLYLIHWPTPAqKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIP-AVDQIELHPQFQQIDT 172
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNPT-VPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPiAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 173 RPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAE 252
Cdd:cd19073 160 LEYCRENDIVITAYSPLARGEV-LRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSED 238
|
....*
gi 1949187231 253 MASID 257
Cdd:cd19073 239 VAKID 243
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-265 |
6.93e-87 |
|
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: 261.17 E-value: 6.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 8 LNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAAS-----GIPRDELFITTKLWNDRHG 82
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 83 AAESRRALEESLTKLGLDYVNLYLIHWPT-------PAQKNA-----------VETWEAFPGYRDEGLTRSIGVSNFDYR 144
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYafergdnPFPKNPdgtirydsthyKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 145 YLPEILDTGII-PAVDQIELHPQFQQidtRPLLA---ENDIKIEAWGPLGQGNVDYAST---------VIGEIAEAHGKS 211
Cdd:cd19106 161 QIDDILSVARIkPAVLQVECHPYLAQ---NELIAhckARGLVVTAYSPLGSPDRPWAKPdepvlleepKVKALAKKYNKS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1949187231 212 WAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRV 265
Cdd:cd19106 238 PAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-265 |
3.46e-86 |
|
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: 258.81 E-value: 3.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASG----IPRDELFITTKLWNDRH 81
Cdd:cd19125 3 FKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAV-------------ETWEAFPGYRDEGLTRSIGVSNFDYRYLPE 148
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHmpepeevlppdipSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 149 ILD-TGIIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYA------STVIGEIAEAHGKSWAQVIIRWHL 221
Cdd:cd19125 163 LLAvARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVkknvlkDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1949187231 222 QRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRV 265
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
6-264 |
5.84e-86 |
|
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: 258.50 E-value: 5.84e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAA----SGIPRDELFITTKLWNDRH 81
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEvfkeGKVKREDLWITSKLWNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNA-----------------VETWEAFPGYRDEGLTRSIGVSNFDYR 144
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGVgfpesgedllslspiplEDTWRAMEELVDKGLCRHIGVSNFSVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 145 YLPEILDTG-IIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGN-----------VDYASTVIGEIAEAHGKSW 212
Cdd:cd19123 164 KLEDLLATArIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepVLLEDPVINKIAEKHGASP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 213 AQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGR 264
Cdd:cd19123 244 AQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
6-259 |
1.14e-85 |
|
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: 257.43 E-value: 1.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAE 85
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRRVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 86 SrrALEESLTKLGLDYVNLYLIHWPTPAQK--------------------NAVETWEAFPGYRDEGLTRSIGVSNFDYRY 145
Cdd:cd19117 86 E--ALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIGVSNFSIKN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 146 LPEIL---DTGIIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVD-YASTVIGEIAEAHGKSWAQVIIRWHL 221
Cdd:cd19117 164 LEKLLaspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPlLKEPVIIKIAKKHGKTPAQVIISWGL 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 1949187231 222 QRGHILFPKSNNRERMAQNFDVfdFTLTDAEMASIDAL 259
Cdd:cd19117 244 QRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
10-260 |
2.38e-85 |
|
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: 256.43 E-value: 2.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 10 DGLTIPQLGFG--VFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALA---ASG--IPRDELFITTKLWNDRHG 82
Cdd:cd19124 1 SGQTMPVIGMGtaSDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGlvKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 83 AAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAVE---------------TWEAFPGYRDEGLTRSIGVSNFDYRYLP 147
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSfpieeedflpfdikgVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 148 EILDTGII-PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYAST------VIGEIAEAHGKSWAQVIIRWH 220
Cdd:cd19124 161 ELLSFATIpPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSNavmesdVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1949187231 221 LQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALE 260
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIP 280
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
3-265 |
4.26e-85 |
|
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: 256.57 E-value: 4.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 3 VPDLTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALA---ASGI-PRDELFITTKLWN 78
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAellEEGVvKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNA------------------VETWEAFPGYRDEGLTRSIGVSN 140
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEgesgtmengmsihdavdvEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 141 FDYRYLPEILDTGII-PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQ--------------GNVDYASTVIGEIA 205
Cdd:cd19154 161 FNNDQIQRILDNARVkPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspAPNLLQDPIVKAIA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 206 EAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRV 265
Cdd:cd19154 241 EKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-259 |
1.41e-83 |
|
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: 250.73 E-value: 1.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 14 IPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAESRRALEES 93
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 94 LTKLGLDYVNLYLIHWPTP-AQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT---GIIpAVDQIELHPQFQQ 169
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPnDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVvgaGAI-ATNQIELSPYLQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 170 IDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLT 249
Cdd:cd19139 160 RKLVAHCKQHGIHVTSYMTLAYGKV-LDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLD 238
|
250
....*....|
gi 1949187231 250 DAEMASIDAL 259
Cdd:cd19139 239 ADDMAAIAAL 248
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-258 |
1.72e-81 |
|
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: 245.99 E-value: 1.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGV----FKVDPKETERIVTD----ALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWndrHG 82
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLVDsvklALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVS---PG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 83 AAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNA---VETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTG-IIPAV 158
Cdd:cd19120 78 IKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGptlAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAkIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 159 DQIELHPQF--QQIDTRPLLAENDIKIEAWGPLG------QGNVDyasTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPK 230
Cdd:cd19120 158 NQIEFHPYLypQQPALLEYCREHGIVVSAYSPLSpltrdaGGPLD---PVLEKIAEKYGVTPAQVLLRWALQKGIVVVTT 234
|
250 260
....*....|....*....|....*...
gi 1949187231 231 SNNRERMAQNFDVFDFTLTDAEMASIDA 258
Cdd:cd19120 235 SSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-259 |
3.00e-81 |
|
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: 245.31 E-value: 3.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 4 PDLTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGA 83
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 84 AESRRALEESLTKLGLDYVNLYLIHWP-TPAQKNAV-----ETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT-GIIP 156
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPdCPSSGKNVketraETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDcSVVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 157 AVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYASTVIgEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRER 236
Cdd:cd19135 163 HVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVT-ELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEER 241
|
250 260
....*....|....*....|...
gi 1949187231 237 MAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19135 242 IKENCQVFDFSLSEEDMATLDSL 264
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-270 |
8.71e-78 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 236.46 E-value: 8.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 12 LTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASGIPRDELFITTKLWNDRHGAAESRRALE 91
Cdd:PRK11172 1 MSIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 92 ESLTKLGLDYVNLYLIHWPTPaqKNAV---ETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT---GIIpAVDQIELHP 165
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWPSP--NDEVsveEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAvgaENI-ATNQIELSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 166 QFQQIDTRPLLAENDIKIEAWGPLGQGNVdYASTVIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFD 245
Cdd:PRK11172 158 YLQNRKVVAFAKEHGIHVTSYMTLAYGKV-LKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQD 236
|
250 260
....*....|....*....|....*
gi 1949187231 246 FTLTDAEMASIDALENGGRVsADPA 270
Cdd:PRK11172 237 LQLDAEDMAAIAALDRNGRL-VSPE 260
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-269 |
5.29e-77 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 236.23 E-value: 5.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 4 PDLTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAASG----IPRDELFITTKLWND 79
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 80 RHGAAesRRALEESLTKLGLDYVNLYLIHWPTPAQKNAV----------------------ETWEAFPGYRDEGLTRSIG 137
Cdd:cd19112 81 DHGHV--IEACKDSLKKLQLDYLDLYLVHFPVATKHTGVgttgsalgedgvldidvtisleTTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 138 VSNFDYRYLPEILDTGII-PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQG--NVDYASTV-------IGEIAEA 207
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIkPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaaNAEWFGSVsplddpvLKDLAKK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 208 HGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRVSADP 269
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-259 |
1.96e-75 |
|
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: 231.15 E-value: 1.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 8 LNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALA-----ASGIPRDELFITTKLWNDRHG 82
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKellkeEPGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 83 AAESRRALEESLTKLGLDYVNLYLIHWP-----------TPAQKN------------AVETWEAFPGYRDEGLTRSIGVS 139
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpLTAVPTnggevdldlsvsLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 140 NFDYRYLPEILD-TGIIPAVDQIELHPQFQQidtRPLLA---ENDIKIEAWGPLGqGNVD-----YASTVIGEIAEAHGK 210
Cdd:cd19118 161 NFSIDHLQAIIEeTGVVPAVNQIEAHPLLLQ---DELVDyckSKNIHITAYSPLG-NNLAglpllVQHPEVKAIAAKLGK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1949187231 211 SWAQVIIRWHLQRGHILFPKSNNRERMAQNFDvfDFTLTDAEMASIDAL 259
Cdd:cd19118 237 TPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
6-264 |
9.55e-72 |
|
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: 222.79 E-value: 9.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRAL----AASGIPRDELFITTKLWNDRH 81
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLkkwiDSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRRALEESLTKLGLDYVNLYLIHWPT--------------------PAQKNAVETWEAFPGYRDEGLTRSIGVSNF 141
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 142 DYRYLPEILDTGII-PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYAST----------------VIGEI 204
Cdd:cd19155 164 NREQMARILKNARIkPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgsspdllqdpVVKAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 205 AEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGR 264
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-259 |
5.96e-71 |
|
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: 220.56 E-value: 5.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVD--PK-ETERIVTDALEVGYRHIDTAAVYGNEEGVGRAL----AASGIPRDELFITTKLWN 78
Cdd:cd19108 3 VKLNDGHFIPVLGFGTYAPEevPKsKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAESRRALEESLTKLGLDYVNLYLIHWPT---------PAQKN------AVE---TWEAFPGYRDEGLTRSIGVSN 140
Cdd:cd19108 83 TFHRPELVRPALEKSLKKLQLDYVDLYLIHFPValkpgeelfPKDENgklifdTVDlcaTWEAMEKCKDAGLAKSIGVSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 141 FDYRYLPEILDT-GII--PAVDQIELHPQFQQidtRPLLA---ENDIKIEAWGPLG----QGNVDYAS------TVIGEI 204
Cdd:cd19108 163 FNRRQLEMILNKpGLKykPVCNQVECHPYLNQ---SKLLDfckSKDIVLVAYSALGsqrdKEWVDQNSpvlledPVLCAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1949187231 205 AEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGL 294
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-264 |
2.98e-70 |
|
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: 218.14 E-value: 2.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALA---ASG-IPRDELFITTKLWNDRHGAAES 86
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 87 RRALEESLTKLGLDYVNLYLIHWPTP------------AQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGI 154
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGfvnkkdkgerelASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 155 I-PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQ-GNVDYAST----------VIGEIAEAHGKSWAQVIIRWHLQ 222
Cdd:cd19111 161 VkPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWpdqpdlledpTVLAIAKELDKTPAQVLLRFVLQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1949187231 223 RGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGR 264
Cdd:cd19111 241 RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
5-259 |
1.03e-69 |
|
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: 216.63 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 5 DLTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVG---RALAASGIPRDELFITTKLWNDRH 81
Cdd:cd19121 3 SFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGegiKEAIAGGVKREDLFVTTKLWSTYH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAEsrRALEESLTKLGLDYVNLYLIHWPTPAQKNA---------------------VETWEAFPGYRDEGLTRSIGVSN 140
Cdd:cd19121 83 RRVE--LCLDRSLKSLGLDYVDLYLVHWPVLLNPNGnhdlfptlpdgsrdldwdwnhVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 141 FDYRYLPEILDTG-IIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQ-GNVDYASTVIGEIAEAHGKSWAQVIIR 218
Cdd:cd19121 161 YSIPYLEELLKHAtVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGStGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1949187231 219 WHLQRGHILFPKSNNRERMAQNFDVFDFtlTDAEMASIDAL 259
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-271 |
5.65e-68 |
|
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: 213.05 E-value: 5.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 2 SVPDLTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNE----EGVGRALAASGIPRDELFITTKLW 77
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEveagQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 78 NDRHGAAESRRALEESLTKLGLDYVNLYLIHWPT------PA---------------QKNAV--ETWEAFPGYRDEGLTR 134
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIalkyvdPAvryppgwfydgkkveFSNAPiqETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 135 SIGVSNFDYRYLPEILDTG-IIPAVDQIELHPQFQQIDTRPLLAENDIKIEAW---GPLG------QGNVDYAS----TV 200
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYArIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYssfGPQSfleldlPGAKDTPPlfehDV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187231 201 IGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRVSaDPAD 271
Cdd:cd19115 241 IKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFN-NPLN 310
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-259 |
2.18e-67 |
|
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: 210.46 E-value: 2.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAA----SGIPRDELFITTKLWNDRHGAAESRRAL 90
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 91 EESLTKLGLDYVNLYLIHWPTPAQKNAV------------------ETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD- 151
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDgdprddnqiqslskkpleDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNy 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 152 TGIIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYASTVIG-----EIAEAHGKSWAQVIIRWHLQR--- 223
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTFLNdselkALATKYNTTPPQVIIAWHLQKwpk 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 1949187231 224 GHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19128 242 NYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-267 |
1.00e-65 |
|
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: 207.27 E-value: 1.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAA----SGIPRDELFITTKLWNDRHGAAES 86
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEkikeQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 87 RRALEESLTKLGLDYVNLYLIHWPT------------------PAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPE 148
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnviPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 149 ILDT-GII--PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNVDYAS---------TVIGEIAEAHGKSWAQVI 216
Cdd:cd19107 161 ILNKpGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKpedpslledPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1949187231 217 IRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRVSA 267
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACA 291
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-271 |
3.37e-65 |
|
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: 205.76 E-value: 3.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 4 PDLTLNDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNE----EGVGRALAASGIPRDELFITTKLWND 79
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEkevgEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 80 RHGAAESRRALEESLTKLGLDYVNLYLIHWPTpAQKNA-------------------------VETWEAFPGYRDEGLTR 134
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPI-AFKFVpieekyppgfycgdgdnfvyedvpiLDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 135 SIGVSNFDYRYLPEILDTGII-PAVDQIELHPQFQQidtrPLLAE----NDIKIEAW---GP-----LGQGNVDYAST-- 199
Cdd:cd19113 160 SIGVSNFPGALILDLLRGATIkPAVLQIEHHPYLQQ----PKLIEyaqkAGITITAYssfGPqsfveLNQGRALNTPTlf 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187231 200 ---VIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRVSaDPAD 271
Cdd:cd19113 236 ehdTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFN-DPWD 309
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
11-259 |
2.09e-64 |
|
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: 203.88 E-value: 2.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKvDPKETER-----IVTDALEVGYRHIDTAAVYGNEEGVGRA----LAASGIPRDELFITTKLWNDRH 81
Cdd:cd19109 1 GNSIPIIGLGTYS-EPKTTPKgacaeAVKVAIDTGYRHIDGAYIYQNEHEVGQAirekIAEGKVKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRRALEESLTKLGLDYVNLYLIHWPT---PA---------------QKNAVETWEAFPGYRDEGLTRSIGVSNFDY 143
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMafkPGdeiyprdengkwlyhKTNLCATWEALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 144 RYLPEILDTGII---PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGN----VDYAS------TVIGEIAEAHGK 210
Cdd:cd19109 160 RQLELILNKPGLkhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwVNVSSpplledPLLNSIGKKYNK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1949187231 211 SWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEAL 288
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-264 |
1.89e-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: 201.25 E-value: 1.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGR----ALAASGIPRDELFITTKLWNDRHGAAES 86
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRgirkAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 87 RRALEESLTKLGLDYVNLYLIHWPTPA------------------------QKNAVETWEAFPGYRDEGLTRSIGVSNFD 142
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAayvdpaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 143 YRYLPEILD-TGIIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLG--------QGNVDYAS----TVIGEIAEAHG 209
Cdd:cd19114 161 VQLILDLLTyAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtKHLKHFTNllehPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1949187231 210 KSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGR 264
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
14-273 |
9.87e-61 |
|
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: 194.41 E-value: 9.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 14 IPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRALAAS----GIPRDELFITTKLWNDRHGAAESRRA 89
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKikegVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 90 LEESLTKLGLDYVNLYLIHWP------------------TPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD 151
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPmgfkpgepdlpldrsgmvIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 152 TG---IIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLG--QGNVDYA-STVIGEIAEAHGKSWAQVIIRWHLQRGH 225
Cdd:cd19110 164 KPglrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGgsCEGVDLIdDPVIQRIAKKHGKSPAQILIRFQIQRNV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1949187231 226 ILFPKSNNRERMAQNFDVFDFTLTDAEMASIDALENGGRVSADPADVN 273
Cdd:cd19110 244 IVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITEN 291
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-259 |
5.87e-58 |
|
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: 186.75 E-value: 5.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 16 QLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAASGIPRDELFITTKL------WNDRHGAAES 86
Cdd:pfam00248 7 QLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSGGSKENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 87 RRALEESLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIP-AVDQIELHP 165
Cdd:pfam00248 87 RKSLEESLKRLGTDYIDLYYLHWPDPDTPIE-ETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPiVAVQVEYNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 166 QFQQIDT--RPLLAENDIKIEAWGPLGQGNVDYAST--------------------------VIGEIAEAHGKSWAQVII 217
Cdd:pfam00248 166 LRRRQEEelLEYCKKNGIPLIAYSPLGGGLLTGKYTrdpdkgpgerrrllkkgtplnlealeALEEIAKEHGVSPAQVAL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1949187231 218 RWHLQ--RGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:pfam00248 246 RWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-243 |
8.72e-58 |
|
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: 186.51 E-value: 8.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRA----LAASGIPRDELFITTKLWNDRHGAA 84
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAmqevFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 85 ESRRALEESLTKLGLDYVNLYLIHWP---------TPAQKNA----------VETWEAFPGYRDEGLTRSIGVSNFDYRY 145
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqDPRDANGnviyddgvtlLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 146 LPEILDTGII-PAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQG---NVdYASTVIGEIAEAHGKSWAQVIIRWHL 221
Cdd:cd19129 161 LREIFEAARIkPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmepKL-LEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260
....*....|....*....|..
gi 1949187231 222 QRGHILFPKSNNRERMAQNFDV 243
Cdd:cd19129 240 QRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-257 |
2.39e-57 |
|
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: 184.35 E-value: 2.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKV---------DPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALaaSGIPRDELFITTKLWN 78
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdysDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI--KGFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRYLPE----ILDTGI 154
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIE-ETLRAMEELVEEGKIRYIGVSNFSLEELEEaqsyLKKGPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 155 IpaVDQIELHPQFQQI--DTRPLLAENDIKIEAWGPLGQG--NVDYASTVIGEIAEAHGKSWAQVIIRWHLQRGH-ILFP 229
Cdd:cd19072 158 V--ANQVEYNLFDREEesGLLPYCQKNGIAIIAYSPLEKGklSNAKGSPLLDEIAKKYGKTPAQIALNWLISKPNvIAIP 235
|
250 260
....*....|....*....|....*...
gi 1949187231 230 KSNNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19072 236 KASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-259 |
1.17e-56 |
|
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: 183.59 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 7 TLNDGLTIPQLGFGVFKVD--PKETERIVTDALEVGYRHIDTAAVYGNEEGVGRAL-----AASGIPRDELFITTKLWND 79
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVrdflkENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 80 RHGAAESRRALEESLTKLGLDYVNLYLIHWPTPAQK----------------------NAVETWEAFPGYRDEGLTRSIG 137
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKndqrspklgpdgkyvilkdlteNPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 138 VSNFDYRYLPEILDTG-IIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLGQGNvDYAST--------VIGEIAEAH 208
Cdd:cd19122 162 VSNWTIPGLKKLLSFAkVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQN-QVPSTgervsenpTLNEVAEKG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1949187231 209 GKSWAQVIIRWHLQRGHILFPKSNNRERMAQNFDVFDftLTDAEMASIDAL 259
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQV 289
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-259 |
5.91e-52 |
|
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: 171.53 E-value: 5.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVFKVDPK--ETERIVTDALEVGYRHIDTAAVYGNEEGVG----RALAASGIPRDELFITTKLWND 79
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHEDraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGeaikRAIDDGSIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 80 RHGAAEsrRALEESLTKLGLDYVNLYLIHWP--------------TPAQKNA----------VETWEAFPGYRDEGLTRS 135
Cdd:cd19119 84 FYDEVE--RSLDESLKALGLDYVDLLLVHWPvcfekdsddsgkpfTPVNDDGktryaasgdhITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 136 IGVSNFDYRYLPEILDT-GIIPAVDQIELHPQFQQIDTRPLLAENDIKIEAWGPLG-QGNVDYASTVIGEIAEAHGKSWA 213
Cdd:cd19119 162 IGVSNYSIVYLERLIKEcKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGsHGAPNLKNPLVKKIAEKYNVSTG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1949187231 214 QVIIRWHLQRGHILFPKSNNRERMAQNFDVfdFTLTDAEMASIDAL 259
Cdd:cd19119 242 DILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-257 |
9.93e-50 |
|
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: 164.73 E-value: 9.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 6 LTLNDGLTIPQLGFGVF-----KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASgipRDELFITTKLW 77
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 78 NDRHGAAESRRALEESLTKLGLDYVNLYLIHWP--TPAQknavETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT--G 153
Cdd:cd19138 80 PSNASRQGTVRACERSLRRLGTDYLDLYLLHWRggVPLA----ETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVpgG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 154 IIPAVDQIELHPQFQQI--DTRPLLAENDIKIEAWGPLGQGN----VDYASTVIGEIAEAHGKSWAQVIIRWHLQRGHIL 227
Cdd:cd19138 156 GNCAANQVLYNLGSRGIeyDLLPWCREHGVPVMAYSPLAQGGllrrGLLENPTLKEIAARHGATPAQVALAWVLRDGNVI 235
|
250 260 270
....*....|....*....|....*....|.
gi 1949187231 228 -FPKSNNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19138 236 aIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
18-258 |
3.15e-46 |
|
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: 156.59 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 18 GFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAAsgiPRDELFITTKLWNDRHGAAESRRALEESL 94
Cdd:cd19085 14 GYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNLTPEDVRKSCERSL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 95 TKLGLDYVNLYLIHWPTPaQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIpAVDQIELHPQFQQI--DT 172
Cdd:cd19085 91 KRLGTDYIDLYQIHWPSS-DVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI-DSNQLPYNLLWRAIeyEI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 173 RPLLAENDIKIEAWGPLGQG-------------------------------NVDYASTVIGEIAEAHGKSWAQVIIRWHL 221
Cdd:cd19085 169 LPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdartrlfrhfepgaeeETFEALEKLKEIADELGVTMAQLALAWVL 248
|
250 260 270
....*....|....*....|....*....|....*....
gi 1949187231 222 QRGHILFP--KSNNRERMAQNFDVFDFTLTDAEMASIDA 258
Cdd:cd19085 249 QQPGVTSVivGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
9-259 |
7.13e-45 |
|
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: 153.80 E-value: 7.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFG--VF-----KVDPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAasGIPRDELFITTKL-- 76
Cdd:COG0667 8 RSGLKVSRLGLGtmTFggpwgGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALK--GRPRDDVVIATKVgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 -----WNDRHGAAES-RRALEESLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRYLPEIL 150
Cdd:COG0667 86 rmgpgPNGRGLSREHiRRAVEASLRRLGTDYIDLYQLHRPDPDTPIE-ETLGALDELVREGKIRYIGVSNYSAEQLRRAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 151 DT--GIIP-AVDQIELHPQFQQIDTR--PLLAENDIKIEAWGPLGQG------------------NVDYASTV------- 200
Cdd:COG0667 165 AIaeGLPPiVAVQNEYSLLDRSAEEEllPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdraATNFVQGYlternla 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949187231 201 ----IGEIAEAHGKSWAQVIIRWHLQRGHILFP----KSnnRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:COG0667 245 lvdaLRAIAAEHGVTPAQLALAWLLAQPGVTSVipgaRS--PEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
11-257 |
3.96e-41 |
|
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: 143.44 E-value: 3.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVF--------KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAasGIpRDELFITTK---L 76
Cdd:cd19084 1 DLKVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALK--GR-RDDVVIATKcglR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 WNDRHGAAES------RRALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFDYRYLP 147
Cdd:cd19084 78 WDGGKGVTKDlspesiRKEVEQSLRRLQTDYIDLYQIHWPdpnTPIE----ETAEALEKLKKEGKIRYIGVSNFSVEQLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 148 EILDTGIIPAVdQIELHPQFQQI--DTRPLLAENDIKIEAWGPLGQG--------NVDYAST------------------ 199
Cdd:cd19084 154 EARKYGPIVSL-QPPYSMLEREIeeELLPYCRENGIGVLPYGPLAQGlltgkykkEPTFPPDdrrsrfpffrgenfeknl 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187231 200 ----VIGEIAEAHGKSWAQVIIRWHLQRGHILF----PKsnNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19084 233 eivdKLKEIAEKYGKSLAQLAIAWTLAQPGVTSaivgAK--NPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-257 |
7.30e-41 |
|
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: 141.55 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKVDPKETERIVTD---------ALEVGYRHIDTAAVYG---NEEGVGRALaaSGIPRDELFITTKLWN 78
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTPDYSRDeemvellktAIELGYTHIDTAEMYGgghTEELVGKAI--KDFPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAESRRALEESLTKLGLDYVNLYLIHWPTPaQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIPAV 158
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNP-NIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 159 -DQIELHPQFQQIDTRPLLA---ENDIKIEAWGPLGQGNVDYASTViGEIAEAHGKSWAQVIIRWHLQRGHIL-FPKSNN 233
Cdd:cd19137 158 cNQVKYNLEDRDPERDGLLEycqKNGITVVAYSPLRRGLEKTNRTL-EEIAKNYGKTIAQIALAWLIQKPNVVaIPKAGR 236
|
250 260
....*....|....*....|....
gi 1949187231 234 RERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19137 237 VEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
26-257 |
1.45e-39 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 139.29 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 26 PKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASGiPRDELFITTKLWND--RHGAAESRRALEESLTKLGLD 100
Cdd:cd19093 25 DEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAPLpwRLTRRSVVKALKASLERLGLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 101 YVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD----TGIIPAVDQIE---LHPQFQQIDTR 173
Cdd:cd19093 104 SIDLYQLHWPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKalkeRGVPLASNQVEyslLYRDPEQNGLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 174 PLLAENDIKIEAWGPLGQG--------------------------NVDYASTVIGEIAEAHGKSWAQVIIRWHLQRGHIL 227
Cdd:cd19093 184 PACDELGITLIAYSPLAQGlltgkyspenpppggrrrlfgrknleKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGVVP 263
|
250 260 270
....*....|....*....|....*....|
gi 1949187231 228 FPKSNNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19093 264 IPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-242 |
1.52e-39 |
|
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: 137.26 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFGVF----KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASGIpRDELFITTKLWND-------- 79
Cdd:cd06660 1 SRLGLGTMtfggDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-RDDVVIATKGGHPpggdpsrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 80 RHGAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT-----GI 154
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVE-ETLEALNELVREGKIRYIGVSNWSAERLAEALAYakahgLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 155 IPAVDQIE---LHPQFQQIDTRPLLAENDIKIEAWGPLGQGNvdyastvigeiaeahgkswAQVIIRWHLQRGHILFP-- 229
Cdd:cd06660 159 GFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARGP-------------------AQLALAWLLSQPFVTVPiv 219
|
250
....*....|...
gi 1949187231 230 KSNNRERMAQNFD 242
Cdd:cd06660 220 GARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-252 |
2.56e-32 |
|
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: 119.97 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFGV-----FKVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASGIPRDELFITTK----L 76
Cdd:cd19092 1 PEGLEVSRLVLGCmrladWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgirL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 WNDRHG---------AAESRRALEESLTKLGLDYVNLYLIHWPTPAQkNAVETWEAFPGYRDEGLTRSIGVSNFD---YR 144
Cdd:cd19092 81 GDDPRPgrikhydtsKEHILASVEGSLKRLGTDYLDLLLLHRPDPLM-DPEEVAEAFDELVKSGKVRYFGVSNFTpsqIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 145 YLPEILDTGIIpaVDQIELHP-QFQQIDTRPL--LAENDIKIEAWGPLGQGNVDYAST--------VIGEIAEAHGKSWA 213
Cdd:cd19092 160 LLQSYLDQPLV--TNQIELSLlHTEAIDDGTLdyCQLLDITPMAWSPLGGGRLFGGFDerfqrlraALEELAEEYGVTIE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1949187231 214 QVIIRWhLQR--GHILfP--KSNNRERMAQNFDVFDFTLTDAE 252
Cdd:cd19092 238 AIALAW-LLRhpARIQ-PilGTTNPERIRSAVKALDIELTREE 278
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
11-261 |
1.32e-31 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 119.92 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVF---KVDPKETERIVTDALEVGYRHIDTAAVYGN-EEGVGRALAAsgiPRDELFITTKLWNDRHGAAES 86
Cdd:COG1453 10 GLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKLPPWVRDPEDM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 87 RRALEESLTKLGLDYVNLYLIH-------WPTPAQKNavETWEAFPGYRDEGLTRSIGVSNFD-YRYLPEILDTGIIPAV 158
Cdd:COG1453 87 RKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPG--GALEALEKAKAEGKIRHIGFSTHGsLEVIKEAIDTGDFDFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 159 dQIELHP--QFQQIDTR--PLLAENDIKIEAWGPLGQGNVDYASTVIGEIAEAhGKSWAQVIIRWHLQ--RGHILFPKSN 232
Cdd:COG1453 165 -QLQYNYldQDNQAGEEalEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLCP-PLSPAEWALRFLLShpEVTTVLSGMS 242
|
250 260 270
....*....|....*....|....*....|.
gi 1949187231 233 NRERMAQNFDVFD--FTLTDAEMASIDALEN 261
Cdd:COG1453 243 TPEQLDENLKTADnlEPLTEEELAILERLAE 273
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
24-259 |
2.01e-31 |
|
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: 118.29 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 24 VDPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAasGIPRDELFITTK--LWNDRHGAAES------RRALEE 92
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLK--EYNRNEVVIATKgaHKFGGDGSVLNnspeflRSAVEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 93 SLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIPAV-DQIELHPQFQQID 171
Cdd:cd19083 108 SLKRLNTDYIDLYYIHFPDGETPKA-EAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDVLqGEYNLLQREAEED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 172 TRPLLAENDIKIEAWGPLGQG-------------------------------NVDYASTViGEIAEAHGKSWAQVIIRWH 220
Cdd:cd19083 187 ILPYCVENNISFIPYFPLASGllagkytkdtkfpdndlrndkplfkgerfseNLDKVDKL-KSIADEKGVTVAHLALAWY 265
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1949187231 221 LQRGHI--LFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19083 266 LTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-259 |
5.25e-31 |
|
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: 117.00 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAASgipRDELFITTK---LWND-----RHGA 83
Cdd:cd19102 14 GGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKGL---RDRPIVATKcglLWDEegrirRSLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 84 AES-RRALEESLTKLGLDYVNLYLIHWPTPAQkNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIPAVdQIE 162
Cdd:cd19102 91 PASiRAECEASLRRLGVDVIDLYQIHWPDPDE-PIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIASL-QPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 163 ---LHPQFQQiDTRPLLAENDIKIEAWGPLGQG--------------------------NVDYAST------VIGEIAEA 207
Cdd:cd19102 169 yslLRRGIEA-EILPFCAEHGIGVIVYSPMQSGlltgkmtpervaslpaddwrrrspffQEPNLARnlalvdALRPIAER 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1949187231 208 HGKSWAQVIIRWHLQRGHIL--FPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19102 248 HGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-240 |
1.69e-30 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 114.25 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFGVFK-------VDPKETERIVTDALEVGYRHIDTAAVYGN-EEGVGRALaaSGIPRDELFITTKLW------NDR 80
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGthgeggRDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 81 HG--AAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRyLPEILDTGIIPAV 158
Cdd:cd19095 79 KDfsPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTG-EVLETLEDLKAAGKVRYIGVSGDGEE-LEAAIASGVFDVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 159 dQIELHP-QFQQIDTRPLLAENDIKIEAWGPLGQG----------NVDYASTVIGEIAEAHGKSWAQVIIRWHLQRG--H 225
Cdd:cd19095 157 -QLPYNVlDREEEELLPLAAEAGLGVIVNRPLANGrlrrrvrrrpLYADYARRPEFAAEIGGATWAQAALRFVLSHPgvS 235
|
250
....*....|....*
gi 1949187231 226 ILFPKSNNRERMAQN 240
Cdd:cd19095 236 SAIVGTTNPEHLEEN 250
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-155 |
8.06e-29 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 109.49 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFG---VFKVDPKETERIVTDALEVGYRHIDTAAVYGN-EEGVGRALAAsgiPRDELFITTKLWNdrHGAAES 86
Cdd:cd19100 8 GLKVSRLGFGggpLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGA--RDYEGA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187231 87 RRALEESLTKLGLDYVNLYLIH-------WPTPAQKNAVetWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGII 155
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHavdteedLDQVFGPGGA--LEALLEAKEEGKIRFIGISGHSPEVLLRALETGEF 156
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-192 |
1.38e-27 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 106.41 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 12 LTIPQLGFGVF--------KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAAsgiPRDELFITTKLWNDR 80
Cdd:cd19086 1 LEVSEIGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 81 HG---------AAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD 151
Cdd:cd19086 78 DGgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1949187231 152 TGIIPAVdQIELHPqFQQIDTR---PLLAENDIKIEAWGPLGQG 192
Cdd:cd19086 158 RGGIDVV-QVIYNL-LDQRPEEelfPLAEEHGVGVIARVPLASG 199
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-229 |
3.10e-27 |
|
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: 105.76 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 14 IPQLGFGVFKV----------DPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAASGiprDELFITTKL---- 76
Cdd:cd19088 1 VSRLGYGAMRLtgpgiwgppaDREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYP---DDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 ----WNDRHGAAES-RRALEESLTKLGLDYVNLYLIHWPTPAQKNAvETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILD 151
Cdd:cd19088 78 tgpgWWGPDGSPEYlRQAVEASLRRLGLDRIDLYQLHRIDPKVPFE-EQLGALAELQDEGLIRHIGLSNVTVAQIEEARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 152 TGIIPAVdQIELHPQFQQ----IDTrplLAENDIKIEAWGPLGQGNVDYASTVIGEIAEAHGKSWAQVIIRWHLQRGHIL 227
Cdd:cd19088 157 IVRIVSV-QNRYNLANRDdegvLDY---CEAAGIAFIPWFPLGGGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVM 232
|
..
gi 1949187231 228 FP 229
Cdd:cd19088 233 LP 234
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
9-257 |
5.98e-27 |
|
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: 106.14 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFG--VF--KVDPKETERIVTDALEVGYRHIDTAAVY-----GNEEG-----VGRALAASGiPRDELFITT 74
Cdd:cd19081 4 RTGLSVSPLCLGtmVFgwTADEETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGesetiIGRWLKSRG-KRDRVVIAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 75 KL----WNDRHG--AAESRRALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFDYRY 145
Cdd:cd19081 83 KVgfpmGPNGPGlsRKHIRRAVEASLRRLQTDYIDLYQAHWDdpaTPLE----ETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 146 LPEILDT----GIIPAVdqiELHPQFQ-------QIDTRPLLAENDIKIEAWGPLGQG--------------------NV 194
Cdd:cd19081 159 LQEALELsrqhGLPRYV---SLQPEYNlvdresfEGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeAA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187231 195 DYAST--------VIGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNR--ERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19081 236 KRYLNerglrildALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARtvEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
15-219 |
4.06e-26 |
|
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: 103.02 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFG--------VFKVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALaaSGIPRDELFITTKL-WNDRHG 82
Cdd:cd19096 1 SVLGFGtmrlpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEAL--KEGPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 83 AAESRRALEESLTKLGLDYVNLYLIHWP-TPAQKNAVETWEAFPG---YRDEGLTRSIGVSNFD-YRYLPEILDTGIIPA 157
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHGLnSPEWLEKARKGGLLEFlekAKKEGLIRHIGFSFHDsPELLKEILDSYDFDF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187231 158 VdQIELHPQFQQIDTR-PLL---AENDIKIEAWGPLGQGNVDYASTVIGEIAEAHGKSWAQVIIRW 219
Cdd:cd19096 159 V-QLQYNYLDQENQAGrPGIeyaAKKGMGVIIMEPLKGGGLANNPPEALAILCGAPLSPAEWALRF 223
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-258 |
9.81e-26 |
|
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: 103.12 E-value: 9.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFGVFKV---------DPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASgipRDELFITTK- 75
Cdd:cd19149 6 KSGIEASVIGLGTWAIgggpwwggsDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 76 -LWNDRHG----------------AAES-RRALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTR 134
Cdd:cd19149 83 gLRWDREGgsfffvrdgvtvyknlSPESiREEVEQSLKRLGTDYIDLYQTHWQdveTPIE----ETMEALEELKRQGKIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 135 SIGVSNFDYRYLPEILDTGIIpAVDQielhPQFQQIDTR------PLLAENDIKIEAWGPLGQG----NVDYASTVIGE- 203
Cdd:cd19149 159 AIGASNVSVEQIKEYVKAGQL-DIIQ----EKYSMLDRGiekellPYCKKNNIAFQAYSPLEQGlltgKITPDREFDAGd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 204 -------------------------IAEAHGKSWAQVIIRWHLQRGHILFP--KSNNRERMAQNFDVFDFTLTDAEMASI 256
Cdd:cd19149 234 arsgipwfspenrekvlallekwkpLCEKYGCTLAQLVIAWTLAQPGITSAlcGARKPEQAEENAKAGDIRLSAEDIATM 313
|
..
gi 1949187231 257 DA 258
Cdd:cd19149 314 RS 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
9-256 |
4.37e-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: 101.14 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFGVF-------KVDPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAAsgiPRDELFITTKLWN 78
Cdd:cd19076 7 TQGLEVSALGLGCMgmsafygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVIATKFGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAES----------RRALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFD--- 142
Cdd:cd19076 84 VRDPGSGFrgvdgrpeyvRAACEASLKRLGTDVIDLYYQHRVdpnVPIE----ETVGAMAELVEEGKVRYIGLSEASadt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 143 ----YRYLPeildtgiIPAVdQIELHPQFQQIDTR--PLLAENDIKIEAWGPLGQG-------------NVDYAST---- 199
Cdd:cd19076 160 irraHAVHP-------ITAV-QSEYSLWTRDIEDEvlPTCRELGIGFVAYSPLGRGfltgaikspedlpEDDFRRNnprf 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 200 -------------VIGEIAEAHGKSWAQVIIRWHLQRGHILF--PKSNNRERMAQNFDVFDFTLTDAEMASI 256
Cdd:cd19076 232 qgenfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGDDIVpiPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-139 |
4.38e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 99.97 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFkVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAasGIPRDELFITTK--LWNDRHGAAE 85
Cdd:cd19105 10 GLKVSRLGFGGG-GLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKasPRLDKKDKAE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187231 86 SRRALEESLTKLGLDYVNLYLIHWPTPAQKNAV--ETWEAFPGYRDEGLTRSIGVS 139
Cdd:cd19105 87 LLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLneELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
9-259 |
7.11e-25 |
|
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: 100.77 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFG-------------VFKVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASgipRDELFI 72
Cdd:cd19091 8 RSGLKVSELALGtmtfgggggffgaWGGVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR---RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 73 TTKLW-------NDRhGAAESR--RALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSN 140
Cdd:cd19091 85 ATKVRgrmgegpNDV-GLSRHHiiRAVEASLKRLGTDYIDLYQLHGFdalTPLE----ETLRALDDLVRQGKVRYIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 141 FDYRYLPEILDTGIIPAVDQIELHPQFQQIDTR-------PLLAENDIKIEAWGPLGQG--------------------- 192
Cdd:cd19091 160 FSAWQIMKALGISERRGLARFVALQAYYSLLGRdlehelmPLALDQGVGLLVWSPLAGGllsgkyrrgqpapegsrlrrt 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187231 193 -------NVDYASTVIG---EIAEAHGKSWAQVIIRWHLQR--GHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19091 240 gfdfppvDRERGYDVVDalrEIAKETGATPAQVALAWLLSRptVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
25-259 |
2.98e-23 |
|
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: 96.22 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 25 DPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAASGiPRDELFITTKL---WNDRHG------AAESRRALEE 92
Cdd:cd19148 23 DEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGEvvrnssPARIRKEVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 93 SLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFDyrylPEILDT--GIIP-AVDQIELHPQ 166
Cdd:cd19148 102 SLRRLQTDYIDLYQVHWPdplVPIE----ETAEALKELLDEGKIRAIGVSNFS----PEQMETfrKVAPlHTVQPPYNLF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 167 FQQI--DTRPLLAENDIKIEAWGPLGQG------------------NVD----------YASTV--IGEIAEAH-GKSWA 213
Cdd:cd19148 174 EREIekDVLPYARKHNIVTLAYGALCRGllsgkmtkdtkfegddlrRTDpkfqeprfsqYLAAVeeLDKLAQERyGKSVI 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1949187231 214 QVIIRWHLQRGH--ILFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19148 254 HLAVRWLLDQPGvsIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
16-192 |
4.11e-23 |
|
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: 95.31 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 16 QLGFGVFKVDPKETERIVTDALEVGYRHIDTAAVYGN-EEGVGRALAasGIPRDELFITTKLwnDRHG-------AAESR 87
Cdd:cd19090 9 GLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKV--GRLPedtadysADRVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 88 RALEESLTKLGLDYVNLYLIH------WPTPAQKN-AVETWEAFpgyRDEGLTRSIGVSNFDYRYLPEILDTGIIPAV-- 158
Cdd:cd19090 85 RSVEESLERLGRDRIDLLMIHdpervpWVDILAPGgALEALLEL---KEEGLIKHIGLGGGPPDLLRRAIETGDFDVVlt 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1949187231 159 -------DQIELHPQFqqidtrPLLAENDIKIEAWGPLGQG 192
Cdd:cd19090 162 anrytllDQSAADELL------PAAARHGVGVINASPLGMG 196
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
9-257 |
4.19e-23 |
|
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: 96.11 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFG----------VFKVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAaSGIPRDELFITTK 75
Cdd:cd19079 7 NSGLKVSRLCLGcmsfgdpkwrPWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALK-EFAPRDEVVIATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 76 LWN----DRHGAAESR----RALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNF--- 141
Cdd:cd19079 86 VYFpmgdGPNGRGLSRkhimAEVDASLKRLGTDYIDLYQIHRWdyeTPIE----ETLEALHDVVKSGKVRYIGASSMyaw 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 142 ---DYRYLPEILdtGIIPAVDQIELHPQFQQIDTR---PLLAENDIKIEAWGPLGQG-------------NVDYASTV-- 200
Cdd:cd19079 162 qfaKALHLAEKN--GWTKFVSMQNHYNLLYREEERemiPLCEEEGIGVIPWSPLARGrlarpwgdtterrRSTTDTAKlk 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187231 201 --------------IGEIAEAHGKSWAQVIIRWHLQRGHILFP--KSNNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19079 240 ydyfteadkeivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
37-258 |
3.21e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 93.43 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 37 LEVGYRHIDTAAVYGN-EEGVGR---ALAASGIPRDELFITTKLWNDRH----GAAESRRALEESLTKLGLDYVNLYLIH 108
Cdd:cd19101 33 VDAGLTTFDCADIYGPaEELIGEfrkRLRRERDAADDVQIHTKWVPDPGeltmTRAYVEAAIDRSLKRLGVDRLDLVQFH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 109 WPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIPAVDQIelhpQFQQIDTRP------LLAENDIK 182
Cdd:cd19101 113 WWDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAGVPIVSNQV----QYSLLDRRPengmaaLCEDHGIK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 183 IEAWGPLGQG-------NVD--------------YASTV---------------IGEIAEAHGKSWAQVIIRWHLQR--- 223
Cdd:cd19101 189 LLAYGTLAGGllsekylGVPeptgpaletrslqkYKLMIdewggwdlfqellrtLKAIADKHGVSIANVAVRWVLDQpgv 268
|
250 260 270
....*....|....*....|....*....|....*.
gi 1949187231 224 -GHILfpKSNNRERMAQNFDVFDFTLTDAEMASIDA 258
Cdd:cd19101 269 aGVIV--GARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-226 |
1.65e-21 |
|
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: 91.50 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFG---VF--KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAasGIPRDELFITTKL-W---- 77
Cdd:cd19074 1 GLKVSELSLGtwlTFggQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWptgp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 78 --NDRhGAaeSRR----ALEESLTKLGLDYVNLYLIHWP---TPaqknAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPE 148
Cdd:cd19074 79 gpNDR-GL--SRKhifeSIHASLKRLQLDYVDIYYCHRYdpeTP----LEETVRAMDDLIRQGKILYWGTSEWSAEQIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 149 ILDTG-----IIPAVDQIELHPQFQQIDT--RPLLAENDIKIEAWGPLGQG----------------------------- 192
Cdd:cd19074 152 AHDLArqfglIPPVVEQPQYNMLWREIEEevIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrr 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1949187231 193 ----NVDYASTVIGEIAEAHGKSWAQVIIRWHLQRGHI 226
Cdd:cd19074 232 lltdENLEKVKKLKPIADELGLTLAQLALAWCLRNPAV 269
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
3-256 |
3.91e-20 |
|
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: 87.88 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 3 VPDLTL-NDGLTIPQLGFGVFKVD----PKETE----RIVTDALEVGYRHIDTAAVYG-NEEGVGRALAASGIPRDELFI 72
Cdd:cd19144 1 IPTRTLgRNGPSVPALGFGAMGLSafygPPKPDeerfAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 73 TTKLWNDRHGAAES----------RRALEESLTKLGLDYVNLYLIHW---PTPAQKnaveTWEAFPGYRDEGLTRSIGVS 139
Cdd:cd19144 81 ATKFGIEKNVETGEysvdgspeyvKKACETSLKRLGVDYIDLYYQHRvdgKTPIEK----TVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 140 NFDYRYLPEILDTGIIPAVdQIELHPQFQQIDTRPL-----LAENDIKIEAWGPLGQGNV-------------DYASTV- 200
Cdd:cd19144 157 ECSAETLRRAHAVHPIAAV-QIEYSPFSLDIERPEIgvldtCRELGVAIVAYSPLGRGFLtgairspddfeegDFRRMAp 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949187231 201 ----------------IGEIAEAHGKSWAQVIIRWHLQRGH--ILFPKSNNRERMAQNFDVFDFTLTDAEMASI 256
Cdd:cd19144 236 rfqaenfpknlelvdkIKAIAKKKNVTAGQLTLAWLLAQGDdiIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-139 |
5.32e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 86.81 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 16 QLG--FGVF----KVDPKETERIVTDALEVGYRHIDTAAVYGN-EEGVGRALAASgiprDELFITTKLWNDRHGAAESRR 88
Cdd:cd19097 9 QFGldYGIAnksgKPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL----DKFKIITKLPPLKEDKKEDEA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1949187231 89 A----LEESLTKLGLDYVNLYLIHWPTPAQKNAVETWEAFPGYRDEGLTRSIGVS 139
Cdd:cd19097 85 AieasVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGVS 139
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
11-257 |
3.80e-19 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 84.98 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFKV--------DPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAAsgiPRDELFITTKL--- 76
Cdd:cd19078 1 GLEVSAIGLGCMGMshgygpppDKEEMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKP---FRDQVVIATKFgfk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 ---WNDRHGAAES-----RRALEESLTKLGLDYVNLYLIHWPTPaqKNAVET-WEAFPGYRDEGLTRSIGVSNFDYRYLP 147
Cdd:cd19078 78 idgGKPGPLGLDSrpehiRKAVEGSLKRLQTDYIDLYYQHRVDP--NVPIEEvAGTMKELIKEGKIRHWGLSEAGVETIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 148 EILDTGIIPAVdQIELHPQFQQIDTR--PLLAENDIKIEAWGPLGQG--------NVDYAST------------------ 199
Cdd:cd19078 156 RAHAVCPVTAV-QSEYSMMWREPEKEvlPTLEELGIGFVPFSPLGKGfltgkideNTKFDEGddraslprftpealeanq 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949187231 200 ----VIGEIAEAHGKSWAQVIIRWHL-QRGHIL-FPKSNNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19078 235 alvdLLKEFAEEKGATPAQIALAWLLaKKPWIVpIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
15-192 |
6.44e-19 |
|
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: 83.95 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFG------VFKVDPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAasGIPRDELFITTKL--------- 76
Cdd:cd19162 1 PRLGLGaaslgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 ---------WNdrHGAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAV-ETWEAFPGYRDEGLTRSIGVSNFDYRYL 146
Cdd:cd19162 79 grpagadrrFD--FSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALtDAFPALEELRAEGVVGAIGVGVTDWAAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1949187231 147 PEILDTGIIPAVDQIELHPQFQQIDTRPLL---AENDIKIEAWGPLGQG 192
Cdd:cd19162 157 LRAARRADVDVVMVAGRYTLLDRRAATELLplcAAKGVAVVAAGVFNSG 205
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
11-141 |
1.96e-18 |
|
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: 83.01 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGV--F--KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASgipRDELFITTKL------W 77
Cdd:cd19087 10 GLKVSRLCLGTmnFggRTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKVfgpmgdD 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187231 78 NDRHGAaeSRR----ALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNF 141
Cdd:cd19087 87 PNDRGL--SRRhirrAVEASLRRLQTDYIDLYQMHHFdrdTPLE----ETLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-192 |
3.73e-18 |
|
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: 81.83 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFG------VFK-VDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALaaSGIPRDELFITTKLwn 78
Cdd:cd19163 8 KTGLKVSKLGFGasplggVFGpVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL--KGIPRDSYYLATKV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAES----------RRALEESLTKLGLDYVNLYLIHWPTPAQKNAV---ETWEAFPGYRDEGLTRSIGVSNFDYRY 145
Cdd:cd19163 84 GRYGLDPDkmfdfsaeriTKSVEESLKRLGLDYIDIIQVHDIEFAPSLDQilnETLPALQKLKEEGKVRFIGITGYPLDV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 146 LPEILDTGIIpAVDQIELHPQFQQIDTR-----PLLAENDIKIEAWGPLGQG 192
Cdd:cd19163 164 LKEVLERSPV-KIDTVLSYCHYTLNDTSllellPFFKEKGVGVINASPLSMG 214
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-153 |
4.02e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 79.62 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFG-------VFKVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALaaSGIPrDELFITTK--LWN 78
Cdd:cd19104 9 GLKVSELTFGgggigglMGRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRAL--KGLP-AGPYITTKvrLDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAES--RRALEESLTKLGLDYVNLYLIH--------WPTPA--------QKNAVetWEAFPGYRDEGLTRSIGVSN 140
Cdd:cd19104 86 DDLGDIGGqiERSVEKSLKRLKRDSVDLLQLHnrigderdKPVGGtlsttdvlGLGGV--ADAFERLRSEGKIRFIGITG 163
|
170
....*....|....
gi 1949187231 141 FD-YRYLPEILDTG 153
Cdd:cd19104 164 LGnPPAIRELLDSG 177
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
25-257 |
1.31e-16 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 78.03 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 25 DPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASgipRDELFITTKL-WNDRHGAAES--------RRALEE 92
Cdd:cd19080 29 DREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYtMNRRPGDPNAggnhrknlRRSVEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 93 SLTKLGLDYVNLYLIHWP---TPAQknavETWEAFpgyrdEGLTRS-----IGVSNF------------DYRYLPEildt 152
Cdd:cd19080 106 SLRRLQTDYIDLLYVHAWdftTPVE----EVMRAL-----DDLVRAgkvlyVGISDTpawvvarantlaELRGWSP---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 153 giiPAVDQIELHPQFQQI--DTRPLLAENDIKIEAWGPLGQG------NVDYAST-----------------------VI 201
Cdd:cd19080 173 ---FVALQIEYSLLERTPerELLPMARALGLGVTPWSPLGGGlltgkyQRGEEGRageakgvtvgfgklternwaivdVV 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187231 202 GEIAEAHGKSWAQVIIRWHLQRGHILFP--KSNNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19080 250 AAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-140 |
3.67e-16 |
|
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: 76.44 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 17 LGFGVF--KVDPKETERIVTDALEVGYRHIDTAAVYGNEEGVGRA-------LAASGIpRDELFITTK--------LWND 79
Cdd:cd19082 5 LGTADFgtRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServigewLKSRGN-RDKVVIATKgghpdledMSRS 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187231 80 RHGAAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNA--VETWEAFpgyRDEGLTRSIGVSN 140
Cdd:cd19082 84 RLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGeiVDTLNEL---VRAGKIRAFGASN 143
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
10-257 |
4.22e-16 |
|
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: 76.51 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 10 DGLTIPQLGFGV-------FKVDPKETERIVTDALEVGYRHIDTAAVYG------NEEGVGRALAASGIPRDELFITTK- 75
Cdd:cd19077 1 NGKLVGPIGLGLmgltwrpNPTPDEEAFETMKAALDAGSNLWNGGEFYGppdphaNLKLLARFFRKYPEYADKVVLSVKg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 76 ----LWNDRHGAAES-RRALEESLTKLG-LDYVNLYlihwpTPAQKN-AV---ETWEAFPGYRDEGLTRSIGVSNFDYRY 145
Cdd:cd19077 81 gldpDTLRPDGSPEAvRKSIENILRALGgTKKIDIF-----EPARVDpNVpieETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 146 LPEILDTGIIPAVdQIELHPQFQQI---DTRPLLAENDIKIEAWGPLGQG------------------------------ 192
Cdd:cd19077 156 IRRAHAVHPIAAV-EVEYSLFSREIeenGVLETCAELGIPIIAYSPLGRGlltgriksladipegdfrrhldrfngenfe 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187231 193 -NVDYASTVIgEIAEAHGKSWAQVIIRW--HLQRGHIL-FPKSNNRERMAQNFDVFDFTLTDAEMASID 257
Cdd:cd19077 235 kNLKLVDALQ-ELAEKKGCTPAQLALAWilAQSGPKIIpIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
20-161 |
5.21e-16 |
|
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: 76.03 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 20 GVFKVDPKETE--RIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASGIPRDELFITTKLWNDRHG-----AAESRRA 89
Cdd:cd19153 24 GVYGDGLEQDEavAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVGRYRDSefdysAERVRAS 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949187231 90 LEESLTKLGLDYVNLYLIHWPTPAQKNAV--ETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDTGIIPAVDQI 161
Cdd:cd19153 104 VATSLERLHTTYLDVVYLHDIEFVDYDTLvdEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLDAV 177
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-259 |
2.28e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 74.29 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 18 GFGVF--KVDPKETERIVTDALEVGYRHIDTAAVYG---NEEGVGRALAAsgIPRDELFITTKLWNDRHGAAESRRA--L 90
Cdd:cd19103 21 GDQVFgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR--YPREDYIISTKFTPQIAGQSADPVAdmL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 91 EESLTKLGLDYVNLYLIHWPTPAQKNaveTWEAFPGYRdEGLTRSIGVSNF---DYRYLPEILDTGIIPaVDQIELHPQ- 166
Cdd:cd19103 99 EGSLARLGTDYIDIYWIHNPADVERW---TPELIPLLK-SGKVKHVGVSNHnlaEIKRANEILAKAGVS-LSAVQNHYSl 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 167 -FQQIDTRPLLA---ENDIKIEAWGPLGQGNVDYAST---------------------------VIGEIAEAHGKSWAQV 215
Cdd:cd19103 174 lYRSSEEAGILDyckENGITFFAYMVLEQGALSGKYDtkhplpegsgraetynpllpqleeltaVMAEIGAKHGASIAQV 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1949187231 216 IIRWHLQRGHILFPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19103 254 AIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-223 |
2.64e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 73.91 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 19 FGVfKVDPKETERIVTDALEVGYRHIDTAAVYG----------NEEGVGRALAASGIpRDELFITTKL---WNDRHGAAE 85
Cdd:cd19752 10 FGT-RTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvggeSERLIGRWLKDRGN-RDDVVIATKVgagPRDPDGGPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 86 S---------RRALEESLTKLGLDYVNLYLIH---WPTPAQknavETWEAFPGYRDEGLTRSIGVSNFD----------- 142
Cdd:cd19752 88 SpeglsaetiEQEIDKSLRRLGTDYIDLYYAHvddRDTPLE----ETLEAFNELVKAGKVRAIGASNFAawrlerarqia 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 143 --------------YRYL-PE---------ILDTGIIpavDQIELHPQFQQIDTRPLLA---ENDIKIEAWGPLGQGNvD 195
Cdd:cd19752 164 rqqgwaefsaiqqrHSYLrPRpgadfgvqrIVTDELL---DYASSRPDLTLLAYSPLLSgayTRPDRPLPEQYDGPDS-D 239
|
250 260
....*....|....*....|....*...
gi 1949187231 196 YASTVIGEIAEAHGKSWAQVIIRWHLQR 223
Cdd:cd19752 240 ARLAVLEEVAGELGATPNQVVLAWLLHR 267
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
11-257 |
5.81e-15 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 73.49 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFK----VDPKETER-IVTDALEVGYRHIDTAAVYG-----NEEGVGRALAASGIP-RDELFITTK---- 75
Cdd:PRK09912 22 GLRLPALSLGLWHnfghVNALESQRaILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagyd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 76 LWNDRHGAAESRR----ALEESLTKLGLDYVNLYLIHW---PTPAQknavETWEAFPGYRDEGLTRSIGVSNFD---YRY 145
Cdd:PRK09912 102 MWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSHRvdeNTPME----ETASALAHAVQSGKALYVGISSYSperTQK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 146 LPEILDTGIIP-AVDQIELHPQFQQIDTRPL---LAENDIKIEAWGPLGQG----------------------------- 192
Cdd:PRK09912 178 MVELLREWKIPlLIHQPSYNLLNRWVDKSGLldtLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpk 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187231 193 -----NVDyASTVIGEIAEAHGKSWAQVIIRWHLQRGHI--LFPKSNNRERMAQNFDVF-DFTLTDAEMASID 257
Cdd:PRK09912 258 mlteaNLN-SLRLLNEMAQQRGQSMAQMALSWLLKDERVtsVLIGASRAEQLEENVQALnNLTFSTEELAQID 329
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
36-259 |
8.31e-15 |
|
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: 72.98 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 36 ALEVGYRHIDTAAVY---------G-NEEGVGRALAASGiPRDELFITTKL--------WND----RHGAAESRRALEES 93
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqGrTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRgggtRLDRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 94 LTKLGLDYVNLYLIHWP---TP-----------AQKNAV---ETWEAFPGYRDEGLTRSIGVSN-FDY---RYLpEILDT 152
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPdryTPlfgggyytepsEEEDSVsfeEQLEALGELVKAGKIRHIGLSNeTPWgvmKFL-ELAEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 153 GIIPAVDQIE-----LHPQFQqidtrPLLAE----NDIKIEAWGPLGQG------------------------------- 192
Cdd:cd19094 185 LGLPRIVSIQnpyslLNRNFE-----EGLAEachrENVGLLAYSPLAGGvltgkyldgaarpeggrlnlfpgymaryrsp 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 193 NVDYASTVIGEIAEAHGKSWAQVIIRWHLQRGHIlfpKSN-----NRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:cd19094 260 QALEAVAEYVKLARKHGLSPAQLALAWVRSRPFV---TSTiigatTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-219 |
2.38e-14 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 71.43 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 18 GFGVF--KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASgiprDELFITTK---LWNDRHGAAESRRA 89
Cdd:cd19075 9 TFGSQgrFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELGLGE----RGFKIDTKanpGVGGGLSPENVRKQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 90 LEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT----G-IIPAVdqi 161
Cdd:cd19075 85 LETSLKRLKVDKVDVFYLHAPdrsTPLE----ETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEIckenGwVLPTV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 162 elhpqFQ--------QIDTR--PLLAENDIKIEAWGPLGQG------------------------------------NVD 195
Cdd:cd19075 158 -----YQgmynaitrQVETElfPCLRKLGIRFYAYSPLAGGfltgkykysedkagggrfdpnnalgklyrdrywkpsYFE 232
|
250 260
....*....|....*....|....
gi 1949187231 196 yASTVIGEIAEAHGKSWAQVIIRW 219
Cdd:cd19075 233 -ALEKVEEAAEKEGISLAEAALRW 255
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
9-226 |
9.05e-14 |
|
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: 69.98 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFGVFK----VDPKETER-IVTDALEVGYRHIDTAAVYGNEEG-----VGRALAASGIP-RDELFITTK-- 75
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdYTSPEEAReLLRTAFDLGITHFDLANNYGPPPGsaeenFGRILKRDLRPyRDELVISTKag 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 76 --LWNDRHGAAESRR----ALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFD---Y 143
Cdd:cd19089 86 ygMWPGPYGDGGSRKyllaSLDQSLKRMGLDYVDIFYHHRYdpdTPLE----ETMTALADAVRSGKALYVGISNYPgakA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 144 RYLPEIL-DTGIIPAVDQIELHPQFQQIDTR--PLLAENDIKIEAWGPLGQG--NVDYAS-------------------- 198
Cdd:cd19089 162 RRAIALLrELGVPLIIHQPRYSLLDRWAEDGllEVLEEAGIGFIAFSPLAQGllTDKYLNgippdsrraaeskflteeal 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 1949187231 199 --------TVIGEIAEAHGKSWAQVIIRWHLQRGHI 226
Cdd:cd19089 242 tpekleqlRKLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
9-161 |
9.36e-14 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 69.81 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFG------VFKVDPKETERI-VTDALEVGYRHIDTAAVYGN---EEGVGRALAASGIPRDELFITTKLWN 78
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFGPVSEEDAIAsVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHG----AAESRRALEESLTKLGLDYVNLYLIHWPTPAQKNAV--ETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT 152
Cdd:PLN02587 86 YGEGfdfsAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIvnETIPALQKLKESGKVRFIGITGLPLAIFTYVLDR 165
|
....*....
gi 1949187231 153 GIIPAVDQI 161
Cdd:PLN02587 166 VPPGTVDVI 174
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-219 |
1.22e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 66.57 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 12 LTIPQLGFGVFKVDP-----KETERIVTDALEVGYRHIDTAAVYGN---EEGVGRAL----AASGIPRDELFITTK---- 75
Cdd:cd19099 1 LTLSSLGLGTYRGDSddetdEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALreliEKGGIKRDEVVIVTKagyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 76 ---------------LWNDRHGAAES--------------RRALEESLTKLGLDYVNLYLIHWPtPAQ----------KN 116
Cdd:cd19099 81 pgdgdeplrplkyleEKLGRGLIDVAdsaglrhcispaylEDQIERSLKRLGLDTIDLYLLHNP-EEQllelgeeefyDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 117 AVETWEAFPGYRDEGLTRSIGVS-NFDYRYLPE----ILDTGIIPAVD------------QIELHPQFQQIDTRP----- 174
Cdd:cd19099 160 LEEAFEALEEAVAEGKIRYYGIStWDGFRAPPAlpghLSLEKLVAAAEevggdnhhfkviQLPLNLLEPEALTEKntvkg 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 175 -------LLAENDIKIEAWGPLGQGNVDYASTVIGEIAEAHGKSWAQVIIRW 219
Cdd:cd19099 240 ealslleAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGATLAQRALQF 291
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
16-259 |
1.61e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 63.06 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 16 QL-GFGVFKvDPKETERIVT---DALEVGYRHIDTAAVYG---NEEGVGRALAasgiP-RDELFITTKL---------WN 78
Cdd:PRK10376 26 QLaGPGVFG-PPKDRDAAIAvlrEAVALGVNHIDTSDFYGphvTNQLIREALH----PyPDDLTIVTKVgarrgedgsWL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 79 DRHGAAESRRALEESLTKLG---LDYVNLYLIHWPT-PAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEilDTGI 154
Cdd:PRK10376 101 PAFSPAELRRAVHDNLRNLGldvLDVVNLRLMGDGHgPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAE--ARKI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 155 IPAV---DQIEL-HPQFQQ-IDTrplLAENDIKIEAWGPLGqGNVDYASTVIGEIAEAHGKSWAQVIIRWHLQRGH--IL 227
Cdd:PRK10376 179 AEIVcvqNHYNLaHRADDAlIDA---LARDGIAYVPFFPLG-GFTPLQSSTLSDVAASLGATPMQVALAWLLQRSPniLL 254
|
250 260 270
....*....|....*....|....*....|..
gi 1949187231 228 FPKSNNRERMAQNFDVFDFTLTDAEMASIDAL 259
Cdd:PRK10376 255 IPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
28-139 |
1.65e-11 |
|
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: 63.06 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 28 ETERIVTDALEVGYRHIDTAAVYGNEEGV-GRALAA--SGIPRDELFITTKLwnDRHGAAE-------SRRALEESLTKL 97
Cdd:cd19164 35 PPVDIVRRALELGIRAFDTSPYYGPSEIIlGRALKAlrDEFPRDTYFIITKV--GRYGPDDfdyspewIRASVERSLRRL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1949187231 98 GLDYVNLYLIH---WPTPAqknavETWEAFP---GYRDEGLTRSIGVS 139
Cdd:cd19164 113 HTDYLDLVYLHdveFVADE-----EVLEALKelfKLKDEGKIRNVGIS 155
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-192 |
3.14e-11 |
|
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: 62.63 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFG-------VFKVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAasGIPRDELFITTKL-------- 76
Cdd:cd19152 1 PKLGFGtaplgnlYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR--ELGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 ----------WNDRH-------GAAESRRALEESLTKLGLDYVNLYLIH-------WPTPAQKNAVETWEAFPGY---RD 129
Cdd:cd19152 79 eveptfepgfWNPLPfdavfdySYDGILRSIEDSLQRLGLSRIDLLSIHdpdedlaGAESDEHFAQAIKGAFRALeelRE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 130 EGLTRSIGVSNFDYRYLPEILDTGIIPAV---------DQIELHPQFqqidtrPLLAENDIKIEAWGPLGQG 192
Cdd:cd19152 159 EGVIKAIGLGVNDWEVILRILEEADLDWVmlagrytllDHSAARELL------PECEKRGVKVVNAGPFNSG 224
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
9-113 |
4.55e-11 |
|
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: 62.23 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFGVF-----KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASGIPRDELFITTKL-WND 79
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1949187231 80 RHGAAESR--------RALEESLTKLGLDYVNLYLIHWPTPA 113
Cdd:cd19143 88 GGPPPNDRglsrkhivEGTKASLKRLQLDYVDLVFCHRPDPA 129
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
11-254 |
7.31e-11 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 61.32 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFK----VDPKETER-IVTDALEVGYRHIDTAAVYG-----NEEGVGRALAASGIP-RDELFITTK---- 75
Cdd:cd19150 9 GLKLPALSLGLWHnfgdDTPLETQRaILRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAGyRDELIISTKagyd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 76 LWNDRHGAAESRR----ALEESLTKLGLDYVNLYLIHW---PTPAQknavETWEAFPGYRDEGLTRSIGVSNFD---YRY 145
Cdd:cd19150 89 MWPGPYGEWGSRKyllaSLDQSLKRMGLDYVDIFYSHRfdpDTPLE----ETMGALDHAVRSGKALYVGISSYSperTRE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 146 LPEILDTGIIPA-------------VDQIELhpqfqqIDTrplLAENDIKIEAWGPLGQG-------------------- 192
Cdd:cd19150 165 AAAILRELGTPLlihqpsynmlnrwVEESGL------LDT---LQELGVGCIAFTPLAQGlltdkylngipegsrasker 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187231 193 ----------NVDYASTvIGEIAEAHGKSWAQVIIRWHLQRGHI--LFPKSNNRERMAQNFDVFD-FTLTDAEMA 254
Cdd:cd19150 236 slspkmlteaNLNSIRA-LNEIAQKRGQSLAQMALAWVLRDGRVtsALIGASRPEQLEENVGALDnLTFSADELA 309
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-141 |
9.50e-11 |
|
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: 60.88 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 9 NDGLTIPQLGFGVFK----VDPKETER-IVTDALEVGYRHIDTAAVYG-----NEEGVGRALAASGIP-RDELFITTK-- 75
Cdd:cd19151 7 RSGLKLPAISLGLWHnfgdVDRYENSRaMLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKPyRDELIISTKag 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187231 76 --LWNDRHGAAESRR----ALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNF 141
Cdd:cd19151 87 ytMWPGPYGDWGSKKyliaSLDQSLKRMGLDYVDIFYHHRPdpeTPLE----ETMGALDQIVRQGKALYVGISNY 157
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
11-108 |
3.60e-09 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 56.32 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVFK-----VDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASGIPRDELFITTKL-WNDR- 80
Cdd:cd19142 10 GLRVSNVGLGTWStfstaISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIyWSYGs 89
|
90 100 110
....*....|....*....|....*....|..
gi 1949187231 81 HGAAESRR----ALEESLTKLGLDYVNLYLIH 108
Cdd:cd19142 90 EERGLSRKhiieSVRASLRRLQLDYIDIVIIH 121
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
36-140 |
1.93e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 54.47 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 36 ALEVGYRHIDTAAVYG----------NEEGVGRALAASGiPRDELFITTKLWNDRHGAAES------------RRALEES 93
Cdd:PRK10625 39 AVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSGPSRNNDKGirpnqaldrkniREALHDS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187231 94 LTKLGLDYVNLYLIHWP----------------TPAQKNAVETWEAFPGYRDEGLTRSIGVSN 140
Cdd:PRK10625 118 LKRLQTDYLDLYQVHWPqrptncfgklgyswtdSAPAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
11-256 |
2.67e-08 |
|
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: 53.59 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGV-----FKVDPK-ETERI--VTDALEVGYRHIDTAAVYG---NEEGVGRALaaSGIPRDELFITTKL--- 76
Cdd:cd19145 9 GLEVSAQGLGCmglsgDYGAPKpEEEGIalIHHAFNSGVTFLDTSDIYGpntNEVLLGKAL--KDGPREKVQLATKFgih 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 77 ------WNDRHGAAESRRALEESLTKLGLDYVNLYLIH---WPTPAQ------KNAVEtweafpgyrdEGLTRSIGVSNF 141
Cdd:cd19145 87 eiggsgVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHridTTVPIEitmgelKKLVE----------EGKIKYIGLSEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 142 DYRYLPEILDTGIIPAVdQIE--LHPQFQQIDTRPLLAENDIKIEAWGPLGQG-------------NVDYASTV------ 200
Cdd:cd19145 157 SADTIRRAHAVHPITAV-QLEwsLWTRDIEEEIIPTCRELGIGIVPYSPLGRGffagkakleelleNSDVRKSHprfqge 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187231 201 -----------IGEIAEAHGKSWAQVIIRWHLQRGH--ILFPKSNNRERMAQNFDVFDFTLTDAEMASI 256
Cdd:cd19145 236 nleknkvlyerVEALAKKKGCTPAQLALAWVLHQGEdvVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
11-192 |
3.54e-08 |
|
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: 53.60 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVF-----KVDPKETERIVTDALEVGYRHIDTAAVY--GNEEGV-GRALAASGIPRDELFITTKL-WNdrh 81
Cdd:cd19141 9 GLRVSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYaaGKAEIVlGKILKKKGWRRSSYVITTKIfWG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRR---------ALEESLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFDYRYLPEI 149
Cdd:cd19141 86 GKAETERglsrkhiieGLKASLERLQLEYVDIVFANRPdpnTPME----EIVRAFTHVINQGMAMYWGTSRWSAMEIMEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 150 LDTG-----IIPAVDQIELHpQFQQIDTRPLLAENDIKIE----AWGPLGQG 192
Cdd:cd19141 162 YSVArqfnlIPPIVEQAEYH-LFQREKVEMQLPELFHKIGvgamTWSPLACG 212
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
11-192 |
5.68e-07 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 50.04 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVF-----KVDPKETERIVTDALEVGYRHIDTAAVY--GNEEGV-GRALAASGIPRDELFITTKL-WNdrh 81
Cdd:cd19159 10 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVIlGSIIKKKGWRRSSLVITTKLyWG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRRALEE---------SLTKLGLDYVNLYLIHWP---TPAQknavETWEAFPGYRDEGLTRSIGVSNFDYRYLPEI 149
Cdd:cd19159 87 GKAETERGLSRkhiieglkgSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 150 LDTG-----IIPAVDQIELHpQFQQIDTRPLLAE--NDIKIEA--WGPLGQG 192
Cdd:cd19159 163 YSVArqfnmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACG 213
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
26-258 |
1.89e-06 |
|
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: 48.19 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 26 PKETERIVTDAL-EVGYRHIDTAAVY---GNEEGVGRALAASGIpRDELFITTKL-------------WNDRHGAAESRR 88
Cdd:cd19146 33 DKETAFKLLDAFyEQGGNFIDTANNYqgeESERWVGEWMASRGN-RDEMVLATKYttgyrrggpikikSNYQGNHAKSLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 89 -ALEESLTKLGLDYVNLYLIHW-----------------------------PTPAQknAVETWEAFPgyRDEGLTR---- 134
Cdd:cd19146 112 lSVEASLKKLQTSYIDILYVHWwdyttsipelmqslnhlvaagkvlylgvsDTPAW--VVSKANAYA--RAHGLTQfvvy 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 135 ----SIGVSNFDYRYLPEILDTG--IIP----AVDQIELHPQFQQIDTRP----LLAENDIKIeawgplgqgnvdyaSTV 200
Cdd:cd19146 188 qghwSAAFRDFERDILPMCEAEGmaLAPwgvlGQGQFRTEEEFKRRGRSGrkggPQTEKERKV--------------SEK 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 201 IGEIAEAHGKSWAQVIIRWHLQRGHILFPKSNNR--ERMAQNFDVFDFTLTDAEMASIDA 258
Cdd:cd19146 254 LEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRkvEHLKGNIEALGISLSDEEIQEIED 313
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
11-194 |
2.68e-06 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 47.77 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVF-----KVDPKETERIVTDALEVGYRHIDTAAVY--GNEEGV-GRALAASGIPRDELFITTKL-WNdrh 81
Cdd:cd19158 10 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRRAL---------EESLTKLGLDYVNLYLIHWPTPaQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT 152
Cdd:cd19158 87 GKAETERGLsrkhiieglKASLERLQLEYVDVVFANRPDP-NTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1949187231 153 G-----IIPAVDQIELHpQFQQIDTRPLLAE--NDIKIEA--WGPLGQGNV 194
Cdd:cd19158 166 ArqfnlIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGIV 215
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
11-192 |
5.16e-06 |
|
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: 46.90 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 11 GLTIPQLGFGVF-----KVDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAASGIPRDELFITTKL-WNdrh 81
Cdd:cd19160 12 GLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIyWG--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 82 GAAESRRALEE---------SLTKLGLDYVNLYLIHwPTPAQKNAVETWEAFPGYRDEGLTRSIGVSNFDYRYLPEILDT 152
Cdd:cd19160 89 GQAETERGLSRkhiieglrgSLDRLQLEYVDIVFAN-RSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1949187231 153 G-----IIPAVDQIELHpQFQQIDTRPLLAENDIKIE----AWGPLGQG 192
Cdd:cd19160 168 ArqfnlIPPVCEQAEYH-LFQREKVEMQLPELYHKIGvgsvTWSPLACG 215
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-108 |
2.89e-05 |
|
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: 44.62 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 15 PQLGFG------VFK-VDPKETERIVTDALEVGYRHIDTAAVYGN---EEGVGRALAAsgIPRDELFITTK----LWNDR 80
Cdd:cd19161 1 SELGLGtaglgnLYTaVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKvgrlLKPAR 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1949187231 81 HGAAESR---------------------RALEESLTKLGLDYVNLYLIH 108
Cdd:cd19161 79 EGSVPDPngfvdplpfeivydysydgimRSFEDSLQRLGLNRIDILYVH 127
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
25-92 |
2.43e-04 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 41.78 E-value: 2.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187231 25 DPKETERIVTDALEvgyRHIDTAAVY----GNEeGVGRALAASGIPRDELFITTKLwndrhgAAESRRALEE 92
Cdd:cd06307 169 DDELAYELLRELLA---RHPDLVGIYnaggGNE-GIARALREAGRARRVVFIGHEL------TPETRRLLRD 230
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-112 |
4.45e-04 |
|
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: 41.18 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 40 GYRHIDTAAVYGN-EEGVGRALAASGIPRDELFITTKL-------WN--------DRHGAAESRRALEESLTKLGlDYVN 103
Cdd:cd19098 48 GVRYFDAARSYGRaEEFLGSWLRSRNIAPDAVFVGSKWgytytadWQvdaavhevKDHSLARLLKQWEETRSLLG-KHLD 126
|
....*....
gi 1949187231 104 LYLIHWPTP 112
Cdd:cd19098 127 LYQIHSATL 135
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
38-109 |
9.67e-04 |
|
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: 39.81 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187231 38 EVGYRHIDTAAVYGNEEG---VGRALAASGIpRDELFITTKLWND--RHGAAESRRA-------------LEESLTKLGL 99
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDykAYEVGKGKAVnycgnhkrslhvsVRDSLRKLQT 123
|
90
....*....|
gi 1949187231 100 DYVNLYLIHW 109
Cdd:cd19147 124 DWIDILYVHW 133
|
|
| |
