|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-276 |
0e+00 |
|
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: 513.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHWPGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELHP 167
Cdd:cd19156 81 STLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 168 LFQQRTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNV 247
Cdd:cd19156 161 LLTQEPLRKFCKEKNIAVEAWSPLGQGK---LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDV 237
|
250 260
....*....|....*....|....*....
gi 408407927 248 WDFKLTEEEMRQIDELNEDKRIGGDPDNF 276
Cdd:cd19156 238 FDFELTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-274 |
2.32e-175 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 483.79 E-value: 2.32e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 12 NSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEKTLA 91
Cdd:COG0656 1 NGVEIPALGLGTWQL-PGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 92 AFERSRELLGLEYIDLYLIHWPGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELHPLFQQ 171
Cdd:COG0656 80 AFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 172 RTLREFCKQHNIAITAWSPLGSGeeaGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFK 251
Cdd:COG0656 160 RELLAFCREHGIVVEAYSPLGRG---KLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFE 236
|
250 260
....*....|....*....|...
gi 408407927 252 LTEEEMRQIDELNEDKRIGGDPD 274
Cdd:COG0656 237 LSDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-274 |
4.06e-162 |
|
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: 450.69 E-value: 4.06e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 7 CVTLHNSVRMPQLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGY 86
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 87 EKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELH 166
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 167 PLFQQRTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFN 246
Cdd:cd19157 161 PRLTQKELRDYCKKQGIQLEAWSPLMQGQ---LLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENAD 237
|
250 260
....*....|....*....|....*...
gi 408407927 247 VWDFKLTEEEMRQIDELNEDKRIGGDPD 274
Cdd:cd19157 238 VFDFELSQEDMDKIDALNENLRVGPDPD 265
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-264 |
1.76e-152 |
|
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: 426.08 E-value: 1.76e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHWPGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELHP 167
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 168 LFQQRTLREFCKQHNIAITAWSPLGSGeeaGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNV 247
Cdd:cd19126 161 YLTQKELRGYCKSKGIVVEAWSPLGQG---GLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADI 237
|
250
....*....|....*..
gi 408407927 248 WDFKLTEEEMRQIDELN 264
Cdd:cd19126 238 FDFELSEDDMTAIDALN 254
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-261 |
8.59e-150 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 418.81 E-value: 8.59e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEKTLAAFER 95
Cdd:cd19071 1 MPLIGLGTYKL-KPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 96 SRELLGLEYIDLYLIHWPG-------KKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELHPL 168
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVpgkeggsKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 169 FQQRTLREFCKQHNIAITAWSPLGSGEEaGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVW 248
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGRGRR-PLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVF 238
|
250
....*....|...
gi 408407927 249 DFKLTEEEMRQID 261
Cdd:cd19071 239 DFELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-264 |
2.06e-144 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 405.60 E-value: 2.06e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQV-SNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHW--PGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVEL 165
Cdd:cd19131 81 STLRAFDESLRKLGLDYVDLYLIHWpvPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 166 HPLFQQRTLREFCKQHNIAITAWSPLGSGeeaGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENF 245
Cdd:cd19131 161 HPRFQQRELRAFHAKHGIQTESWSPLGQG---GLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENF 237
|
250
....*....|....*....
gi 408407927 246 NVWDFKLTEEEMRQIDELN 264
Cdd:cd19131 238 DVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-264 |
3.64e-137 |
|
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: 387.32 E-value: 3.64e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHWPgkkkFVD---TWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVE 164
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQP----FGDvygAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 165 LHPLFQQRTLREFCKQHNIAITAWSPLGSGeEAGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQEN 244
Cdd:cd19133 157 THPFNQQIEAVEFLKKYGVQIEAWGPFAEG-RNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAEN 235
|
250 260
....*....|....*....|
gi 408407927 245 FNVWDFKLTEEEMRQIDELN 264
Cdd:cd19133 236 FDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-264 |
7.11e-126 |
|
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: 359.03 E-value: 7.11e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQdGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP-PEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHWPGKKKF---VDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVE 164
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPVPNDFdrtIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 165 LHPLFQQRTLREFCKQHNIAITAWSPLG-------SGEEAGI--LKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKS 235
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygaSGPTGPGdvLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKS 239
|
250 260
....*....|....*....|....*....
gi 408407927 236 TNKGRIQENFNVWDFKLTEEEMRQIDELN 264
Cdd:cd19127 240 VHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-263 |
4.72e-123 |
|
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: 351.93 E-value: 4.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRES----GVPREEVWVTTKVWNSDQGYEKTLA 91
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 92 AFERSRELLGLEYIDLYLIHWPGKKKF-----------VDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMV 160
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLkpsdprnaelrRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 161 NQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGeEAGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGR 240
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG-DLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPER 239
|
250 260
....*....|....*....|...
gi 408407927 241 IQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19136 240 IAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
6-263 |
7.31e-116 |
|
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: 333.52 E-value: 7.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 6 NCVTLHNSVRMPQLGLGVWraQDGAETANAVRWAI-EAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQ 84
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTS--HSGGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 85 GYEKTLAAFERSRELLGLEYIDLYLIHWPG--------KKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKI 156
Cdd:cd19135 81 GYESTKQAFEASLKRLGVDYLDLYLLHWPDcpssgknvKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 157 RPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKST 236
Cdd:cd19135 161 VPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK---ALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKST 237
|
250 260
....*....|....*....|....*..
gi 408407927 237 NKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19135 238 KEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-276 |
1.63e-114 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 330.50 E-value: 1.63e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQDgAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKRP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KtlAAFERSRELLGLEYIDLYLIHWP--GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVEL 165
Cdd:PRK11565 86 R--EALEESLKKLQLDYVDLYLMHWPvpAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 166 HPLFQQRTLREFCKQHNIAITAWSPLGSGEEaGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENF 245
Cdd:PRK11565 164 HPLMQQRQLHAWNATHKIQTESWSPLAQGGK-GVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENF 242
|
250 260 270
....*....|....*....|....*....|.
gi 408407927 246 NVWDFKLTEEEMRQIDELNEDKRIGGDPDNF 276
Cdd:PRK11565 243 DVFDFRLDKDELGEIAKLDQGKRLGPDPDQF 273
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-269 |
1.38e-112 |
|
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: 326.55 E-value: 1.38e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 7 CVTLHNSVRMPQLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRE----SGVPREEVWVTTKVWNS 82
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREkiaeGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 83 DQGYEKTLAAFERSRELLGLEYIDLYLIHWP-----------------GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPH 145
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesngdgslSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 146 HLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAGI------LKNHVLGEIAKKHNKSPAQV 219
Cdd:cd19116 162 QINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQtnppprLDDPTLVAIAKKYGKTTAQI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 408407927 220 VIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRI 269
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-264 |
3.38e-112 |
|
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: 323.84 E-value: 3.38e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 10 LHNSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEKT 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYPL-KGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 90 LAAFERSRELLGLEYIDLYLIHW--PGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELHP 167
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHWpnPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 168 LFQQRTLREFCKQHNIAITAWSPLGSGEeaGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNV 247
Cdd:cd19132 160 YFPQAEQRAYHREHGIVTQSWSPLGRGS--GLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAI 237
|
250
....*....|....*..
gi 408407927 248 WDFKLTEEEMRQIDELN 264
Cdd:cd19132 238 FDFELSDEDMAAIAALD 254
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-261 |
1.56e-109 |
|
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: 316.91 E-value: 1.56e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAQdGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEKTLAAFER 95
Cdd:cd19073 1 IPALGLGTWQLR-GDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 96 SRELLGLEYIDLYLIHWPGKKKFV-DTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTL 174
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWPNPTVPLeETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 175 REFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTE 254
Cdd:cd19073 160 LEYCRENDIVITAYSPLARGE---VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTS 236
|
....*..
gi 408407927 255 EEMRQID 261
Cdd:cd19073 237 EDVAKID 243
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-268 |
2.26e-108 |
|
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: 316.25 E-value: 2.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 10 LHNSVRMPQLGLGVWRAQDGaETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRES-----GVPREEVWVTTKVWNSDQ 84
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPG-QVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 85 GYEKTLAAFERSRELLGLEYIDLYLIHWP-----GKKKF---------------VDTWKALEKLYEEKKVRAIGVSNFEP 144
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPyaferGDNPFpknpdgtirydsthyKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 145 HHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGS-------GEEAGILKNHVLGEIAKKHNKSPA 217
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSpdrpwakPDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 408407927 218 QVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWR 290
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
7-269 |
7.79e-106 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 308.89 E-value: 7.79e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 7 CVTLHNSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESG----VPREEVWVTTKVWNS 82
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTWQA-DPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 83 DQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKKK---------------FVDTWKALEKLYEEKKVRAIGVSNFEPHHL 147
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKkgahmpepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 148 TELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGE----EAGILKNHVLGEIAKKHNKSPAQVVIRW 223
Cdd:cd19125 161 EDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGttwvKKNVLKDPIVTKVAEKLGKTPAQVALRW 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 408407927 224 DIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRI 269
Cdd:cd19125 241 GLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
7-268 |
2.64e-105 |
|
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: 308.19 E-value: 2.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 7 CVTLHNSVRMPQLGLGVWRAQdGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRE---SGV-PREEVWVTTKVWNS 82
Cdd:cd19154 3 SITLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 83 DQGYEKTLAAFERSRELLGLEYIDLYLIH--WPGKK------------------KFVDTWKALEKLYEEKKVRAIGVSNF 142
Cdd:cd19154 82 EHAPEDVEEALRESLKKLQLEYVDLYLIHapAAFKDdegesgtmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVSNF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 143 EPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAGILKNH------------VLGEIAK 210
Cdd:cd19154 162 NNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspapnllqdpIVKAIAE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 408407927 211 KHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19154 242 KHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-270 |
5.15e-105 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 306.01 E-value: 5.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQDgAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSD-DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHWPGKK--KFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVEL 165
Cdd:cd19134 82 ASQAACRASLERLGLDYVDLYLIHWPAGRegKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 166 HPLFQQRTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENF 245
Cdd:cd19134 162 HPLLNQAELRKVNAQHGIVTQAYSPLGVGR---LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNL 238
|
250 260
....*....|....*....|....*
gi 408407927 246 NVWDFKLTEEEMRQIDELNEDKRIG 270
Cdd:cd19134 239 DVFDFELTADHMDALDGLDDGTRFR 263
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-263 |
1.19e-102 |
|
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: 299.56 E-value: 1.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 11 HNSVRMPQLGLGVWRAQdGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEKTL 90
Cdd:cd19140 3 VNGVRIPALGLGTYPLT-GEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 91 AAFERSRELLGLEYIDLYLIHWPGKK-KFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVELHPLF 169
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWPNKDvPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 170 QQRTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDI-QHGIVTIPKSTNKGRIQENFNVW 248
Cdd:cd19140 162 DQRKLLDAAREHGIALTAYSPLARGE---VLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIF 238
|
250
....*....|....*
gi 408407927 249 DFKLTEEEMRQIDEL 263
Cdd:cd19140 239 DFTLSDEEMARIAAL 253
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-268 |
3.90e-101 |
|
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: 297.40 E-value: 3.90e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQDGaETANAVRWAIEAGYRHIDTAYIYSNERGVGQGI----RESGVPREEVWVTTKVWNSD 83
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKPG-EVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 84 QGYEKTLAAFERSRELLGLEYIDLYLIHWP-GKKKFV------------------DTWKALEKLYEEKKVRAIGVSNFEP 144
Cdd:cd19123 83 HAPEDVLPALEKTLADLQLDYLDLYLMHWPvALKKGVgfpesgedllslspipleDTWRAMEELVDKGLCRHIGVSNFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 145 HHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGE---------EAGILKNHVLGEIAKKHNKS 215
Cdd:cd19123 163 KKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegEPVLLEDPVINKIAEKHGAS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 408407927 216 PAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19123 243 PAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-264 |
1.69e-98 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 289.50 E-value: 1.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAQDgAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYE 87
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPP-ADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHW--PGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVEL 165
Cdd:cd19130 81 EPAAAFAESLAKLGLDQVDLYLVHWptPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 166 HPLFQQRTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENF 245
Cdd:cd19130 161 HPAYQQRTIRDWAQAHDVKIEAWSPLGQGK---LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNL 237
|
250
....*....|....*....
gi 408407927 246 NVWDFKLTEEEMRQIDELN 264
Cdd:cd19130 238 DVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-263 |
9.78e-95 |
|
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: 280.92 E-value: 9.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 9 TLHNSVRMPQLGLGVWRAQDGaETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQgyEK 88
Cdd:cd19117 7 KLNTGAEIPAVGLGTWQSKPN-EVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWH--RR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 89 TLAAFERSRELLGLEYIDLYLIHWP----------------GKKK------FVDTWKALEKLYEEKKVRAIGVSNFEPHH 146
Cdd:cd19117 84 VEEALDQSLKKLGLDYVDLYLMHWPvpldpdgndflfkkddGTKDhepdwdFIKTWELMQKLPATGKVKAIGVSNFSIKN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 147 LTELFK--SCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSgEEAGILKNHVLGEIAKKHNKSPAQVVIRWD 224
Cdd:cd19117 164 LEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS-TNAPLLKEPVIIKIAKKHGKTPAQVIISWG 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 408407927 225 IQHGIVTIPKSTNKGRIQENFNVWDfkLTEEEMRQIDEL 263
Cdd:cd19117 243 LQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDEL 279
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
16-262 |
3.67e-92 |
|
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: 273.72 E-value: 3.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGV---WRAQDGA----ETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEK 88
Cdd:cd19120 4 IPAIAFGTgtaWYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIKDPRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 89 tlaAFERSRELLGLEYIDLYLIHWP-----GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQV 163
Cdd:cd19120 84 ---ALRKSLAKLGVDYVDLYLIHSPffakeGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAVNQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 164 ELHPLF--QQRTLREFCKQHNIAITAWSPLGS-GEEAGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGR 240
Cdd:cd19120 161 EFHPYLypQQPALLEYCREHGIVVSAYSPLSPlTRDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEER 240
|
250 260
....*....|....*....|..
gi 408407927 241 IQENFNVWDFKLTEEEMRQIDE 262
Cdd:cd19120 241 MKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
6-269 |
2.61e-91 |
|
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: 272.86 E-value: 2.61e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 6 NCVTLHNSVRMPQLGLGVWRAQDgAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRE---SG-VPREEVWVTTKV-- 79
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSP-EEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLpp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 -WNSDQGYEKTLAAferSRELLGLEYIDLYLIHWP----------------GKKK------FVDTWKALEKLYEEKKVRA 136
Cdd:cd19155 81 gGNRREKVEKFLLK---SLEKLQLDYVDLYLIHFPvgslskeddsgkldptGEHKqdyttdLLDIWKAMEAQVDQGLTRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 137 IGVSNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGS--------------GEEAGILKN 202
Cdd:cd19155 158 IGLSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfspgtgspsGSSPDLLQD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408407927 203 HVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRI 269
Cdd:cd19155 238 PVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
14-268 |
1.19e-90 |
|
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: 270.52 E-value: 1.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 14 VRMPQLGLGVWRAQdGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIR---ESG-VPREEVWVTTKVWNSDQGYEKT 89
Cdd:cd19111 2 FPMPVIGLGTYQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 90 LAAFERSRELLGLEYIDLYLIHWP------GKKKF--------VDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCK 155
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPcgfvnkKDKGErelassdvTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 156 IRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGS---------GEEAGILKNHVLGEIAKKHNKSPAQVVIRWDIQ 226
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpgranqslwPDQPDLLEDPTVLAIAKELDKTPAQVLLRFVLQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 408407927 227 HGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19111 241 RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
15-263 |
3.44e-87 |
|
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: 261.43 E-value: 3.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLGVWRAQDGAE-TANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRE---SGV--PREEVWVTTKVWNSDQGYEK 88
Cdd:cd19124 4 TMPVIGMGTASDPPSPEdIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGLvkSRDELFVTSKLWCSDAHPDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 89 TLAAFERSRELLGLEYIDLYLIHWP-----GKKKF---------VD---TWKALEKLYEEKKVRAIGVSNFEPHHLTELF 151
Cdd:cd19124 84 VLPALKKSLRNLQLEYVDLYLIHWPvslkpGKFSFpieeedflpFDikgVWEAMEECQRLGLTKAIGVSNFSCKKLQELL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 152 KSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAG----ILKNHVLGEIAKKHNKSPAQVVIRWDIQH 227
Cdd:cd19124 164 SFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWgsnaVMESDVLKEIAAAKGKTVAQVSLRWVYEQ 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 408407927 228 GIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19124 244 GVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-263 |
1.28e-86 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 260.04 E-value: 1.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 10 LHNSVRMPQLGLGVWRAQDGaETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRES-----GVPREEVWVTTKVWNSDQ 84
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPG-EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 85 GYEKTLAAFERSRELLGLEYIDLYLIHWPGKKKF-------------------------VDTWKALEKLYEEKKVRAIGV 139
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPtgdlnpltavptnggevdldlsvslVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 140 SNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGE--EAGILKNHVLGEIAKKHNKSPA 217
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLagLPLLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 408407927 218 QVVIRWDIQHGIVTIPKSTNKGRIQENFNvwDFKLTEEEMRQIDEL 263
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-263 |
1.03e-84 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 255.15 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 9 TLHNSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRES---GVPREEVWVTTKVWNSDqg 85
Cdd:cd19121 5 KLNTGASIPAVGLGTWQA-KAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 86 YEKTLAAFERSRELLGLEYIDLYLIHWP-----------------GKKKF------VDTWKALEKLYEEKKVRAIGVSNF 142
Cdd:cd19121 82 HRRVELCLDRSLKSLGLDYVDLYLVHWPvllnpngnhdlfptlpdGSRDLdwdwnhVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 143 EPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSgEEAGILKNHVLGEIAKKHNKSPAQVVIR 222
Cdd:cd19121 162 SIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS-TGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 408407927 223 WDIQHGIVTIPKSTNKGRIQENFNVWDFklTEEEMRQIDEL 263
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-269 |
2.60e-83 |
|
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: 252.34 E-value: 2.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLGVWRAQDGAETAnAVRWAIEAGYRHIDTAYIYSNERGVGQGI----RESGVPREEVWVTTKVWNSDqgYEKTL 90
Cdd:cd19107 3 KMPILGLGTWKSPPGQVTE-AVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTF--HEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 91 A--AFERSRELLGLEYIDLYLIHWP--------------------GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLT 148
Cdd:cd19107 80 VkgACQKTLSDLKLDYLDLYLIHWPtgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 149 ELFKS--CKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGS-------GEEAGILKNHVLGEIAKKHNKSPAQV 219
Cdd:cd19107 160 RILNKpgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwakPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 408407927 220 VIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRI 269
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRA 289
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
15-273 |
3.16e-82 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 249.49 E-value: 3.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLGVWRAQDGaETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIR----ESGVPREEVWVTTKVWNSdqGYEKTL 90
Cdd:cd19110 3 DIPAVGLGTWKASPG-EVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekikEGVVRREDLFIVSKLWCT--CHKKSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 91 --AAFERSRELLGLEYIDLYLIHWPGKKK--------------------FVDTWKALEKLYEEKKVRAIGVSNFEPHHLT 148
Cdd:cd19110 80 vkTACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 149 ELFK--SCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLG-SGEEAGILKNHVLGEIAKKHNKSPAQVVIRWDI 225
Cdd:cd19110 160 RLLNkpGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGgSCEGVDLIDDPVIQRIAKKHGKSPAQILIRFQI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 408407927 226 QHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRIGGDP 273
Cdd:cd19110 240 QRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-268 |
4.82e-82 |
|
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: 249.32 E-value: 4.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESG----VPREEVWVTTKVWNSD 83
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWNSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 84 QGYekTLAAFERSRELLGLEYIDLYLIHWPGKKK------------------------FVDTWKALEKLYEEKKVRAIGV 139
Cdd:cd19112 82 HGH--VIEACKDSLKKLQLDYLDLYLVHFPVATKhtgvgttgsalgedgvldidvtisLETTWHAMEKLVSAGLVRSIGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 140 SNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSG----EEAGI---LKNHVLGEIAKKH 212
Cdd:cd19112 160 SNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaEWFGSvspLDDPVLKDLAKKY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 408407927 213 NKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19112 240 GKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-263 |
6.70e-82 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 246.88 E-value: 6.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAQDGAeTANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEKTLAAFER 95
Cdd:cd19139 1 IPAFGLGTFRLKDDV-VIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 96 SRELLGLEYIDLYLIHWPGKKKFV---DTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMV-NQVELHPLFQQ 171
Cdd:cd19139 80 SLEKLRTDYVDLTLIHWPSPNDEVpveEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAtNQIELSPYLQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 172 RTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFK 251
Cdd:cd19139 160 RKLVAHCKQHGIHVTSYMTLAYGK---VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLT 236
|
250
....*....|..
gi 408407927 252 LTEEEMRQIDEL 263
Cdd:cd19139 237 LDADDMAAIAAL 248
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
7-268 |
1.63e-79 |
|
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: 242.52 E-value: 1.63e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 7 CVTLHNSVRMPQLGLGVWRAQD--GAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIR---ESG-VPREEVWVTTKVW 80
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRskiADGtVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 81 NSDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKKK--------------------FVDTWKALEKLYEEKKVRAIGVS 140
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKpgeelfpkdengklifdtvdLCATWEAMEKCKDAGLAKSIGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 141 NFEPHHLTELFKS--CKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAG--------ILKNHVLGEIAK 210
Cdd:cd19108 162 NFNRRQLEMILNKpgLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEwvdqnspvLLEDPVLCALAK 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 408407927 211 KHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19108 242 KHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
16-268 |
2.45e-79 |
|
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: 242.40 E-value: 2.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVW---RAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRES----GVPREEVWVTTKVWNSDQGYEK 88
Cdd:cd19109 4 IPIIGLGTYsepKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 89 TLAAFERSRELLGLEYIDLYLIHWP---------------GKKKF-----VDTWKALEKLYEEKKVRAIGVSNFEPHHLT 148
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPmafkpgdeiyprdenGKWLYhktnlCATWEALEACKDAGLVKSIGVSNFNRRQLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 149 ELFKS--CKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAG--------ILKNHVLGEIAKKHNKSPAQ 218
Cdd:cd19109 164 LILNKpgLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIwvnvssppLLEDPLLNSIGKKYNKTAAQ 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 408407927 219 VVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19109 244 VVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-267 |
4.58e-79 |
|
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: 241.25 E-value: 4.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWR-AQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIR----ESGVPREEVWVTTKVWNS 82
Cdd:cd19119 4 FKLNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 83 dqGYEKTLAAFERSRELLGLEYIDLYLIHWP----------GKKKF----------------VDTWKALEKLYEEKKVRA 136
Cdd:cd19119 84 --FYDEVERSLDESLKALGLDYVDLLLVHWPvcfekdsddsGKPFTpvnddgktryaasgdhITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 137 IGVSNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGeEAGILKNHVLGEIAKKHNKSP 216
Cdd:cd19119 162 IGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSH-GAPNLKNPLVKKIAEKYNVST 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 408407927 217 AQVVIRWDIQHGIVTIPKSTNKGRIQENFNVwdFKLTEEEMRQIDELNEDK 267
Cdd:cd19119 241 GDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGEKY 289
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-276 |
8.35e-78 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 238.47 E-value: 8.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQG----IRESGVPREEVWVTTKVWNSD 83
Cdd:cd19115 5 VKLNSGYDMPLVGFGLWKV-NNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGvaraIKEGIVKREDLFIVSKLWNTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 84 QGYEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVD-------------------------TWKALEKLYEEKKVRAIG 138
Cdd:cd19115 84 HDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDpavryppgwfydgkkvefsnapiqeTWTAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 139 VSNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLG----------SGEEAGILKNH-VLGE 207
Cdd:cd19115 164 VSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldlpGAKDTPPLFEHdVIKS 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 408407927 208 IAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRIgGDPDNF 276
Cdd:cd19115 244 IAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF-NNPLNY 311
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-263 |
2.43e-76 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 233.57 E-value: 2.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLGVWRAQDgAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRE----SGVPREEVWVTTKVWNSDQGYEKTLAA 92
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 93 FERSRELLGLEYIDLYLIHWP--------------------GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFK 152
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqslSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 153 SCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAG---ILKNHVLGEIAKKHNKSPAQVVIRWDIQHGI 229
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGnltFLNDSELKALATKYNTTPPQVIIAWHLQKWP 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 408407927 230 VT---IPKSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19128 241 KNysvIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-278 |
2.71e-76 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 233.38 E-value: 2.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAQDGAeTANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRESGVPREEVWVTTKVWNSDQGYEKTLAAFER 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQV-VIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 96 SRELLGLEYIDLYLIHWPGKKKFVDTWKALEKLYEEKK---VRAIGVSNFEPHHLTELFKSC-KIRPMVNQVELHPLFQQ 171
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAKKqglTREIGISNFTIALMKQAIAAVgAENIATNQIELSPYLQN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 172 RTLREFCKQHNIAITAWSPLGSGEeagILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFK 251
Cdd:PRK11172 162 RKVVAFAKEHGIHVTSYMTLAYGK---VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQ 238
|
250 260
....*....|....*....|....*..
gi 408407927 252 LTEEEMRQIDELNEDKRIgGDPDNFFP 278
Cdd:PRK11172 239 LDAEDMAAIAALDRNGRL-VSPEGLAP 264
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-273 |
3.19e-76 |
|
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: 234.65 E-value: 3.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNSVRMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIR----ESGVPREEVWVTTKVWNSD 83
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKL-DNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNraidEGLVKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 84 QGYEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFV--------------------------DTWKALEKLYEEKKVRAI 137
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVpieekyppgfycgdgdnfvyedvpilDTWKALEKLVDAGKIKSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 138 GVSNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLG--SGEEAG---------ILKNHVLG 206
Cdd:cd19113 162 GVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqSFVELNqgralntptLFEHDTIK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408407927 207 EIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRIgGDP 273
Cdd:cd19113 242 SIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF-NDP 307
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-262 |
3.51e-76 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 233.89 E-value: 3.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 11 HNSVRMPQLGLGVWrAQDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRE----SGVPREEVWVTTKVWNSDQGY 86
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 87 EKTLAAFERSRELLGLEYIDLYLIH-----WPGKK----------------KFVDTWKALEKLYEEKKVRAIGVSNFEPH 145
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHtpfafQPGDEqdprdangnviyddgvTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 146 HLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAGILKNHVLGEIAKKHNKSPAQVVIRWDI 225
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 408407927 226 QHGIVTIPKSTNKGRIQENFNVwdFKLTEEEMRQIDE 262
Cdd:cd19129 240 QRGTALLTTSKTPSRIRENFDI--STLPEDAMREINE 274
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-261 |
1.27e-73 |
|
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: 226.34 E-value: 1.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLGVW--------RAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIResGVPREEVWVTTKVWNSD 83
Cdd:cd19072 3 EVPVLGLGTWgigggmskDYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK--GFDREDLFITTKVSPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 84 QGYEKTLAAFERSRELLGLEYIDLYLIHWPGKK-KFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMV-N 161
Cdd:cd19072 81 LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSiPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIVaN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 162 QVELHPLFQ--QRTLREFCKQHNIAITAWSPLGSGEEAGILKNHVLGEIAKKHNKSPAQVVIRWDIQH-GIVTIPKSTNK 238
Cdd:cd19072 161 QVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNI 240
|
250 260
....*....|....*....|...
gi 408407927 239 GRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19072 241 EHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
7-261 |
3.71e-72 |
|
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: 222.51 E-value: 3.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 7 CVTLHNSVRMPQLGLGVWRAQDGAETA----NAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESgvpREEVWVTTKV 79
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMGEDPAKRaqeiEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 WNSDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPM 159
Cdd:cd19138 79 LPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 160 V-NQVELHplFQQR----TLREFCKQHNIAITAWSPLGSGEEA--GILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIV-T 231
Cdd:cd19138 159 AaNQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLrrGLLENPTLKEIAARHGATPAQVALAWVLRDGNViA 236
|
250 260 270
....*....|....*....|....*....|
gi 408407927 232 IPKSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19138 237 IPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-264 |
7.13e-72 |
|
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: 222.57 E-value: 7.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 19 LGLGVWRAQDG------AETANAVRWAIEAGYRHIDTAYIY---SNERGVGQGIRESGVPREEVWVTTKVWNSDQGY--- 86
Cdd:pfam00248 1 IGLGTWQLGGGwgpiskEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWpsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 87 ---EKTLAAFERSRELLGLEYIDLYLIHWPGKKKFV-DTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQ 162
Cdd:pfam00248 81 gskENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIeETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 163 VELHPLF--QQRTLREFCKQHNIAITAWSPLGSG------------------------EEAGILKNHVLGEIAKKHNKSP 216
Cdd:pfam00248 161 VEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkgTPLNLEALEALEEIAKEHGVSP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 408407927 217 AQVVIRWDIQH--GIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELN 264
Cdd:pfam00248 241 AQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
15-268 |
1.05e-71 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 222.82 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLGVWRAqDGAETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIR----ESGVPREEVWVTTKVWNSDQGYEKTL 90
Cdd:cd19114 3 KMPLVGFGTAKI-KANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRkaiqEGLVKREDLFIVTKLWNNFHGKDHVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 91 AAFERSRELLGLEYIDLYLIHWPGKKKFVD--------------------------TWKALEKLYEEKKVRAIGVSNFEP 144
Cdd:cd19114 82 EAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaenypflwkdkelkkfpleqspmqeCWREMEKLVDAGLVRNIGIANFNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 145 HHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSG----------EEAGILKNHVLGEIAKKHNK 214
Cdd:cd19114 162 QLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkHFTNLLEHPVVKKLADKHKR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 408407927 215 SPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKR 268
Cdd:cd19114 242 DTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-265 |
4.87e-66 |
|
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: 207.86 E-value: 4.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 9 TLHNSVRMPQLGLGVWrAQDGA--ETANAVRWAIEAGYRHIDTAYIYSNERGVGQGIRE-----SGVPREEVWVTTKVWN 81
Cdd:cd19122 2 TLNNGVKIPAVGFGTF-ANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 82 SDQGYEKTLAAFERSRELLGLEYIDLYLIHWP--------------GKKKFV----------DTWKALEKLYEEKKVRAI 137
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPiaaekndqrspklgPDGKYVilkdltenpePTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 138 GVSNFEPHHLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGS-------GEEagILKNHVLGEIAK 210
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvpstGER--VSENPTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 408407927 211 KHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDfkLTEEEMRQIDELNE 265
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
14-261 |
9.61e-57 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 183.16 E-value: 9.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 14 VRMPQLGLGVWR---------AQDgAETANAVRWAIEAGYRHIDTAYIYS---NERGVGQGIREsgVPREEVWVTTKVWN 81
Cdd:cd19137 2 EKIPALGLGTWGiggfltpdySRD-EEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 82 SDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKK-KFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMV 160
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNiPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 161 NQVELHPL---FQQRTLREFCKQHNIAITAWSPLGSGEEagiLKNHVLGEIAKKHNKSPAQVVIRWDIQH-GIVTIPKST 236
Cdd:cd19137 159 NQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLE---KTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAG 235
|
250 260
....*....|....*....|....*
gi 408407927 237 NKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19137 236 RVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
14-263 |
1.57e-53 |
|
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: 176.52 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 14 VRMPQLGLG------VWRAQDGAETANAVRWAIEAGYRHIDTAYIYS---NERGVGQGIResGVPREEVWVTTKV----- 79
Cdd:COG0667 11 LKVSRLGLGtmtfggPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALK--GRPRDDVVIATKVgrrmg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 ---WNSDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKK-KFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCK 155
Cdd:COG0667 89 pgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDtPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 156 --IRPMVNQVELHPLFQQ--RTLREFCKQHNIAITAWSPLGSG---------------------------EEAGILKNHV 204
Cdd:COG0667 169 glPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdraatnfvqgylTERNLALVDA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408407927 205 LGEIAKKHNKSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:COG0667 249 LRAIAAEHGVTPAQLALAWLLAQPGVTsvIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-261 |
4.14e-51 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 169.63 E-value: 4.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 18 QLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESgvpREEVWVTTKV---WNSDQGYEKTL- 90
Cdd:cd19084 13 AIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKCglrWDGGKGVTKDLs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 91 -----AAFERSRELLGLEYIDLYLIHWP-GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIrpMVNQVE 164
Cdd:cd19084 90 pesirKEVEQSLRRLQTDYIDLYQIHWPdPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGPI--VSLQPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 165 LHPLFQQ--RTLREFCKQHNIAITAWSPLGSG------------EEAGILKNH----------------VLGEIAKKHNK 214
Cdd:cd19084 168 YSMLEREieEELLPYCRENGIGVLPYGPLAQGlltgkykkeptfPPDDRRSRFpffrgenfeknleivdKLKEIAEKYGK 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 408407927 215 SPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19084 248 SLAQLAIAWTLAQPGVTsaIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-266 |
4.19e-51 |
|
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: 169.30 E-value: 4.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLGVW--------RAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIREsgvPREEVWVTTKVWNSDQG 85
Cdd:cd19085 2 SRLGLGCWqfgggywwGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 86 YEKTLAAFERSRELLGLEYIDLYLIHWP-GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIrpMVNQVE 164
Cdd:cd19085 79 PEDVRKSCERSLKRLGTDYIDLYQIHWPsSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI--DSNQLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 165 LHPLFQQ--RTLREFCKQHNIAITAWSPLGSG------------------------EEAGILKN-----HVLGEIAKKHN 213
Cdd:cd19085 157 YNLLWRAieYEILPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdartrlfrhFEPGAEEEtfealEKLKEIADELG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 408407927 214 KSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNED 266
Cdd:cd19085 237 VTMAQLALAWVLQQPGVTsvIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
15-261 |
3.28e-50 |
|
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: 167.02 E-value: 3.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLGVWRAQDG----------AETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGvPREEVWVTTKVWN 81
Cdd:cd19093 1 EVSPLGLGTWQWGDRlwwgygeygdEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 82 --SDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVD--TWKALEKLYEEKKVRAIGVSNFEPHHL---TELFKSC 154
Cdd:cd19093 80 lpWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIeaLMDGLADAVEEGLVRAVGVSNYSADQLrraHKALKER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 155 KIRPMVNQVE---LHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAG--------------------------ILKnhVL 205
Cdd:cd19093 160 GVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGkyspenpppggrrrlfgrknlekvqpLLD--AL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 408407927 206 GEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19093 238 EEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-245 |
9.55e-46 |
|
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: 153.83 E-value: 9.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLGVWR---AQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGVpREEVWVTTKVWNSDQGYEKT- 89
Cdd:cd06660 1 SRLGLGTMTfggDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 90 -------LAAFERSRELLGLEYIDLYLIHWPGKKKFVD-TWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCK----IR 157
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEeTLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 158 PMVNQVE---LHPLFQQRTLREFCKQHNIAITAWSPLGSGeeagilknhvlgeiakkhnksPAQVVIRWDIQHGIVT--I 232
Cdd:cd06660 160 FAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARG---------------------PAQLALAWLLSQPFVTvpI 218
|
250
....*....|...
gi 408407927 233 PKSTNKGRIQENF 245
Cdd:cd06660 219 VGARSPEQLEENL 231
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
8-256 |
2.26e-43 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 149.53 E-value: 2.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNS-VRMPQLGLGVWRAQDG----AETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGVPREEVWVTTKV 79
Cdd:COG4989 4 IKLGASgLSVSRIVLGCMRLGEWdlspAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTKC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 ---------WNS----DQGYEKTLAAFERSRELLGLEYIDLYLIHWPgkkkfvD-------TWKALEKLYEEKKVRAIGV 139
Cdd:COG4989 84 girlpsearDNRvkhyDTSKEHIIASVEGSLRRLGTDYLDLLLLHRP------DplmdpeeVAEAFDELKASGKVRHFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 140 SNFEPHHLTELFKSCKIRPMVNQVELHPL----FQQRTLrEFCKQHNIAITAWSPLGSG-------EEAGILKNhVLGEI 208
Cdd:COG4989 158 SNFTPSQFELLQSALDQPLVTNQIELSLLhtdaFDDGTL-DYCQLNGITPMAWSPLAGGrlfggfdEQFPRLRA-ALDEL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 408407927 209 AKKHNKSPAQVVIRWDIQH--GIVTIPKSTNKGRIQENFNVWDFKLTEEE 256
Cdd:COG4989 236 AEKYGVSPEAIALAWLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
16-256 |
1.32e-42 |
|
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: 147.32 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAQDGAETA----NAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGVPREEVWVTTK---------- 78
Cdd:cd19092 6 VSRLVLGCMRLADWGESAeellSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgirlgddpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 79 ---VWNSDQGYEKTLAAFERSRELLGLEYIDLYLIHWPgkKKFVDTW---KALEKLYEEKKVRAIGVSNFEPHHLTELFK 152
Cdd:cd19092 86 pgrIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRP--DPLMDPEevaEAFDELVKSGKVRYFGVSNFTPSQIELLQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 153 SCKIRPMVNQVEL----HPLFQQRTLrEFCKQHNIAITAWSPLGSGEEAG--------ILKnhVLGEIAKKHNKSPAQVV 220
Cdd:cd19092 164 YLDQPLVTNQIELsllhTEAIDDGTL-DYCQLLDITPMAWSPLGGGRLFGgfderfqrLRA--ALEELAEEYGVTIEAIA 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 408407927 221 IRWDIQH--GIVTIPKSTNKGRIQENFNVWDFKLTEEE 256
Cdd:cd19092 241 LAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-263 |
2.17e-39 |
|
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: 139.35 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 22 GVWRAQDGAETANAVRWAIEAGYRHIDTAYIYS---NERGVGQGIRESgvpREEVWVTTK---VWNSDQGYEKTL----- 90
Cdd:cd19102 18 GGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKGL---RDRPIVATKcglLWDEEGRIRRSLkpasi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 91 -AAFERSRELLGLEYIDLYLIHWP-GKKKFVDTWKALEKLYEEKKVRAIGVSNFEphhlTELFKSC-KIRPM-VNQVE-- 164
Cdd:cd19102 95 rAECEASLRRLGVDVIDLYQIHWPdPDEPIEEAWGALAELKEEGKVRAIGVSNFS----VDQMKRCqAIHPIaSLQPPys 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 165 -LHPLFQQRTLReFCKQHNIAITAWSPLGSG--------------EEAGILKNH----------------VLGEIAKKHN 213
Cdd:cd19102 171 lLRRGIEAEILP-FCAEHGIGVIVYSPMQSGlltgkmtpervaslPADDWRRRSpffqepnlarnlalvdALRPIAERHG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 408407927 214 KSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19102 250 RTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-261 |
1.15e-37 |
|
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: 135.02 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 8 VTLHNS-VRMPQLGLGVWR---------AQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGvPREEVW 74
Cdd:cd19079 3 VRLGNSgLKVSRLCLGCMSfgdpkwrpwVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 75 VTTKVWN------SDQGYEKT--LAAFERSRELLGLEYIDLYLIHW-----PgkkkFVDTWKALEKLYEEKKVRAIGVSN 141
Cdd:cd19079 82 IATKVYFpmgdgpNGRGLSRKhiMAEVDASLKRLGTDYIDLYQIHRwdyetP----IEETLEALHDVVKSGKVRYIGASS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 142 FEPHHLTELFKSCKIR---PMVNQVELHPLFQQRTLRE---FCKQHNIAITAWSPLGSG----------------EEAGI 199
Cdd:cd19079 158 MYAWQFAKALHLAEKNgwtKFVSMQNHYNLLYREEEREmipLCEEEGIGVIPWSPLARGrlarpwgdtterrrstTDTAK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 408407927 200 LKNHV-----------LGEIAKKHNKSPAQVVIRWDIQHGIVTIP--KSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19079 238 LKYDYfteadkeivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-253 |
5.62e-34 |
|
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: 123.87 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVW-RAQDGAETANAVRWAIEAGYRHIDTAYIY---SNERGvgqgIRESGVPR-EEVWVTTKV---------WN 81
Cdd:cd19088 9 MRLTGPGIWgPPADREEAIAVLRRALELGVNFIDTADSYgpdVNERL----IAEALHPYpDDVVIATKGglvrtgpgwWG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 82 SDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKK-KFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMV 160
Cdd:cd19088 85 PDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKvPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIVSVQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 161 NQvelHPLFQQRT--LREFCKQHNIAITAWSPLGSGEEAGILknHVLGEIAKKHNKSPAQVVIRWDIQHG--IVTIPKST 236
Cdd:cd19088 165 NR---YNLANRDDegVLDYCEAAGIAFIPWFPLGGGDLAQPG--GLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTS 239
|
250
....*....|....*..
gi 408407927 237 NKGRIQENFNVWDFKLT 253
Cdd:cd19088 240 SVEHLEENLAAAGLRLS 256
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
14-263 |
7.58e-34 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 126.09 E-value: 7.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 14 VRMPQLGLGVWRAQ--DGAETANAVRWAIEAGYRHIDTAYIYSN-ERGVGQGIREsgvPREEVWVTTK--VWNSDqgYEK 88
Cdd:COG1453 11 LEVSVLGFGGMRLPrkDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKlpPWVRD--PED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 89 TLAAFERSRELLGLEYIDLYLIHWPGKKKFVDT-------WKALEKLYEEKKVRAIGVSNfepHHLTELFKSCkirpmVN 161
Cdd:COG1453 86 MRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKvlkpggaLEALEKAKAEGKIRHIGFST---HGSLEVIKEA-----ID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 162 -------QVELHPLFQQRTLR----EFCKQHNIAITAWSPLGSGEeagiLKNH--VLGEIAKKhNKSPAQVVIRWDIQHG 228
Cdd:COG1453 158 tgdfdfvQLQYNYLDQDNQAGeealEAAAEKGIGVIIMKPLKGGR----LANPpeKLVELLCP-PLSPAEWALRFLLSHP 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 408407927 229 IVTIPKS--TNKGRIQENFNVWD--FKLTEEEMRQIDEL 263
Cdd:COG1453 233 EVTTVLSgmSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
40-261 |
1.94e-31 |
|
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: 118.47 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 40 IEAGYRHIDTAYIYSN----------ERGVGQGIRESGvPREEVWVTTKV--WNSDQGY----EKTLAAFERSRELLGLE 103
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSRG-KRDRVVIATKVgfPMGPNGPglsrKHIRRAVEASLRRLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 104 YIDLYLIHWPgkkkfvD-------TWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCK----IRPMVNQVE---LHPLF 169
Cdd:cd19081 115 YIDLYQAHWD------DpatpleeTLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEynlVDRES 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 170 QQRTLREFCKQHNIAITAWSPLGSG----------------EEAGILKNH----------VLGEIAKKHNKSPAQVVIRW 223
Cdd:cd19081 189 FEGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstRRGEAAKRYlnerglrildALDEVAAEHGATPAQVALAW 268
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 408407927 224 DIQHGIVTIP--KSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19081 269 LLARPGVTAPiaGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
28-263 |
3.76e-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: 117.91 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 28 DGAETANAVRWAIEAGYRHIDTAYIYS---NERGVGQGIRESGvpREEVWVTTK----------VWNSDQGYEKtlAAFE 94
Cdd:cd19083 31 DEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN--RNEVVIATKgahkfggdgsVLNNSPEFLR--SAVE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 95 RSRELLGLEYIDLYLIHWP-GKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRpmVNQVElHPLFQQ-- 171
Cdd:cd19083 107 KSLKRLNTDYIDLYYIHFPdGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVD--VLQGE-YNLLQRea 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 172 -RTLREFCKQHNIAITAWSPLGSGEEAG-----------ILKNHV-----------------LGEIAKKHNKSPAQVVIR 222
Cdd:cd19083 184 eEDILPYCVENNISFIPYFPLASGLLAGkytkdtkfpdnDLRNDKplfkgerfsenldkvdkLKSIADEKGVTVAHLALA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 408407927 223 WDI-QHGI-VTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19083 264 WYLtRPAIdVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
24-261 |
4.73e-31 |
|
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: 117.41 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 24 WRAQDGAETANAVRWAIEAGYRHIDTAYIYS---NERGVGQGIRESGvPREEVWVTTKV---WNSDQGY------EKTLA 91
Cdd:cd19148 19 WGGTDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGEVvrnsspARIRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 92 AFERSRELLGLEYIDLYLIHWPGKKK-FVDTWKALEKLYEEKKVRAIGVSNFEPHHLtELFKscKIRPM-VNQVELHpLF 169
Cdd:cd19148 98 EVEDSLRRLQTDYIDLYQVHWPDPLVpIEETAEALKELLDEGKIRAIGVSNFSPEQM-ETFR--KVAPLhTVQPPYN-LF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 170 QQ---RTLREFCKQHNIAITAWSPLGSG-----------EEAGILKNHV-----------------LGEIAKKH-NKSPA 217
Cdd:cd19148 174 EReieKDVLPYARKHNIVTLAYGALCRGllsgkmtkdtkFEGDDLRRTDpkfqeprfsqylaaveeLDKLAQERyGKSVI 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 408407927 218 QVVIRWDIQHGIVTIP--KSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19148 254 HLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-260 |
1.22e-30 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 116.16 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 14 VRMPQLGLGV------WRAQDGAETANAVRWAIEAGYRHIDTAYIY---SNERGVGQGIREsgvPREEVWVTTK---VWN 81
Cdd:cd19076 10 LEVSALGLGCmgmsafYGPADEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIATKfgiVRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 82 SDQGYEKTL-------AAFERSRELLGLEYIDLYLIHWPGKKKFV-DTWKALEKLYEEKKVRAIGVSNFEPhhlTELFKS 153
Cdd:cd19076 87 PGSGFRGVDgrpeyvrAACEASLKRLGTDVIDLYYQHRVDPNVPIeETVGAMAELVEEGKVRYIGLSEASA---DTIRRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 154 CKIRPMVN-QVELHPlfQQRTLRE----FCKQHNIAITAWSPLGSGEEAGILKN-------------------------- 202
Cdd:cd19076 164 HAVHPITAvQSEYSL--WTRDIEDevlpTCRELGIGFVAYSPLGRGFLTGAIKSpedlpeddfrrnnprfqgenfdknlk 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408407927 203 --HVLGEIAKKHNKSPAQVVIRWDIQHG--IVTIPKSTNKGRIQENFNVWDFKLTEEEMRQI 260
Cdd:cd19076 242 lvEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
9-263 |
2.21e-30 |
|
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: 115.79 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 9 TLHNS-VRMPQLGLG------------VWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESgvpREE 72
Cdd:cd19091 5 TLGRSgLKVSELALGtmtfgggggffgAWGGVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR---RDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 73 VWVTTKVW--------NSDQGYEKTLAAFERSRELLGLEYIDLYLIH-WPGKKKFVDTWKALEKLYEEKKVRAIGVSNF- 142
Cdd:cd19091 82 VLIATKVRgrmgegpnDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHgFDALTPLEETLRALDDLVRQGKVRYIGVSNFs 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 143 -----------EPHHLTelfksckiRPMVNQV-----------ELHPLfqqrtlrefCKQHNIAITAWSPLGSG------ 194
Cdd:cd19091 162 awqimkalgisERRGLA--------RFVALQAyysllgrdlehELMPL---------ALDQGVGLLVWSPLAGGllsgky 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 195 -----------------------EEAGILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWD 249
Cdd:cd19091 225 rrgqpapegsrlrrtgfdfppvdRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAG 304
|
330
....*....|....
gi 408407927 250 FKLTEEEMRQIDEL 263
Cdd:cd19091 305 LSLTPEEIARLDKV 318
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
19-262 |
1.58e-29 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 113.52 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 19 LGLGVWRA--------QDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESgvpREEVWVTTK---VWNSDQ 84
Cdd:cd19149 14 IGLGTWAIgggpwwggSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcglRWDREG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 85 GYE----------KTLAA------FERSRELLGLEYIDLYLIHWPGKKKFV-DTWKALEKLYEEKKVRAIGVSNFEPHHL 147
Cdd:cd19149 91 GSFffvrdgvtvyKNLSPesireeVEQSLKRLGTDYIDLYQTHWQDVETPIeETMEALEELKRQGKIRAIGASNVSVEQI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 148 TELFKSCKIRpmVNQVELHPL--FQQRTLREFCKQHNIAITAWSPLGSG------------EEAGILKNHVLGE------ 207
Cdd:cd19149 171 KEYVKAGQLD--IIQEKYSMLdrGIEKELLPYCKKNNIAFQAYSPLEQGlltgkitpdrefDAGDARSGIPWFSpenrek 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408407927 208 ----------IAKKHNKSPAQVVIRWDI-QHGIVT-IPKSTNKGRIQENFNVWDFKLTEEEMRQIDE 262
Cdd:cd19149 249 vlallekwkpLCEKYGCTLAQLVIAWTLaQPGITSaLCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
39-271 |
9.26e-29 |
|
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: 111.77 E-value: 9.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 39 AIEAGYRHIDTAYIY-SNERGVGQGIRESGVPREEVWVTTKV-----------W-NSDQGYEKTlaAFERSRELLGLEYI 105
Cdd:cd19144 43 AFELGCTFWDTADIYgDSEELIGRWFKQNPGKREKIFLATKFgieknvetgeySvDGSPEYVKK--ACETSLKRLGVDYI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 106 DLYLIH-WPGKKKFVDTWKALEKLYEEKKVRAIGVSnfEPHHLTeLFKSCKIRPMVN-QVELHPLF-----QQRTLREFC 178
Cdd:cd19144 121 DLYYQHrVDGKTPIEKTVAAMAELVQEGKIKHIGLS--ECSAET-LRRAHAVHPIAAvQIEYSPFSldierPEIGVLDTC 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 179 KQHNIAITAWSPLGSG------------------------EEAGILKNHVL----GEIAKKHNKSPAQVVIRWDIQHG-- 228
Cdd:cd19144 198 RELGVAIVAYSPLGRGfltgairspddfeegdfrrmaprfQAENFPKNLELvdkiKAIAKKKNVTAGQLTLAWLLAQGdd 277
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 408407927 229 IVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDELNEDKRIGG 271
Cdd:cd19144 278 IIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEVVG 320
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-194 |
5.43e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 107.57 E-value: 5.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLGVWRAQDG--AETANAVRWAIEAGYRHIDTAYIYSN-ERGVGQGIREsgvPREEVWVTTKVWNSDqgYEKTLAAF 93
Cdd:cd19100 12 SRLGFGGGPLGRLsqEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARD--YEGAKRDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 94 ERSRELLGLEYIDLYLIHWPGKKKFVDT-------WKALEKLYEEKKVRAIGVSNfepHHLTELFKSCKIRPM------V 160
Cdd:cd19100 87 ERSLKRLGTDYIDLYQLHAVDTEEDLDQvfgpggaLEALLEAKEEGKIRFIGISG---HSPEVLLRALETGEFdvvlfpI 163
|
170 180 190
....*....|....*....|....*....|....*
gi 408407927 161 NQVELH-PLFQQRTLREfCKQHNIAITAWSPLGSG 194
Cdd:cd19100 164 NPAGDHiDSFREELLPL-AREKGVGVIAMKVLAGG 197
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
14-255 |
7.50e-27 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 106.14 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 14 VRMPQLGLGVWR---AQDGAETANA-VRWAIEAGYRHIDTAYIYSN---ERGVGQGIResGVPREEVWVTTKV-WN-SDQ 84
Cdd:cd19074 2 LKVSELSLGTWLtfgGQVDDEDAKAcVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWPtGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 85 GYEKTLA------AFERSRELLGLEYIDLYLIHwpgkkKF------VDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFK 152
Cdd:cd19074 80 PNDRGLSrkhifeSIHASLKRLQLDYVDIYYCH-----RYdpetplEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 153 SCK----IRPMVNQVELHPLFQQRT--LREFCKQHNIAITAWSPLGSG-----------EEAGILKNHV----------- 204
Cdd:cd19074 155 LARqfglIPPVVEQPQYNMLWREIEeeVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipPPSRSRATDEdnrdkkrrllt 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408407927 205 ---------LGEIAKKHNKSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWDFKLTEE 255
Cdd:cd19074 235 denlekvkkLKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-244 |
1.92e-26 |
|
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: 103.82 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLGVWRAQDGAetANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIResGVPREEVWVTTKVWNSDQGY--EKT 89
Cdd:cd19105 12 KVSRLGFGGGGLPRES--PELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPRLDKKdkAEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 90 LAAFERSRELLGLEYIDLYLIH---WPGKKKFVDTW-KALEKLYEEKKVRAIGVS--NFEPHHLTELFKSCKIRpmVNQV 163
Cdd:cd19105 88 LKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELlEALEKLKKEGKVRFIGFSthDNMAEVLQAAIESGWFD--VIMV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 164 ELHPLFQQRTLREF---CKQHNIAITAWSPLGSGEEAGILKNHVLGEIAkkhnkSPAQVVIRWDIQHGIVT--IPKSTNK 238
Cdd:cd19105 166 AYNFLNQPAELEEAlaaAAEKGIGVVAMKTLAGGYLQPALLSVLKAKGF-----SLPQAALKWVLSNPRVDtvVPGMRNF 240
|
....*.
gi 408407927 239 GRIQEN 244
Cdd:cd19105 241 AELEEN 246
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-255 |
2.94e-26 |
|
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: 104.17 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLG------VWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN-ERGVGQGIREsgVPREEVWVTTKV-----WNSDQ 84
Cdd:cd19090 1 SALGLGtaglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE--LPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 85 GYEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVD------TWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRP 158
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDilapggALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGDFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 159 MVNQVELHPLFQQ--RTLREFCKQHNIAITAWSPLGSGEEAGILKNHV-----------------LGEIAKKHNKSPAQV 219
Cdd:cd19090 159 VLTANRYTLLDQSaaDELLPAAARHGVGVINASPLGMGLLAGRPPERVrytyrwlspelldrakrLYELCDEHGVPLPAL 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 408407927 220 VIRWDIQHGIV--TIPKSTNKGRIQENFNVWDFKLTEE 255
Cdd:cd19090 239 ALRFLLRDPRIstVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-244 |
8.30e-26 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 101.79 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 18 QLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIREsgvPREEVWVTTKVWNSDQGYEKT----- 89
Cdd:cd19086 12 GLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFGNRFDGGPERpqdfs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 90 ----LAAFERSRELLGLEYIDLYLIH-----WPGKKkfvDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPMv 160
Cdd:cd19086 89 peyiREAVEASLKRLGTDYIDLYQLHnppdeVLDND---ELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGIDVV- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 161 nQVELHpLFQQRTLREF---CKQHNIAITAWSPLGSGEEAGILknhvlgeiakkhnkspAQVVIRWDIQHGIVT--IPKS 235
Cdd:cd19086 165 -QVIYN-LLDQRPEEELfplAEEHGVGVIARVPLASGLLTGKL----------------AQAALRFILSHPAVStvIPGA 226
|
....*....
gi 408407927 236 TNKGRIQEN 244
Cdd:cd19086 227 RSPEQVEEN 235
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-262 |
2.04e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 102.29 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN-ERGVGQGIRE---SGVPREEVWVTTKvW---NSDQGYEK 88
Cdd:cd19101 9 MWQLSGGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRlrrERDAADDVQIHTK-WvpdPGELTMTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 89 TL--AAFERSRELLGLEYIDLYLIHW--PGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKScKIRPMVNQVE 164
Cdd:cd19101 88 AYveAAIDRSLKRLGVDRLDLVQFHWwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDA-GVPIVSNQVQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 165 lHPLFQQRTLRE---FCKQHNIAITAWSPLGSG-----------------------------EEAG-------ILKnhVL 205
Cdd:cd19101 167 -YSLLDRRPENGmaaLCEDHGIKLLAYGTLAGGllsekylgvpeptgpaletrslqkyklmiDEWGgwdlfqeLLR--TL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 408407927 206 GEIAKKHNKSPAQVVIRWDIQHGIV--TIPKSTNKGRIQENFNVWDFKLTEEEMRQIDE 262
Cdd:cd19101 244 KAIADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
39-263 |
5.17e-25 |
|
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: 101.49 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 39 AIEAGYRHIDTAYIY----------SNERGVGQGIRESGvPREEVWVTTKV--------W----NSDQGYEKTLAAFERS 96
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWprggGTRLDRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 97 RELLGLEYIDLYLIHWP-------GKKKFV------------DTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIR 157
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPdrytplfGGGYYTepseeedsvsfeEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 158 ---PMVN-QVELHPLFQQR--TLREFCKQHNIAITAWSPLGSG-------EEAGILKNH--------------------- 203
Cdd:cd19094 186 glpRIVSiQNPYSLLNRNFeeGLAEACHRENVGLLAYSPLAGGvltgkylDGAARPEGGrlnlfpgymaryrspqaleav 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 408407927 204 -VLGEIAKKHNKSPAQVVIRWDIQHGIV--TIPKSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19094 266 aEYVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-231 |
5.42e-25 |
|
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: 99.94 E-value: 5.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLG------VWRAQDGAETANA-VRWAIEAGYRHIDTAYIYSN---ERGVGQGIREsgVPREEVWVTTKV-WNSDQG 85
Cdd:cd19096 1 SVLGFGtmrlpeSDDDSIDEEKAIEmIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 86 YEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVDT------WKALEKLYEEKKVRAIGVSnFepHHLTELFKscKI--- 156
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKarkgglLEFLEKAKKEGLIRHIGFS-F--HDSPELLK--EIlds 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 157 RPM-VNQVELHPLFQQRTLR----EFCKQHNIAITAWSPLGSGeeaGILKN-HVLGEIAKKHNKSPAQVVIRWDIQHGIV 230
Cdd:cd19096 154 YDFdFVQLQYNYLDQENQAGrpgiEYAAKKGMGVIIMEPLKGG---GLANNpPEALAILCGAPLSPAEWALRFLLSHPEV 230
|
.
gi 408407927 231 T 231
Cdd:cd19096 231 T 231
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
40-261 |
1.03e-22 |
|
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: 94.98 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 40 IEAGYRHIDTAYIYSN---ERGVGQGIRESgvpREEVWVTTK-VWNSDQG-------YEKTL-AAFERSRELLGLEYIDL 107
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKyTMNRRPGdpnaggnHRKNLrRSVEASLRRLQTDYIDL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 108 YLIH-WPGKKKFVDTWKALEKLYEEKKVRAIGVSNF------------EPHHLTelfksckirPMVN-QVELHPLfqQRT 173
Cdd:cd19080 118 LYVHaWDFTTPVEEVMRALDDLVRAGKVLYVGISDTpawvvarantlaELRGWS---------PFVAlQIEYSLL--ERT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 174 L-REF---CKQHNIAITAWSPLGSG---------------------EEAGILKNH------VLGEIAKKHNKSPAQVVIR 222
Cdd:cd19080 187 PeRELlpmARALGLGVTPWSPLGGGlltgkyqrgeegrageakgvtVGFGKLTERnwaivdVVAAVAEELGRSAAQVALA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 408407927 223 WDIQHGIVTIP--KSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19080 267 WVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-244 |
2.62e-22 |
|
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: 92.68 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLGVWRAQDG------AETANAVRWAIEAGYRHIDTAYIYSN-ERGVGQGIreSGVPREEVWVTTKVWNSDQG---- 85
Cdd:cd19095 1 SVLGLGTSGIGRVwgvpseAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGTHGEGgrdr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 86 ----YEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVDT-WKALEKLYEEKKVRAIGVSNFEPHHL----TELFKscki 156
Cdd:cd19095 79 kdfsPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEvLETLEDLKAAGKVRYIGVSGDGEELEaaiaSGVFD---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 157 rpmVNQVELHPLFQ-QRTLREFCKQHNIAITAWSPLGSG----EEAGILKNHVLGEIAKKHN----KSPAQVVIRWDIQH 227
Cdd:cd19095 155 ---VVQLPYNVLDReEEELLPLAAEAGLGVIVNRPLANGrlrrRVRRRPLYADYARRPEFAAeiggATWAQAALRFVLSH 231
|
250
....*....|....*....
gi 408407927 228 GIVT--IPKSTNKGRIQEN 244
Cdd:cd19095 232 PGVSsaIVGTTNPEHLEEN 250
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-263 |
3.46e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 93.55 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 16 MPQLGLGVWRAQDGAETANAVRW--------------AIEAGYRHIDTAYIY---SNERGVGQGIREsgVPREEVWVTTK 78
Cdd:cd19103 4 LPKIALGTWSWGSGGAGGDQVFGnhldedtlkavfdkAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 79 V--WNSDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKkkfVDTW-KALEKLYEEKKVRAIGVSNfepHHLTELFKSCK 155
Cdd:cd19103 82 FtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPAD---VERWtPELIPLLKSGKVKHVGVSN---HNLAEIKRANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 156 IRPM----VNQVE-----LHPLFQQRTLREFCKQHNIAITAWS-----------------PLGSGEEA---GILK----- 201
Cdd:cd19103 156 ILAKagvsLSAVQnhyslLYRSSEEAGILDYCKENGITFFAYMvleqgalsgkydtkhplPEGSGRAEtynPLLPqleel 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408407927 202 NHVLGEIAKKHNKSPAQVVIRWDIQHGIVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19103 236 TAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
39-263 |
4.21e-22 |
|
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: 93.41 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 39 AIEAGYRHIDTAYIYSN---ERGVGQGIRESgvpREEVWVTTKV------WNSDQGYE--KTLAAFERSRELLGLEYIDL 107
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKVfgpmgdDPNDRGLSrrHIRRAVEASLRRLQTDYIDL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 108 YLIH-WPGKKKFVDTWKALEKLYEEKKVRAIGVSNF------------EPHHLTElFKSckIRPMVN----QVELHPLfq 170
Cdd:cd19087 116 YQMHhFDRDTPLEETLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaARRGLLR-FVS--EQPMYNllkrQAELEIL-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 171 qrtlrEFCKQHNIAITAWSPLGSG-----------EEAGILKNHVLG-----------------EIAKKHNKSPAQVVIR 222
Cdd:cd19087 191 -----PAARAYGLGVIPYSPLAGGlltgkygkgkrPESGRLVERARYqarygleeyrdiaerfeALAAEAGLTPASLALA 265
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 408407927 223 WDIQHGIVTIP--KSTNKGRIQENFNVWDFKLTEEEMRQIDEL 263
Cdd:cd19087 266 WVLSHPAVTSPiiGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
19-227 |
4.22e-22 |
|
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: 93.39 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 19 LGLGVWRAQDGAETANAVRWAI----EAGYRHIDTAYIYSN---ERGVGQGiresGVPREEVWVTTKVwNSDQG----YE 87
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLdaflERGHTEIDTARVYPDgtsEELLGEL----GLGERGFKIDTKA-NPGVGgglsPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 88 KTLAAFERSRELLGLEYIDLYLIHWPGKK-KFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCK----IRPMVNQ 162
Cdd:cd19075 80 NVRKQLETSLKRLKVDKVDVFYLHAPDRStPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 163 -----------VELHPLfqqrtLREfckqHNIAITAWSPLGSG--------EEAGILK-----NHVLG------------ 206
Cdd:cd19075 160 gmynaitrqveTELFPC-----LRK----LGIRFYAYSPLAGGfltgkykySEDKAGGgrfdpNNALGklyrdrywkpsy 230
|
250 260
....*....|....*....|....*....
gi 408407927 207 --------EIAKKHNKSPAQVVIRWDIQH 227
Cdd:cd19075 231 fealekveEAAEKEGISLAEAALRWLYHH 259
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
15-258 |
7.82e-22 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 92.23 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 15 RMPQLGLG------VWRAQDGAETANAVRWAIEAGYRHIDTAYIYsnergvGQGIRES-------GVPREEVWVTTKV-- 79
Cdd:cd19163 12 KVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWY------GQGRSETvlgkalkGIPRDSYYLATKVgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 ----WNS--DQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKKKFVD-----TWKALEKLYEEKKVRAIGVSNFEPHHLT 148
Cdd:cd19163 86 ygldPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDqilneTLPALQKLKEEGKVRFIGITGYPLDVLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 149 ELFK--SCKI-------RPMVNQVELhplfqqRTLREFCKQHNIAITAWSPLGSG--EEAGILKNH-----------VLG 206
Cdd:cd19163 166 EVLErsPVKIdtvlsycHYTLNDTSL------LELLPFFKEKGVGVINASPLSMGllTERGPPDWHpaspeikeacaKAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 408407927 207 EIAKKHNKSPAQVVIRWDIQH--GIVTIPKSTNKGRIQENFNVWDFKLTEEEMR 258
Cdd:cd19163 240 AYCKSRGVDISKLALQFALSNpdIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
40-245 |
1.09e-20 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 89.15 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 40 IEAGYRHIDTAYIYSN-------ERGVGQGIRESGVpREEVWVTTK--------VWNSDQGYEKTLAAFERSRELLGLEY 104
Cdd:cd19082 27 VELGGNFIDTARVYGDwvergasERVIGEWLKSRGN-RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 105 IDLYLIHW--PGKK--KFVDTwkaLEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIR----PMVNQVEL------HPLFQ 170
Cdd:cd19082 106 IDLYFLHRddPSVPvgEIVDT---LNELVRAGKIRAFGASNWSTERIAEANAYAKAHglpgFAASSPQWslarpnEPPWP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 171 QRTL-------REFCKQHNIAITAWSPLGSG-------EEAGILKN--------------HVLGEIAKKHNKSPAQVVIR 222
Cdd:cd19082 183 GPTLvamdeemRAWHEENQLPVFAYSSQARGffskraaGGAEDDSElrrvyyseenferlERAKELAEEKGVSPTQIALA 262
|
250 260
....*....|....*....|....*
gi 408407927 223 WDIQHGIVTIP--KSTNKGRIQENF 245
Cdd:cd19082 263 YVLNQPFPTVPiiGPRTPEQLRDSL 287
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
18-262 |
2.31e-20 |
|
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: 88.44 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 18 QLGLGVWR-------AQDGAETANAVRWAIEAGYRHIDTAYIY---SNERGVGQGIREsgvPREEVWVTTK-VWNSDQGY 86
Cdd:cd19078 6 AIGLGCMGmshgygpPPDKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKfGFKIDGGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 87 EKTL----------AAFERSRELLGLEYIDLYLIHWPGKKKFV-DTWKALEKLYEEKKVRAIGVSNFEPHHLTelfKSCK 155
Cdd:cd19078 83 PGPLgldsrpehirKAVEGSLKRLQTDYIDLYYQHRVDPNVPIeEVAGTMKELIKEGKIRHWGLSEAGVETIR---RAHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 156 IRPMVN-QVELHPLFQ--QRTLREFCKQHNIAITAWSPLGSGEEAGILKNH----------------------------V 204
Cdd:cd19078 160 VCPVTAvQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENtkfdegddraslprftpealeanqalvdL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 205 LGEIAKKHNKSPAQVVIRWDIQHG--IVTIPKSTNKGRIQENFNVWDFKLTEEEMRQIDE 262
Cdd:cd19078 240 LKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-223 |
3.41e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 88.14 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 18 QLGLGVWRAQDGAET----ANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRES----GVPREEVWVTTKV------- 79
Cdd:cd19099 5 SLGLGTYRGDSDDETdeeyREALKAALDSGINVIDTAINYRGgrsERLIGKALRELiekgGIKRDEVVIVTKAgyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 --------W--------NSDQGYEKTL----------AAFERSRELLGLEYIDLYLIHWP-------GKKKFVD----TW 122
Cdd:cd19099 85 deplrplkYleeklgrgLIDVADSAGLrhcispayleDQIERSLKRLGLDTIDLYLLHNPeeqllelGEEEFYDrleeAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 123 KALEKLYEEKKVRAIGVSNFE--------PHHLTELFKSCKIRPMVN--------QVELHPLFQQ------------RTL 174
Cdd:cd19099 165 EALEEAVAEGKIRYYGISTWDgfrappalPGHLSLEKLVAAAEEVGGdnhhfkviQLPLNLLEPEaltekntvkgeaLSL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 408407927 175 REFCKQHNIAITAWSPLGSGEEAGILKnhVLGEIAKKHNKSPAQVVIRW 223
Cdd:cd19099 245 LEAAKELGLGVIASRPLNQGQLLGELR--LADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
36-260 |
5.01e-20 |
|
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: 87.49 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 36 VRWAIEAGYRHIDTAYIY---SNERGVGQGIResGVPREEVWVTTKVWNSDQGYEKTL---------AAFERSRELLGLE 103
Cdd:cd19145 39 IHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQLATKFGIHEIGGSGVEvrgdpayvrAACEASLKRLDVD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 104 YIDLYLIHWPGKKKFVD-TWKALEKLYEEKKVRAIGVSNFEPhhlTELFKSCKIRPmVNQVELHPLFQQRTLRE----FC 178
Cdd:cd19145 117 YIDLYYQHRIDTTVPIEiTMGELKKLVEEGKIKYIGLSEASA---DTIRRAHAVHP-ITAVQLEWSLWTRDIEEeiipTC 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 179 KQHNIAITAWSPLGSG------------------------EEAGILKNHVLGE----IAKKHNKSPAQVVIRWDIQHG-- 228
Cdd:cd19145 193 RELGIGIVPYSPLGRGffagkakleellensdvrkshprfQGENLEKNKVLYErveaLAKKKGCTPAQLALAWVLHQGed 272
|
250 260 270
....*....|....*....|....*....|..
gi 408407927 229 IVTIPKSTNKGRIQENFNVWDFKLTEEEMRQI 260
Cdd:cd19145 273 VVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
18-261 |
3.48e-19 |
|
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: 85.37 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 18 QLGLG----VWRAQDGA-ETANAV-RWAIEAGYRHIDTAYIY------SNERGVGQGIRESGVPREEVWVTTKV-WNSD- 83
Cdd:cd19077 7 PIGLGlmglTWRPNPTPdEEAFETmKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKGgLDPDt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 84 QGYEKTLAAFERS-----RELLGLEYIDLYLihwPGKkkfVD-------TWKALEKLYEEKKVRAIGVSnfEPHHLTeLF 151
Cdd:cd19077 87 LRPDGSPEAVRKSienilRALGGTKKIDIFE---PAR---VDpnvpieeTIKALKELVKEGKIRGIGLS--EVSAET-IR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 152 KSCKIRPMV-NQVELHPLFQ---QRTLREFCKQHNIAITAWSPLGSGEEAGILKN------------------------- 202
Cdd:cd19077 158 RAHAVHPIAaVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRGLLTGRIKSladipegdfrrhldrfngenfeknl 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 408407927 203 ---HVLGEIAKKHNKSPAQVVIRWDIQHG---IVTIPKSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:cd19077 238 klvDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-194 |
1.11e-15 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 75.09 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLGV-----WRAQDGAETANAVRWAIEAGYRHIDTAYIYsnerGVGQGIRESGV-----PREEVWVTTKV------- 79
Cdd:cd19162 1 PRLGLGAaslgnLARAGEDEAAATLDAAWDAGIRYFDTAPLY----GLGLSERRLGAalarhPRAEYVVSTKVgrllepg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 -----------WnsDQGYEKTLAAFERSRELLGLEYIDLYLIHWPGKK---KFVDTWKALEKLYEEKKVRAIGVSNFEPH 145
Cdd:cd19162 77 aagrpagadrrF--DFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHllqALTDAFPALEELRAEGVVGAIGVGVTDWA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 408407927 146 HLTELFKsckiRPMVNQVEL---HPLFQQRTLREF---CKQHNIAITAWSPLGSG 194
Cdd:cd19162 155 ALLRAAR----RADVDVVMVagrYTLLDRRAATELlplCAAKGVAVVAAGVFNSG 205
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
13-256 |
3.07e-15 |
|
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: 74.22 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 13 SVRMPQLGLGVWR---AQDGAETANA-VRWAIEAGYRHIDTAYIY-----SNERGVGQGIRESGVP-REEVWVTTKV--- 79
Cdd:cd19089 8 GLHLPAISLGLWHnfgDYTSPEEARElLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRPyRDELVISTKAgyg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 -W---NSDQGYEKTL-AAFERSRELLGLEYIDLYLIHWPGKKKFVD-TWKALEKLYEEKKVRAIGVSNFEP---HHLTEL 150
Cdd:cd19089 88 mWpgpYGDGGSRKYLlASLDQSLKRMGLDYVDIFYHHRYDPDTPLEeTMTALADAVRSGKALYVGISNYPGakaRRAIAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 151 FKSCKIRPMVNQVELHpLFQQ---RTLREFCKQHNIAITAWSPLGSG----------------------------EEAGI 199
Cdd:cd19089 168 LRELGVPLIIHQPRYS-LLDRwaeDGLLEVLEEAGIGFIAFSPLAQGlltdkylngippdsrraaeskflteealTPEKL 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 200 LKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWD-FKLTEEE 256
Cdd:cd19089 247 EQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTsvLIGASSPSQLEDNVAALKnLDFSEEE 306
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-262 |
7.01e-15 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 73.40 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 18 QLGLGVW----RAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGVPREEVWVTTKV-W------NSD 83
Cdd:cd19143 15 ALSFGSWvtfgNQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWggggppPND 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 84 QG------YEKTLAAFERsrelLGLEYIDLYLIHWPgkkkfvD-------TWKALEKLYEEKKVRAIGVSNFEPHHLTEL 150
Cdd:cd19143 95 RGlsrkhiVEGTKASLKR----LQLDYVDLVFCHRP------DpatpieeTVRAMNDLIDQGKAFYWGTSEWSAQQIEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 151 FKSCK----IRPMVNQVELHPLFQQRTLREF---CKQHNIAITAWSPLGSG------------------EEAGILKNHV- 204
Cdd:cd19143 165 HEIADrlglIPPVMEQPQYNLFHRERVEVEYaplYEKYGLGTTTWSPLASGlltgkynngipegsrlalPGYEWLKDRKe 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 408407927 205 ------------LGEIAKKHNKSPAQVVIRWDIQHGIV--TIPKSTNKGRIQENFNVWDF--KLTEEEMRQIDE 262
Cdd:cd19143 245 elgqekiekvrkLKPIAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEENLKALEVlpKLTPEVMEKIEA 318
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-222 |
1.05e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 72.17 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 39 AIEAGYRHIDTAYIYSN-ERGVGQGIRESGVPReevwVTTKV----WNSDQGYEKTLAAFERSRELLGLEYIDLYLIHWP 113
Cdd:cd19097 35 ALKAGINTLDTAPAYGDsEKVLGKFLKRLDKFK----IITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 114 G--KKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRpMVnQVELHpLFQQR-----TLREFcKQHNIAIT 186
Cdd:cd19097 111 DdlLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKID-II-QLPFN-ILDQRflksgLLAKL-KKKGIEIH 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 408407927 187 AWS--------------PLGSGEEAGILKNhvLGEIAKKHNKSPAQVVIR 222
Cdd:cd19097 187 ARSvflqglllmepdklPAKFAPAKPLLKK--LHELAKKLGLSPLELALG 234
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-246 |
1.12e-14 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 72.64 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLG------VWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIREsgVPREEVWVTTKV-------- 79
Cdd:cd19152 1 PKLGFGtaplgnLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE--LGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 ----------WNS-------DQGYEKTLAAFERSRELLGLEYIDLYLIH-------WPGKKKFVDTW-----KALEKLYE 130
Cdd:cd19152 79 eveptfepgfWNPlpfdavfDYSYDGILRSIEDSLQRLGLSRIDLLSIHdpdedlaGAESDEHFAQAikgafRALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 131 EKKVRAIGVSNFEPHHLTELFKSCKI-RPMV-------NQVELHPLFQQrtlrefCKQHNIAITAWSPLGSGEEAG---- 198
Cdd:cd19152 159 EGVIKAIGLGVNDWEVILRILEEADLdWVMLagrytllDHSAARELLPE------CEKRGVKVVNAGPFNSGFLAGgdnf 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408407927 199 ------------ILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFN 246
Cdd:cd19152 233 dyyeygpappelIARRDRIEALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVA 294
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-232 |
1.94e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 71.91 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 22 GVWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESgvpREEVWVTTKV----WNSDQGYEKTLAAFE 94
Cdd:cd19104 24 GLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL---PAGPYITTKVrldpDDLGDIGGQIERSVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 95 RSRELLGLEYIDLYLIH--------WPGKKKFV--------DTWKALEKLYEEKKVRAIGVSNF-EPHHLTELFKSCKIR 157
Cdd:cd19104 101 KSLKRLKRDSVDLLQLHnrigderdKPVGGTLSttdvlglgGVADAFERLRSEGKIRFIGITGLgNPPAIRELLDSGKFD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 158 pMVNQV-------------ELHPLFQQRTLREFCKQHNIAITAWSPLGSG-----EEAGILKNHVLG------------- 206
Cdd:cd19104 181 -AVQVYynllnpsaaearpRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAGalttsLDRGREAPPTSDsdvaidfrraaaf 259
|
250 260
....*....|....*....|....*...
gi 408407927 207 -EIAKKHNKSPAQVVIRWDIQH-GIVTI 232
Cdd:cd19104 260 rALAREWGETLAQLAHRFALSNpGVSTV 287
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
14-266 |
1.16e-13 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 70.02 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 14 VRMPQLGLGVWRA---QDGAETANAV-RWAIEAGYRHIDTAYIY-----SNERGVGQGIRESGVP-REEVWVTTK----V 79
Cdd:PRK09912 23 LRLPALSLGLWHNfghVNALESQRAIlRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKagydM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 WNSDQGYEKT----LAAFERSRELLGLEYIDLYLIHWPGKKK-FVDTWKALEKLYEEKKVRAIGVSNFEP---HHLTELF 151
Cdd:PRK09912 103 WPGPYGSGGSrkylLASLDQSLKRMGLEYVDIFYSHRVDENTpMEETASALAHAVQSGKALYVGISSYSPertQKMVELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 152 KSCKIRPMVNQVE---LHPLFQQRTLREFCKQHNIAITAWSPLGSG-------------------------------EEA 197
Cdd:PRK09912 183 REWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpkmlTEA 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408407927 198 GILKNHVLGEIAKKHNKSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVW-DFKLTEEEMRQIDELNED 266
Cdd:PRK09912 263 NLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVQALnNLTFSTEELAQIDQHIAD 334
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
27-159 |
6.52e-13 |
|
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: 67.56 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 27 QDGAETANA---VRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGVPREEVWVTTKV-----WNSDQGYEKTLAAFER 95
Cdd:cd19153 27 GDGLEQDEAvaiVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVgryrdSEFDYSAERVRASVAT 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408407927 96 SRELLGLEYIDLYLIHwpgKKKFVD-------TWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCKIRPM 159
Cdd:cd19153 107 SLERLHTTYLDVVYLH---DIEFVDydtlvdeALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSL 174
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-199 |
1.27e-12 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 66.72 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 12 NSVRMPQLGLGVWRA---QDGAETANA-VRWAIEAGYRHIDTAYIYSNERG---VGQGIRESGVPREEVWVTTKV-WN-- 81
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstAISEEQAEEiVTLAYENGINYFDTSDAFTSGQAeteLGRILKKKGWKRSSYIVSTKIyWSyg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 82 -SDQGYEKT--LAAFERSRELLGLEYIDLYLIHwpgkkkfvdtwKALEKLYEEKKVRAI------------GVSNFEPHH 146
Cdd:cd19142 89 sEERGLSRKhiIESVRASLRRLQLDYIDIVIIH-----------KADPMCPMEEVVRAMsylidnglimywGTSRWSPVE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 147 LTELFKSCK----IRPMVNQVELHPLFQQRT---LREFCKQHNIAITAWSPLGSGEEAGI 199
Cdd:cd19142 158 IMEAFSIARqfncPTPICEQSEYHMFCREKMelyMPELYNKVGVGLITWSPLSLGLDPGI 217
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
11-265 |
1.31e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 66.80 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 11 HNSVRMPQLGLGV--WRAQDGAETANA-VRWAIEAGYRHIDTAYIYS-NERGVGQGIRESGV--------PREEVWVTTK 78
Cdd:PRK10625 8 HSSLEVSTLGLGTmtFGEQNSEADAHAqLDYAVAQGINLIDVAEMYPvPPRPETQGLTETYIgnwlakrgSREKLIIASK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 79 V----WNSDQGYEKTLA--------AFERSRELLGLEYIDLYLIHWP-------GKKKF-----------VDTWKALEKL 128
Cdd:PRK10625 88 VsgpsRNNDKGIRPNQAldrknireALHDSLKRLQTDYLDLYQVHWPqrptncfGKLGYswtdsapavslLETLDALAEQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 129 YEEKKVRAIGVSNFEPH------HLTELFKSCKIRPMVNQVELHPLFQQRTLREFCKQHNIAITAWSPLGSGEEAGILKN 202
Cdd:PRK10625 168 QRAGKIRYIGVSNETAFgvmrylHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 203 ----------------HVLGE-----------IAKKHNKSPAQVVIRWDIQHGIV--TIPKSTNKGRIQENFNVWDFKLT 253
Cdd:PRK10625 248 gakpagarntlfsrftRYSGEqtqkavaayvdIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLS 327
|
330
....*....|..
gi 408407927 254 EEEMRQIDELNE 265
Cdd:PRK10625 328 EEVLAEIEAVHQ 339
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-233 |
1.58e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 66.20 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 40 IEAGYRHIDTAYIYS----------NERGVGQGIRESGVpREEVWVTTKV---------WNSD---QGYEKTLAAFERSR 97
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGRWLKDRGN-RDDVVIATKVgagprdpdgGPESpegLSAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 98 ELLGLEYIDLYLIHwpgkkkfVD--------TWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCK-------------- 155
Cdd:cd19752 106 RRLGTDYIDLYYAH-------VDdrdtpleeTLEAFNELVKAGKVRAIGASNFAAWRLERARQIARqqgwaefsaiqqrh 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 156 --IRPMVNQvelhPLFQQRTLR----EFCKQH-NIAITAWSPLGSGE--------------EAGILKNHVLGEIAKKHNK 214
Cdd:cd19752 179 syLRPRPGA----DFGVQRIVTdellDYASSRpDLTLLAYSPLLSGAytrpdrplpeqydgPDSDARLAVLEEVAGELGA 254
|
250
....*....|....*....
gi 408407927 215 SPAQVVIRWDIQHGIVTIP 233
Cdd:cd19752 255 TPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
17-222 |
2.03e-12 |
|
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: 66.20 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 17 PQLGLG------VWRAQDGAETANAVRWAIEAGYRHIDTAYIYSN---ERGVGQGIREsgVPREEVWVTTKV-------- 79
Cdd:cd19161 1 SELGLGtaglgnLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkpar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 80 ---------W--------NSDQGYEKTLAAFERSRELLGLEYIDLYLIH-----WPGKKKFVDTW--------KALEKLY 129
Cdd:cd19161 79 egsvpdpngFvdplpfeiVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHdigvyTHGDRKERHHFaqlmsggfKALEELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 130 EEKKVRAIGVSNFEPHHLTELFKSCKIRPMVNQVElHPLFQQRTLREF---CKQHNIAITAWSPLGSgeeaGILKNHVLG 206
Cdd:cd19161 159 KAGVIKAFGLGVNEVQICLEALDEADLDCFLLAGR-YSLLDQSAEEEFlprCEQRGTSLVIGGVFNS----GILATGTKS 233
|
250
....*....|....*.
gi 408407927 207 EIAKKHNKSPAQVVIR 222
Cdd:cd19161 234 GAKFNYGDAPAEIISR 249
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
18-261 |
6.04e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 61.52 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 18 QL-GLGVWRAQDGAETANAV-RWAIEAGYRHIDTAYIY----SNergvgQGIRESGVP-REEVWVTTKV---------WN 81
Cdd:PRK10376 26 QLaGPGVFGPPKDRDAAIAVlREAVALGVNHIDTSDFYgphvTN-----QLIREALHPyPDDLTIVTKVgarrgedgsWL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 82 SDQGYEKTLAAFERSRELLGLEYIDL------YLIHWPGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTELFKSCK 155
Cdd:PRK10376 101 PAFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 156 IRPMVNQVELhplfQQRT---LREFCKQHNIAITAWSPLGsgeeaGI--LKNHVLGEIAKKHNKSPAQVVIRWDIQHG-- 228
Cdd:PRK10376 181 IVCVQNHYNL----AHRAddaLIDALARDGIAYVPFFPLG-----GFtpLQSSTLSDVAASLGATPMQVALAWLLQRSpn 251
|
250 260 270
....*....|....*....|....*....|...
gi 408407927 229 IVTIPKSTNKGRIQENFNVWDFKLTEEEMRQID 261
Cdd:PRK10376 252 ILLIPGTSSVAHLRENLAAAELVLSEEVLAELD 284
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
11-231 |
3.99e-10 |
|
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: 59.34 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 11 HNSVRMPQLGLGVWR---AQDGAETANA-VRWAIEAGYRHIDTAYIY-----SNERGVGQGIRESGVP-REEVWVTTK-- 78
Cdd:cd19151 7 RSGLKLPAISLGLWHnfgDVDRYENSRAmLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 79 --VWNS---DQGYEKTL-AAFERSRELLGLEYIDLYLIHWPGKKK-FVDTWKALEKLYEEKKVRAIGVSNFEP------- 144
Cdd:cd19151 87 ytMWPGpygDWGSKKYLiASLDQSLKRMGLDYVDIFYHHRPDPETpLEETMGALDQIVRQGKALYVGISNYPPeeareaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 145 HHLTELFKSCKI-RPMVNQVELHPlfqQRTLREFCKQHNIAITAWSPLGSG-----------------EEAGILK-NHV- 204
Cdd:cd19151 167 AILKDLGTPCLIhQPKYSMFNRWV---EEGLLDVLEEEGIGCIAFSPLAQGlltdrylngipedsraaKGSSFLKpEQIt 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 408407927 205 ---------LGEIAKKHNKSPAQVVIRWDIQHGIVT 231
Cdd:cd19151 244 eeklakvrrLNEIAQARGQKLAQMALAWVLRNKRVT 279
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
35-140 |
3.07e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 56.71 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 35 AVRWAIEAGYRHIDTAYIYSN---ERGVGQGIRESGVPREEVWVTTKVWNSDQGY----EKTLAAFERSRELLGLEYIDL 107
Cdd:PLN02587 36 SVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCGRYGEGFdfsaERVTKSVDESLARLQLDYVDI 115
|
90 100 110
....*....|....*....|....*....|....*..
gi 408407927 108 YLIH---WPGKKKFV-DTWKALEKLYEEKKVRAIGVS 140
Cdd:PLN02587 116 LHCHdieFGSLDQIVnETIPALQKLKESGKVRFIGIT 152
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
11-257 |
8.90e-09 |
|
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: 55.54 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 11 HNSVRMPQLGLGVWRAQDGA---ETANAV-RWAIEAGYRHIDTAYIY-----SNERGVGQGIRESGVP-REEVWVTTK-- 78
Cdd:cd19150 7 KSGLKLPALSLGLWHNFGDDtplETQRAIlRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKag 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 79 --VWNSDQG----YEKTLAAFERSRELLGLEYIDLYLIH-WPGKKKFVDTWKALEKLYEEKKVRAIGVSNFEPHHLTE-- 149
Cdd:cd19150 87 ydMWPGPYGewgsRKYLLASLDQSLKRMGLDYVDIFYSHrFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 150 -LFKSCKIRPMVNQVE---LHPLFQQRTLREFCKQHNIAITAWSPLGSG-----------------EEAGILKNHV---- 204
Cdd:cd19150 167 aILRELGTPLLIHQPSynmLNRWVEESGLLDTLQELGVGCIAFTPLAQGlltdkylngipegsrasKERSLSPKMLtean 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408407927 205 ------LGEIAKKHNKSPAQVVIRWDIQHGIVT--IPKSTNKGRIQENFNVWD-FKLTEEEM 257
Cdd:cd19150 247 lnsiraLNEIAQKRGQSLAQMALAWVLRDGRVTsaLIGASRPEQLEENVGALDnLTFSADEL 308
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
30-140 |
2.20e-06 |
|
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: 48.04 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408407927 30 AETANAVRWAIEAGYRHIDTAYIYSN-ERGVGQGIR--ESGVPREEVWVTTKV-----WNSDQGYEKTLAAFERSRELLG 101
Cdd:cd19164 34 IPPVDIVRRALELGIRAFDTSPYYGPsEIILGRALKalRDEFPRDTYFIITKVgrygpDDFDYSPEWIRASVERSLRRLH 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 408407927 102 LEYIDLYLIHwpgKKKFVDTWKALE------KLYEEKKVRAIGVS 140
Cdd:cd19164 114 TDYLDLVYLH---DVEFVADEEVLEalkelfKLKDEGKIRNVGIS 155
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
35-97 |
1.06e-03 |
|
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380511 [Multi-domain] Cd Length: 268 Bit Score: 39.84 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408407927 35 AVRWAIEAGYRHIdtAYIYSNE---------RGVGQGIRESGVPREEVWVTTKVWNSDQGYEKTLAAFERSR 97
Cdd:cd06288 107 ATRHLIEAGHRRI--AFIGGPEdslatrlrlAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLSAPD 176
|
|
| |
