|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
9-275 |
8.47e-144 |
|
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: 404.08 E-value: 8.47e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQ-TAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGlkatGLKREDLFITSKVWNNH 87
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKES----GIPREELFITSKVWNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQI 167
Cdd:cd19157 78 QGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 168 ELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNAS 247
Cdd:cd19157 158 EFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENAD 237
|
250 260
....*....|....*....|....*...
gi 499795780 248 VFDFELDDEDMDRINMLNEDLRVGPNPD 275
Cdd:cd19157 238 VFDFELSQEDMDKIDALNENLRVGPDPD 265
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
13-275 |
3.85e-141 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 397.12 E-value: 3.85e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 13 NGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHLTYDE 92
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVG----EAIAASGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 93 TIAAFNESLAKLDLDYLDLYLIHWPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQIELHPK 172
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 173 LAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFE 252
Cdd:COG0656 157 LQQRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFE 236
|
250 260
....*....|....*....|...
gi 499795780 253 LDDEDMDRINMLNEDLRVGPNPD 275
Cdd:COG0656 237 LSDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
17-262 |
7.17e-114 |
|
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: 327.90 E-value: 7.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 17 IPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHLTYDETIAA 96
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVG----EAIRESGVPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 97 FNESLAKLDLDYLDLYLIHWPGQD-------AFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQIEL 169
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGkeggskeARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 170 HPKLAQKELREYAANMDMKIQAWSPLMQG--QLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNAS 247
Cdd:cd19071 157 HPYLQQKELVEFCKEHGIVVQAYSPLGRGrrPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLD 236
|
250
....*....|....*
gi 499795780 248 VFDFELDDEDMDRIN 262
Cdd:cd19071 237 VFDFELSEEDMAAID 251
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-277 |
8.60e-114 |
|
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: 328.32 E-value: 8.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPE-DQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNH 87
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVG----QGIRESGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQI 167
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 168 ELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNAS 247
Cdd:cd19156 157 ELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFD 236
|
250 260 270
....*....|....*....|....*....|
gi 499795780 248 VFDFELDDEDMDRINMLNEDLRVGPNPDEF 277
Cdd:cd19156 237 VFDFELTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-265 |
2.37e-113 |
|
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: 326.64 E-value: 2.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHL 88
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVG----KAIRASGVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHW--PGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQ 166
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWpvPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 167 IELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNA 246
Cdd:cd19131 158 IELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENF 237
|
250
....*....|....*....
gi 499795780 247 SVFDFELDDEDMDRINMLN 265
Cdd:cd19131 238 DVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
9-265 |
1.27e-112 |
|
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: 324.78 E-value: 1.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAE-VVKNGIINGYRLIDTAAIYGNEKGTGIGIKEglkaTGLKREDLFITSKVWNNH 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETErAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQI 167
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 168 ELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNAS 247
Cdd:cd19126 157 EFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENAD 236
|
250
....*....|....*...
gi 499795780 248 VFDFELDDEDMDRINMLN 265
Cdd:cd19126 237 IFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-265 |
9.24e-104 |
|
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: 302.57 E-value: 9.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAE-VVKNGIINGYRLIDTAAIYGNEKGTGIGIKEglkaTGLKREDLFITSKVWNNH 87
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK----SGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAFEeSWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQI 167
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDVYG-AWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 168 ELHPKLAQKELREYAANMDMKIQAWSPLMQGQ--LLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISN 245
Cdd:cd19133 156 ETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAEN 235
|
250 260
....*....|....*....|
gi 499795780 246 ASVFDFELDDEDMDRINMLN 265
Cdd:cd19133 236 FDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
9-265 |
1.74e-99 |
|
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: 292.00 E-value: 1.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHL 88
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVG----EGIRRSGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAFE---ESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVIN 165
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDrtiQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 166 QIELHPKLAQKELREYAANMDMKIQAWSPL------------MQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLN 233
Cdd:cd19127 157 QVELHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAI 236
|
250 260 270
....*....|....*....|....*....|..
gi 499795780 234 VKSVHTDRMISNASVFDFELDDEDMDRINMLN 265
Cdd:cd19127 237 PKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-264 |
2.55e-95 |
|
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: 281.44 E-value: 2.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 17 IPGLGLGVFQIPEDQTAE-VVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTYDETIA 95
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRqAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 96 AFNESLAKLDLDYLDLYLIHWPGQDAFE-----------ESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVI 164
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKpsdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 165 NQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQL--LKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRM 242
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLrlLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 499795780 243 ISNASVFDFELDDEDMDRINML 264
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-265 |
1.18e-93 |
|
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: 276.84 E-value: 1.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 11 LNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHLTY 90
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVG----EAVRRSGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 91 DETIAAFNESLAKLDLDYLDLYLIHWP--GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQIE 168
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWPnpSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 169 LHPKLAQKELREYAANMDMKIQAWSPLMQGQ-LLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNAS 247
Cdd:cd19132 157 LHPYFPQAEQRAYHREHGIVTQSWSPLGRGSgLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLA 236
|
250
....*....|....*...
gi 499795780 248 VFDFELDDEDMDRINMLN 265
Cdd:cd19132 237 IFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-265 |
3.41e-90 |
|
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: 267.93 E-value: 3.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 8 RVELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNH 87
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVG----AAIAASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWP--GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVIN 165
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPtpAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 166 QIELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISN 245
Cdd:cd19130 157 QIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDN 236
|
250 260
....*....|....*....|
gi 499795780 246 ASVFDFELDDEDMDRINMLN 265
Cdd:cd19130 237 LDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-264 |
6.71e-86 |
|
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: 257.25 E-value: 6.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEglkaTGLKREDLFITSKVWNNHL 88
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTTKLWPSDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHWPG--------QDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKV 160
Cdd:cd19135 81 GYESTKQAFEASLKRLGVDYLDLYLLHWPDcpssgknvKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 161 VPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTD 240
Cdd:cd19135 161 VPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEE 240
|
250 260
....*....|....*....|....
gi 499795780 241 RMISNASVFDFELDDEDMDRINML 264
Cdd:cd19135 241 RIKENCQVFDFSLSEEDMATLDSL 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
9-277 |
3.82e-82 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 248.06 E-value: 3.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNN-H 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVG----KALKEASVAREELFITTKLWNDdH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDEtiaAFNESLAKLDLDYLDLYLIHWP--GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVIN 165
Cdd:PRK11565 83 KRPRE---ALEESLKKLQLDYVDLYLMHWPvpAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 166 QIELHPKLAQKELREYAANMDMKIQAWSPLMQG--QLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMI 243
Cdd:PRK11565 160 QIELHPLMQQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIA 239
|
250 260 270
....*....|....*....|....*....|....
gi 499795780 244 SNASVFDFELDDEDMDRINMLNEDLRVGPNPDEF 277
Cdd:PRK11565 240 ENFDVFDFRLDKDELGEIAKLDQGKRLGPDPDQF 273
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
17-262 |
2.48e-81 |
|
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: 244.87 E-value: 2.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 17 IPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHLTYDETIAA 96
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVG----EAIAESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 97 FNESLAKLDLDYLDLYLIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQIELHPKLAQ 175
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPNPTvPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 176 KELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDD 255
Cdd:cd19073 157 AELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTS 236
|
....*..
gi 499795780 256 EDMDRIN 262
Cdd:cd19073 237 EDVAKID 243
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
10-270 |
1.19e-80 |
|
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: 244.95 E-value: 1.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 10 ELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLT 89
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 90 YDETIAAFNESLAKLDLDYLDLYLIHWP-----GQDAF----------EESWKALETLYAEGKIKAIGVSNFEIHHLERL 154
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkGAHMPepeevlppdiPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 155 KTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL-------MQGQLLKNEVILDIAKKHNKSAAQVILRWDIQ 227
Cdd:cd19125 164 LAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgttwVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499795780 228 QDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRV 270
Cdd:cd19125 244 RGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
9-271 |
1.62e-79 |
|
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: 241.30 E-value: 1.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKeglkATGLKREDLFITSKVWNNHL 88
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA----ASGIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHWPGQDA--FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQ 166
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWPAGREgkYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 167 IELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNA 246
Cdd:cd19134 159 IELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNL 238
|
250 260
....*....|....*....|....*
gi 499795780 247 SVFDFELDDEDMDRINMLNEDLRVG 271
Cdd:cd19134 239 DVFDFELTADHMDALDGLDDGTRFR 263
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-264 |
5.05e-78 |
|
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: 236.77 E-value: 5.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 13 NGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHLTYDE 92
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVG----EAIAASGVPRDELFLTTKVWPDNYSPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 93 TIAAFNESLAKLDLDYLDLYLIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQIELHP 171
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWPNKDvPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 172 KLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQ-DILLNVKSVHTDRMISNASVFD 250
Cdd:cd19140 160 YLDQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFD 239
|
250
....*....|....
gi 499795780 251 FELDDEDMDRINML 264
Cdd:cd19140 240 FTLSDEEMARIAAL 253
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-270 |
1.92e-77 |
|
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: 236.80 E-value: 1.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 8 RVELNNGTKIPGLGLGVFQ-IPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNN 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKlKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 87 HLTYDETIAAFNESLAKLDLDYLDLYLIHWP--------------GQD---AFEESWKALETLYAEGKIKAIGVSNFEIH 149
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesngdGSLsdiDYLETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 150 HLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL----MQGQL-----LKNEVILDIAKKHNKSAAQV 220
Cdd:cd19116 162 QINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrlvPRGQTnppprLDDPTLVAIAKKYGKTTAQI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499795780 221 ILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRV 270
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
6-270 |
3.57e-72 |
|
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: 223.83 E-value: 3.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 6 SDRVELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWN 85
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 86 NHLTYDETIAAFNESLAKLDLDYLDLYLIHWP---------------GQDAF-----EESWKALETLYAEGKIKAIGVSN 145
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmenGMSIHdavdvEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 146 FEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL---------------MQGQLLKNEVILDIA 210
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgranftkstgvsPAPNLLQDPIVKAIA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 211 KKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRV 270
Cdd:cd19154 241 EKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-269 |
1.18e-71 |
|
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: 222.29 E-value: 1.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 11 LNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTY 90
Cdd:cd19123 6 LSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSHAP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 91 DETIAAFNESLAKLDLDYLDLYLIHWP------------GQD-------AFEESWKALETLYAEGKIKAIGVSNFEIHHL 151
Cdd:cd19123 86 EDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesGEDllslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 152 ERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQ------------LLKNEVILDIAKKHNKSAAQ 219
Cdd:cd19123 166 EDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepvLLEDPVINKIAEKHGASPAQ 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499795780 220 VILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLR 269
Cdd:cd19123 246 VLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
11-264 |
1.82e-68 |
|
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: 213.81 E-value: 1.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 11 LNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLK-ATGLKREDLFITSKVWNNHLT 89
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKeEPGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 90 YDETIAAFNESLAKLDLDYLDLYLIHWP-----GQDAFE--------------------ESWKALETLYAEGKIKAIGVS 144
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPvafkpTGDLNPltavptnggevdldlsvslvDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 145 NFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL---MQGQ--LLKNEVILDIAKKHNKSAAQ 219
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLplLVQHPEVKAIAAKLGKTPAQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499795780 220 VILRWDIQQDILLNVKSVHTDRMISNASvfDFELDDEDMDRINML 264
Cdd:cd19118 241 VLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
11-270 |
2.30e-67 |
|
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: 211.47 E-value: 2.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 11 LNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKA-TGLKREDLFITSKVWNNHLT 89
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 90 YDETIAAFNESLAKLDLDYLDLYLIHWP-----GQDAF---------------EESWKALETLYAEGKIKAIGVSNFEIH 149
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPyaferGDNPFpknpdgtirydsthyKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 150 HLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL----------MQGQLLKNEVILDIAKKHNKSAAQ 219
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrpwakpDEPVLLEEPKVKALAKKYNKSPAQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499795780 220 VILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRV 270
Cdd:cd19106 241 ILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
14-262 |
1.77e-66 |
|
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: 207.86 E-value: 1.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLGV----FQIPED----QTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWN 85
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVG----EALKESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 86 NHltyDETIAAFNESLAKLDLDYLDLYLIHWP-----GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKV 160
Cdd:cd19120 77 GI---KDPREALRKSLAKLGVDYVDLYLIHSPffakeGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 161 VPVINQIELHPKLA--QKELREYAANMDMKIQAWSPL------MQGQLLKneVILDIAKKHNKSAAQVILRWDIQQDILL 232
Cdd:cd19120 154 KPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLspltrdAGGPLDP--VLEKIAEKYGVTPAQVLLRWALQKGIVV 231
|
250 260 270
....*....|....*....|....*....|
gi 499795780 233 NVKSVHTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19120 232 VTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
11-264 |
7.70e-66 |
|
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: 206.97 E-value: 7.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 11 LNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIkeglKATGLKREDLFITSKVWNNHltY 90
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFITTKLWCTW--H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 91 DETIAAFNESLAKLDLDYLDLYLIHWP----------------GQDA------FEESWKALETLYAEGKIKAIGVSNFEI 148
Cdd:cd19117 82 RRVEEALDQSLKKLGLDYVDLYLMHWPvpldpdgndflfkkddGTKDhepdwdFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 149 HHLERL--KTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL--MQGQLLKNEVILDIAKKHNKSAAQVILRW 224
Cdd:cd19117 162 KNLEKLlaSPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgsTNAPLLKEPVIIKIAKKHGKTPAQVIISW 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499795780 225 DIQQDILLNVKSVHTDRMISNASVfdFELDDEDMDRINML 264
Cdd:cd19117 242 GLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
11-262 |
7.87e-66 |
|
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: 206.61 E-value: 7.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 11 LNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLkATGLKREDLFITSKVWNNHltY 90
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTY--H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 91 DETIAAFNESLAKLDLDYLDLYLIHWP------GQD-----------------AFEESWKALETLYAEGKIKAIGVSNFE 147
Cdd:cd19121 83 RRVELCLDRSLKSLGLDYVDLYLVHWPvllnpnGNHdlfptlpdgsrdldwdwNHVDTWKQMEKVLKTGKTKAIGVSNYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 148 IHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL--MQGQLLKNEVILDIAKKHNKSAAQVILRWD 225
Cdd:cd19121 163 IPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVLISYQ 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 499795780 226 IQQDILLNVKSVHTDRMISNASVFDFelDDEDMDRIN 262
Cdd:cd19121 243 VARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLN 277
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
13-261 |
4.39e-64 |
|
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: 202.50 E-value: 4.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 13 NGTKIPGLGLGVFQIPED--QTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKAtGL--KREDLFITSKVWNNHL 88
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSpeDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRL-GLvkSRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHWP---GQDAF--------------EESWKALETLYAEGKIKAIGVSNFEIHHL 151
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPvslKPGKFsfpieeedflpfdiKGVWEAMEECQRLGLTKAIGVSNFSCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 152 ERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL-----MQG--QLLKNEVILDIAKKHNKSAAQVILRW 224
Cdd:cd19124 160 QELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgapgtKWGsnAVMESDVLKEIAAAKGKTVAQVSLRW 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 499795780 225 DIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRI 261
Cdd:cd19124 240 VYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-269 |
1.85e-62 |
|
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: 199.18 E-value: 1.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHL 88
Cdd:cd19115 5 VKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHWP-------------------------GQDAFEESWKALETLYAEGKIKAIGV 143
Cdd:cd19115 85 DGERVEPICRKQLADWGIDYFDLFLIHFPialkyvdpavryppgwfydgkkvefSNAPIQETWTAMEKLVDKGLARSIGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 144 SNFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWS---PL------MQGQ-----LLKNEVILDI 209
Cdd:cd19115 165 SNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgPQsfleldLPGAkdtppLFEHDVIKSI 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 210 AKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLR 269
Cdd:cd19115 245 AEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-269 |
5.20e-62 |
|
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: 198.05 E-value: 5.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHL 88
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHWP-------------------GQDAFE-------ESWKALETLYAEGKIKAIG 142
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgDGDNFVyedvpilDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 143 VSNFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSP--------LMQGQ------LLKNEVILD 208
Cdd:cd19113 163 VSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSfgpqsfveLNQGRalntptLFEHDTIKS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499795780 209 IAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLR 269
Cdd:cd19113 243 IAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
14-270 |
8.26e-62 |
|
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: 197.26 E-value: 8.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTYDET 93
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 94 IAAFNESLAKLDLDYLDLYLIHWP-----GQDAFE---------------ESWKALETLYAEGKIKAIGVSNFEIHHLER 153
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPtgfkpGKELFPldesgnvipsdttflDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 154 L--KTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL----------MQGQLLKNEVILDIAKKHNKSAAQVI 221
Cdd:cd19107 161 IlnKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwakpEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499795780 222 LRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRV 270
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRA 289
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-274 |
1.72e-61 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 196.33 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 16 KIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTYDETIA 95
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 96 AFNESLAKLDLDYLDLYLIHWP--------------------GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERL- 154
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPmgfkpgepdlpldrsgmvipSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 155 -KTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL---MQG-QLLKNEVILDIAKKHNKSAAQVILRWDIQQD 229
Cdd:cd19110 163 nKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLggsCEGvDLIDDPVIQRIAKKHGKSPAQILIRFQIQRN 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499795780 230 ILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRVGPNP 274
Cdd:cd19110 243 VIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
17-264 |
1.91e-60 |
|
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: 191.80 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 17 IPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGigikEGLKATGLKREDLFITSKVWNNHLTYDETIAA 96
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 97 FNESLAKLDLDYLDLYLIHWP---GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLER-LKTFAKVVPVINQIELHPK 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPspnDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEaIAVVGAGAIATNQIELSPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 173 LAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFE 252
Cdd:cd19139 157 LQNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLT 236
|
250
....*....|..
gi 499795780 253 LDDEDMDRINML 264
Cdd:cd19139 237 LDADDMAAIAAL 248
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-266 |
2.76e-59 |
|
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: 190.40 E-value: 2.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 6 SDRVELNNGTKIPGLGLGVFQIPED--QTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKV 83
Cdd:cd19119 1 EISFKLNTGASIPALGLGTASPHEDraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 WNNHltYDETIAAFNESLAKLDLDYLDLYLIHWP--------------------GQDAFEES------WKALETLYAEGK 137
Cdd:cd19119 81 WPTF--YDEVERSLDESLKALGLDYVDLLLVHWPvcfekdsddsgkpftpvnddGKTRYAASgdhittYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 138 IKAIGVSNFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL--MQGQLLKNEVILDIAKKHNK 215
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLgsHGAPNLKNPLVKKIAEKYNV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499795780 216 SAAQVILRWDIQQDILLNVKSVHTDRMISNASVfdFELDDEDMDRINMLNE 266
Cdd:cd19119 239 STGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
14-269 |
8.28e-59 |
|
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: 188.86 E-value: 8.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTYDET 93
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 94 IAAFNESLAKLDLDYLDLYLIHWP------GQDAF--------EESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAK 159
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPcgfvnkKDKGErelassdvTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 160 VVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL------------MQGQLLKNEVILDIAKKHNKSAAQVILRWDIQ 227
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgspgranqslwpDQPDLLEDPTVLAIAKELDKTPAQVLLRFVLQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499795780 228 QDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLR 269
Cdd:cd19111 241 RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
14-269 |
5.67e-58 |
|
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: 187.38 E-value: 5.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTYDET 93
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 94 IAAFNESLAKLDLDYLDLYLIHWP--------------------------GQDAFEESWKALETLYAEGKIKAIGVSNFE 147
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPipaayvdpaenypflwkdkelkkfplEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 148 IHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQG-------------QLLKNEVILDIAKKHN 214
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkhftNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499795780 215 KSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLR 269
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-274 |
9.12e-58 |
|
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: 186.92 E-value: 9.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNhl 88
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETIAAFNESLAKLDLDYLDLYLIHWP---------------GQD---------AFEESWKALETLYAEGKIKAIGVS 144
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalGEDgvldidvtiSLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 145 NFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQG----------QLLKNEVILDIAKKHN 214
Cdd:cd19112 161 NYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsvSPLDDPVLKDLAKKYG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 215 KSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRVGPNP 274
Cdd:cd19112 241 KSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-272 |
3.64e-57 |
|
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: 185.13 E-value: 3.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 8 RVELNNGTKIPGLGLGVF---QIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVW 84
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYapeEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 85 NNHLTYDETIAAFNESLAKLDLDYLDLYLIHWP-----GQDAFEE---------------SWKALETLYAEGKIKAIGVS 144
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPvalkpGEELFPKdengklifdtvdlcaTWEAMEKCKDAGLAKSIGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 145 NFEIHHLERL--KTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLmqGQ-------------LLKNEVILDI 209
Cdd:cd19108 162 NFNRRQLEMIlnKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSAL--GSqrdkewvdqnspvLLEDPVLCAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499795780 210 AKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLRVGP 272
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-277 |
5.99e-56 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 180.99 E-value: 5.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 16 KIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEglkaTGLKREDLFITSKVWNNHLTYDETIA 95
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 96 AFNESLAKLDLDYLDLYLIHWPGQD---AFEESWKALETLYAEGKIKAIGVSNFEIHHLER-LKTFAKVVPVINQIELHP 171
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPSPNdevSVEEFMQALLEAKKQGLTREIGISNFTIALMKQaIAAVGAENIATNQIELSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 172 KLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDF 251
Cdd:PRK11172 158 YLQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDL 237
|
250 260
....*....|....*....|....*.
gi 499795780 252 ELDDEDMDRINMLNEDLRVgPNPDEF 277
Cdd:PRK11172 238 QLDAEDMAAIAALDRNGRL-VSPEGL 262
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
14-262 |
1.83e-54 |
|
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: 177.04 E-value: 1.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLGVFQIPEDQTA---------EVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKeglkatGLKREDLFITS 81
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKdysddkkaiEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 82 KVWNNHLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKV 160
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSiPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 161 VPVI-NQIE--LHPKLAQKELREYAANMDMKIQAWSPLMQGQLLK---NEVILDIAKKHNKSAAQVILRWDIQQD-ILLN 233
Cdd:cd19072 155 GPIVaNQVEynLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNakgSPLLDEIAKKYGKTPAQIALNWLISKPnVIAI 234
|
250 260
....*....|....*....|....*....
gi 499795780 234 VKSVHTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19072 235 PKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
14-269 |
5.06e-53 |
|
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: 174.99 E-value: 5.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLGVF----QIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLT 89
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 90 YDETIAAFNESLAKLDLDYLDLYLIHWP---------------GQDAFEES-----WKALETLYAEGKIKAIGVSNFEIH 149
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPmafkpgdeiyprdenGKWLYHKTnlcatWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 150 HLERL--KTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQ-----------LLKNEVILDIAKKHNKS 216
Cdd:cd19109 161 QLELIlnKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499795780 217 AAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLR 269
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
18-264 |
2.27e-49 |
|
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: 164.62 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 18 PGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTYDETIAAF 97
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 98 NESLAKLDLDYLDLYLIHWP--------------------GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTF 157
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqslSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 158 AKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILD------IAKKHNKSAAQVILRWDIQQ--- 228
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTFLNdselkaLATKYNTTPPQVIIAWHLQKwpk 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 499795780 229 DILLNVKSVHTDRMISNASVFDFELDDEDMDRINML 264
Cdd:cd19128 242 NYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
11-266 |
3.40e-49 |
|
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: 164.33 E-value: 3.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 11 LNNGTKIPGLGLGVF--QIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKA-TGLKREDLFITSKVWNNH 87
Cdd:cd19122 3 LNNGVKIPAVGFGTFanEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKEnPSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWP-------------GQDAF-----------EESWKALETLYAEGKIKAIGV 143
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPiaaekndqrspklGPDGKyvilkdltenpEPTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 144 SNFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL-MQGQ-------LLKNEVILDIAKKHNK 215
Cdd:cd19122 163 SNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgSQNQvpstgerVSENPTLNEVAEKGGY 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499795780 216 SAAQVILRWDIQQDILLNVKSVHTDRMISNASVfdFELDDEDMDRINMLNE 266
Cdd:cd19122 243 SLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQVAK 291
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-269 |
7.00e-49 |
|
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: 164.24 E-value: 7.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 7 DRVELNNGTKIPGLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNN 86
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 87 HLTYDETIAAFNESLAKLDLDYLDLYLIHWP------GQDAFE----------------ESWKALETLYAEGKIKAIGVS 144
Cdd:cd19155 82 GNRREKVEKFLLKSLEKLQLDYVDLYLIHFPvgslskEDDSGKldptgehkqdyttdllDIWKAMEAQVDQGLTRSIGLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 145 NFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL-----------------MQGQLLKNEVIL 207
Cdd:cd19155 162 NFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQDPVVK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499795780 208 DIAKKHNKSAAQVILRWDIQQDILLNVKSVHTDRMISNASVFDFELDDEDMDRINMLNEDLR 269
Cdd:cd19155 242 AIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
12-262 |
6.50e-47 |
|
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: 158.77 E-value: 6.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLGVFqIPED-QTAEVVKNGIINGYRLIDTAAIYGNEKGTGIGIKEGLKATGLKREDLFITSKVWNNHLTY 90
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPsATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 91 DETIAAFNESLAKLDLDYLDLYLIHWP-------GQDAFEES--------------WKALETLYAEGKIKAIGVSNFEIH 149
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdEQDPRDANgnviyddgvtlldtWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 150 HLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPL---MQGQLLKNEVILDIAKKHNKSAAQVILRWDI 226
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLghgMEPKLLEDPVITAIARRVNKTPAQVLLAWAI 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 499795780 227 QQDILLNVKSVHTDRMISNasvFDFE-LDDEDMDRIN 262
Cdd:cd19129 240 QRGTALLTTSKTPSRIREN---FDIStLPEDAMREIN 273
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
14-262 |
4.51e-46 |
|
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: 155.42 E-value: 4.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLGVFQI---------PEDQTAEVVKNGIINGYRLIDTAAIYG---NEKGTGIGIKEglkatgLKREDLFITS 81
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdysRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 82 KVWNNHLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKV 160
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNiPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 161 VPVINQIELH---PKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNKSAAQVILRWDIQQDILLNV-KS 236
Cdd:cd19137 155 PIVCNQVKYNledRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAIpKA 234
|
250 260
....*....|....*....|....*.
gi 499795780 237 VHTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19137 235 GRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-261 |
1.14e-44 |
|
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: 152.47 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 19 GLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIgIKEGLKATGLKREDLFITSKVWNN------HLTYDE 92
Cdd:pfam00248 7 QLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEEL-LGEALKDYPVKRDKVVIATKVPDGdgpwpsGGSKEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 93 TIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQIELHP 171
Cdd:pfam00248 86 IRKSLEESLKRLGTDYIDLYYLHWPDPDTpIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 172 --KLAQKELREYAANMDMKIQAWSPLMQGQLLK---------------------------NEVILDIAKKHNKSAAQVIL 222
Cdd:pfam00248 166 lrRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleaLEALEEIAKEHGVSPAQVAL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499795780 223 RWDIQQD----ILLNVKSVhtDRMISNASVFDFELDDEDMDRI 261
Cdd:pfam00248 246 RWALSKPgvtiPIPGASNP--EQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-262 |
3.61e-44 |
|
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: 150.48 E-value: 3.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 9 VELNNGTKIPGLGLGVFQIPED-----QTAEVVKNGIINGYRLIDTAAIYGNekgtgiGIKEGLKATGLK--REDLFITS 81
Cdd:cd19138 3 VTLPDGTKVPALGQGTWYMGEDpakraQEIEALRAGIDLGMTLIDTAEMYGD------GGSEELVGEAIRgrRDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 82 KVWNNHLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTfakvV 161
Cdd:cd19138 77 KVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWA----V 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 162 P-----VINQIELHpkLAQK----ELREYAANMDMKIQAWSPLMQG-----QLLKNEVILDIAKKHNKSAAQVILRWDIQ 227
Cdd:cd19138 153 PgggncAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGgllrrGLLENPTLKEIAARHGATPAQVALAWVLR 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 499795780 228 QDILLNV-KSVHTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19138 231 DGNVIAIpKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
16-262 |
7.39e-36 |
|
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: 129.57 E-value: 7.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 16 KIPGLGLGVFQI--------PEDQTAEVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKEglkatglKREDLFITSKV- 83
Cdd:cd19084 3 KVSRIGLGTWAIggtwwgevDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATKCg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 --WNN------HLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLERL 154
Cdd:cd19084 76 lrWDGgkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNtPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 155 KTFAKVvpVINQIE---LHPKlAQKELREYAANMDMKIQAWSPLMQGQL---------------------------LKNE 204
Cdd:cd19084 156 RKYGPI--VSLQPPysmLERE-IEEELLPYCRENGIGVLPYGPLAQGLLtgkykkeptfppddrrsrfpffrgenfEKNL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499795780 205 VILD----IAKKHNKSAAQVILRWDIQQD----ILLNVKSVhtDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19084 233 EIVDklkeIAEKYGKSLAQLAIAWTLAQPgvtsAIVGAKNP--EQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-268 |
8.52e-36 |
|
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: 129.63 E-value: 8.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 17 IPGLGLGVFQI-----PEDQTAE----VVKNGIINGYRLIDTAAIYGNekgtgiGIKEGL--KATGLKREDLFITSKVWN 85
Cdd:cd19085 1 VSRLGLGCWQFgggywWGDQDDEesiaTIHAALDAGINFFDTAEAYGD------GHSEEVlgKALKGRRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 86 NHLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVvpVI 164
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVpLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI--DS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 165 NQIELHP--KLAQKELREYAANMDMKIQAWSPLMQGqLL-----------------KN----------------EVILDI 209
Cdd:cd19085 153 NQLPYNLlwRAIEYEILPFCREHGIGVLAYSPLAQG-LLtgkfssaedfppgdartRLfrhfepgaeeetfealEKLKEI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499795780 210 AKKHNKSAAQVILRWDIQQDillNVKSV-----HTDRMISNASVFDFELDDEDMDRINMLNEDL 268
Cdd:cd19085 232 ADELGVTMAQLALAWVLQQP---GVTSVivgarNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
12-274 |
2.77e-31 |
|
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: 117.97 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLGVFQI-------PEDQTAEVVKNGIINGYRLIDTAAIYG---NEKGTGigikEGLKatGLKREDLFITS 81
Cdd:COG0667 8 RSGLKVSRLGLGTMTFggpwggvDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLG----EALK--GRPRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 82 KV--------WNNHLTYDETIAAFNESLAkldldyldlylIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLE 152
Cdd:COG0667 82 KVgrrmgpgpNGRGLSREHIRRAVEASLRrlgtdyidlyqLHRPDPDtPIEETLGALDELVREGKIRYIGVSNYSAEQLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 153 R-LKTFAKVVP-VINQIE---LHPKlAQKELREYAANMDMKIQAWSPLMQGqLL-------------------------- 201
Cdd:COG0667 162 RaLAIAEGLPPiVAVQNEyslLDRS-AEEELLPAARELGVGVLAYSPLAGG-LLtgkyrrgatfpegdraatnfvqgylt 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 202 -----KNEVILDIAKKHNKSAAQVILRWDIQQD----ILLNVKSVhtDRMISNASVFDFELDDEDMDRInmlNEDLRVGP 272
Cdd:COG0667 240 ernlaLVDALRAIAAEHGVTPAQLALAWLLAQPgvtsVIPGARSP--EQLEENLAAADLELSAEDLAAL---DAALAAVP 314
|
..
gi 499795780 273 NP 274
Cdd:COG0667 315 AP 316
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
16-262 |
2.65e-27 |
|
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: 106.93 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 16 KIPGLGLGVFQ-----------IPEDQTAEVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKEGLKatglkREDLFITS 81
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELGD-----RDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 82 KVWNNH--LTYDETIAAFNESLAKLDLDYLDLYLIHWPG--QDAFEESWKALETLYAEGKIKAIGVSNFEihhLERLKTF 157
Cdd:cd19093 76 KFAPLPwrLTRRSVVKALKASLERLGLDSIDLYQLHWPGpwYSQIEALMDGLADAVEEGLVRAVGVSNYS---ADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 158 AK------VVPVINQIE---LHPKLAQKELREYAANMDMKIQAWSPLMQG-----------------------QLLKNEV 205
Cdd:cd19093 153 HKalkergVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGlltgkyspenpppggrrrlfgrkNLEKVQP 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499795780 206 ILD----IAKKHNKSAAQVILRWDIQQDILL-----NVKSVhtdrmISNASVFDFELDDEDMDRIN 262
Cdd:cd19093 233 LLDaleeIAEKYGKTPAQVALNWLIAKGVVPipgakNAEQA-----EENAGALGWRLSEEEVAELD 293
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
21-257 |
1.38e-24 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 99.84 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 21 GLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGI-GikEGLKATGLKREDLFITSK-----------VWNNHl 88
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALfG--EALKLSPSLREKIELQTKcgirlpseardNRVKH- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 tYDET----IAAFNESLAKLDLDYLDLYLIHWPgqDAF---EESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVV 161
Cdd:COG4989 99 -YDTSkehiIASVEGSLRRLGTDYLDLLLLHRP--DPLmdpEEVAEAFDELKASGKVRHFGVSNFTPSQFELLQSALDQP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 162 PVINQIE---LHPKLAQKELREYAANMDMKIQAWSPLMQGQLLK---------NEVILDIAKKHNKSAAQVILRWdiqqd 229
Cdd:COG4989 176 LVTNQIElslLHTDAFDDGTLDYCQLNGITPMAWSPLAGGRLFGgfdeqfprlRAALDELAEKYGVSPEAIALAW----- 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 499795780 230 iLLN--------VKSVHTDRMISNASVFDFELDDED 257
Cdd:COG4989 251 -LLRhpagiqpvIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
19-229 |
1.89e-24 |
|
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: 97.97 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 19 GLGLGVF--QIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKG-TGIGikEGLKATGlKREDLFITSKV--------WNNH 87
Cdd:cd06660 4 GLGTMTFggDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSeRLLG--RWLKGRG-NRDDVVIATKGghppggdpSRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAK----VVP 162
Cdd:cd06660 81 LSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTpVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPGF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 163 VINQIE---LHPKLAQKELREYAANMDMKIQAWSPLMQGqllknevildiakkhnksAAQVILRWDIQQD 229
Cdd:cd06660 161 AAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQP 212
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
21-257 |
2.08e-23 |
|
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: 96.47 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 21 GLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGN---EKGTGigikEGLKATGLKREDLFITSKV-----------WNN 86
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFG----EALALNPGLREKIEIQTKCgirlgddprpgRIK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 87 H--LTYDETIAAFNESLAKLDLDYLDLYLIHWPgqDAF---EESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVV 161
Cdd:cd19092 91 HydTSKEHILASVEGSLKRLGTDYLDLLLLHRP--DPLmdpEEVAEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 162 PVINQIE---LHPKLAQKELREYAANMDMKIQAWSPLMQGQLLK---------NEVILDIAKKHNKSAAQVILRWdiqqd 229
Cdd:cd19092 169 LVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGgfderfqrlRAALEELAEEYGVTIEAIALAW----- 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 499795780 230 iLLN--------VKSVHTDRMISNASVFDFELDDED 257
Cdd:cd19092 244 -LLRhpariqpiLGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-264 |
9.80e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 86.57 E-value: 9.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 43 GYRLIDTAAIYG---NEKGTGIGIKEglkatglKREDLFITSK---VWN------NHLTYDETIAAFNESLAKLDLDYLD 110
Cdd:cd19102 39 GINWIDTAAVYGlghSEEVVGRALKG-------LRDRPIVATKcglLWDeegrirRSLKPASIRAECEASLRRLGVDVID 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 111 LYLIHWP-GQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKI 189
Cdd:cd19102 112 LYQIHWPdPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIASLQPPYSLLRRGIEAEILPFCAEHGIGV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 190 QAWSPLMQG-----------------------------QLLKNEVILD----IAKKHNKSAAQVILRWDIQQDillNVKS 236
Cdd:cd19102 192 IVYSPMQSGlltgkmtpervaslpaddwrrrspffqepNLARNLALVDalrpIAERHGRTVAQLAIAWVLRRP---EVTS 268
|
250 260 270
....*....|....*....|....*....|...
gi 499795780 237 V-----HTDRMISNASVFDFELDDEDMDRINML 264
Cdd:cd19102 269 AivgarRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
17-224 |
4.92e-16 |
|
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: 75.72 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 17 IPGLGLGVFQI----------PEDQTAEVVKNGIINGYRLIDTAAIYG---NEKGtgigIKEGLKATGlkrEDLFITSKV 83
Cdd:cd19088 1 VSRLGYGAMRLtgpgiwgppaDREEAIAVLRRALELGVNFIDTADSYGpdvNERL----IAEALHPYP---DDVVIATKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 ---------WNNHLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLER 153
Cdd:cd19088 74 glvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKvPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499795780 154 LKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIqAWSPLMQGQLLKNEVILD-IAKKHNKSAAQVILRW 224
Cdd:cd19088 154 ARAIVRIVSVQNRYNLANRDDEGVLDYCEAAGIAFI-PWFPLGGGDLAQPGGLLAeVAARLGATPAQVALAW 224
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
26-247 |
9.92e-16 |
|
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: 74.91 E-value: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 26 QIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIgIKEGLKatGLKREDLFITSKV-WNNHLTYDETIAAFNESLAKL 104
Cdd:cd19096 17 SIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEI-LGEALK--EGPREKFYLATKLpPWSVKSAEDFRRILEESLKRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 105 DLDYLDLYLIHWPGQDAFEES------WKALETLYAEGKIKAIGVSnfeIHhlERLKTFAKVV---PV-INQIELH---- 170
Cdd:cd19096 94 GVDYIDFYLLHGLNSPEWLEKarkgglLEFLEKAKKEGLIRHIGFS---FH--DSPELLKEILdsyDFdFVQLQYNyldq 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499795780 171 PKLAQKELREYAANMDMKIQAWSPLMQGQLLKN-EVILDIAKKHNKSAAQVILRWdiqqdiLLNVKSVHTdrMISNAS 247
Cdd:cd19096 169 ENQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNpPEALAILCGAPLSPAEWALRF------LLSHPEVTT--VLSGMS 238
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
43-261 |
1.13e-15 |
|
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: 75.39 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 43 GYRLIDTAAIYGN---EKGTGIGIKEglkatglKREDLFITSK---VWNNHLT--------YD-------ETIA-AFNES 100
Cdd:cd19149 46 GINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVLATKcglRWDREGGsfffvrdgVTvyknlspESIReEVEQS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 101 LAKLDLDYLDLYLIHWP-GQDAFEESWKALETLYAEGKIKAIGVSNFEIhhlERLKTFAKVVPV-INQIE---LHPKLaQ 175
Cdd:cd19149 119 LKRLGTDYIDLYQTHWQdVETPIEETMEALEELKRQGKIRAIGASNVSV---EQIKEYVKAGQLdIIQEKysmLDRGI-E 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 176 KELREYAANMDMKIQAWSPLMQGQL--------------LKN-----------------EVILDIAKKHNKSAAQVILRW 224
Cdd:cd19149 195 KELLPYCKKNNIAFQAYSPLEQGLLtgkitpdrefdagdARSgipwfspenrekvlallEKWKPLCEKYGCTLAQLVIAW 274
|
250 260 270
....*....|....*....|....*....|....*....
gi 499795780 225 DIQQDILLNVKSVHTDR--MISNASVFDFELDDEDMDRI 261
Cdd:cd19149 275 TLAQPGITSALCGARKPeqAEENAKAGDIRLSAEDIATM 313
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
12-262 |
1.25e-14 |
|
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: 72.25 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLG--VF--QIPEDQTAEVVKNGIINGYRLIDTAAIY-----GNEKG---TGIGikEGLKATGlKREDLFI 79
Cdd:cd19081 4 RTGLSVSPLCLGtmVFgwTADEETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGeseTIIG--RWLKSRG-KRDRVVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 80 TSKV----WNNH--LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNF------ 146
Cdd:cd19081 81 ATKVgfpmGPNGpgLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATpLEETLGALNDLIRQGKVRYIGASNYsawrlq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 147 EIHHLERLKTFAKVVPVinQIE---LHPKLAQKELREYAANMDMKIQAWSPLMQGQL----------------------L 201
Cdd:cd19081 161 EALELSRQHGLPRYVSL--QPEynlVDRESFEGELLPLCREEGIGVIPYSPLAGGFLtgkyrseadlpgstrrgeaakrY 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499795780 202 KNE-------VILDIAKKHNKSAAQVILRWDIQQD----ILLNVKSVhtDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19081 239 LNErglrildALDEVAAEHGATPAQVALAWLLARPgvtaPIAGARTV--EQLEDLLAAAGLRLTDEEVARLD 308
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-269 |
2.44e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 72.16 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLGVFQIP---EDQTAEVVKNGIINGYRLIDTAAIYGN-EKGTGIGIKEglkatglKREDLFITSKVWNNH 87
Cdd:COG1453 8 KTGLEVSVLGFGGMRLPrkdEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVILATKLPPWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 88 LTYDETIAAFNESLAKLDLDYLDLYLIHWPG-QDAFEES------WKALETLYAEGKIKAIGVSNfeiHHleRLKTFAKV 160
Cdd:COG1453 81 RDPEDMRKDLEESLKRLQTDYIDLYLIHGLNtEEDLEKVlkpggaLEALEKAKAEGKIRHIGFST---HG--SLEVIKEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 161 V-----PVInQIELHP----KLAQKELREYAANMDMKIQAWSPLMQGQLLK-NEVILDIAKKhNKSAAQVILRWdiqqdi 230
Cdd:COG1453 156 IdtgdfDFV-QLQYNYldqdNQAGEEALEAAAEKGIGVIIMKPLKGGRLANpPEKLVELLCP-PLSPAEWALRF------ 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499795780 231 LLNVKSVHT--------DRMISNASVFD-FE-LDDEDMDRINMLNEDLR 269
Cdd:COG1453 228 LLSHPEVTTvlsgmstpEQLDENLKTADnLEpLTEEELAILERLAEELG 276
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
19-256 |
2.98e-14 |
|
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: 71.05 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 19 GLGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGN-EKGTGIGIKEglkatgLKREDLFITSKV-----WNNHLTYDE 92
Cdd:cd19090 9 GLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeDTADYSADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 93 TIAAFNESLAKLDLDYLDLYLIH---WPGQD-------AFEeswkALETLYAEGKIKAIGVSNFEIHHLERLKTFAK--V 160
Cdd:cd19090 83 VRRSVEESLERLGRDRIDLLMIHdpeRVPWVdilapggALE----ALLELKEEGLIKHIGLGGGPPDLLRRAIETGDfdV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 161 VPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLKNEV--------------------ILDIAKKHNKSAAQV 220
Cdd:cd19090 159 VLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPervrytyrwlspelldrakrLYELCDEHGVPLPAL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499795780 221 ILRWdiqqdiLLNVKSVHT--------DRMISNASVFDFELDDE 256
Cdd:cd19090 239 ALRF------LLRDPRISTvlvgasspEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
42-224 |
3.28e-14 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 71.05 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 42 NGYRLIDTAAIYGN---EKGTGigikeglkATGLKREDLFITSKV---WNNHLTYDETIAAFNESLAKLDLDYLDLYLIH 115
Cdd:cd19075 32 RGHTEIDTARVYPDgtsEELLG--------ELGLGERGFKIDTKAnpgVGGGLSPENVRKQLETSLKRLKVDKVDVFYLH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 116 WPgqDA---FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAK----VVPVINQ-----------IELHPKlaqke 177
Cdd:cd19075 104 AP--DRstpLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVYQgmynaitrqveTELFPC----- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 178 LREYaanmDMKIQAWSPL-------------------------MQGQLLKN-----------EVILDIAKKHNKSAAQVI 221
Cdd:cd19075 177 LRKL----GIRFYAYSPLaggfltgkykysedkagggrfdpnnALGKLYRDrywkpsyfealEKVEEAAEKEGISLAEAA 252
|
...
gi 499795780 222 LRW 224
Cdd:cd19075 253 LRW 255
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-264 |
4.63e-14 |
|
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: 70.91 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 29 EDQTAEVVKNGIINGYRLIDTAAIYG---NEKGTGIGIKEglkatgLKREDLFITSKVWNNHLTYDETI--------AAF 97
Cdd:cd19083 32 EEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKE------YNRNEVVIATKGAHKFGGDGSVLnnspeflrSAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 98 NESLAKLDLDYLDLYLIHWP-GQDAFEESWKALETLYAEGKIKAIGVSNFEihhLERLKTFAK---VVPVINQIELHPKL 173
Cdd:cd19083 106 EKSLKRLNTDYIDLYYIHFPdGETPKAEAVGALQELKDEGKIRAIGVSNFS---LEQLKEANKdgyVDVLQGEYNLLQRE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 174 AQKELREYAANMDMKIQAWSPLMQGQL--------------LKNEVIL-----------------DIAKKHNKSAAQVIL 222
Cdd:cd19083 183 AEEDILPYCVENNISFIPYFPLASGLLagkytkdtkfpdndLRNDKPLfkgerfsenldkvdklkSIADEKGVTVAHLAL 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499795780 223 RWDIQQDILLNV--KSVHTDRMISNASVFDFELDDEDMDRINML 264
Cdd:cd19083 263 AWYLTRPAIDVVipGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-262 |
6.71e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 70.32 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 42 NGYRLIDTAAIYGN-EKGTGIGIKEgLKATGLKREDLFITSKvW-----NNHLTYDETIAAFNESLAKLDLDYLDLYLIH 115
Cdd:cd19101 35 AGLTTFDCADIYGPaEELIGEFRKR-LRRERDAADDVQIHTK-WvpdpgELTMTRAYVEAAIDRSLKRLGVDRLDLVQFH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 116 W--PGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLkTFAKVVPVINQIE--LHPKLAQKELREYAANMDMKIQA 191
Cdd:cd19101 113 WwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREI-LDAGVPIVSNQVQysLLDRRPENGMAALCEDHGIKLLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 192 WSPLMQG--------------------QLLKNEVILD-----------------IAKKHNKSAAQVILRWDIQQDillNV 234
Cdd:cd19101 192 YGTLAGGllsekylgvpeptgpaletrSLQKYKLMIDewggwdlfqellrtlkaIADKHGVSIANVAVRWVLDQP---GV 268
|
250 260 270
....*....|....*....|....*....|...
gi 499795780 235 KSV-----HTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19101 269 AGVivgarNSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
29-262 |
2.69e-13 |
|
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: 68.49 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 29 EDQTAEVVKNGIINGYRLIDTAAIYGNEKGTGIgIKEGLKATGlKREDLFITSKV---WNNHLTY--DETIAAFNE---- 99
Cdd:cd19148 24 EKEAIETIHKALDLGINLIDTAPVYGFGLSEEI-VGKALKEYG-KRDRVVIATKVgleWDEGGEVvrNSSPARIRKeved 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 100 SLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIhhlERLKTFAKVVPV-INQ--IELHPKLAQ 175
Cdd:cd19148 102 SLRRLQTDYIDLYQVHWPDPLVpIEETAEALKELLDEGKIRAIGVSNFSP---EQMETFRKVAPLhTVQppYNLFEREIE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 176 KELREYAANMDMKIQAWSPLMQGQL--------------LKN-----------------EVILDIAKKH-NKSAAQVILR 223
Cdd:cd19148 179 KDVLPYARKHNIVTLAYGALCRGLLsgkmtkdtkfegddLRRtdpkfqeprfsqylaavEELDKLAQERyGKSVIHLAVR 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499795780 224 WDIQQDILlnvkSV------HTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19148 259 WLLDQPGV----SIalwgarKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-202 |
1.51e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 65.58 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLG---VFQIPEDQTAEVVKNGIINGYRLIDTAAIYGN-EKGTGIGIKEglkatglKREDLFITSKVWNNhlT 89
Cdd:cd19100 8 GLKVSRLGFGggpLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATKTGAR--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 90 YDETIAAFNESLAKLDLDYLDLYLIH------WPGQDAFE-ESWKALETLYAEGKIKAIGVSNfeiHHLERLKTFAK--- 159
Cdd:cd19100 79 YEGAKRDLERSLKRLGTDYIDLYQLHavdteeDLDQVFGPgGALEALLEAKEEGKIRFIGISG---HSPEVLLRALEtge 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499795780 160 ---VVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQLLK 202
Cdd:cd19100 156 fdvVLFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLS 201
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
12-262 |
1.65e-12 |
|
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: 66.45 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLG----------VFQIPEDQTAEVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKEGLKatglkREDLF 78
Cdd:cd19079 7 NSGLKVSRLCLGcmsfgdpkwrPWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFAP-----RDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 79 ITSKVWNN--------HLTYDETIAAFNESLAKLDLDYLDLYLIHWPgqDA---FEESWKALETLYAEGKIKAIGVSNF- 146
Cdd:cd19079 82 IATKVYFPmgdgpngrGLSRKHIMAEVDASLKRLGTDYIDLYQIHRW--DYetpIEETLEALHDVVKSGKVRYIGASSMy 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 147 -----EIHHLERLKTFAKVVPVINQIELhpkLAQKELRE---YAANMDMKIQAWSPLMQGQLL----------------- 201
Cdd:cd19079 160 awqfaKALHLAEKNGWTKFVSMQNHYNL---LYREEEREmipLCEEEGIGVIPWSPLARGRLArpwgdtterrrsttdta 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 202 ---------KNEVILD----IAKKHNKSAAQVILRWdiqqdiLLNVKSVH--------TDRMISNASVFDFELDDEDMDR 260
Cdd:cd19079 237 klkydyfteADKEIVDrveeVAKERGVSMAQVALAW------LLSKPGVTapivgatkLEHLEDAVAALDIKLSEEEIKY 310
|
..
gi 499795780 261 IN 262
Cdd:cd19079 311 LE 312
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-262 |
2.23e-12 |
|
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: 66.10 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLG-------------VFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNekgtgiGIKEGL--KATGLKRED 76
Cdd:cd19091 8 RSGLKVSELALGtmtfgggggffgaWGGVDQEEADRLVDIALDAGINFFDTADVYSE------GESEEIlgKALKGRRDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 77 LFITSKVWN------NH--LTYDETIAAFNESLAKLDLDYLDLYLIH-WPGQDAFEESWKALETLYAEGKIKAIGVSNF- 146
Cdd:cd19091 82 VLIATKVRGrmgegpNDvgLSRHHIIRAVEASLKRLGTDYIDLYQLHgFDALTPLEETLRALDDLVRQGKVRYIGVSNFs 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 147 -----------EIHHLERlktfakvvPVINQieLHPKLA----QKELREYAANMDMKIQAWSPLMQGQL----------- 200
Cdd:cd19091 162 awqimkalgisERRGLAR--------FVALQ--AYYSLLgrdlEHELMPLALDQGVGLLVWSPLAGGLLsgkyrrgqpap 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 201 ----LKN-----------------EVILDIAKKHNKSAAQVILRWDIQQD----ILLNVKSVHtdRMISNASVFDFELDD 255
Cdd:cd19091 232 egsrLRRtgfdfppvdrergydvvDALREIAKETGATPAQVALAWLLSRPtvssVIIGARNEE--QLEDNLGAAGLSLTP 309
|
....*..
gi 499795780 256 EDMDRIN 262
Cdd:cd19091 310 EEIARLD 316
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
19-262 |
1.15e-11 |
|
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: 63.80 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 19 GLGL-----GVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTG--IGIKEGLKATGLKREDLFITSKV-WNNH-LT 89
Cdd:cd19077 9 GLGLmgltwRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKGgLDPDtLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 90 YDETIAAFNESLAKLDLDYLDLYLIhwpgqDAF-----------EESWKALETLYAEGKIKAIGVSnfEIHHlERLKTFA 158
Cdd:cd19077 89 PDGSPEAVRKSIENILRALGGTKKI-----DIFeparvdpnvpiEETIKALKELVKEGKIRGIGLS--EVSA-ETIRRAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 159 KVVPV-INQIELHP---KLAQKELREYAANMDMKIQAWSPLMQGQL---LKN---------------------------- 203
Cdd:cd19077 161 AVHPIaAVEVEYSLfsrEIEENGVLETCAELGIPIIAYSPLGRGLLtgrIKSladipegdfrrhldrfngenfeknlklv 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499795780 204 EVILDIAKKHNKSAAQVILRWDIQQ---DILLNVKSVHTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19077 241 DALQELAEKKGCTPAQLALAWILAQsgpKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-144 |
2.21e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 62.22 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLGVFQIPEDQtAEVVKNGIINGYRLIDTAAIYGNEKGTGIgIKEGLKatGLKREDLFITSKVWN--NHLT 89
Cdd:cd19105 8 KTGLKVSRLGFGGGGLPRES-PELLRRALDLGINYFDTAEGYGNGNSEEI-IGEALK--GLRRDKVFLATKASPrlDKKD 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499795780 90 YDETIAAFNESLAKLDLDYLDLYLIHWPGQDA----FEESWKALETLYAEGKIKAIGVS 144
Cdd:cd19105 84 KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEerllNEELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
18-239 |
2.62e-11 |
|
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: 62.25 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 18 PGLGLGVFQI-------PEDQTAEVVKNGIINGYRLIDTAAIYGN-EKGTGIGIKeglkatGLKREDLFITSKVW----- 84
Cdd:cd19095 1 SVLGLGTSGIgrvwgvpSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGthgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 85 ---NNHLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAF-EESWKALETLYAEGKIKAIGVSNFEIHHLERLKTfaKV 160
Cdd:cd19095 75 grdRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELtGEVLETLEDLKAAGKVRYIGVSGDGEELEAAIAS--GV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 161 VPVInQIELHP-KLAQKELREYAANMDMKIQAWSPLMQGQLLKNEVILDIAKKHNK-----------SAAQVILRWdiqq 228
Cdd:cd19095 153 FDVV-QLPYNVlDREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARrpefaaeiggaTWAQAALRF---- 227
|
250
....*....|.
gi 499795780 229 diLLNVKSVHT 239
Cdd:cd19095 228 --VLSHPGVSS 236
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
12-261 |
1.90e-10 |
|
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: 60.53 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLGVFQI--------PEDQTAEVVKNGIINGYRLIDTAAIYG-NEKGTGIGIKeglKATGlKREDLFITSK 82
Cdd:cd19144 8 RNGPSVPALGFGAMGLsafygppkPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFK---QNPG-KREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 83 VWNNHLTYDETIAAFNE----------SLAKLDLDYLDLYLIH-WPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHL 151
Cdd:cd19144 84 FGIEKNVETGEYSVDGSpeyvkkacetSLKRLGVDYIDLYYQHrVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 152 ERLktfAKVVPVIN-QIELHP-----KLAQKELREYAANMDMKIQAWSPLMQGQLL------------------------ 201
Cdd:cd19144 164 RRA---HAVHPIAAvQIEYSPfsldiERPEIGVLDTCRELGVAIVAYSPLGRGFLTgairspddfeegdfrrmaprfqae 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499795780 202 ---KN----EVILDIAKKHNKSAAQVILRWDIQQ--DILLNVKSVHTDRMISNASVFDFELDDEDMDRI 261
Cdd:cd19144 241 nfpKNlelvDKIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
20-200 |
6.53e-10 |
|
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: 57.87 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 20 LGLGVFQI-------PEDQTA-EVVKNGIINGYRLIDTAAIYGNekgtgiGIKEGL--KATGLKREDLFITSKV------ 83
Cdd:cd19086 6 IGFGTWGLggdwwgdVDDAEAiRALRAALDLGINFFDTADVYGD------GHSERLlgKALKGRRDKVVIATKFgnrfdg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 ---WNNHLTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAF--EESWKALETLYAEGKIKAIGVSnfeIHHLERLKTFA 158
Cdd:cd19086 80 gpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLdnDELFEALEKLKQEGKIRAYGVS---VGDPEEALAAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499795780 159 K-----VVPVI-NQIELHPklaQKELREYAANMDMKIQAWSPLMQGQL 200
Cdd:cd19086 157 RrggidVVQVIyNLLDQRP---EEELFPLAEEHGVGVIARVPLASGLL 201
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-229 |
1.48e-09 |
|
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: 57.34 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 42 NGYRLIDTAAIYGNEKGTGIG------IKEGLKATGlKREDLFITSKVWNNHLTYDETIAAFnESLAKLDLDYLDLYLIH 115
Cdd:cd19752 29 AGGNFLDTANNYAFWTEGGVGgeserlIGRWLKDRG-NRDDVVIATKVGAGPRDPDGGPESP-EGLSAETIEQEIDKSLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 116 WPGQD--------------AFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKV--VPVINQIE-----LHPK-- 172
Cdd:cd19752 107 RLGTDyidlyyahvddrdtPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQqgWAEFSAIQqrhsyLRPRpg 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 173 -------LAQKELREYAA-NMDMKIQAWSPLMQGQLLKNE-----------------VILDIAKKHNKSAAQVILRWDIQ 227
Cdd:cd19752 187 adfgvqrIVTDELLDYASsRPDLTLLAYSPLLSGAYTRPDrplpeqydgpdsdarlaVLEEVAGELGATPNQVVLAWLLH 266
|
..
gi 499795780 228 QD 229
Cdd:cd19752 267 RT 268
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
12-261 |
1.93e-09 |
|
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: 57.23 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLGVF-------QIPEDQTAEVVKNGIINGYRLIDTAAIYG---NEKGTGIGIKEGlkatglkREDLFITS 81
Cdd:cd19076 7 TQGLEVSALGLGCMgmsafygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 82 KvWNNHLTYDETIAAFN-----------ESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIH 149
Cdd:cd19076 80 K-FGIVRDPGSGFRGVDgrpeyvraaceASLKRLGTDVIDLYYQHRVDPNVpIEETVGAMAELVEEGKVRYIGLSEASAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 150 HLERLktfAKVVPVIN-QIE--LHPKLAQKELREYAANMDMKIQAWSPL--------------------------MQGQ- 199
Cdd:cd19076 159 TIRRA---HAVHPITAvQSEysLWTRDIEDEVLPTCRELGIGFVAYSPLgrgfltgaikspedlpeddfrrnnprFQGEn 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 200 LLKNEVILD----IAKKHNKSAAQVILRWDIQQ--DILL--NVKSVHtdRMISNASVFDFELDDEDMDRI 261
Cdd:cd19076 236 FDKNLKLVEkleaIAAEKGCTPAQLALAWVLAQgdDIVPipGTKRIK--YLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
42-200 |
3.91e-09 |
|
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: 56.43 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 42 NGYRLIDTAAIYGN---EKGTGIGIKEglkatglKREDLFITSKV------WNNH--LTYDETIAAFNESLAKLDLDYLD 110
Cdd:cd19087 42 AGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKVfgpmgdDPNDrgLSRRHIRRAVEASLRRLQTDYID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 111 LYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNF------------EIHHLERlktFAKVVPVIN----QIELhpkl 173
Cdd:cd19087 115 LYQMHHFDRDTpLEETLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaARRGLLR---FVSEQPMYNllkrQAEL---- 187
|
170 180
....*....|....*....|....*..
gi 499795780 174 aqkELREYAANMDMKIQAWSPLMQGQL 200
Cdd:cd19087 188 ---EILPAARAYGLGVIPYSPLAGGLL 211
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-224 |
4.75e-09 |
|
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: 56.17 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 20 LGLGVFQIPEDQT-----AEVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKEGLKATGLKREDLFITSKVwnNHLTYD 91
Cdd:cd19099 6 LGLGTYRGDSDDEtdeeyREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKA--GYIPGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 92 -ETIAAFNESLAKLDLDYLDLYL----------------------------------IHWP-------GQDAF----EES 125
Cdd:cd19099 84 gDEPLRPLKYLEEKLGRGLIDVAdsaglrhcispayledqierslkrlgldtidlylLHNPeeqllelGEEEFydrlEEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 126 WKALETLYAEGKIKAIGVS----------NFEIHHLERLKTFAKVV-------PVI----NQIEL----HPKLAQKELR- 179
Cdd:cd19099 164 FEALEEAVAEGKIRYYGIStwdgfrappaLPGHLSLEKLVAAAEEVggdnhhfKVIqlplNLLEPealtEKNTVKGEALs 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499795780 180 --EYAANMDMKIQAWSPLMQGQLLK-NEVILDIAKKHNKSAAQVILRW 224
Cdd:cd19099 244 llEAAKELGLGVIASRPLNQGQLLGeLRLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
42-229 |
5.43e-09 |
|
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: 55.64 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 42 NGYRLIDTAAIYGNEKGTG-----IGikEGLKATGlKREDLFITSK--------VWNNHLTYDETIAAFNESLAKLDLDY 108
Cdd:cd19082 29 LGGNFIDTARVYGDWVERGaservIG--EWLKSRG-NRDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 109 LDLYLIHW--PGQDAfEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVV----PVINQIELhpKLAQ------- 175
Cdd:cd19082 106 IDLYFLHRddPSVPV-GEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHglpgFAASSPQW--SLARpneppwp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 176 --------KELREYAANMDMKIQAWSPLMQG-------------QLLKN-----------EVILDIAKKHNKSAAQVILR 223
Cdd:cd19082 183 gptlvamdEEMRAWHEENQLPVFAYSSQARGffskraaggaeddSELRRvyyseenferlERAKELAEEKGVSPTQIALA 262
|
....*.
gi 499795780 224 WDIQQD 229
Cdd:cd19082 263 YVLNQP 268
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
14-256 |
2.04e-08 |
|
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: 54.13 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 14 GTKIPGLGLG---VF--QIPEDQTAEVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKeglkatGLKREDLFITSKV-- 83
Cdd:cd19074 1 GLKVSELSLGtwlTFggQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK------GWPRESYVISTKVfw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 ----WNNH--LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKT 156
Cdd:cd19074 75 ptgpGPNDrgLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETpLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 157 FAK----VVPVINQIELHpKLAQK---ELREYAANMDMKIQAWSPLMQG----------------------------QLL 201
Cdd:cd19074 155 LARqfglIPPVVEQPQYN-MLWREieeEVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrRLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499795780 202 KNEVI------LDIAKKHNKSAAQVILRWDIQQDillNVKSV-----HTDRMISNASVFDFELDDE 256
Cdd:cd19074 234 TDENLekvkklKPIADELGLTLAQLALAWCLRNP---AVSSAiigasRPEQLEENVKASGVKLSPE 296
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
12-154 |
6.30e-08 |
|
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: 52.54 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLG------VFQIPEDQT--AEVVKNGIINGYRLIDTAAIYGNEKGTGIgIKEGLKATGLKREDLFITSKV 83
Cdd:cd19153 7 IALGNVSPVGLGtaalggVYGDGLEQDeaVAIVAEAFAAGINHFDTSPYYGAESSEAV-LGKALAALQVPRSSYTVATKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 W----NNHLTYDETIAA-FNESLAKLDLDYLDLYLIH---WPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIHHLERL 154
Cdd:cd19153 86 GryrdSEFDYSAERVRAsVATSLERLHTTYLDVVYLHdieFVDYDTlVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRA 165
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
20-143 |
1.36e-07 |
|
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: 51.84 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 20 LGLGVFQIPEDQTAEVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKEglkatgLKREDLFITSKV------------- 83
Cdd:cd19152 10 LGNLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE------LGREDYVISTKVgrllvplqevept 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 -----WNNH-------LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDAFEESWK------------ALETLYAEGKIK 139
Cdd:cd19152 84 fepgfWNPLpfdavfdYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafrALEELREEGVIK 163
|
....
gi 499795780 140 AIGV 143
Cdd:cd19152 164 AIGL 167
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
42-262 |
1.62e-07 |
|
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: 51.41 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 42 NGYRLIDTAAIY-----GNEKG-TGIGIKEGLKATGlKREDLFITSKV--------WNNH----LTYDETIAAFNESLAK 103
Cdd:cd19094 30 EGVNFIDTAEMYpvppsPETQGrTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRGggtrLDRENIREAVEGSLKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 104 LDLDYLDLYLIHWP-------------------GQDAFEESWKALETLYAEGKIKAIGVSN------FEIHHLERLKTFA 158
Cdd:cd19094 109 LGTDYIDLYQLHWPdrytplfgggyytepseeeDSVSFEEQLEALGELVKAGKIRHIGLSNetpwgvMKFLELAEQLGLP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 159 KVVPVINQIELhpkLAQK---ELREYAANMDMKIQAWSPLMQGQL----LKNE--------------------------- 204
Cdd:cd19094 189 RIVSIQNPYSL---LNRNfeeGLAEACHRENVGLLAYSPLAGGVLtgkyLDGAarpeggrlnlfpgymaryrspqaleav 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499795780 205 -VILDIAKKHNKSAAQVILRWDIQQDIllnVKSV---HTD----RMISNAsvFDFELDDEDMDRIN 262
Cdd:cd19094 266 aEYVKLARKHGLSPAQLALAWVRSRPF---VTSTiigATTleqlKENIDA--FDVPLSDELLAEID 326
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
18-144 |
2.12e-07 |
|
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: 51.21 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 18 PGLGLG------VFQIPEDQTAEVVKNGIINGYRLIDTAAIYG---NEKGTGIGIKeglkatGLKREDLFITSKV----- 83
Cdd:cd19162 1 PRLGLGaaslgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA------RHPRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499795780 84 -------------WNnhLTYDETIAAFNESLAKLDLDYLDLYLIHWPG---QDAFEESWKALETLYAEGKIKAIGVS 144
Cdd:cd19162 75 pgaagrpagadrrFD--FSADGIRRSIEASLERLGLDRLDLVFLHDPDrhlLQALTDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-223 |
8.62e-07 |
|
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: 49.06 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 26 QIPEDQTAEVVKNGIINGYRLIDTAAIYGN-EKGTGIGIKeglkatglKREDLFITSKV----WNNHLTYDETIAAFNES 100
Cdd:cd19097 22 KPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLK--------RLDKFKIITKLpplkEDKKEDEAAIEASVEAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 101 LAKLDLDYLDLYLIHWPGQ--DAFEESWKALETLYAEGKIKAIGVSnfeIHHLERLKTFAKVVPV-INQIELHP---KLA 174
Cdd:cd19097 94 LKRLKVDSLDGLLLHNPDDllKHGGKLVEALLELKKEGLIRKIGVS---VYSPEELEKALESFKIdIIQLPFNIldqRFL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499795780 175 QKELREYAANMDMKIQAWSPLMQGQLLKNEVIL---------------DIAKKHNKSAAQVILR 223
Cdd:cd19097 171 KSGLLAKLKKKGIEIHARSVFLQGLLLMEPDKLpakfapakpllkklhELAKKLGLSPLELALG 234
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-195 |
8.81e-06 |
|
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: 46.30 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 13 NGTKIPGLGLGVFQ-----IPEDQTAEVVKNGIINGYRLIDTAAIYGNEKG-TGIGikEGLKATGLKREDLFITSKV-WN 85
Cdd:cd19142 9 SGLRVSNVGLGTWStfstaISEEQAEEIVTLAYENGINYFDTSDAFTSGQAeTELG--RILKKKGWKRSSYIVSTKIyWS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 86 NH-----LTYDETIAAFNESLAKLDLDYLDLYLIHwpGQDA---FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTF 157
Cdd:cd19142 87 YGseergLSRKHIIESVRASLRRLQLDYIDIVIIH--KADPmcpMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499795780 158 AK----VVPVINQIELHPKLAQK-ELreYAANMDMKI----QAWSPL 195
Cdd:cd19142 165 ARqfncPTPICEQSEYHMFCREKmEL--YMPELYNKVgvglITWSPL 209
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
113-262 |
4.83e-05 |
|
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: 44.13 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 113 LIH-WPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKV----VPVINQIELHpkLAQKEL-REY---AA 183
Cdd:cd19080 119 YVHaWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELrgwsPFVALQIEYS--LLERTPeRELlpmAR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 184 NMDMKIQAWSPLMQGQLL--------------------------KNEVILD----IAKKHNKSAAQVILRWDIQQDILLN 233
Cdd:cd19080 197 ALGLGVTPWSPLGGGLLTgkyqrgeegrageakgvtvgfgklteRNWAIVDvvaaVAEELGRSAAQVALAWVRQKPGVVI 276
|
170 180 190
....*....|....*....|....*....|.
gi 499795780 234 --VKSVHTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19080 277 piIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
21-169 |
5.15e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 43.80 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 21 GLGVFQIPEDQTA--EVVKNGIINGYRLIDTAAIYGNEKGTGIgIKEGLKATglkREDLFITSKV---------WNNHLT 89
Cdd:PRK10376 29 GPGVFGPPKDRDAaiAVLREAVALGVNHIDTSDFYGPHVTNQL-IREALHPY---PDDLTIVTKVgarrgedgsWLPAFS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 90 YDETIAAFNESL------AKLDLDYLDLYLIHWPGQDAFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAKVVPV 163
Cdd:PRK10376 105 PAELRRAVHDNLrnlgldVLDVVNLRLMGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCV 184
|
....*.
gi 499795780 164 INQIEL 169
Cdd:PRK10376 185 QNHYNL 190
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
12-161 |
5.56e-05 |
|
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: 43.69 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLG------VF-QIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKG-TGIGikeglKA-TGLKREDLFITSK 82
Cdd:cd19163 8 KTGLKVSKLGFGasplggVFgPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSeTVLG-----KAlKGIPRDSYYLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 83 V------WNNHL--TYDETIAAFNESLAKLDLDYLDLYLIH----WPGQD-AFEESWKALETLYAEGKIKAIGVSNFEih 149
Cdd:cd19163 83 VgrygldPDKMFdfSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDqILNETLPALQKLKEEGKVRFIGITGYP-- 160
|
170
....*....|..
gi 499795780 150 hlerLKTFAKVV 161
Cdd:cd19163 161 ----LDVLKEVL 168
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
20-261 |
7.18e-05 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 43.69 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 20 LGLGVFQIPEdQTAEV-----VKNGIINGYRLIDTAAIYG-----NEKG-TGIGIKEGLKATGlKREDLFITSKVWNNHL 88
Cdd:PRK10625 16 LGLGTMTFGE-QNSEAdahaqLDYAVAQGINLIDVAEMYPvpprpETQGlTETYIGNWLAKRG-SREKLIIASKVSGPSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 89 TYDETI------------AAFNESLAKLDLDYLDLYLIHWP-------GQDAFEESWKA-----LETLYA------EGKI 138
Cdd:PRK10625 94 NNDKGIrpnqaldrknirEALHDSLKRLQTDYLDLYQVHWPqrptncfGKLGYSWTDSApavslLETLDAlaeqqrAGKI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 139 KAIGVSN------FEIHHLERLKTFAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQL------------ 200
Cdd:PRK10625 174 RYIGVSNetafgvMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLtgkylngakpag 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 201 LKNEVI------------------LDIAKKHNKSAAQVILRWDIQQ----DILLNVKSVhtDRMISNASVFDFELDDEDM 258
Cdd:PRK10625 254 ARNTLFsrftrysgeqtqkavaayVDIAKRHGLDPAQMALAFVRRQpfvaSTLLGATTM--EQLKTNIESLHLTLSEEVL 331
|
...
gi 499795780 259 DRI 261
Cdd:PRK10625 332 AEI 334
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
20-262 |
1.04e-04 |
|
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: 42.99 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 20 LGLGVF-------QIPEDQTA-EVVKNGIINGYRLIDTAAIYG---NEKGTGigikEGLKAtglKREDLFITSKV----- 83
Cdd:cd19078 7 IGLGCMgmshgygPPPDKEEMiELIRKAVELGITFFDTAEVYGpytNEELVG----EALKP---FRDQVVIATKFgfkid 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 84 --WNNHLTYD---ETI-AAFNESLAKLDLDYLDLYLIHWPGQD-AFEESWKALETLYAEGKIKAIGVSNFEIHHLERLKT 156
Cdd:cd19078 80 ggKPGPLGLDsrpEHIrKAVEGSLKRLQTDYIDLYYQHRVDPNvPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 157 FAKVVPVINQIELHPKLAQKELREYAANMDMKIQAWSPLMQGQLL---------------------------KNEVILD- 208
Cdd:cd19078 160 VCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTgkidentkfdegddraslprftpealeANQALVDl 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499795780 209 ---IAKKHNKSAAQVILRWdiqqdiLLNVK--------SVHTDRMISNASVFDFELDDEDMDRIN 262
Cdd:cd19078 240 lkeFAEEKGATPAQIALAW------LLAKKpwivpipgTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-261 |
4.05e-04 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 41.17 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 21 GLGVF--QIPEDQTAEVVKNGIINGYRLIDTAAIYG---NEKGTGIGIKEglkatgLKREDLFITSKVWNN--HLTYDET 93
Cdd:cd19103 21 GDQVFgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR------YPREDYIISTKFTPQiaGQSADPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 94 IAAFNESLAKLDLDYLDLYLIHWPgQDAfeESW-KALETLYAEGKIKAIGVSNFEIHHLERLKTF-----AKVVPVINQI 167
Cdd:cd19103 95 ADMLEGSLARLGTDYIDIYWIHNP-ADV--ERWtPELIPLLKSGKVKHVGVSNHNLAEIKRANEIlakagVSLSAVQNHY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 168 EL-HPKLAQKELREYAANMDMKIQAWSPLMQGQLLK----------------------------NEVILDIAKKHNKSAA 218
Cdd:cd19103 172 SLlYRSSEEAGILDYCKENGITFFAYMVLEQGALSGkydtkhplpegsgraetynpllpqleelTAVMAEIGAKHGASIA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499795780 219 QVILRWDIQQDIL--LNVKSVHTDRMISNASvfDFELDDEDMDRI 261
Cdd:cd19103 252 QVAIAWAIAKGTTpiIGVTKPHHVEDAARAA--SITLTDDEIKEL 294
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
13-198 |
4.82e-04 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 40.84 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 13 NGTKIPGLGLGVF-----QIPEDQTAEVVKNGIINGYRLIDTAAIYGNEKGTgIGIKEGLKATGLKREDLFITSKV-WNN 86
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAE-VVLGNIIKKKGWRRSSLVITTKIfWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 87 H------LTYDETIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFEIHHLERLKTFAK 159
Cdd:cd19158 88 KaetergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499795780 160 ----VVPVINQIELHpkLAQKE-----LREYAANMDMKIQAWSPLMQG 198
Cdd:cd19158 168 qfnlIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACG 213
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
8-228 |
2.09e-03 |
|
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: 38.95 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 8 RVEL-NNGTKIPGLGLGVF--------QIPEDQTAEVVKNGIINGYRLIDTAAIYG---NEKGTGIGIKEGLkatglkRE 75
Cdd:cd19145 2 RVKLgSQGLEVSAQGLGCMglsgdygaPKPEEEGIALIHHAFNSGVTFLDTSDIYGpntNEVLLGKALKDGP------RE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 76 DLFITSK-----VWNNHLTY----DETIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSN 145
Cdd:cd19145 76 KVQLATKfgiheIGGSGVEVrgdpAYVRAACEASLKRLDVDYIDLYYQHRIDTTVpIEITMGELKKLVEEGKIKYIGLSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 146 FEIHHLERLKTFAKVVPVinQIE--LHPKLAQKELREYAANMDMKIQAWSPLMQG------------------------- 198
Cdd:cd19145 156 ASADTIRRAHAVHPITAV--QLEwsLWTRDIEEEIIPTCRELGIGIVPYSPLGRGffagkakleellensdvrkshprfq 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 499795780 199 --QLLKNEVIL----DIAKKHNKSAAQVILRWDIQQ 228
Cdd:cd19145 234 geNLEKNKVLYerveALAKKKGCTPAQLALAWVLHQ 269
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
20-154 |
2.15e-03 |
|
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: 38.80 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 20 LGLGVF-----QIPEDQ-TAEVVKNGIINGYRLIDTAAIYGN-EKGTGigikEGLKA--TGLKREDLFITSKVwnNHLTY 90
Cdd:cd19164 18 FGAATFsyqytTDPESIpPVDIVRRALELGIRAFDTSPYYGPsEIILG----RALKAlrDEFPRDTYFIITKV--GRYGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 91 DEtiaaFN-----------ESLAKLDLDYLDLYLIHwpgqD----AFEESWKALETLY---AEGKIKAIGVSNFEIHHLE 152
Cdd:cd19164 92 DD----FDyspewirasveRSLRRLHTDYLDLVYLH----DvefvADEEVLEALKELFklkDEGKIRNVGISGYPLPVLL 163
|
..
gi 499795780 153 RL 154
Cdd:cd19164 164 RL 165
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
27-148 |
8.47e-03 |
|
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: 36.92 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 27 IPEDQTAEVVKNGIINGYRLIDTAAIYGN---EKGTGIGIKEglkatgLKREDLFITSKV-----------------WNN 86
Cdd:cd19161 17 VSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE------KPRDEFVLSTKVgrllkparegsvpdpngFVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 87 HL--------TYDETIAAFNESLAKLDLDYLDLYLIH-----WPGQDAFEESW--------KALETLYAEGKIKAI--GV 143
Cdd:cd19161 91 PLpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHdigvyTHGDRKERHHFaqlmsggfKALEELKKAGVIKAFglGV 170
|
....*
gi 499795780 144 SNFEI 148
Cdd:cd19161 171 NEVQI 175
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
12-224 |
9.85e-03 |
|
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: 36.85 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 12 NNGTKIPGLGLGVFQIPEDQTAEVVKNGII-----NGYRLIDTAAIYGNEKGT-----GIGIKEGLKAtglKREDLFITS 81
Cdd:cd19089 6 RSGLHLPAISLGLWHNFGDYTSPEEARELLrtafdLGITHFDLANNYGPPPGSaeenfGRILKRDLRP---YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 82 KV----W---------NNHLtydetIAAFNESLAKLDLDYLDLYLIHWPGQDA-FEESWKALETLYAEGKIKAIGVSNFE 147
Cdd:cd19089 83 KAgygmWpgpygdggsRKYL-----LASLDQSLKRMGLDYVDIFYHHRYDPDTpLEETMTALADAVRSGKALYVGISNYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499795780 148 IHHLERLKTF---AKVVPVINQIE---LHPKlAQKELREYAANMDMKIQAWSPLMQGQL--------------------- 200
Cdd:cd19089 158 GAKARRAIALlreLGVPLIIHQPRyslLDRW-AEDGLLEVLEEAGIGFIAFSPLAQGLLtdkylngippdsrraaeskfl 236
|
250 260 270
....*....|....*....|....*....|....
gi 499795780 201 -------LKNEVIL---DIAKKHNKSAAQVILRW 224
Cdd:cd19089 237 teealtpEKLEQLRklnKIAAKRGQSLAQLALSW 270
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