|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
7-272 |
0e+00 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 524.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 7 VKLANGVEMPRLGFGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYE 86
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 87 STLAAFDESLRKLELDYVDLYLIHWPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHP 166
Cdd:cd19156 81 STLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 167 QLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDF 246
Cdd:cd19156 161 LLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDF 240
|
250 260
....*....|....*....|....*.
gi 16802865 247 ELTEEEVAKISGLNKDERTGPDPDNF 272
Cdd:cd19156 241 ELTAEEIRQIDGLNTDHRYGPDPDNF 266
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-270 |
7.17e-178 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 489.95 E-value: 7.17e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYESTLA 90
Cdd:COG0656 1 NGVEIPALGLGTWQL-PGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 91 AFDESLRKLELDYVDLYLIHWPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQ 170
Cdd:COG0656 80 AFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 171 EPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTE 250
Cdd:COG0656 160 RELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSD 239
|
250 260
....*....|....*....|
gi 16802865 251 EEVAKISGLNKDERTGPDPD 270
Cdd:COG0656 240 EDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-270 |
2.34e-172 |
|
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: 476.11 E-value: 2.34e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGY 85
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 86 ESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELH 165
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 166 PQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFD 245
Cdd:cd19157 161 PRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFD 240
|
250 260
....*....|....*....|....*
gi 16802865 246 FELTEEEVAKISGLNKDERTGPDPD 270
Cdd:cd19157 241 FELSQEDMDKIDALNENLRVGPDPD 265
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
7-260 |
3.56e-156 |
|
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: 434.94 E-value: 3.56e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 7 VKLANGVEMPRLGFGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYE 86
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 87 STLAAFDESLRKLELDYVDLYLIHWPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHP 166
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 167 QLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDF 246
Cdd:cd19126 161 YLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDF 240
|
250
....*....|....
gi 16802865 247 ELTEEEVAKISGLN 260
Cdd:cd19126 241 ELSEDDMTAIDALN 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
6-260 |
5.32e-147 |
|
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: 411.77 E-value: 5.32e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGY 85
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQV-SNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 86 ESTLAAFDESLRKLELDYVDLYLIHWPV--KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIE 163
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPVpaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 164 LHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADI 243
Cdd:cd19131 160 LHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDV 239
|
250
....*....|....*..
gi 16802865 244 FDFELTEEEVAKISGLN 260
Cdd:cd19131 240 FDFELDADDMQAIAGLD 256
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-256 |
3.73e-144 |
|
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: 404.17 E-value: 3.73e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 15 MPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYESTLAAFDE 94
Cdd:cd19071 1 MPLIGLGTYKL-KPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 95 SLRKLELDYVDLYLIHWPVKGK-------FKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHPQ 167
Cdd:cd19071 80 SLKDLGLDYLDLYLIHWPVPGKeggskeaRLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 168 LTQEPLRKFCAENNIVVEAWSPLGNG--KLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFD 245
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGRGrrPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|.
gi 16802865 246 FELTEEEVAKI 256
Cdd:cd19071 240 FELSEEDMAAI 250
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
7-260 |
1.66e-134 |
|
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: 380.00 E-value: 1.66e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 7 VKLANGVEMPRLGFGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYE 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 87 STLAAFDESLRKLELDYVDLYLIHWPVkGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHP 166
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPF-GDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIETHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 167 QLTQEPLRKFCAENNIVVEAWSPLGNGK--LLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIF 244
Cdd:cd19133 160 FNQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIF 239
|
250
....*....|....*.
gi 16802865 245 DFELTEEEVAKISGLN 260
Cdd:cd19133 240 DFELSDEDMEAIAALD 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
7-260 |
1.00e-128 |
|
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: 365.96 E-value: 1.00e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 7 VKLANGVEMPRLGFGVWKVQdGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYE 86
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP-PEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 87 STLAAFDESLRKLELDYVDLYLIHWPVKGKFKDT---WRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIE 163
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRTiqaYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 164 LHPQLTQEPLRKFCAENNIVVEAWSPLG------------NGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKS 231
Cdd:cd19127 160 LHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygasgptgPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKS 239
|
250 260
....*....|....*....|....*....
gi 16802865 232 VHQERIIQNADIFDFELTEEEVAKISGLN 260
Cdd:cd19127 240 VHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
15-259 |
2.38e-120 |
|
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: 344.62 E-value: 2.38e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 15 MPRLGFGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKES----GIKREDLFVTTKLWNAEQGYESTLA 90
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 91 AFDESLRKLELDYVDLYLIHWPVKGKFK-----------DTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMV 159
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKpsdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 160 NQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG--KLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERI 237
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGdlRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 16802865 238 IQNADIFDFELTEEEVAKISGL 259
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 ... |
9-260 |
1.35e-118 |
|
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: 340.02 E-value: 1.35e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 9 LANGVEMPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYEST 88
Cdd:cd19132 1 LNDGTQIPAIGFGTYPL-KGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 89 LAAFDESLRKLELDYVDLYLIHWPV--KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHP 166
Cdd:cd19132 80 LRTIEESLYRLGLDYVDLYLIHWPNpsRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 167 QLTQEPLRKFCAENNIVVEAWSPLGNG-KLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFD 245
Cdd:cd19132 160 YFPQAEQRAYHREHGIVTQSWSPLGRGsGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFD 239
|
250
....*....|....*
gi 16802865 246 FELTEEEVAKISGLN 260
Cdd:cd19132 240 FELSDEDMAAIAALD 254
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
6-265 |
2.52e-115 |
|
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: 333.09 E-value: 2.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQA----IKESGIKREDLFVTTKLWNA 81
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 82 EQGYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFK-----------------DTWRAFEKLYKDKRVRAIGVCNFHEH 144
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENndsesngdgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 145 HLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGKL---------LSNPEIKAIADAHGKSVAQV 215
Cdd:cd19116 162 QINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgqtnppprLDDPTLVAIAKKYGKTTAQI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16802865 216 ILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDERT 265
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-273 |
8.38e-114 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 328.57 E-value: 8.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 1 MNLKDTVKLANGVEMPRLGFGVWKVQDgDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWN 80
Cdd:PRK11565 1 MANPTVIKLQDGNVMPQLGLGVWQASN-EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 81 AEQGyeSTLAAFDESLRKLELDYVDLYLIHWPV--KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPM 158
Cdd:PRK11565 80 DDHK--RPREALEESLKKLQLDYVDLYLMHWPVpaIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 159 VNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG--KLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQER 236
Cdd:PRK11565 158 INQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSR 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 16802865 237 IIQNADIFDFELTEEEVAKISGLNKDERTGPDPDNFN 273
Cdd:PRK11565 238 IAENFDVFDFRLDKDELGEIAKLDQGKRLGPDPDQFG 274
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-266 |
3.13e-113 |
|
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: 326.43 E-value: 3.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVQDgDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGY 85
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSD-DEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 86 ESTLAAFDESLRKLELDYVDLYLIHWPV--KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIE 163
Cdd:cd19134 81 TASQAACRASLERLGLDYVDLYLIHWPAgrEGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 164 LHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADI 243
Cdd:cd19134 161 LHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDV 240
|
250 260
....*....|....*....|...
gi 16802865 244 FDFELTEEEVAKISGLNKDERTG 266
Cdd:cd19134 241 FDFELTADHMDALDGLDDGTRFR 263
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
5-259 |
1.70e-112 |
|
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: 324.66 E-value: 1.70e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 5 DTVKLANGVEMPRLGFGVWkvQDGDEAVNSVKWAI-EAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQ 83
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTS--HSGGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 84 GYESTLAAFDESLRKLELDYVDLYLIHWP--------VKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEI 155
Cdd:cd19135 81 GYESTKQAFEASLKRLGVDYLDLYLLHWPdcpssgknVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 156 APMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQE 235
Cdd:cd19135 161 VPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEE 240
|
250 260
....*....|....*....|....
gi 16802865 236 RIIQNADIFDFELTEEEVAKISGL 259
Cdd:cd19135 241 RIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-260 |
8.00e-104 |
|
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: 302.60 E-value: 8.00e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 9 LANGVEMPRLGFGVWKVQDGDEAvNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYEST 88
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQ-RAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 89 LAAFDESLRKLELDYVDLYLIHWPV--KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHP 166
Cdd:cd19130 83 AAAFAESLAKLGLDQVDLYLVHWPTpaAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 167 QLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDF 246
Cdd:cd19130 163 AYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDF 242
|
250
....*....|....
gi 16802865 247 ELTEEEVAKISGLN 260
Cdd:cd19130 243 DLTDTEIAAIDALD 256
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-264 |
1.07e-100 |
|
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: 296.22 E-value: 1.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 9 LANGVEMPRLGFGVWKVQDGdEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKES-----GIKREDLFVTTKLWNAEQ 83
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPG-QVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 84 GYESTLAAFDESLRKLELDYVDLYLIHWPVKGK--------------------FKDTWRAFEKLYKDKRVRAIGVCNFHE 143
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFErgdnpfpknpdgtirydsthYKETWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 144 HHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG----------KLLSNPEIKAIADAHGKSVA 213
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPdrpwakpdepVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 16802865 214 QVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWR 290
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-256 |
1.42e-100 |
|
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: 293.79 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 15 MPRLGFGVWKVQdGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYESTLAAFDE 94
Cdd:cd19073 1 IPALGLGTWQLR-GDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 95 SLRKLELDYVDLYLIHWPVKGK-FKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPL 173
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWPNPTVpLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFLYQAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 174 RKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEV 253
Cdd:cd19073 160 LEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDV 239
|
...
gi 16802865 254 AKI 256
Cdd:cd19073 240 AKI 242
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
6-264 |
1.53e-99 |
|
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: 293.16 E-value: 1.53e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVQDGdEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAI----KESGIKREDLFVTTKLWNA 81
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKPG-EVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 82 EQGYESTLAAFDESLRKLELDYVDLYLIHWPV---KGKFK----------------DTWRAFEKLYKDKRVRAIGVCNFH 142
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPValkKGVGFpesgedllslspipleDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 143 EHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG------------KLLSNPEIKAIADAHGK 210
Cdd:cd19123 162 VKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdrpaamkaegepVLLEDPVINKIAEKHGA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16802865 211 SVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19123 242 SPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-264 |
4.53e-96 |
|
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: 284.30 E-value: 4.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 4 KDTVKLANGVEMPRLGFGVWKVQdGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKE---SGI-KREDLFVTTKLW 79
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 80 NAEQGYESTLAAFDESLRKLELDYVDLYLIH--WPVKG------------------KFKDTWRAFEKLYKDKRVRAIGVC 139
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHapAAFKDdegesgtmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 140 NFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGN---------------GKLLSNPEIKAI 204
Cdd:cd19154 160 NFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspaPNLLQDPIVKAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 205 ADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-259 |
4.74e-95 |
|
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: 279.91 E-value: 4.74e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 10 ANGVEMPRLGFGVWKVQdGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYESTL 89
Cdd:cd19140 3 VNGVRIPALGLGTYPLT-GEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 90 AAFDESLRKLELDYVDLYLIHWPVK-GKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHPQL 168
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWPNKdVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYHPYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 169 TQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDL-QIGVVTIPKSVHQERIIQNADIFDFE 247
Cdd:cd19140 162 DQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIFDFT 241
|
250
....*....|..
gi 16802865 248 LTEEEVAKISGL 259
Cdd:cd19140 242 LSDEEMARIAAL 253
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-264 |
1.73e-94 |
|
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: 280.00 E-value: 1.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 8 KLANGVEMPRLGFGVWKvQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESG----IKREDLFVTTKLWNAEQ 83
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQ-ADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 84 GYESTLAAFDESLRKLELDYVDLYLIHWPVKGK---------------FKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKE 148
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKkgahmpepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 149 LMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGN-------GKLLSNPEIKAIADAHGKSVAQVILRWDL 221
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSpgttwvkKNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16802865 222 QIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLnKDER 264
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI-EQQR 284
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-259 |
4.82e-93 |
|
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: 276.07 E-value: 4.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVW-KVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKE---SG--IKREDLFVTTKLWNAEQG 84
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGlvKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 YESTLAAFDESLRKLELDYVDLYLIHWPV---KGKF--------------KDTWRAFEKLYKDKRVRAIGVCNFHEHHLK 147
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVslkPGKFsfpieeedflpfdiKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 148 ELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLG-------NGKLLSNPEIKAIADAHGKSVAQVILRWD 220
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGapgtkwgSNAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 16802865 221 LQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGL 259
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-261 |
1.55e-92 |
|
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: 274.76 E-value: 1.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 2 NLKDTVKLANGVEMPRLGFGVWKVQDGdEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNA 81
Cdd:cd19117 1 PSSKTFKLNTGAEIPAVGLGTWQSKPN-EVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 82 EQgyESTLAAFDESLRKLELDYVDLYLIHWPVKGK----------------------FKDTWRAFEKLYKDKRVRAIGVC 139
Cdd:cd19117 80 WH--RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDpdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 140 NFHEHHLKELMED--AEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLG--NGKLLSNPEIKAIADAHGKSVAQV 215
Cdd:cd19117 158 NFSIKNLEKLLASpsAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGstNAPLLKEPVIIKIAKKHGKTPAQV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16802865 216 ILRWDLQIGVVTIPKSVHQERIIQNADIfdFELTEEEVAKISGLNK 261
Cdd:cd19117 238 IISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-257 |
9.31e-89 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 264.48 E-value: 9.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGV----WKVQDGD---EAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNaeqG 84
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSP---G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 YESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKDT-----WRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMV 159
Cdd:cd19120 78 IKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPtlaeaWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 160 NQIELHPQLT--QEPLRKFCAENNIVVEAWSPLG------NGKLlsNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKS 231
Cdd:cd19120 158 NQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSpltrdaGGPL--DPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTS 235
|
250 260
....*....|....*....|....*.
gi 16802865 232 VHQERIIQNADIFDFELTEEEVAKIS 257
Cdd:cd19120 236 SKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-259 |
3.01e-82 |
|
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: 248.48 E-value: 3.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 9 LANGVEMPRLGFGVWKVQDGdEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKES-----GIKREDLFVTTKLWNAEQ 83
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPG-EVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 84 GYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFK-------------------------DTWRAFEKLYKDKRVRAIGV 138
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTgdlnpltavptnggevdldlsvslvDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 139 CNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG-----KLLSNPEIKAIADAHGKSVA 213
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNlaglpLLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16802865 214 QVILRWDLQIGVVTIPKSVHQERIIQNADifDFELTEEEVAKISGL 259
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
6-273 |
1.33e-80 |
|
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: 245.47 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESG----IKREDLFVTTKLWNA 81
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 82 EQGYesTLAAFDESLRKLELDYVDLYLIHWPVKGK------------------------FKDTWRAFEKLYKDKRVRAIG 137
Cdd:cd19112 81 DHGH--VIEACKDSLKKLQLDYLDLYLVHFPVATKhtgvgttgsalgedgvldidvtisLETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 138 VCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG----------KLLSNPEIKAIADA 207
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsvSPLDDPVLKDLAKK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16802865 208 HGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDERTGpDPDNFN 273
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTN-QPAKFW 303
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-272 |
4.79e-79 |
|
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: 241.56 E-value: 4.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNE----EGVGQAIKESGIKREDLFVTTKLWNA 81
Cdd:cd19115 4 TVKLNSGYDMPLVGFGLWKV-NNDTCADQVYNAIKAGYRLFDGACDYGNEveagQGVARAIKEGIVKREDLFIVSKLWNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 82 EQGYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKD-------------------------TWRAFEKLYKDKRVRAI 136
Cdd:cd19115 83 FHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDpavryppgwfydgkkvefsnapiqeTWTAMEKLVDKGLARSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 137 GVCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLG--------------NGKLLSNPEIK 202
Cdd:cd19115 163 GVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldlpgakdTPPLFEHDVIK 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 203 AIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDERTGpDPDNF 272
Cdd:cd19115 243 SIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFN-NPLNY 311
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
12-264 |
3.27e-78 |
|
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: 239.24 E-value: 3.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKVQDGdEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAI----KESGIKREDLFVTTKLWNAEQGYES 87
Cdd:cd19107 1 GAKMPILGLGTWKSPPG-QVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 88 TLAAFDESLRKLELDYVDLYLIHWPV--------------------KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLK 147
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 148 ELMEDAEIA--PMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLG----------NGKLLSNPEIKAIADAHGKSVAQV 215
Cdd:cd19107 160 RILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwakpeDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16802865 216 ILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-264 |
3.81e-78 |
|
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: 238.96 E-value: 3.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 4 KDTVKLANGVEMPRLGFGVWKVQDgDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKE---SG-IKREDLFVTTKL- 78
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQSSP-EEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 --WNAEQGYESTLAAfdeSLRKLELDYVDLYLIHWPV--------------KGKFK--------DTWRAFEKLYKDKRVR 134
Cdd:cd19155 80 pgGNRREKVEKFLLK---SLEKLQLDYVDLYLIHFPVgslskeddsgkldpTGEHKqdyttdllDIWKAMEAQVDQGLTR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 135 AIGVCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGN-----------------GKLLS 197
Cdd:cd19155 157 SIGLSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfspgtgspsgssPDLLQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16802865 198 NPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19155 237 DPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-256 |
1.61e-77 |
|
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: 236.27 E-value: 1.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 8 KLANGVEMPRLGFGVWKvQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKES---GIKREDLFVTTKLWNAEqg 84
Cdd:cd19121 5 KLNTGASIPAVGLGTWQ-AKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 YESTLAAFDESLRKLELDYVDLYLIHWPVK---------------GK--------FKDTWRAFEKLYKDKRVRAIGVCNF 141
Cdd:cd19121 82 HRRVELCLDRSLKSLGLDYVDLYLVHWPVLlnpngnhdlfptlpdGSrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 142 HEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGN--GKLLSNPEIKAIADAHGKSVAQVILRW 219
Cdd:cd19121 162 SIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGStgSPLISDEPVVEIAKKHNVGPGTVLISY 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 16802865 220 DLQIGVVTIPKSVHQERIIQNADIFDFelTEEEVAKI 256
Cdd:cd19121 242 QVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKL 276
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-264 |
7.72e-77 |
|
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: 235.08 E-value: 7.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKVQdGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIK---ESG-IKREDLFVTTKLWNAEQGYES 87
Cdd:cd19111 1 GFPMPVIGLGTYQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 88 TLAAFDESLRKLELDYVDLYLIHWPVKGKFK--------------DTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDA 153
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVNKkdkgerelassdvtSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 154 EIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGN-GK-----------LLSNPEIKAIADAHGKSVAQVILRWDL 221
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRanqslwpdqpdLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16802865 222 QIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-264 |
4.97e-76 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 233.88 E-value: 4.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNE----EGVGQAIKESGIKREDLFVTTKLWNA 81
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKL-DNATAADQIYQAIKAGYRLFDGAEDYGNEkevgEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 82 EQGYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFK--------------------------DTWRAFEKLYKDKRVRA 135
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVpieekyppgfycgdgdnfvyedvpilDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 136 IGVCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLG--------NGK------LLSNPEI 201
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvelnQGRalntptLFEHDTI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16802865 202 KAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19113 241 KSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
14-269 |
6.52e-73 |
|
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: 225.61 E-value: 6.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 14 EMPRLGFGVWKVQDGdEAVNSVKWAIEAGYISIDTAAAYKNEEGVG----QAIKESGIKREDLFVTTKLWNAEQGYESTL 89
Cdd:cd19110 3 DIPAVGLGTWKASPG-EVTEAVKVAIDAGYRHFDCAYLYHNESEVGagirEKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 90 AAFDESLRKLELDYVDLYLIHWPVKGK--------------------FKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKEL 149
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKpgepdlpldrsgmvipsdtdFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 150 MEDA--EIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG----KLLSNPEIKAIADAHGKSVAQVILRWDLQI 223
Cdd:cd19110 162 LNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGScegvDLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16802865 224 GVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDERTGPDP 269
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFP 287
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
15-272 |
1.61e-71 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 220.67 E-value: 1.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 15 MPRLGFGVWKVQdGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYESTLAAFDE 94
Cdd:PRK11172 3 IPAFGLGTFRLK-DQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 95 SLRKLELDYVDLYLIHWPVKGKFKDTWRAFEKLYKDKR---VRAIGVCNFHEHHLKELME---DAEIApmVNQIELHPQL 168
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAKKqglTREIGISNFTIALMKQAIAavgAENIA--TNQIELSPYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 169 TQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFEL 248
Cdd:PRK11172 160 QNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQL 239
|
250 260
....*....|....*....|....
gi 16802865 249 TEEEVAKISGLNKDERTgPDPDNF 272
Cdd:PRK11172 240 DAEDMAAIAALDRNGRL-VSPEGL 262
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-267 |
2.15e-71 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 221.72 E-value: 2.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVQD--GDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIK---ESG-IKREDLFVTTKLW 79
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRskiADGtVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 80 NAEQGYESTLAAFDESLRKLELDYVDLYLIHWPV-------------KGK-------FKDTWRAFEKLyKDK-RVRAIGV 138
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPValkpgeelfpkdeNGKlifdtvdLCATWEAMEKC-KDAgLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 139 CNFHEHHLKELMEDAEIA--PMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGK-----------LLSNPEIKAIA 205
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRdkewvdqnspvLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16802865 206 DAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDERTGP 267
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
15-259 |
5.08e-70 |
|
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: 216.07 E-value: 5.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 15 MPRLGFGVWKVQDgDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKESGIKREDLFVTTKLWNAEQGYESTLAAFDE 94
Cdd:cd19139 1 IPAFGLGTFRLKD-DVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 95 SLRKLELDYVDLYLIHWPVKGK---FKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELME---DAEIApmVNQIELHPQL 168
Cdd:cd19139 80 SLEKLRTDYVDLTLIHWPSPNDevpVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAvvgAGAIA--TNQIELSPYL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 169 TQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFEL 248
Cdd:cd19139 158 QNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTL 237
|
250
....*....|.
gi 16802865 249 TEEEVAKISGL 259
Cdd:cd19139 238 DADDMAAIAAL 248
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-257 |
1.35e-69 |
|
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: 215.56 E-value: 1.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKV--------QDGDEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKesGIKREDLFVTTKLWN 80
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 81 AEQGYESTLAAFDESLRKLELDYVDLYLIHWPV-KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELME---DAEIA 156
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNpSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSylkKGPIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 157 pmVNQIELHpQLTQEPLRK---FCAENNIVVEAWSPLGNGKLLS---NPEIKAIADAHGKSVAQVILRWDLQI-GVVTIP 229
Cdd:cd19072 159 --ANQVEYN-LFDREEESGllpYCQKNGIAIIAYSPLEKGKLSNakgSPLLDEIAKKYGKTPAQIALNWLISKpNVIAIP 235
|
250 260
....*....|....*....|....*...
gi 16802865 230 KSVHQERIIQNADIFDFELTEEEVAKIS 257
Cdd:cd19072 236 KASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-259 |
4.17e-69 |
|
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: 215.08 E-value: 4.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFGVWKVQDgDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKE----SGIKREDLFVTTKLWNAEQGYESTLAA 91
Cdd:cd19128 2 PRLGFGTYKITE-SESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 92 FDESLRKLELDYVDLYLIHWPV--------------------KGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELME 151
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLafdmdtdgdprddnqiqslsKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 152 DAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLG------NGKLLSNPEIKAIADAHGKSVAQVILRWDLQIGV 225
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGgsygdgNLTFLNDSELKALATKYNTTPPQVIIAWHLQKWP 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 16802865 226 VT---IPKSVHQERIIQNADIFDFELTEEEVAKISGL 259
Cdd:cd19128 241 KNysvIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-256 |
5.00e-68 |
|
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: 212.74 E-value: 5.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 5 DTVKLANGVEMPRLGFGVWK-VQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIK----ESGIKREDLFVTTKLW 79
Cdd:cd19119 2 ISFKLNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 80 NAEqgYESTLAAFDESLRKLELDYVDLYLIHWPV--------KGKFK------------------DTWRAFEKLYKDKRV 133
Cdd:cd19119 82 PTF--YDEVERSLDESLKALGLDYVDLLLVHWPVcfekdsddSGKPFtpvnddgktryaasgdhiTTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 134 RAIGVCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGK--LLSNPEIKAIADAHGKS 211
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGapNLKNPLVKKIAEKYNVS 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16802865 212 VAQVILRWDLQIGVVTIPKSVHQERIIQNADIfdFELTEEEVAKI 256
Cdd:cd19119 240 TGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKL 282
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-264 |
9.08e-66 |
|
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: 207.34 E-value: 9.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVW---KVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKES----GIKREDLFVTTKLWNAEQG 84
Cdd:cd19109 1 GNSIPIIGLGTYsepKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 YESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKD--------------------TWRAFEKLYKDKRVRAIGVCNFHEH 144
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDeiyprdengkwlyhktnlcaTWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 145 HLKELMEDAEIA--PMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGK-----------LLSNPEIKAIADAHGKS 211
Cdd:cd19109 161 QLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 16802865 212 VAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-264 |
1.44e-65 |
|
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: 206.64 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVG----QAIKESGIKREDLFVTTKLWNAEQGYES 87
Cdd:cd19114 1 GDKMPLVGFGTAKI-KANETEEVIYNAIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 88 TLAAFDESLRKLELDYVDLYLIHWPVKGKF--------------------------KDTWRAFEKLYKDKRVRAIGVCNF 141
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPIPAAYvdpaenypflwkdkelkkfpleqspmQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 142 HEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG-------------KLLSNPEIKAIADAH 208
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkhftNLLEHPVVKKLADKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16802865 209 GKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLNKDER 264
Cdd:cd19114 240 KRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-243 |
2.23e-64 |
|
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: 203.46 E-value: 2.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWkVQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKE----SGIKREDLFVTTKLWNAEQGYE 86
Cdd:cd19129 2 GSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 87 STLAAFDESLRKLELDYVDLYLIHWPV--------------------KG-KFKDTWRAFEKLYKDKRVRAIGVCNFHEHH 145
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFafqpgdeqdprdangnviydDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 146 LKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG---KLLSNPEIKAIADAHGKSVAQVILRWDLQ 222
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmepKLLEDPVITAIARRVNKTPAQVLLAWAIQ 240
|
250 260
....*....|....*....|.
gi 16802865 223 IGVVTIPKSVHQERIIQNADI 243
Cdd:cd19129 241 RGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-256 |
1.65e-63 |
|
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: 200.17 E-value: 1.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLANGVEMPRLGFGVWKVQDG----DEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKESgikREDLFVTTKL 78
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMGEDpakrAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 --WNAeqGYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIA 156
Cdd:cd19138 79 lpSNA--SRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 157 PMV-NQIELHpqLTQE----PLRKFCAENNIVVEAWSPLGNG-----KLLSNPEIKAIADAHGKSVAQVILRWDL-QIGV 225
Cdd:cd19138 157 NCAaNQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGgllrrGLLENPTLKEIAARHGATPAQVALAWVLrDGNV 234
|
250 260 270
....*....|....*....|....*....|.
gi 16802865 226 VTIPKSVHQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19138 235 IAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-261 |
2.23e-63 |
|
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: 200.93 E-value: 2.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 8 KLANGVEMPRLGFGVWkVQDGD--EAVNSVKWAIEAGYISIDTAAAYKNEEGVGQAIKE-----SGIKREDLFVTTKLWN 80
Cdd:cd19122 2 TLNNGVKIPAVGFGTF-ANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 81 AEQGYESTLAAFDESLRKLELDYVDLYLIHWPV--------------KGKF----------KDTWRAFEKLYKDKRVRAI 136
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIaaekndqrspklgpDGKYvilkdltenpEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 137 GVCNFHEHHLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNG--------KLLSNPEIKAIADAH 208
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQnqvpstgeRVSENPTLNEVAEKG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 16802865 209 GKSVAQVILRWDLQIGVVTIPKSVHQERIIQNADIfdFELTEEEVAKISGLNK 261
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQVAK 291
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-252 |
1.06e-56 |
|
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: 182.77 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKV---------QDgDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgIKREDLFVTTKLW 79
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdysRD-EEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 80 NAEQGYESTLAAFDESLRKLELDYVDLYLIHWPVKG-KFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPM 158
Cdd:cd19137 78 PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNiPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 159 VNQIELH---PQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQI-GVVTIPKSVHQ 234
Cdd:cd19137 158 CNQVKYNledRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRV 237
|
250
....*....|....*...
gi 16802865 235 ERIIQNADIFDFELTEEE 252
Cdd:cd19137 238 EHLKENLKATEIKLSEEE 255
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
18-260 |
4.73e-56 |
|
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: 181.74 E-value: 4.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 18 LGFGVWKVQDG------DEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGIKREDLFVTTKLWNAEQGY--- 85
Cdd:pfam00248 1 IGLGTWQLGGGwgpiskEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWpsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 86 ---ESTLAAFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQ 161
Cdd:pfam00248 81 gskENIRKSLEESLKRLGTDYIDLYYLHWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 162 IELHP--QLTQEPLRKFCAENNIVVEAWSPLGNGKLLS---------------------------NPEIKAIADAHGKSV 212
Cdd:pfam00248 161 VEYNLlrRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleaLEALEEIAKEHGVSP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16802865 213 AQVILRWDLQI--GVVTIPKSVHQERIIQNADIFDFELTEEEVAKISGLN 260
Cdd:pfam00248 241 AQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-256 |
6.59e-53 |
|
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: 173.87 E-value: 6.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVW--------KVQDgDEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKEsgiKREDLFVTTK--- 77
Cdd:cd19084 1 DLKVSRIGLGTWaiggtwwgEVDD-QESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG---RRDDVVIATKcgl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 78 LWNAEQGY------ESTLAAFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELM 150
Cdd:cd19084 77 RWDGGKGVtkdlspESIRKEVEQSLRRLQTDYIDLYQIHWPdPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 151 EDAEIApmVNQIE---LHPQlTQEPLRKFCAENNIVVEAWSPLGNGkLLS-----------------NP----------- 199
Cdd:cd19084 157 KYGPIV--SLQPPysmLERE-IEEELLPYCRENGIGVLPYGPLAQG-LLTgkykkeptfppddrrsrFPffrgenfeknl 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16802865 200 ----EIKAIADAHGKSVAQVILRWDL-QIGVVTI---PKSVHQerIIQNADIFDFELTEEEVAKI 256
Cdd:cd19084 233 eivdKLKEIAEKYGKSLAQLAIAWTLaQPGVTSAivgAKNPEQ--LEENAGALDWELTEEELKEI 295
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
12-256 |
8.31e-47 |
|
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: 158.80 E-value: 8.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFG------VWKVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKesGIKREDLFVTTKL---- 78
Cdd:COG0667 10 GLKVSRLGLGtmtfggPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVVIATKVgrrm 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 ----WNAEQGYESTLAAFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDA 153
Cdd:COG0667 88 gpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPdPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 154 E-IAPMV-NQIELHPqLTQEPLRK---FCAENNIVVEAWSPLGNGkLLSNP----------------------------- 199
Cdd:COG0667 168 EgLPPIVaVQNEYSL-LDRSAEEEllpAARELGVGVLAYSPLAGG-LLTGKyrrgatfpegdraatnfvqgylternlal 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16802865 200 --EIKAIADAHGKSVAQVILRWDLQIGVVTIP----KSVHQerIIQNADIFDFELTEEEVAKI 256
Cdd:COG0667 246 vdALRAIAAEHGVTPAQLALAWLLAQPGVTSVipgaRSPEQ--LEENLAAADLELSAEDLAAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-257 |
1.07e-45 |
|
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: 155.05 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFGVW--------KVQDGDEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKEsgiKREDLFVTTKLWNAEQG 84
Cdd:cd19085 2 SRLGLGCWqfgggywwGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 YESTLAAFDESLRKLELDYVDLYLIHWPVKG-KFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIApmVNQI- 162
Cdd:cd19085 79 PEDVRKSCERSLKRLGTDYIDLYQIHWPSSDvPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID--SNQLp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 163 ----------ELHPqltqeplrkFCAENNIVVEAWSPLGNGkLLS----------------------NPE---------- 200
Cdd:cd19085 157 ynllwraieyEILP---------FCREHGIGVLAYSPLAQG-LLTgkfssaedfppgdartrlfrhfEPGaeeetfeale 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16802865 201 -IKAIADAHGKSVAQVILRWDLQIGVVTipkSV-----HQERIIQNADIFDFELTEEEVAKIS 257
Cdd:cd19085 227 kLKEIADELGVTMAQLALAWVLQQPGVT---SVivgarNPEQLEENAAAVDLELSPSVLERLD 286
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
14-256 |
3.33e-45 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 153.92 E-value: 3.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 14 EMPRLGFGVWkvQDGD------------EAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGiKREDLFVTTKL 78
Cdd:cd19093 1 EVSPLGLGTW--QWGDrlwwgygeygdeDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 WNA--EQGYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKD--TWRAFEKLYKDKRVRAIGVCNFHEHHLK---ELME 151
Cdd:cd19093 78 APLpwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIeaLMDGLADAVEEGLVRAVGVSNYSADQLRrahKALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 152 DAEIAPMVNQIE---LHPQLTQEPLRKFCAENNIVVEAWSPLGNGKL-----LSNP----------------------EI 201
Cdd:cd19093 158 ERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGLLtgkysPENPppggrrrlfgrknlekvqplldAL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16802865 202 KAIADAHGKSVAQVILRWDLQIGVVTIP--KSVHQERiiQNADIFDFELTEEEVAKI 256
Cdd:cd19093 238 EEIAEKYGKTPAQVALNWLIAKGVVPIPgaKNAEQAE--ENAGALGWRLSEEEVAEL 292
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-259 |
1.22e-40 |
|
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: 142.43 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 17 RLGFGVWKV-----------QDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgiKREDLFVTTK---LW 79
Cdd:cd19102 3 TIGLGTWAIggggwgggwgpQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKG---LRDRPIVATKcglLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 80 NAE----QGY--ESTLAAFDESLRKLELDYVDLYLIHWPVKGK-FKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMED 152
Cdd:cd19102 80 DEEgrirRSLkpASIRAECEASLRRLGVDVIDLYQIHWPDPDEpIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 153 AEIApmVNQIE---LHPQLTQEPLRkFCAENNIVVEAWSPLGNGkLLS-------------------NPE---------- 200
Cdd:cd19102 160 HPIA--SLQPPyslLRRGIEAEILP-FCAEHGIGVIVYSPMQSG-LLTgkmtpervaslpaddwrrrSPFfqepnlarnl 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16802865 201 -----IKAIADAHGKSVAQVILRWDLQIGVVT--IPKSVHQERIIQNADIFDFELTEEEVAKISGL 259
Cdd:cd19102 236 alvdaLRPIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-229 |
8.34e-40 |
|
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: 138.04 E-value: 8.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFGVWKV---QDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGiKREDLFVTTKLWNAEQGYEST- 88
Cdd:cd06660 1 SRLGLGTMTFggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRG-NRDDVVIATKGGHPPGGDPSRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 89 -------LAAFDESLRKLELDYVDLYLIHW-----PVkgkfKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAE-- 154
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHRddpstPV----EETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKah 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 155 --IAPMVNQIE---LHPQLTQEPLRKFCAENNIVVEAWSPLGNGkllsnpeikaiadahgksVAQVILRWDLQIGVVTIP 229
Cdd:cd06660 156 glPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPFVTVP 217
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
6-257 |
1.84e-36 |
|
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: 131.63 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLAN-GVEMPRLGFGVWKV--------QDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgiKREDLF 73
Cdd:cd19149 1 YRKLGKsGIEASVIGLGTWAIgggpwwggSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 74 VTTK---LWNAEQGY----------------ESTLAAFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRV 133
Cdd:cd19149 78 LATKcglRWDREGGSfffvrdgvtvyknlspESIREEVEQSLKRLGTDYIDLYQTHWQdVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 134 RAIGVCNFHEHHLKELMEDAEIApmVNQIE---LHPQLTQEPLrKFCAENNIVVEAWSPLGNGkLLSNP----------- 199
Cdd:cd19149 158 RAIGASNVSVEQIKEYVKAGQLD--IIQEKysmLDRGIEKELL-PYCKKNNIAFQAYSPLEQG-LLTGKitpdrefdagd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 200 ---------------------EIKAIADAHGKSVAQVILRWDL-QIGVVTI---PKSVHQerIIQNADIFDFELTEEEVA 254
Cdd:cd19149 234 arsgipwfspenrekvlalleKWKPLCEKYGCTLAQLVIAWTLaQPGITSAlcgARKPEQ--AEENAKAGDIRLSAEDIA 311
|
...
gi 16802865 255 KIS 257
Cdd:cd19149 312 TMR 314
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
10-252 |
6.16e-36 |
|
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: 129.60 E-value: 6.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 10 ANGVEMPRLGFGVWKVQDG----DEAVNSVKWAIEAGYISIDTA---AAYKNEEGVGQAIKESGIKREDLFVTTK----L 78
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWgesaEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALALNPGLREKIEIQTKcgirL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 WNAEQG---------YESTLAAFDESLRKLELDYVDLYLIHWPvkgkfkD-------TWRAFEKLYKDKRVRAIGVCNFH 142
Cdd:cd19092 81 GDDPRPgrikhydtsKEHILASVEGSLKRLGTDYLDLLLLHRP------DplmdpeeVAEAFDELVKSGKVRYFGVSNFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 143 EHHLKELMEDAEIAPMVNQIELHPqLTQEPLR----KFCAENNIVVEAWSPLGNGKLLSNP---------EIKAIADAHG 209
Cdd:cd19092 155 PSQIELLQSYLDQPLVTNQIELSL-LHTEAIDdgtlDYCQLLDITPMAWSPLGGGRLFGGFderfqrlraALEELAEEYG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16802865 210 KSVAQVILRWDLQI--GVVTIPKSVHQERIIQNADIFDFELTEEE 252
Cdd:cd19092 234 VTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
7-254 |
2.97e-31 |
|
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: 117.69 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 7 VKLAN-GVEMPRLGFG----------VWKVqDGDEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKESgIKREDL 72
Cdd:cd19079 3 VRLGNsGLKVSRLCLGcmsfgdpkwrPWVL-DEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEF-APRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 73 FVTTKLWNAEQGYEST--------LAAFDESLRKLELDYVDLYLIHW-----PvkgkFKDTWRAFEKLYKDKRVRAIGVC 139
Cdd:cd19079 81 VIATKVYFPMGDGPNGrglsrkhiMAEVDASLKRLGTDYIDLYQIHRwdyetP----IEETLEALHDVVKSGKVRYIGAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 140 NFHEHHLKELMEDAEI---APMVNQIELHPQLTQEPLR---KFCAENNIVVEAWSPLGNGKLLSNPE------------- 200
Cdd:cd19079 157 SMYAWQFAKALHLAEKngwTKFVSMQNHYNLLYREEERemiPLCEEEGIGVIPWSPLARGRLARPWGdtterrrsttdta 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16802865 201 -----------------IKAIADAHGKSVAQVILRWDLQIGVVTIP-----KSvhqERIIQNADIFDFELTEEEVA 254
Cdd:cd19079 237 klkydyfteadkeivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivgatKL---EHLEDAVAALDIKLSEEEIK 309
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
6-259 |
7.13e-31 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 116.75 E-value: 7.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLA-NGVEMPRLGFGVWKVQ--------DGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESgiKREDLF 73
Cdd:cd19083 1 KVKLGkSDIDVNPIGLGTNAVGghnlypnlDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY--NRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 74 VTTKLWNAEQGYESTL--------AAFDESLRKLELDYVDLYLIHWPVKGKFKD-TWRAFEKLYKDKRVRAIGVCNFHEH 144
Cdd:cd19083 79 IATKGAHKFGGDGSVLnnspeflrSAVEKSLKRLNTDYIDLYYIHFPDGETPKAeAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 145 HLKELMEDAEIAPMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGKL-------LSNPE----------------- 200
Cdd:cd19083 159 QLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLagkytkdTKFPDndlrndkplfkgerfse 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16802865 201 -------IKAIADAHGKSVAQVILRWDLQ---IGVVtIPKSVHQERIIQNADIFDFELTEEEVAKISGL 259
Cdd:cd19083 239 nldkvdkLKSIADEKGVTVAHLALAWYLTrpaIDVV-IPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
11-256 |
3.31e-30 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 116.07 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWKVQ--DGDEAVNSVKWAIEAG--YIsiDTAAAY-KNEEGVGQAIKESgikREDLFVTTKLWNAEQGY 85
Cdd:COG1453 9 TGLEVSVLGFGGMRLPrkDEEEAEALIRRAIDNGinYI--DTARGYgDSEEFLGKALKGP---RDKVILATKLPPWVRDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 86 ESTLAAFDESLRKLELDYVDLYLIH-------WPVKGKFKDTWRAFEKLYKDKRVRAIGVCNfheHH----LKELMEDAE 154
Cdd:COG1453 84 EDMRKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPGGALEALEKAKAEGKIRHIGFST---HGslevIKEAIDTGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 155 IApMVnQIELHPQLTQEPLR----KFCAENNIVVEAWSPLGNGKLLSNPE-IKAIADAhGKSVAQVILRWDLQI-GVVTI 228
Cdd:COG1453 161 FD-FV-QLQYNYLDQDNQAGeealEAAAEKGIGVIIMKPLKGGRLANPPEkLVELLCP-PLSPAEWALRFLLSHpEVTTV 237
|
250 260 270
....*....|....*....|....*....|...
gi 16802865 229 ---PKSVHQerIIQNADIFD-FE-LTEEEVAKI 256
Cdd:COG1453 238 lsgMSTPEQ--LDENLKTADnLEpLTEEELAIL 268
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
6-256 |
1.41e-29 |
|
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: 113.08 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLAN-GVEMPRLGFGV------WKVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgiKREDLFVT 75
Cdd:cd19076 2 TRKLGTqGLEVSALGLGCmgmsafYGPADEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 76 TK---LWNAEQGY-------ESTLAAFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRVRAIGvcnfheh 144
Cdd:cd19076 79 TKfgiVRDPGSGFrgvdgrpEYVRAACEASLKRLGTDVIDLYYQHRVdPNVPIEETVGAMAELVEEGKVRYIG------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 145 hLKELMED-----AEIAPMVN-QIELHPQlTQEP---LRKFCAENNIVVEAWSPLGNGkLLS-----------------N 198
Cdd:cd19076 152 -LSEASADtirraHAVHPITAvQSEYSLW-TRDIedeVLPTCRELGIGFVAYSPLGRG-FLTgaikspedlpeddfrrnN 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16802865 199 P---------------EIKAIADAHGKSVAQVILRWDLQIG--VVTIPKSVHQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19076 229 PrfqgenfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
17-256 |
2.18e-29 |
|
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: 112.79 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 17 RLGFGVWKV-------QDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGiKREDLFVTTKL---WNAEQ 83
Cdd:cd19148 6 RIALGTWAIggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVgleWDEGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 84 GY--ESTLAAF----DESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIA 156
Cdd:cd19148 85 EVvrNSSPARIrkevEDSLRRLQTDYIDLYQVHWPdPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 157 PMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGkLLS-----------------NP---------------EIKAI 204
Cdd:cd19148 165 TVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRG-LLSgkmtkdtkfegddlrrtDPkfqeprfsqylaaveELDKL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16802865 205 ADAH-GKSVAQVILRWDLQIGVVTIP--KSVHQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19148 244 AQERyGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEI 298
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-242 |
1.04e-27 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 106.79 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 17 RLGFGVW-------KVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgiKREDLFVTTKLWN------ 80
Cdd:cd19086 5 EIGFGTWglggdwwGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKG---RRDKVVIATKFGNrfdggp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 81 -AEQGY--ESTLAAFDESLRKLELDYVDLYLIH-WPVK-GKFKDTWRAFEKLYKDKRVRAIGVC-NFHEhHLKELMEDAE 154
Cdd:cd19086 82 eRPQDFspEYIREAVEASLKRLGTDYIDLYQLHnPPDEvLDNDELFEALEKLKQEGKIRAYGVSvGDPE-EALAALRRGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 155 IAPMvnQIELHPqLTQEPLRKF---CAENNIVVEAWSPLGNGkLLSnpeikaiadahGKsVAQVILRWDL-QIGVVT-IP 229
Cdd:cd19086 161 IDVV--QVIYNL-LDQRPEEELfplAEEHGVGVIARVPLASG-LLT-----------GK-LAQAALRFILsHPAVSTvIP 224
|
250
....*....|....*
gi 16802865 230 --KSVHQerIIQNAD 242
Cdd:cd19086 225 gaRSPEQ--VEENAA 237
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-222 |
3.10e-27 |
|
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: 105.74 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVwkVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKesGIKREDLFVTTK--LWNAEQGYE 86
Cdd:cd19105 10 GLKVSRLGFGG--GGLPRESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALK--GLRRDKVFLATKasPRLDKKDKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 87 STLAAFDESLRKLELDYVDLYLIH---WPVKGKFKDTW-RAFEKLYKDKRVRAIGV-CNFHEHH-LKELMEDAEI-APMV 159
Cdd:cd19105 86 ELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELlEALEKLKKEGKVRFIGFsTHDNMAEvLQAAIESGWFdVIMV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16802865 160 NQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLlsNPEIKAIADAHGKSVAQVILRWDLQ 222
Cdd:cd19105 166 AYNFLNQPAELEEALAAAAEKGIGVVAMKTLAGGYL--QPALLSVLKAKGFSLPQAALKWVLS 226
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
20-256 |
4.52e-27 |
|
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: 106.93 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 20 FGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKEsgiKREDLFVTTK--LWNAE------QGYEST 88
Cdd:cd19091 30 FGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKG---RRDDVLIATKvrGRMGEgpndvgLSRHHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 89 LAAFDESLRKLELDYVDLYLIH-WPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAE----IAPMVNQI- 162
Cdd:cd19091 107 IRAVEASLKRLGTDYIDLYQLHgFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQAy 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 163 ----------ELHPqltqeplrkFCAENNIVVEAWSPLGNGkLLS--------NPE------------------------ 200
Cdd:cd19091 187 ysllgrdlehELMP---------LALDQGVGLLVWSPLAGG-LLSgkyrrgqpAPEgsrlrrtgfdfppvdrergydvvd 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16802865 201 -IKAIADAHGKSVAQVILRWDLQIGVVTI----PKSVHQerIIQNADIFDFELTEEEVAKI 256
Cdd:cd19091 257 aLREIAKETGATPAQVALAWLLSRPTVSSviigARNEEQ--LEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-229 |
1.75e-26 |
|
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: 103.84 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFGVWKV---------QDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGikrEDLFVTTKL----- 78
Cdd:cd19088 2 SRLGYGAMRLtgpgiwgppADREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvrt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 ----WNAEQGYESTLAAFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDA 153
Cdd:cd19088 79 gpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIdPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 154 EIAPMVNQIEL-HPQltQEPLRKFCAENNIVVEAWSPLGNGKLLSN-PEIKAIADAHGKSVAQVILRWDLQIG--VVTIP 229
Cdd:cd19088 159 RIVSVQNRYNLaNRD--DEGVLDYCEAAGIAFIPWFPLGGGDLAQPgGLLAEVAARLGATPAQVALAWLLARSpvMLPIP 236
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
16-227 |
7.22e-26 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 102.25 E-value: 7.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFG------VWKVQ-DGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgIKREDLFVTTKL-WNAEQG 84
Cdd:cd19096 1 SVLGFGtmrlpeSDDDSiDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKE--GPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 YESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKDT------WRAFEKLYKDKRVRAIGVcNFH--EHHLKELMEDAEIA 156
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKarkgglLEFLEKAKKEGLIRHIGF-SFHdsPELLKEILDSYDFD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16802865 157 pmVNQIELH----PQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNP-EIKAIADAHGKSVAQVILRWDLQIGVVT 227
Cdd:cd19096 158 --FVQLQYNyldqENQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNPpEALAILCGAPLSPAEWALRFLLSHPEVT 231
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-227 |
1.69e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 100.63 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKVQDGD--EAVNSVKWAIEAG--YIsiDTAAAYKN-EEGVGQAIKEsgiKREDLFVTTKLWnaEQGYE 86
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSqeEAAAIIRRALDLGinYF--DTAPSYGDsEEKIGKALKG---RRDKVFLATKTG--ARDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 87 STLAAFDESLRKLELDYVDLYLIH------WPVKGKFKD-TWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIA--- 156
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLHavdteeDLDQVFGPGgALEALLEAKEEGKIRFIGISGHSPEVLLRALETGEFDvvl 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16802865 157 PMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSnPEIKAIADAhgksvaqviLRWDLQIGVVT 227
Cdd:cd19100 161 FPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLS-GDPLDPEQA---------LRYALSLPPVD 221
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
39-256 |
9.66e-25 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 100.37 E-value: 9.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 39 IEAGYISIDTAAAY----------KNEEGVGQAIKESGiKREDLFVTTKL--WNAEQGY----ESTLAAFDESLRKLELD 102
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgfPMGPNGPglsrKHIRRAVEASLRRLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 103 YVDLYLIHW-----PVkgkfKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPMVNQIELHPQ-------LTQ 170
Cdd:cd19081 115 YIDLYQAHWddpatPL----EETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEynlvdreSFE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 171 EPLRKFCAENNIVVEAWSPLGNGKL----------------------LSNP-------EIKAIADAHGKSVAQVILRWDL 221
Cdd:cd19081 191 GELLPLCREEGIGVIPYSPLAGGFLtgkyrseadlpgstrrgeaakrYLNErglrildALDEVAAEHGATPAQVALAWLL 270
|
250 260 270
....*....|....*....|....*....|....*....
gi 16802865 222 QIGVVTIP----KSVHQERiiQNADIFDFELTEEEVAKI 256
Cdd:cd19081 271 ARPGVTAPiagaRTVEQLE--DLLAAAGLRLTDEEVARL 307
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
16-242 |
1.09e-24 |
|
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: 98.85 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFGVWKVQDG------DEAVNSVKWAIEAGYISIDTAAAYKN-EEGVGQAIkeSGIKREDLFVTTKLWNAEQG---- 84
Cdd:cd19095 1 SVLGLGTSGIGRVwgvpseAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGTHGEGgrdr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 ----YESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKDT-WRAFEKLYKDKRVRAIGVCNFHEhHLKELMEDAEIApmV 159
Cdd:cd19095 79 kdfsPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEvLETLEDLKAAGKVRYIGVSGDGE-ELEAAIASGVFD--V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 160 NQIELHP-QLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPE-----------IKAIADAHGKSVAQVILRWDLQIGVVT 227
Cdd:cd19095 156 VQLPYNVlDREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRrrplyadyarrPEFAAEIGGATWAQAALRFVLSHPGVS 235
|
250
....*....|....*..
gi 16802865 228 --IPKSVHQERIIQNAD 242
Cdd:cd19095 236 saIVGTTNPEHLEENLA 252
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
16-251 |
8.02e-24 |
|
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: 97.24 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFG------VWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKN-EEGVGQAIKEsgIKREDLFVTTKL-----WNAEQ 83
Cdd:cd19090 1 SALGLGtaglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE--LPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 84 GYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKD------TWRAFEKLYKDKRVRAIGV-CNFHEHHLKELME-DAEI 155
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDilapggALEALLELKEEGLIKHIGLgGGPPDLLRRAIETgDFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 156 APMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNP--------------------EIKAIADAHGKSVAQV 215
Cdd:cd19090 159 VLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPpervrytyrwlspelldrakRLYELCDEHGVPLPAL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16802865 216 ILRWDLQI----GVVTIPKSVhqERIIQNADIFDFELTEE 251
Cdd:cd19090 239 ALRFLLRDprisTVLVGASSP--EELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-256 |
6.76e-23 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 95.59 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKLA-NGVEMPRLGFGVWKVQDG-------DEAVNSVKWAIEAGYISIDTAAAY-KNEEGVGQAIKESGIKREDLFVTT 76
Cdd:cd19144 3 TRTLGrNGPSVPALGFGAMGLSAFygppkpdEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWFKQNPGKREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 77 KL---WNAEQGYEST-------LAAFDESLRKLELDYVDLYLIHwPVKGK--FKDTWRAFEKLYKDKRVRAIGVcnfHEH 144
Cdd:cd19144 83 KFgieKNVETGEYSVdgspeyvKKACETSLKRLGVDYIDLYYQH-RVDGKtpIEKTVAAMAELVQEGKIKHIGL---SEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 145 HLKELMEDAEIAPMVN-QIELHP-----QLTQEPLRKFCAENNIVVEAWSPLGNGKL---LSNPE--------------- 200
Cdd:cd19144 159 SAETLRRAHAVHPIAAvQIEYSPfsldiERPEIGVLDTCRELGVAIVAYSPLGRGFLtgaIRSPDdfeegdfrrmaprfq 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16802865 201 -------------IKAIADAHGKSVAQVILRWDLQIG--VVTIPKSVHQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19144 239 aenfpknlelvdkIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
38-259 |
1.46e-22 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 94.56 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 38 AIEAGYISIDTAAAY---KNEEGVGQAIKEsgiKREDLFVTTKL------WNAEQGYES--TLAAFDESLRKLELDYVDL 106
Cdd:cd19087 39 ALDAGINFFDTADVYgggRSEEIIGRWIAG---RRDDIVLATKVfgpmgdDPNDRGLSRrhIRRAVEASLRRLQTDYIDL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 107 YLIH-WPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAE---------IAPMVNQIELHPQLTQEPLrkf 176
Cdd:cd19087 116 YQMHhFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAArrgllrfvsEQPMYNLLKRQAELEILPA--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 177 CAENNIVVEAWSPLGNGkLLS-------------------------NPE-------IKAIADAHGKSVAQVILRWDLQIG 224
Cdd:cd19087 193 ARAYGLGVIPYSPLAGG-LLTgkygkgkrpesgrlveraryqarygLEEyrdiaerFEALAAEAGLTPASLALAWVLSHP 271
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16802865 225 VVT--I--PKSVHQ-ERIIQNADIfdfELTEEEVAKISGL 259
Cdd:cd19087 272 AVTspIigPRTLEQlEDSLAALEI---TLTPELLAEIDEL 308
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-256 |
2.44e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 93.81 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 14 EMPRLGFGVW-------KVQDGDEAVNSVKWAIEAGYISIDTAAAYKN-EEGVGQAIKE---SGIKREDLFVTTKLwnAE 82
Cdd:cd19101 1 TISRVINGMWqlsgghgGIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRlrrERDAADDVQIHTKW--VP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 83 QGYESTL------AAFDESLRKLELDYVDLYLIHW--PVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMeDAE 154
Cdd:cd19101 79 DPGELTMtrayveAAIDRSLKRLGVDRLDLVQFHWwdYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL-DAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 155 IAPMVNQIE--LHPQLTQEPLRKFCAENNIVVEAWSPLGNGkLLSN-----PE--------------------------- 200
Cdd:cd19101 158 VPIVSNQVQysLLDRRPENGMAALCEDHGIKLLAYGTLAGG-LLSEkylgvPEptgpaletrslqkyklmidewggwdlf 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 201 ------IKAIADAHGKSVAQVILRWDLQ--------IGVVTipksvhQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19101 237 qellrtLKAIADKHGVSIANVAVRWVLDqpgvagviVGARN------SEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
8-254 |
9.68e-21 |
|
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: 89.15 E-value: 9.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 8 KLAN-GVEMPRLGFG------VWKVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKesGIKREDLFVTTK 77
Cdd:cd19163 5 KLGKtGLKVSKLGFGasplggVFGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYYLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 78 LWNAEQG--------YESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKD-----TWRAFEKLYKDKRVRAIGVCNFHEH 144
Cdd:cd19163 83 VGRYGLDpdkmfdfsAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDqilneTLPALQKLKEEGKVRFIGITGYPLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 145 HLKELMEDAEIApmVNQI------ELHPQLTQEpLRKFCAENNIVVEAWSPLGNGkLLSN----------PEIKAIA--- 205
Cdd:cd19163 163 VLKEVLERSPVK--IDTVlsychyTLNDTSLLE-LLPFFKEKGVGVINASPLSMG-LLTErgppdwhpasPEIKEACaka 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16802865 206 ----DAHGKSVAQVILRWDLQ-IGV-VTIPKSVHQERIIQNADIFDFELTEEEVA 254
Cdd:cd19163 239 aaycKSRGVDISKLALQFALSnPDIaTTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
12-251 |
2.35e-20 |
|
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: 88.03 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKV---QDGDEAVNS-VKWAIEAGYISIDTAAAYKN---EEGVGQAIKesGIKREDLFVTTKL-WNA-E 82
Cdd:cd19074 1 GLKVSELSLGTWLTfggQVDDEDAKAcVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWPTgP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 83 QGYESTLA------AFDESLRKLELDYVDLYLIHwpvkgKFKD------TWRAFEKLYKDKRVRAIGVCnfhEHHLKELM 150
Cdd:cd19074 79 GPNDRGLSrkhifeSIHASLKRLQLDYVDIYYCH-----RYDPetpleeTVRAMDDLIRQGKILYWGTS---EWSAEQIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 151 EDAEIA-------PMVNQIELHpQLTQEP---LRKFCAENNIVVEAWSPLGNGKL---------------LSNPEI---- 201
Cdd:cd19074 151 EAHDLArqfglipPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQGLLtgkyrdgipppsrsrATDEDNrdkk 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16802865 202 ---------------KAIADAHGKSVAQVILRWDLQIGVVT--IPKSVHQERIIQNADIFDFELTEE 251
Cdd:cd19074 230 rrlltdenlekvkklKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
39-229 |
5.68e-19 |
|
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: 84.14 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 39 IEAGYISIDTAAAY-------KNEEGVGQAIKESGiKREDLFVTTK-----LWNAEQGY---ESTLAAFDESLRKLELDY 103
Cdd:cd19082 27 VELGGNFIDTARVYgdwvergASERVIGEWLKSRG-NRDKVVIATKgghpdLEDMSRSRlspEDIRADLEESLERLGTDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 104 VDLYLIHW-----PVkGKFKDTwraFEKLYKDKRVRAIGVCNFHEHHLKELMEDAE---------------IAPMVNQIE 163
Cdd:cd19082 106 IDLYFLHRddpsvPV-GEIVDT---LNELVRAGKIRAFGASNWSTERIAEANAYAKahglpgfaasspqwsLARPNEPPW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 164 LHPQLT--QEPLRKFCAENNIVVEAWSPLGNG--------KLLSNPE----------------IKAIADAHGKSVAQVIL 217
Cdd:cd19082 182 PGPTLVamDEEMRAWHEENQLPVFAYSSQARGffskraagGAEDDSElrrvyyseenferlerAKELAEEKGVSPTQIAL 261
|
250
....*....|..
gi 16802865 218 RWDLQIGVVTIP 229
Cdd:cd19082 262 AYVLNQPFPTVP 273
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
18-256 |
1.28e-18 |
|
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: 83.44 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 18 LGFGVWKVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgiKREDLFVTTKL---WNAEQGYESTL-- 89
Cdd:cd19078 14 MSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKFgfkIDGGKPGPLGLds 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 90 ------AAFDESLRKLELDYVDLYLIHWP--------VKGKFKDtwrafekLYKDKRVRAIGVCnfhEHHLKELMEDAEI 155
Cdd:cd19078 91 rpehirKAVEGSLKRLQTDYIDLYYQHRVdpnvpieeVAGTMKE-------LIKEGKIRHWGLS---EAGVETIRRAHAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 156 APMV---NQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGkLLS---------------------NPE----------- 200
Cdd:cd19078 161 CPVTavqSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKG-FLTgkidentkfdegddraslprfTPEaleanqalvdl 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16802865 201 IKAIADAHGKSVAQVILRWDLQIG--VVTIPKSVHQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19078 240 LKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-228 |
1.65e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 83.47 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFG------VWKVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKEsgiKREDLFVTTK----L 78
Cdd:cd19104 9 GLKVSELTFGgggiggLMGRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKG---LPAGPYITTKvrldP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 WNAEQGYESTLAAFDESLRKLELDYVDLYLIH--------WPVKGKF--------KDTWRAFEKLYKDKRVRAIG-VCNF 141
Cdd:cd19104 86 DDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHnrigderdKPVGGTLsttdvlglGGVADAFERLRSEGKIRFIGiTGLG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 142 HEHHLKELMEDAEIApMVNQI---------ELHPQLT--QEP--LRKFCAENNIVVEAWSPLGNGKLLSNP--------- 199
Cdd:cd19104 166 NPPAIRELLDSGKFD-AVQVYynllnpsaaEARPRGWsaQDYggIIDAAAEHGVGVMGIRVLAAGALTTSLdrgreappt 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16802865 200 -------------EIKAIADAHGKSVAQVILRWDLQI-GVVTI 228
Cdd:cd19104 245 sdsdvaidfrraaAFRALAREWGETLAQLAHRFALSNpGVSTV 287
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
39-256 |
2.66e-17 |
|
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: 79.96 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 39 IEAGYISIDTAAAYKN---EEGVGQAIKEsgiKREDLFVTTKL-WNAEQG--------YESTLAAFDESLRKLELDYVDL 106
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAG---NRDRIVLATKYtMNRRPGdpnaggnhRKNLRRSVEASLRRLQTDYIDL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 107 YLIHW-----PVkgkfKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEI---APMVN-QIElHPQLTQEPLRKF- 176
Cdd:cd19080 118 LYVHAwdfttPV----EEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELrgwSPFVAlQIE-YSLLERTPERELl 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 177 --CAENNIVVEAWSPLGNGKLLS--------------------------NPEI----KAIADAHGKSVAQVILRWDLQIG 224
Cdd:cd19080 193 pmARALGLGVTPWSPLGGGLLTGkyqrgeegrageakgvtvgfgklterNWAIvdvvAAVAEELGRSAAQVALAWVRQKP 272
|
250 260 270
....*....|....*....|....*....|....*.
gi 16802865 225 VVTIP----KSVHQerIIQNADIFDFELTEEEVAKI 256
Cdd:cd19080 273 GVVIPiigaRTLEQ--LKDNLGALDLTLSPEQLARL 306
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
38-256 |
3.42e-17 |
|
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: 79.92 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 38 AIEAGYISIDTAAAY----------KNEEGVGQAIKESGiKREDLFVTTKL--------WNAEQG----YESTLAAFDES 95
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRGGGtrldRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 96 LRKLELDYVDLYLIHWPVKG-------------------KFKDTWRAFEKLYKDKRVRAIGVCNfhehhlkE----LMED 152
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPDRYtplfgggyytepseeedsvSFEEQLEALGELVKAGKIRHIGLSN-------EtpwgVMKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 153 AEIAPMVNQieLHPQLTQEPL----RKF-------CAENNIVVEAWSPLG----NGKLLSNP------------------ 199
Cdd:cd19094 179 LELAEQLGL--PRIVSIQNPYsllnRNFeeglaeaCHRENVGLLAYSPLAggvlTGKYLDGAarpeggrlnlfpgymary 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16802865 200 ----------EIKAIADAHGKSVAQVILRWDLQ--------IGVVTIpksvhqERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19094 257 rspqaleavaEYVKLARKHGLSPAQLALAWVRSrpfvtstiIGATTL------EQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-219 |
2.22e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 74.66 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 17 RLGFGVWKVQDGD----EAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKES----GIKREDLFVTTK-------- 77
Cdd:cd19099 5 SLGLGTYRGDSDDetdeEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELiekgGIKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 78 ------LWNAEQGYESTL-------------------AAFDESLRKLELDYVDLYLIHWP-----------VKGKFKDTW 121
Cdd:cd19099 85 deplrpLKYLEEKLGRGLidvadsaglrhcispayleDQIERSLKRLGLDTIDLYLLHNPeeqllelgeeeFYDRLEEAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 122 RAFEKLYKDKRVRAIGV----------CNFHEHHLKELMEDAEIA------------PMvNQIEL----HPQLTQ---EP 172
Cdd:cd19099 165 EALEEAVAEGKIRYYGIstwdgfrappALPGHLSLEKLVAAAEEVggdnhhfkviqlPL-NLLEPealtEKNTVKgeaLS 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16802865 173 LRKFCAENNIVVEAWSPLGNGKLLS-NPEIKAIADAHGKSVAQVILRW 219
Cdd:cd19099 244 LLEAAKELGLGVIASRPLNQGQLLGeLRLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
21-219 |
7.82e-15 |
|
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: 72.97 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 21 GVWKVQDGDEAVNSVKwaiEAGYISIDTAAAY---KNEEGVGQAikesGIKREDLFVTTKlWNAEQG----YESTLAAFD 93
Cdd:cd19075 15 RFTTAEAAAELLDAFL---ERGHTEIDTARVYpdgTSEELLGEL----GLGERGFKIDTK-ANPGVGgglsPENVRKQLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 94 ESLRKLELDYVDLYLIHWPVKG-KFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAE----IAPMVNQ------- 161
Cdd:cd19075 87 TSLKRLKVDKVDVFYLHAPDRStPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVYQgmynait 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 162 ----IELHPQltqepLRKFcaenNIVVEAWSPLGNGkLLSNP-------------------------------------E 200
Cdd:cd19075 167 rqveTELFPC-----LRKL----GIRFYAYSPLAGG-FLTGKykysedkagggrfdpnnalgklyrdrywkpsyfealeK 236
|
250
....*....|....*....
gi 16802865 201 IKAIADAHGKSVAQVILRW 219
Cdd:cd19075 237 VEEAAEKEGISLAEAALRW 255
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
12-219 |
1.39e-14 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 72.24 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVW----KVQDGDEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKESGIKREDLFVTTKL-WNAEQ 83
Cdd:cd19143 10 GLKVSALSFGSWvtfgNQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 84 GYEST--------LAAFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRV--------------RAIGVCn 140
Cdd:cd19143 90 PPPNDrglsrkhiVEGTKASLKRLQLDYVDLVFCHRPdPATPIEETVRAMNDLIDQGKAfywgtsewsaqqieEAHEIA- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 141 fHEHHLkelmedaeIAPMVNQIE---LHPQLTQEPLRKFCAENNIVVEAWSPLGNGKL-------------LSNP----- 199
Cdd:cd19143 169 -DRLGL--------IPPVMEQPQynlFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLtgkynngipegsrLALPgyewl 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 16802865 200 ----------------EIKAIADAHGKSVAQVILRW 219
Cdd:cd19143 240 kdrkeelgqekiekvrKLKPIAEELGCSLAQLAIAW 275
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-138 |
7.12e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 69.48 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 29 DEAVNSVKWAIEAGYISIDTAAAYKN-EEGVGQAIKesgiKREDLFVTTKL----WNAEQGYESTLAAFDESLRKLELDY 103
Cdd:cd19097 26 KEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLK----RLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDS 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 16802865 104 VDLYLIHWP--VKGKFKDTWRAFEKLYKDKRVRAIGV 138
Cdd:cd19097 102 LDGLLLHNPddLLKHGGKLVEALLELKKEGLIRKIGV 138
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
6-256 |
1.09e-13 |
|
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: 69.77 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 6 TVKL-ANGVEMPRLGFGVWKVQDGD-------EAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKesGIKREDLFV 74
Cdd:cd19145 2 RVKLgSQGLEVSAQGLGCMGLSGDYgapkpeeEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK--DGPREKVQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 75 TTKLWNAEQGYESTL---------AAFDESLRKLELDYVDLYLIHW-----PVkgkfKDTWRAFEKLYKDKRVRAIGvcn 140
Cdd:cd19145 80 ATKFGIHEIGGSGVEvrgdpayvrAACEASLKRLDVDYIDLYYQHRidttvPI----EITMGELKKLVEEGKIKYIG--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 141 fhehhLKELMEDA-----EIAPMVN-QIE--LHPQLTQEPLRKFCAENNIVVEAWSPLGNG------KLLSNPE------ 200
Cdd:cd19145 153 -----LSEASADTirrahAVHPITAvQLEwsLWTRDIEEEIIPTCRELGIGIVPYSPLGRGffagkaKLEELLEnsdvrk 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16802865 201 -------------------IKAIADAHGKSVAQVILRWDLQIG--VVTIPKSVHQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19145 228 shprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-259 |
1.31e-13 |
|
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: 69.28 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 38 AIEAGYISIDTAAAY---KNEEGVGQAIKEsgIKREDLFVTTKL--WNAEQGYESTLAAFDESLRKLELDYVDLYLIHWP 112
Cdd:cd19103 41 AMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 113 VkgkfkDTWRAFEK---LYKDKRVRAIGVCNFHEHHLK---ELMEDA--EIAPMVNQIEL-HPQLTQEPLRKFCAENNIV 183
Cdd:cd19103 119 A-----DVERWTPElipLLKSGKVKHVGVSNHNLAEIKranEILAKAgvSLSAVQNHYSLlYRSSEEAGILDYCKENGIT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 184 VEAWS-----------------PLGNGKLLS-----------NPEIKAIADAHGKSVAQVILRWDLQIGVVTI--PKSVH 233
Cdd:cd19103 194 FFAYMvleqgalsgkydtkhplPEGSGRAETynpllpqleelTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIigVTKPH 273
|
250 260
....*....|....*....|....*.
gi 16802865 234 QerIIQNADIFDFELTEEEVAKISGL 259
Cdd:cd19103 274 H--VEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-256 |
2.76e-12 |
|
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: 65.34 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFG----VWK---VQDgDEAVNSVKWAIEAGYISIDTAAAY------KNEEGVGQAIKESGIKREDLFVTTK 77
Cdd:cd19077 1 NGKLVGPIGLGlmglTWRpnpTPD-EEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 78 --LWNAEQGYESTLAAF----DESLRKL-ELDYVDLY-LIHWPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKEL 149
Cdd:cd19077 80 ggLDPDTLRPDGSPEAVrksiENILRALgGTKKIDIFePARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 150 MEDAEIApmVNQIELHPqLTQEPLR----KFCAENNIVVEAWSPLGNGkLLS---------------------NPE---- 200
Cdd:cd19077 160 HAVHPIA--AVEVEYSL-FSREIEEngvlETCAELGIPIIAYSPLGRG-LLTgriksladipegdfrrhldrfNGEnfek 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16802865 201 -------IKAIADAHGKSVAQVILRWDLQIG---VVTIPKSVHQERIIQNADIFDFELTEEEVAKI 256
Cdd:cd19077 236 nlklvdaLQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-229 |
1.82e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 63.12 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 39 IEAGYISIDTAAAY----------KNEEGVGQAIKESGiKREDLFVTTKL---------WNAE---QGYESTLAAFDESL 96
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDRG-NRDDVVIATKVgagprdpdgGPESpegLSAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 97 RKLELDYVDLYLIHWPVKGK-FKDTWRAFEKLYKDKRVRAIGVCNFH------------EHHLKE---------LMEDAE 154
Cdd:cd19752 106 RRLGTDYIDLYYAHVDDRDTpLEETLEAFNELVKAGKVRAIGASNFAawrlerarqiarQQGWAEfsaiqqrhsYLRPRP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 155 IAPMVNQIELHPQLTQeplrkFCAEN-NIVVEAWSPLGNG------KLLSNPE-----------IKAIADAHGKSVAQVI 216
Cdd:cd19752 186 GADFGVQRIVTDELLD-----YASSRpDLTLLAYSPLLSGaytrpdRPLPEQYdgpdsdarlavLEEVAGELGATPNQVV 260
|
250
....*....|...
gi 16802865 217 LRWDLQIGVVTIP 229
Cdd:cd19752 261 LAWLLHRTPAIIP 273
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
16-251 |
2.17e-11 |
|
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: 62.76 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFGVWKV-----QDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKesGIKREDLFVTTKL--------- 78
Cdd:cd19162 1 PRLGLGAASLgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 ---------WN-AEQGyesTLAAFDESLRKLELDYVDLYLIHWPVKG---KFKDTWRAFEKLYKDKRVRAIGVCNFHEHH 145
Cdd:cd19162 79 grpagadrrFDfSADG---IRRSIEASLERLGLDRLDLVFLHDPDRHllqALTDAFPALEELRAEGVVGAIGVGVTDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 146 LKELMEDAEI-APMV-NQIELHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNP--------------------EIKA 203
Cdd:cd19162 156 LLRAARRADVdVVMVaGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDpagdrydyrpatpevlararRLAA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16802865 204 IADAHGKSVAQVILRWDLQ----IGVVTIPKSVHQerIIQNADIFDFELTEE 251
Cdd:cd19162 236 VCRRYGVPLPAAALQFPLRhpavASVVVGAASPAE--LRDNLALLRTPIPAE 285
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
29-234 |
6.89e-11 |
|
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: 61.40 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 29 DEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKESGIKREDLFVTTKLWN-AEQGYESTL----AAFDESLRKLE 100
Cdd:cd19153 33 DEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVGRyRDSEFDYSAervrASVATSLERLH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 101 LDYVDLYLIHWPVKGKF----KDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAEIAPM-VNQIELHPQLTQEPLRK 175
Cdd:cd19153 113 TTYLDVVYLHDIEFVDYdtlvDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLdAVLSYCHLTLQDARLES 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 176 ----FCAENNIVVEAWSPLGNGKLLS---------NPEIK---AIADAH----GKSVAQVILRWDL--QIGVVTI---PK 230
Cdd:cd19153 193 dapgLVRGAGPHVINASPLSMGLLTSqgpppwhpaSGELRhyaAAADAVcasvEASLPDLALQYSLaaHAGVGTVllgPS 272
|
....
gi 16802865 231 SVHQ 234
Cdd:cd19153 273 SLAQ 276
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
11-202 |
1.12e-10 |
|
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: 60.94 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWKV--QDGDEAVNS--VKWAIEAGYISIDTAAAYKN---EEGVGQAIKESGIKREDLFVTTKL-WN-- 80
Cdd:cd19142 9 SGLRVSNVGLGTWSTfsTAISEEQAEeiVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIyWSyg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 81 -AEQGY--ESTLAAFDESLRKLELDYVDLYLIH-----WPVkgkfKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMED 152
Cdd:cd19142 89 sEERGLsrKHIIESVRASLRRLQLDYIDIVIIHkadpmCPM----EEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16802865 153 AE----IAPMVNQIELHPqLTQEPLRKFCAE--NNIVVE--AWSPLGNGKLLSNPEIK 202
Cdd:cd19142 165 ARqfncPTPICEQSEYHM-FCREKMELYMPElyNKVGVGliTWSPLSLGLDPGISEET 221
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
16-251 |
4.77e-10 |
|
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: 59.16 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 16 PRLGFG------VWKVQDGDEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGikREDLFVTTKL-------- 78
Cdd:cd19152 1 PKLGFGtaplgnLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYgagLSEERLGAALRELG--REDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 ----------WN-----AEQ--GYESTLAAFDESLRKLELDYVDLYLIHWPVKGKFKDTW------------RAFEKLYK 129
Cdd:cd19152 79 eveptfepgfWNplpfdAVFdySYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgafRALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 130 DKRVRAIGV-CNFHEhHLKELMEDAEI-APMV-NQIELhpqLTQEPLRKF---CAENNIVVEAWSPLGNGkLLSNPE--- 200
Cdd:cd19152 159 EGVIKAIGLgVNDWE-VILRILEEADLdWVMLaGRYTL---LDHSAARELlpeCEKRGVKVVNAGPFNSG-FLAGGDnfd 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 201 -----------------IKAIADAHGKSVAQVILRWDLQIGVVT--IPKSVHQERIIQNADIFDFELTEE 251
Cdd:cd19152 234 yyeygpappeliarrdrIEALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVALLATEIPAA 303
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
12-138 |
6.30e-10 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 58.64 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFG------VWKVQDGDEAVNSVKWAIEAGYISIDTAAAYKN---EEGVGQAIKESGIKREDLFVTTKLWNAE 82
Cdd:PLN02587 8 GLKVSSVGFGasplgsVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCGRYG 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16802865 83 QGY----ESTLAAFDESLRKLELDYVDLYLIHWPVKGKF----KDTWRAFEKLYKDKRVRAIGV 138
Cdd:PLN02587 88 EGFdfsaERVTKSVDESLARLQLDYVDILHCHDIEFGSLdqivNETIPALQKLKESGKVRFIGI 151
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
12-254 |
3.44e-09 |
|
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: 56.50 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWK----VQDGDEAVNSVKWAIEAGYISIDTAAAYKNEEGVgqAIKESGI--------KREDLFVTTKLw 79
Cdd:cd19089 8 GLHLPAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLANNYGPPPGS--AEENFGRilkrdlrpYRDELVISTKA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 80 naeqGYES-------------TLAAFDESLRKLELDYVDLYLIH-----WPVkgkfKDTWRAFEKLYKDKRVRAIGVCNF 141
Cdd:cd19089 85 ----GYGMwpgpygdggsrkyLLASLDQSLKRMGLDYVDIFYHHrydpdTPL----EETMTALADAVRSGKALYVGISNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 142 HE---HHLKELMEDAEIAPMVNQIE---LHPQLtQEPLRKFCAENNIVVEAWSPLGNGkLLS------------------ 197
Cdd:cd19089 157 PGakaRRAIALLRELGVPLIIHQPRyslLDRWA-EDGLLEVLEEAGIGFIAFSPLAQG-LLTdkylngippdsrraaesk 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16802865 198 -------NPE-------IKAIADAHGKSVAQVILRWDLQIGVVTipkSV-----HQERIIQNADIFD-FELTEEEVA 254
Cdd:cd19089 235 flteealTPEkleqlrkLNKIAAKRGQSLAQLALSWVLRDPRVT---SVligasSPSQLEDNVAALKnLDFSEEELA 308
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
11-256 |
1.81e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 54.61 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWK----VQDGDEAVNSVKWAIEAGYISIDTAAAY-----KNEEGVGQAIKES-GIKREDLFVTTK--- 77
Cdd:PRK09912 21 SGLRLPALSLGLWHnfghVNALESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDfAAYRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 78 -LWNAEQGYEST----LAAFDESLRKLELDYVDLYLIHWPVKGK-FKDTWRAFEKLYKDKRVRAIGVCNF---HEHHLKE 148
Cdd:PRK09912 101 dMWPGPYGSGGSrkylLASLDQSLKRMGLEYVDIFYSHRVDENTpMEETASALAHAVQSGKALYVGISSYspeRTQKMVE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 149 LMEDAEIAPMVNQIE---LHPQLTQEPLRKFCAENNIVVEAWSPLGNG----------------------------KLLS 197
Cdd:PRK09912 181 LLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKMLT 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16802865 198 NPEIKAI------ADAHGKSVAQVILRW---DLQIGVVTIPKSvHQERIIQNADIF-DFELTEEEVAKI 256
Cdd:PRK09912 261 EANLNSLrllnemAQQRGQSMAQMALSWllkDERVTSVLIGAS-RAEQLEENVQALnNLTFSTEELAQI 328
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
37-140 |
2.39e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 54.09 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 37 WAIEAGYISIDTAAAYK----------NEEGVGQAIKESGiKREDLFVTTKLWNAEQGYESTL------------AAFDE 94
Cdd:PRK10625 38 YAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSGPSRNNDKGIrpnqaldrknirEALHD 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16802865 95 SLRKLELDYVDLYLIHWPVK-----GKFKDTW----------RAFEKLYKDKR---VRAIGVCN 140
Cdd:PRK10625 117 SLKRLQTDYLDLYQVHWPQRptncfGKLGYSWtdsapavsllETLDALAEQQRagkIRYIGVSN 180
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
12-254 |
6.04e-08 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 52.79 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVW-KVQDGDEAVNS---VKWAIEAGYISIDTAAAY-----KNEEGVGQAIKESGIK-REDLFVTTK---- 77
Cdd:cd19151 9 GLKLPAISLGLWhNFGDVDRYENSramLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKagyt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 78 LWNAEQG----YESTLAAFDESLRKLELDYVDLYLIHWPVKGK-FKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKE---L 149
Cdd:cd19151 89 MWPGPYGdwgsKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETpLEETMGALDQIVRQGKALYVGISNYPPEEAREaaaI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 150 MEDAEIAPMVNQ--IELHPQLTQEPLRKFCAENNIVVEAWSPLGNGkLLSN------PE--------------------- 200
Cdd:cd19151 169 LKDLGTPCLIHQpkYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQG-LLTDrylngiPEdsraakgssflkpeqiteekl 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16802865 201 -----IKAIADAHGKSVAQVILRWDLQIGVVT---IPKSvHQERIIQNADIFD-FELTEEEVA 254
Cdd:cd19151 248 akvrrLNEIAQARGQKLAQMALAWVLRNKRVTsvlIGAS-KPSQIEDAVGALDnREFSEEELA 309
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
12-254 |
3.00e-07 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 50.53 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKVQDGDEAVNS----VKWAIEAGYISIDTAAAY-----KNEEGVGQAIKES-GIKREDLFVTTK---- 77
Cdd:cd19150 9 GLKLPALSLGLWHNFGDDTPLETqraiLRTAFDLGITHFDLANNYgpppgSAEENFGRILREDfAGYRDELIISTKagyd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 78 LWNAEQG----YESTLAAFDESLRKLELDYVDLYLIH-WPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKE---L 149
Cdd:cd19150 89 MWPGPYGewgsRKYLLASLDQSLKRMGLDYVDIFYSHrFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREaaaI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 150 MEDAEIAPMVNQIE---LHPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSN-----PE--------------------- 200
Cdd:cd19150 169 LRELGTPLLIHQPSynmLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKylngiPEgsraskerslspkmlteanln 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16802865 201 ----IKAIADAHGKSVAQVILRWDLQIGVVT---IPKSvHQERIIQNADIFD-FELTEEEVA 254
Cdd:cd19150 249 siraLNEIAQKRGQSLAQMALAWVLRDGRVTsalIGAS-RPEQLEENVGALDnLTFSADELA 309
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
11-106 |
1.44e-06 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 48.83 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWKV---QDGDE-AVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGIKREDLFVTTKL-WNAE 82
Cdd:cd19160 11 SGLRVSCLGLGTWVTfgsQISDEtAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVVTTKIyWGGQ 90
|
90 100 110
....*....|....*....|....*....|
gi 16802865 83 QGYESTLA------AFDESLRKLELDYVDL 106
Cdd:cd19160 91 AETERGLSrkhiieGLRGSLDRLQLEYVDI 120
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
29-252 |
4.01e-06 |
|
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: 47.32 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 29 DEAVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGikREDLFVTTK----LWNAEQG----------------- 84
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYghgLAEHRLGDFLREKP--RDEFVLSTKvgrlLKPAREGsvpdpngfvdplpfeiv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 85 ----YESTLAAFDESLRKLELDYVDLYLIH---------WPVKGKFKDT----WRAFEKLYKDKRVRAIG-------VCN 140
Cdd:cd19161 98 ydysYDGIMRSFEDSLQRLGLNRIDILYVHdigvythgdRKERHHFAQLmsggFKALEELKKAGVIKAFGlgvnevqICL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 141 fhehhlkELMEDAEI--APMVNQIELHPQLTQEPLRKFCAENNIVVEAWSPLgNGKLLSNP------------------- 199
Cdd:cd19161 178 -------EALDEADLdcFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVF-NSGILATGtksgakfnygdapaeiisr 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 200 --EIKAIADAHGKSVAQVILRWDLQIGVVtipKSV-----HQERIIQNADIFDFELTEEE 252
Cdd:cd19161 250 vmEIEKICDAYNVPLAAAALQFPLRHPAV---ASVltgarNPAQLRQNVEAFQTDIPEEL 306
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
11-112 |
4.72e-06 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 46.96 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWKV---QDGDE-AVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGIKREDLFVTTKL-WNAE 82
Cdd:cd19159 9 SGLRVSCLGLGTWVTfggQISDEvAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 16802865 83 QGYESTLA------AFDESLRKLELDYVDLYLIHWP 112
Cdd:cd19159 89 AETERGLSrkhiieGLKGSLQRLQLEYVDVVFANRP 124
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
12-112 |
1.13e-05 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 45.90 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 12 GVEMPRLGFGVWKV---QDGDE-AVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGIKREDLFVTTKL-WNA-- 81
Cdd:cd19141 9 GLRVSCLGLGTWVTfgsQISDEvAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKKGWRRSSYVITTKIfWGGka 88
|
90 100 110
....*....|....*....|....*....|....*
gi 16802865 82 --EQGY--ESTLAAFDESLRKLELDYVDLYLIHWP 112
Cdd:cd19141 89 etERGLsrKHIIEGLKASLERLQLEYVDIVFANRP 123
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
17-260 |
1.57e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 45.35 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 17 RLGFG--------VW-KVQDGDEAVNSVKWAIEAGYISIDTAAAY----KNeegvgQAIKES-GIKREDLFVTTKL---- 78
Cdd:PRK10376 19 RLGYGamqlagpgVFgPPKDRDAAIAVLREAVALGVNHIDTSDFYgphvTN-----QLIREAlHPYPDDLTIVTKVgarr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 79 -----WNAEQGYESTLAAFDESLRKLELDYVDL------YLIHWPVKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLK 147
Cdd:PRK10376 94 gedgsWLPAFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 148 ELMEDAEIAPMVNQIELhPQLTQEPLRKFCAENNIVVEAWSPLGNGKLLSNPEIKAIADAHGKSVAQVILRWDLQIG--V 225
Cdd:PRK10376 174 EARKIAEIVCVQNHYNL-AHRADDALIDALARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnI 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 16802865 226 VTIP--KSVHQERiiQNADIFDFELTEEEVAKISGLN 260
Cdd:PRK10376 253 LLIPgtSSVAHLR--ENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
11-193 |
1.61e-05 |
|
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: 45.46 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 11 NGVEMPRLGFGVWKVQDG---DE-AVNSVKWAIEAGYISIDTAAAY---KNEEGVGQAIKESGIKREDLFVTTKL-WNAE 82
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGqitDEmAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 83 QGYESTLA------AFDESLRKLELDYVDLYLIHWP-VKGKFKDTWRAFEKLYKDKRVRAIGVCNFHEHHLKELMEDAE- 154
Cdd:cd19158 89 AETERGLSrkhiieGLKASLERLQLEYVDVVFANRPdPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16802865 155 ---IAPMVNQIELH---PQLTQEPLRKFCAENNIVVEAWSPLGNG 193
Cdd:cd19158 169 fnlIPPICEQAEYHmfqREKVEVQLPELFHKIGVGAMTWSPLACG 213
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
40-111 |
2.39e-05 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 44.82 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 40 EAGYISIDTAAAYKNEEG---VGQAIKESGIkREDLFVTTKLWNAEQGYE---------------STLAAFDESLRKLEL 101
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDYKAYEvgkgkavnycgnhkrSLHVSVRDSLRKLQT 123
|
90
....*....|
gi 16802865 102 DYVDLYLIHW 111
Cdd:cd19147 124 DWIDILYVHW 133
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
40-111 |
2.91e-03 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 38.56 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 40 EAGYISIDTAAAYKNEEG---VGQAIKESGIkREDLFVTTKLWNAEQGYE--------------STLAAFDESLRKLELD 102
Cdd:cd19146 46 EQGGNFIDTANNYQGEESerwVGEWMASRGN-RDEMVLATKYTTGYRRGGpikiksnyqgnhakSLRLSVEASLKKLQTS 124
|
....*....
gi 16802865 103 YVDLYLIHW 111
Cdd:cd19146 125 YIDILYVHW 133
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
35-138 |
5.57e-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: 37.64 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16802865 35 VKWAIEAGYISIDTAAAYKNEEGV-GQAIK--ESGIKREDLFVTTKLwnaeqGYESTlAAFD-----------ESLRKLE 100
Cdd:cd19164 40 VRRALELGIRAFDTSPYYGPSEIIlGRALKalRDEFPRDTYFIITKV-----GRYGP-DDFDyspewirasveRSLRRLH 113
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16802865 101 LDYVDLYLIHWPVKGKFKDTWRAFEKL--YKDK-RVRAIGV 138
Cdd:cd19164 114 TDYLDLVYLHDVEFVADEEVLEALKELfkLKDEgKIRNVGI 154
|
|
| |
