|
Name |
Accession |
Description |
Interval |
E-value |
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-272 |
9.08e-152 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 424.08 E-value: 9.08e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGRE 87
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEE-AAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA----SGVPREELFVTTKVWNDNHGYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 88 NVAAAYEASLSRLGLKYLDLYLVHWPGTNEavMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQVEY 167
Cdd:COG0656 76 DTLAAFEESLERLGLDYLDLYLIHWPGPGP--YVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 168 HPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIF 247
Cdd:COG0656 154 HPYLQQRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAF 233
|
250 260
....*....|....*....|....*
gi 446375467 248 DFELSDEQMTRIDGLNQDKRIGPDP 272
Cdd:COG0656 234 DFELSDEDMAAIDALDRGERLGPDP 258
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
5-272 |
7.14e-134 |
|
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: 379.43 E-value: 7.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGlestGIAREDLFITSKLYFEDF 84
Cdd:cd19157 3 TLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKES----GIPREELFITSKVWNADQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEavMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQ 164
Cdd:cd19157 79 GYDSTLKAFEASLERLGLDYLDLYLIHWPVKGK--YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 165 VEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENF 244
Cdd:cd19157 157 VEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENA 236
|
250 260
....*....|....*....|....*...
gi 446375467 245 QIFDFELSDEQMTRIDGLNQDKRIGPDP 272
Cdd:cd19157 237 DVFDFELSQEDMDKIDALNENLRVGPDP 264
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
12-260 |
6.40e-124 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 353.32 E-value: 6.40e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 12 MPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGRENVAA 91
Cdd:cd19071 1 MPLIGLGTYKLKPEE-TAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRE----SGVPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 92 AYEASLSRLGLKYLDLYLVHWPGTNEAV-----MVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQVE 166
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKEGgskeaRLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 167 YHPYLTQHKLKLYLAAQRIVMESWSPLMNA--QILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENF 244
Cdd:cd19071 156 LHPYLQQKELVEFCKEHGIVVQAYSPLGRGrrPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENL 235
|
250
....*....|....*.
gi 446375467 245 QIFDFELSDEQMTRID 260
Cdd:cd19071 236 DVFDFELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
3-263 |
8.76e-120 |
|
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: 343.20 E-value: 8.76e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 3 VKTFYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGlestGIAREDLFITSKLYFE 82
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDE-AASAVREALEVGYRSIDTAAIYGNEEGVGKAIRAS----GVPREELFITTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 83 DFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVI 162
Cdd:cd19131 76 DQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 163 NQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISE 242
Cdd:cd19131 156 NQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAE 235
|
250 260
....*....|....*....|.
gi 446375467 243 NFQIFDFELSDEQMTRIDGLN 263
Cdd:cd19131 236 NFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-263 |
2.48e-118 |
|
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: 339.41 E-value: 2.48e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRagleSTGIAREDLFITSKLYFEDF 84
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIR----ESGVPREELFVTTKLWNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEavMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQ 164
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK--FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 165 VEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENF 244
Cdd:cd19126 156 VEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENA 235
|
250
....*....|....*....
gi 446375467 245 QIFDFELSDEQMTRIDGLN 263
Cdd:cd19126 236 DIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-274 |
7.43e-117 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 336.41 E-value: 7.43e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 4 KTFYNGNTMPQIGLGTFRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRagleSTGIAREDLFITSKLYFED 83
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR----ESGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 84 FGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEavMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVIN 163
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK--FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 164 QVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISEN 243
Cdd:cd19156 155 QIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQEN 234
|
250 260 270
....*....|....*....|....*....|.
gi 446375467 244 FQIFDFELSDEQMTRIDGLNQDKRIGPDPKN 274
Cdd:cd19156 235 FDVFDFELTAEEIRQIDGLNTDHRYGPDPDN 265
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-263 |
1.02e-112 |
|
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: 325.30 E-value: 1.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDF 84
Cdd:cd19133 2 TLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK----SGIPREELFITTKLWIQDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEavmVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQ 164
Cdd:cd19133 78 GYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDV---YGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 165 VEYHPYLTQHKLKLYLAAQRIVMESWSPLM--NAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISE 242
Cdd:cd19133 155 IETHPFNQQIEAVEFLKKYGVQIEAWGPFAegRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAE 234
|
250 260
....*....|....*....|.
gi 446375467 243 NFQIFDFELSDEQMTRIDGLN 263
Cdd:cd19133 235 NFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
12-262 |
1.93e-111 |
|
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: 322.27 E-value: 1.93e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 12 MPQIGLGTFRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGRENVAA 91
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 92 AYEASLSRLGLKYLDLYLVHWPGT---------NEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVI 162
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVqglkpsdprNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 163 NQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQ--ILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRI 240
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDlrLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERI 240
|
250 260
....*....|....*....|..
gi 446375467 241 SENFQIFDFELSDEQMTRIDGL 262
Cdd:cd19136 241 AENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-263 |
1.59e-105 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 307.41 E-value: 1.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDF 84
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPPEE-TADAVATALADGYRLIDTAAAYGNEREVGEGIRR----SGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWPGTNE-AVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVIN 163
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDfDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 164 QVEYHPYLTQHKLKLYLAAQRIVMESWSPL------------MNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTI 231
Cdd:cd19127 157 QVELHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAI 236
|
250 260 270
....*....|....*....|....*....|..
gi 446375467 232 PKSVTPNRISENFQIFDFELSDEQMTRIDGLN 263
Cdd:cd19127 237 PKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-262 |
2.57e-105 |
|
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: 306.94 E-value: 2.57e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRveNDENCMESVKYAI-EQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGR 86
Cdd:cd19135 9 NGVEMPILGLGTSH--SGGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTTKLWPSDYGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 87 ENVAAAYEASLSRLGLKYLDLYLVHWPGT------NEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKP 160
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPDCpssgknVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 161 VINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRI 240
Cdd:cd19135 163 HVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERI 242
|
250 260
....*....|....*....|..
gi 446375467 241 SENFQIFDFELSDEQMTRIDGL 262
Cdd:cd19135 243 KENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
9-264 |
2.35e-104 |
|
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: 304.19 E-value: 2.35e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFRVeNDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGREN 88
Cdd:cd19132 4 GTQIPAIGFGTYPL-KGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRHHGYEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 89 VAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQVEYH 168
Cdd:cd19132 79 ALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 169 PYLTQHKLKLYLAAQRIVMESWSPL-MNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIF 247
Cdd:cd19132 159 PYFPQAEQRAYHREHGIVTQSWSPLgRGSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIF 238
|
250
....*....|....*..
gi 446375467 248 DFELSDEQMTRIDGLNQ 264
Cdd:cd19132 239 DFELSDEDMAAIAALDR 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
5-272 |
2.48e-102 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 299.68 E-value: 2.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGiragLESTGIAREDLFITSKLYFEDf 84
Cdd:PRK11565 8 KLQDGNVMPQLGLGVWQASNEE-VITAIHKALEVGYRSIDTAAIYKNEEGVGKA----LKEASVAREELFITTKLWNDD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 gRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQ 164
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 165 VEYHPYLTQHKLKLYLAAQRIVMESWSPLmnAQ----ILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRI 240
Cdd:PRK11565 161 IELHPLMQQRQLHAWNATHKIQTESWSPL--AQggkgVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRI 238
|
250 260 270
....*....|....*....|....*....|..
gi 446375467 241 SENFQIFDFELSDEQMTRIDGLNQDKRIGPDP 272
Cdd:PRK11565 239 AENFDVFDFRLDKDELGEIAKLDQGKRLGPDP 270
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-268 |
1.66e-100 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 295.73 E-value: 1.66e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGRE 87
Cdd:cd19116 7 DGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHERE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 88 NVAAAYEASLSRLGLKYLDLYLVHWP-GTNEAVM--------------VDTWKGMEDLYKNNNVKNIGVSNFEPEHLEAL 152
Cdd:cd19116 87 QVEPALRESLKRLGLDYVDLYLIHWPvAFKENNDsesngdgslsdidyLETWRGMEDLVKLGLTRSIGVSNFNSEQINRL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 153 LAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL--MNAQI-------LNDETIKDIAQELGKSPAQVVLRWN 223
Cdd:cd19116 167 LSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFgrLVPRGqtnppprLDDPTLVAIAKKYGKTTAQIVLRYL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446375467 224 VQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRI 268
Cdd:cd19116 247 IDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-263 |
1.37e-94 |
|
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: 279.49 E-value: 1.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVEnDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGRE 87
Cdd:cd19130 6 DGNSIPQLGYGVFKVP-PADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAA----SGIPRDELFVTTKLWNDRHDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 88 NVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQVEY 167
Cdd:cd19130 81 EPAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 168 HPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIF 247
Cdd:cd19130 161 HPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVF 240
|
250
....*....|....*.
gi 446375467 248 DFELSDEQMTRIDGLN 263
Cdd:cd19130 241 DFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
12-260 |
1.59e-94 |
|
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: 278.77 E-value: 1.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 12 MPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGRENVAA 91
Cdd:cd19073 1 IPALGLGTWQLRGDD-CANAVKEALELGYRHIDTAEIYNNEAEVGEAIAE----SGVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 92 AYEASLSRLGLKYLDLYLVHWPGtNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQVEYHPYL 171
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWPN-PTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFHPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 172 TQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFEL 251
Cdd:cd19073 155 YQAELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWEL 234
|
....*....
gi 446375467 252 SDEQMTRID 260
Cdd:cd19073 235 TSEDVAKID 243
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
6-267 |
5.58e-93 |
|
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: 276.96 E-value: 5.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 6 FYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGL-ESTGIAREDLFITSKLYFEDF 84
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQ-VKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWP---------------GTNEAVMVD---TWKGMEDLYKNNNVKNIGVSNFEP 146
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpknpdGTIRYDSTHykeTWKAMEKLVDKGLVKAIGLSNFNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 147 EHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMN----------AQILNDETIKDIAQELGKSPA 216
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSpdrpwakpdePVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446375467 217 QVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKR 267
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWR 290
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-268 |
2.64e-92 |
|
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: 274.61 E-value: 2.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGREN 88
Cdd:cd19125 8 GAKIPAVGLGTWQADPGV-VGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAPED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 89 VAAAYEASLSRLGLKYLDLYLVHWP---------GTNEAV----MVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQ 155
Cdd:cd19125 87 VPPALEKTLKDLQLDYLDLYLIHWPvrlkkgahmPEPEEVlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 156 VSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL-------MNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAV 228
Cdd:cd19125 167 ARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgttwVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQRGT 246
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446375467 229 VTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRI 268
Cdd:cd19125 247 SVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
8-262 |
3.10e-91 |
|
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: 270.67 E-value: 3.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGRE 87
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEE-CTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAA----SGVPRDELFLTTKVWPDNYSPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 88 NVAAAYEASLSRLGLKYLDLYLVHWPGtNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQVEY 167
Cdd:cd19140 79 DFLASVEESLRKLRTDYVDLLLLHWPN-KDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 168 HPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHA-VVTIPKSVTPNRISENFQI 246
Cdd:cd19140 158 HPYLDQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQEgVAAIPKATNPERLEENLDI 237
|
250
....*....|....*.
gi 446375467 247 FDFELSDEQMTRIDGL 262
Cdd:cd19140 238 FDFTLSDEEMARIAAL 253
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-269 |
3.81e-91 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 270.96 E-value: 3.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDF 84
Cdd:cd19134 4 TLNDDNTMPVIGLGVGELSDDE-AERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAA----SGIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQ 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 165 VEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENF 244
Cdd:cd19134 159 IELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNL 238
|
250 260
....*....|....*....|....*
gi 446375467 245 QIFDFELSDEQMTRIDGLNQDKRIG 269
Cdd:cd19134 239 DVFDFELTADHMDALDGLDDGTRFR 263
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-267 |
9.98e-90 |
|
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: 268.51 E-value: 9.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 1 MEVKTFYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLY 80
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSKPGE-VGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 81 FEDFGRENVAAAYEASLSRLGLKYLDLYLVHWP-----------------GTNEAVMVDTWKGMEDLYKNNNVKNIGVSN 143
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedllSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 144 FEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL--------MNAQ----ILNDETIKDIAQEL 211
Cdd:cd19123 160 FSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLgsgdrpaaMKAEgepvLLEDPVINKIAEKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 212 GKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKR 267
Cdd:cd19123 240 GASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-262 |
2.50e-89 |
|
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: 266.97 E-value: 2.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGI-AREDLFITSKLYFEDFGR 86
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGE-VGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGvKREDLFITSKLWNNSHRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 87 ENVAAAYEASLSRLGLKYLDLYLVHWP-----GTNEAVM------------------VDTWKGMEDLYKNNNVKNIGVSN 143
Cdd:cd19118 82 EYVEPALDDTLKELGLDYLDLYLIHWPvafkpTGDLNPLtavptnggevdldlsvslVDTWKAMVELKKTGKVKSIGVSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 144 FEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMN-----AQILNDETIKDIAQELGKSPAQV 218
Cdd:cd19118 162 FSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNnlaglPLLVQHPEVKAIAAKLGKTPAQV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446375467 219 VLRWNVQHAVVTIPKSVTPNRISENFQifDFELSDEQMTRIDGL 262
Cdd:cd19118 242 LIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-267 |
9.76e-87 |
|
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: 261.19 E-value: 9.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVeNDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDF 84
Cdd:cd19154 5 TLSNGVKMPLIGLGTWQS-KGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWP----------GTNEAVM--------VDTWKGMEDLYKNNNVKNIGVSNFEP 146
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesGTMENGMsihdavdvEDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 147 EHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL-----MNA----------QILNDETIKDIAQEL 211
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgrANFtkstgvspapNLLQDPIVKAIAEKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 212 GKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKR 267
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
9-268 |
1.07e-83 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 253.49 E-value: 1.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGREN 88
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQ-VTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 89 VAAAYEASLSRLGLKYLDLYLVHWPG------------------TNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLE 150
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnviPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 151 ALLAQVSI--KPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL----------MNAQILNDETIKDIAQELGKSPAQV 218
Cdd:cd19107 160 RILNKPGLkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwakpEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446375467 219 VLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRI 268
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRA 289
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-266 |
4.56e-81 |
|
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: 245.87 E-value: 4.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYfEDFGRE 87
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNE-VAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKD----SGVPREEIFITTKLW-CTWHRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 88 nVAAAYEASLSRLGLKYLDLYLVHWPG--------------------TNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPE 147
Cdd:cd19117 84 -VEEALDQSLKKLGLDYVDLYLMHWPVpldpdgndflfkkddgtkdhEPDWDFIKTWELMQKLPATGKVKAIGVSNFSIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 148 HLEALLAQVSIK--PVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL--MNAQILNDETIKDIAQELGKSPAQVVLRWN 223
Cdd:cd19117 163 NLEKLLASPSAKivPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgsTNAPLLKEPVIIKIAKKHGKTPAQVIISWG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446375467 224 VQHAVVTIPKSVTPNRISENFQIfdFELSDEQMTRIDGLNQDK 266
Cdd:cd19117 243 LQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHKEY 283
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-276 |
2.81e-80 |
|
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: 244.48 E-value: 2.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 12 MPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGRENVAA 91
Cdd:cd19110 4 IPAVGLGTWKASPGE-VTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 92 AYEASLSRLGLKYLDLYLVHWP----------GTNEAVMV--------DTWKGMEDLYKNNNVKNIGVSNFEPEHLEALL 153
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPmgfkpgepdlPLDRSGMVipsdtdflDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 154 AQ--VSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNA----QILNDETIKDIAQELGKSPAQVVLRWNVQHA 227
Cdd:cd19110 163 NKpgLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGScegvDLIDDPVIQRIAKKHGKSPAQILIRFQIQRN 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446375467 228 VVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRIG--PDPKNLK 276
Cdd:cd19110 243 VIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLAtfPITENHK 293
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
9-260 |
5.63e-80 |
|
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: 242.52 E-value: 5.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGT-------FRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYF 81
Cdd:cd19120 1 GSKIPAIAFGTgtawyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKE----SGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 edfGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVD---TWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSI 158
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTlaeAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 159 KPVINQVEYHPYLTQHKLKL--YLAAQRIVMESWSPLM----NAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIP 232
Cdd:cd19120 154 KPAVNQIEFHPYLYPQQPALleYCREHGIVVSAYSPLSpltrDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVT 233
|
250 260
....*....|....*....|....*...
gi 446375467 233 KSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19120 234 TSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
8-264 |
1.07e-78 |
|
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: 239.86 E-value: 1.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTF-RVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGI----RAGLESTgiaREDLFITSKLYFE 82
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALaealRLGLVKS---RDELFVTSKLWCS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 83 DFGRENVAAAYEASLSRLGLKYLDLYLVHWPGT------------NEAVMVD---TWKGMEDLYKNNNVKNIGVSNFEPE 147
Cdd:cd19124 78 DAHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSlkpgkfsfpieeEDFLPFDikgVWEAMEECQRLGLTKAIGVSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 148 HLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL-------MNAQILNDETIKDIAQELGKSPAQVVL 220
Cdd:cd19124 158 KLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgapgtkwGSNAVMESDVLKEIAAAKGKTVAQVSL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446375467 221 RWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQ 264
Cdd:cd19124 238 RWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
9-267 |
5.49e-75 |
|
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: 231.23 E-value: 5.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTF---RVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFG 85
Cdd:cd19109 1 GNSIPIIGLGTYsepKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 86 RENVAAAYEASLSRLGLKYLDLYLVHWP---------------GT---NEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPE 147
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPmafkpgdeiyprdenGKwlyHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 148 HLEALLAQVSIK--PVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQ-----------ILNDETIKDIAQELGKS 214
Cdd:cd19109 161 QLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446375467 215 PAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKR 267
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-270 |
1.02e-74 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 230.58 E-value: 1.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVE--NDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFG 85
Cdd:cd19108 7 DGHFIPVLGFGTYAPEevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTFHR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 86 RENVAAAYEASLSRLGLKYLDLYLVHWP-----GTN------------EAV-MVDTWKGMEDLYKNNNVKNIGVSNFEPE 147
Cdd:cd19108 87 PELVRPALEKSLKKLQLDYVDLYLIHFPvalkpGEElfpkdengklifDTVdLCATWEAMEKCKDAGLAKSIGVSNFNRR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 148 HLEALLAQ--VSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL----------MNAQI-LNDETIKDIAQELGKS 214
Cdd:cd19108 167 QLEMILNKpgLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALgsqrdkewvdQNSPVlLEDPVLCALAKKHKRT 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 215 PAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRIGP 270
Cdd:cd19108 247 PALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLP 302
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
5-262 |
1.20e-73 |
|
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: 227.03 E-value: 1.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLEStGIAREDLFITSKLYfeDF 84
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAGE-VKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAG-GVKREDLFVTTKLW--ST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWP------GTNEAV---------------MVDTWKGMEDLYKNNNVKNIGVSN 143
Cdd:cd19121 81 YHRRVELCLDRSLKSLGLDYVDLYLVHWPvllnpnGNHDLFptlpdgsrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 144 FEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL--MNAQILNDETIKDIAQELGKSPAQVVLR 221
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446375467 222 WNVQHAVVTIPKSVTPNRISENFQIFDFElsDEQMTRIDGL 262
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
9-267 |
1.63e-72 |
|
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: 224.30 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGREN 88
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEE-VRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 89 VAAAYEASLSRLGLKYLDLYLVHWPGTN------------EAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQV 156
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFvnkkdkgerelaSSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 157 SIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNA------------QILNDETIKDIAQELGKSPAQVVLRWNV 224
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPgranqslwpdqpDLLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446375467 225 QHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKR 267
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-268 |
5.95e-71 |
|
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: 220.86 E-value: 5.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVEnDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDF 84
Cdd:cd19155 5 TFNNGEKMPVVGLGTWQSS-PEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWP----------------GTNEAVM----VDTWKGMEDLYKNNNVKNIGVSNF 144
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptGEHKQDYttdlLDIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 145 EPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMN-----------------AQILNDETIKDI 207
Cdd:cd19155 164 NREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfspgtgspsgssPDLLQDPVVKAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446375467 208 AQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRI 268
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-272 |
1.06e-70 |
|
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: 220.40 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDeNCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDF 84
Cdd:cd19113 4 KLNSGYKMPSVGFGCWKLDNA-TAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAV------------------------MVDTWKGMEDLYKNNNVKNIG 140
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVpieekyppgfycgdgdnfvyedvpILDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 141 VSNFEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSP--------LMNAQILN------DETIKD 206
Cdd:cd19113 163 VSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSfgpqsfveLNQGRALNtptlfeHDTIKS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 207 IAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRIGpDP 272
Cdd:cd19113 243 IAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFN-DP 307
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-273 |
4.48e-70 |
|
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: 218.89 E-value: 4.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDF 84
Cdd:cd19112 4 TLNSGHKMPVIGLGVWRMEPGE-IKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GreNVAAAYEASLSRLGLKYLDLYLVHWP--------GTNEAV--------------MVDTWKGMEDLYKNNNVKNIGVS 142
Cdd:cd19112 83 G--HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvGTTGSAlgedgvldidvtisLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 143 NFEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNA----------QILNDETIKDIAQELG 212
Cdd:cd19112 161 NYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAaanaewfgsvSPLDDPVLKDLAKKYG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446375467 213 KSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRIGPDPK 273
Cdd:cd19112 241 KSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPAK 301
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
12-262 |
1.72e-68 |
|
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: 212.60 E-value: 1.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 12 MPQIGLGTFRVeNDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGRENVAA 91
Cdd:cd19139 1 IPAFGLGTFRL-KDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 92 AYEASLSRLGLKYLDLYLVHWPGTNEAV-MVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVI-NQVEYHP 169
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWPSPNDEVpVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAtNQIELSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 170 YLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDF 249
Cdd:cd19139 156 YLQNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDL 235
|
250
....*....|...
gi 446375467 250 ELSDEQMTRIDGL 262
Cdd:cd19139 236 TLDADDMAAIAAL 248
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-274 |
3.14e-66 |
|
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: 208.81 E-value: 3.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVENDeNCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLY--FEDfg 85
Cdd:cd19115 9 SGYDMPLVGFGLWKVNND-TCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWntFHD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 86 RENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAV-----------------------MVDTWKGMEDLYKNNNVKNIGVS 142
Cdd:cd19115 86 GERVEPICRKQLADWGIDYFDLFLIHFPIALKYVdpavryppgwfydgkkvefsnapIQETWTAMEKLVDKGLARSIGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 143 NFEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWS---PLM-----------NAQILNDETIKDIA 208
Cdd:cd19115 166 NFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgPQSfleldlpgakdTPPLFEHDVIKSIA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 209 QELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKRIGpDPKN 274
Cdd:cd19115 246 EKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFN-NPLN 310
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
11-275 |
3.07e-65 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 204.87 E-value: 3.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 11 TMPQIGLGTFRVeNDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAglesTGIAREDLFITSKLYFEDFGRENVA 90
Cdd:PRK11172 2 SIPAFGLGTFRL-KDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLAKDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 91 AAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWkgMEDLYKNNN---VKNIGVSNFEPEHLEALLAQVSIKPV-INQVE 166
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPSPNDEVSVEEF--MQALLEAKKqglTREIGISNFTIALMKQAIAAVGAENIaTNQIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 167 YHPYLTQHKLKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQI 246
Cdd:PRK11172 155 LSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLA 234
|
250 260
....*....|....*....|....*....
gi 446375467 247 FDFELSDEQMTRIDGLNQDKRIgPDPKNL 275
Cdd:PRK11172 235 QDLQLDAEDMAAIAALDRNGRL-VSPEGL 262
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
13-262 |
2.75e-64 |
|
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: 202.75 E-value: 2.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFRVEnDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGRENVAAA 92
Cdd:cd19128 2 PRLGFGTYKIT-ESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 93 YEASLSRLGLKYLDLYLVHWP------------GTNEAVMV------DTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLA 154
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPlafdmdtdgdprDDNQIQSLskkpleDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 155 QVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNAQ------ILNDETIKDIAQELGKSPAQVVLRWNVQHAV 228
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYgdgnltFLNDSELKALATKYNTTPPQVIIAWHLQKWP 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 446375467 229 VT---IPKSVTPNRISENFQIFDFELSDEQMTRIDGL 262
Cdd:cd19128 241 KNysvIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-260 |
3.51e-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: 203.07 E-value: 3.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFrVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGRE 87
Cdd:cd19129 2 GSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 88 NVAAAYEASLSRLGLKYLDLYLVH-----WPGTNE--------------AVMVDTWKGMEDLYKNNNVKNIGVSNFEPEH 148
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHtpfafQPGDEQdprdangnviyddgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 149 LEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL---MNAQILNDETIKDIAQELGKSPAQVVLRWNVQ 225
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLghgMEPKLLEDPVITAIARRVNKTPAQVLLAWAIQ 240
|
250 260 270
....*....|....*....|....*....|....*
gi 446375467 226 HAVVTIPKSVTPNRISENFQIfdFELSDEQMTRID 260
Cdd:cd19129 241 RGTALLTTSKTPSRIRENFDI--STLPEDAMREIN 273
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
9-260 |
7.48e-63 |
|
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: 198.61 E-value: 7.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTF--------RVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaglestGIAREDLFITS 77
Cdd:cd19072 1 GEEVPVLGLGTWgigggmskDYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 78 KLYFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWPgtNEAV-MVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQV 156
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP--NPSIpIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 157 S-IKPVINQVEYHPYLTQHKLKL--YLAAQRIVMESWSPLMNAQILNDE---TIKDIAQELGKSPAQVVLRWNVQHA-VV 229
Cdd:cd19072 153 KkGPIVANQVEYNLFDREEESGLlpYCQKNGIAIIAYSPLEKGKLSNAKgspLLDEIAKKYGKTPAQIALNWLISKPnVI 232
|
250 260 270
....*....|....*....|....*....|.
gi 446375467 230 TIPKSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19072 233 AIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
9-267 |
1.21e-62 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 199.71 E-value: 1.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFRVENDEnCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLYFEDFGREN 88
Cdd:cd19114 1 GDKMPLVGFGTAKIKANE-TEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 89 VAAAYEASLSRLGLKYLDLYLVHWPGTNEAV------------------------MVDTWKGMEDLYKNNNVKNIGVSNF 144
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPIPAAYVdpaenypflwkdkelkkfpleqspMQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 145 EPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPLMNA-------------QILNDETIKDIAQEL 211
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvtkhlkhftNLLEHPVVKKLADKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 212 GKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRIDGLNQDKR 267
Cdd:cd19114 240 KRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-260 |
7.54e-62 |
|
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: 197.33 E-value: 7.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFR-VENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGLESTGIAREDLFITSKLY--FEDf 84
Cdd:cd19119 8 TGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWptFYD- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 greNVAAAYEASLSRLGLKYLDLYLVHWP-----------------GTNEAVM-------VDTWKGMEDLYKNNNVKNIG 140
Cdd:cd19119 87 ---EVERSLDESLKALGLDYVDLLLVHWPvcfekdsddsgkpftpvNDDGKTRyaasgdhITTYKQLEKIYLDGRAKAIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 141 VSNFEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL--MNAQILNDETIKDIAQELGKSPAQV 218
Cdd:cd19119 164 VSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLgsHGAPNLKNPLVKKIAEKYNVSTGDI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446375467 219 VLRWNVQHAVVTIPKSVTPNRISENFQIfdFELSDEQMTRID 260
Cdd:cd19119 244 LISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLD 283
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-260 |
2.75e-61 |
|
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: 194.77 E-value: 2.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVEND----ENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAglestgiAREDLFITS 77
Cdd:cd19138 4 TLPDGTKVPALGQGTWYMGEDpakrAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 78 KLYFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGtnEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVS 157
Cdd:cd19138 77 KVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRG--GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 158 IKP-VINQVEYH-----------PYLTQHKLKlylaaqriVMeSWSPLMNA-----QILNDETIKDIAQELGKSPAQVVL 220
Cdd:cd19138 155 GGNcAANQVLYNlgsrgieydllPWCREHGVP--------VM-AYSPLAQGgllrrGLLENPTLKEIAARHGATPAQVAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446375467 221 RWNVQH-AVVTIPKSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19138 226 AWVLRDgNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
15-263 |
2.20e-55 |
|
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: 180.59 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRVENDENCM------ESVKYAIEQGYRSIDTAKVYG---NEEQVGagiRAgLESTGIAREDLFITSKLYFEDFG 85
Cdd:pfam00248 1 IGLGTWQLGGGWGPIskeealEALRAALEAGINFIDTAEVYGdgkSEELLG---EA-LKDYPVKRDKVVIATKVPDGDGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 86 ------RENVAAAYEASLSRLGLKYLDLYLVHWPGTNeAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIK 159
Cdd:pfam00248 77 wpsggsKENIRKSLEESLKRLGTDYIDLYYLHWPDPD-TPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 160 PVINQVEYHPY--LTQHKLKLYLAAQRIVMESWSPLM----------NAQILND-----------------ETIKDIAQE 210
Cdd:pfam00248 156 IVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGgglltgkytrDPDKGPGerrrllkkgtplnlealEALEEIAKE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446375467 211 LGKSPAQVVLRWNVQHAVVT--IPKSVTPNRISENFQIFDFELSDEQMTRIDGLN 263
Cdd:pfam00248 236 HGVSPAQVALRWALSKPGVTipIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
5-260 |
2.42e-54 |
|
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: 177.81 E-value: 2.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 5 TFYNGNTMPQIGLGTFRVENDE-NCMESVKYAIEQGYRSIDTAKVYGNEEQVGAGIRAGL-ESTGIAREDLFITSKLYFE 82
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAKgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLkENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 83 DFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNE---------------AVMVD-------TWKGMEDLYKNNNVKNIG 140
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEkndqrspklgpdgkyVILKDltenpepTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 141 VSNFEPEHLEALLAQVSIKPVINQVEYHPYLTQHKLKLYLAAQRIVMESWSPL--------MNAQILNDETIKDIAQELG 212
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgsqnqvpsTGERVSENPTLNEVAEKGG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446375467 213 KSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIfdFELSDEQMTRID 260
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAIN 287
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
9-260 |
6.14e-49 |
|
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: 163.13 E-value: 6.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFRV--------ENDENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGAGIRaglestGIAREDLFITS 77
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIK------DFPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 78 KLYFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAvMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVS 157
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIP-LEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 158 IKPVINQVEY----HPYLTQHKLKlYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHA-VVTIP 232
Cdd:cd19137 154 TPIVCNQVKYnledRDPERDGLLE-YCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPnVVAIP 232
|
250 260
....*....|....*....|....*...
gi 446375467 233 KSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19137 233 KAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-260 |
1.29e-46 |
|
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: 157.77 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGT----------FRVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAGLEstgiaREDLFITSKL 79
Cdd:cd19093 3 SPLGLGTwqwgdrlwwgYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELGD-----RDEVVIATKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 --YFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLE---ALLA 154
Cdd:cd19093 78 apLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRrahKALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 155 QVSIKPVINQVEY---HPYLTQHKLKLYLAAQRIVMESWSPL----------------------MNAQILND-----ETI 204
Cdd:cd19093 158 ERGVPLASNQVEYsllYRDPEQNGLLPACDELGITLIAYSPLaqglltgkyspenpppggrrrlFGRKNLEKvqpllDAL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 205 KDIAQELGKSPAQVVLRWNVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19093 238 EEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-260 |
9.89e-44 |
|
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: 151.10 E-value: 9.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 1 MEVKTFynGNT---MPQIGLGT------FRVENDENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGAGIRaglestGI 68
Cdd:COG0667 1 MEYRRL--GRSglkVSRLGLGTmtfggpWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALK------GR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 69 AREDLFITSKLYF--------EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAvMVDTWKGMEDLYKNNNVKNIG 140
Cdd:COG0667 73 PRDDVVIATKVGRrmgpgpngRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTP-IEETLGALDELVREGKIRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 141 VSNFEPEHLEALL--AQVSIKPVINQVEYHPyLTQ---HKLKLYLAAQRIVMESWSPL---------------------- 193
Cdd:COG0667 152 VSNYSAEQLRRALaiAEGLPPIVAVQNEYSL-LDRsaeEELLPAARELGVGVLAYSPLagglltgkyrrgatfpegdraa 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446375467 194 --MNAQILND------ETIKDIAQELGKSPAQVVLRWNVQHAVVT--IPKSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:COG0667 231 tnFVQGYLTErnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTsvIPGARSPEQLEENLAAADLELSAEDLAALD 307
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
15-260 |
5.76e-39 |
|
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: 138.04 E-value: 5.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGT-------FRVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaglestGIaREDLFITSK--LYFE 82
Cdd:cd19084 7 IGLGTwaiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALK------GR-RDDVVIATKcgLRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 83 DFG-------RENVAAAYEASLSRLGLKYLDLYLVHWPGTN---EavmvDTWKGMEDLYKNNNVKNIGVSNFEPEHLEAL 152
Cdd:cd19084 80 GGKgvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNtpiE----ETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 153 LAQVSIkpVINQVEYHPYLTQHKLKL--YLAAQRIVMESWSPLMNAqIL------------ND----------------- 201
Cdd:cd19084 156 RKYGPI--VSLQPPYSMLEREIEEELlpYCRENGIGVLPYGPLAQG-LLtgkykkeptfppDDrrsrfpffrgenfeknl 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 202 ---ETIKDIAQELGKSPAQVVLRWNVQHAVVTI----PKsvTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19084 233 eivDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSaivgAK--NPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-260 |
9.69e-37 |
|
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: 131.94 E-value: 9.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGT--------FRVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAglestgiAREDLFITSKLYF 81
Cdd:cd19085 2 SRLGLGCwqfgggywWGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAvMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAqvSIKPV 161
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVP-LEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALD--AGRID 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 162 INQVEYH-----------PYLTQHKLKlylaaqriVMeSWSPLmnAQIL-------------ND---------------- 201
Cdd:cd19085 152 SNQLPYNllwraieyeilPFCREHGIG--------VL-AYSPL--AQGLltgkfssaedfppGDartrlfrhfepgaeee 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446375467 202 -----ETIKDIAQELGKSPAQVVLRWNVQHAVVTipkSV-----TPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19085 221 tfealEKLKEIADELGVTMAQLALAWVLQQPGVT---SVivgarNPEQLEENAAAVDLELSPSVLERLD 286
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
13-245 |
2.22e-34 |
|
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: 124.17 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFRV---ENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAGlestgIAREDLFITSKLYF----- 81
Cdd:cd06660 1 SRLGLGTMTFggdGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGR-----GNRDDVVIATKGGHppggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 ---EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVmVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLA---- 154
Cdd:cd06660 76 psrSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPV-EETLEALNELVREGKIRYIGVSNWSAERLAEALAyaka 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 155 QVSIKPVINQVEY---HPYLTQHKLKLYLAAQRIVMESWSPlmnaqilndetikdiaqeLGKSPAQVVLRWNVQHAVVT- 230
Cdd:cd06660 155 HGLPGFAAVQPQYsllDRSPMEEELLDWAEENGLPLLAYSP------------------LARGPAQLALAWLLSQPFVTv 216
|
250
....*....|....*.
gi 446375467 231 -IPKSVTPNRISENFQ 245
Cdd:cd06660 217 pIVGARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-259 |
1.06e-32 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 121.51 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVEN----DENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAglesTGIAREDLFITSK-- 78
Cdd:cd19092 2 EGLEVSRLVLGCMRLADwgesAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALAL----NPGLREKIEIQTKcg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 79 ------------LYFeDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTneavMVDTW---KGMEDLYKNNNVKNIGVSN 143
Cdd:cd19092 78 irlgddprpgriKHY-DTSKEHILASVEGSLKRLGTDYLDLLLLHRPDP----LMDPEevaEAFDELVKSGKVRYFGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 144 FEPEHLEALLAQVSIKPVINQVEYHPYLTQHklkL------YLAAQRIVMESWSPLMNAQILNDET---------IKDIA 208
Cdd:cd19092 153 FTPSQIELLQSYLDQPLVTNQIELSLLHTEA---IddgtldYCQLLDITPMAWSPLGGGRLFGGFDerfqrlraaLEELA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446375467 209 QELGKSPAQVVLRWNVQH--AVVTIPKSVTPNRISENFQIFDFELSDEQMTRI 259
Cdd:cd19092 230 EEYGVTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREEWYEI 282
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-262 |
2.41e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 118.16 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRV-----------ENDENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGAGIRaGLestgiaREDLFITSK-- 78
Cdd:cd19102 4 IGLGTWAIggggwgggwgpQDDRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALK-GL------RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 79 LYFEDFGR-------ENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVmVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEA 151
Cdd:cd19102 77 LLWDEEGRirrslkpASIRAECEASLRRLGVDVIDLYQIHWPDPDEPI-EEAWGALAELKEEGKVRAIGVSNFSVDQMKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 152 LLAqvsIKPV-INQVEYH-----------PYLTQHKLKL--Y-----------LAAQRIVMESW------SPLMN----A 196
Cdd:cd19102 156 CQA---IHPIaSLQPPYSllrrgieaeilPFCAEHGIGVivYspmqsglltgkMTPERVASLPAddwrrrSPFFQepnlA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446375467 197 QILN-DETIKDIAQELGKSPAQVVLRWNVQHAVVT--IPKSVTPNRISENFQIFDFELSDEQMTRIDGL 262
Cdd:cd19102 233 RNLAlVDALRPIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
32-260 |
8.86e-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: 106.16 E-value: 8.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 32 VKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAglestgiAREDLFITSKLYFE------DFG--RENVAAAYEASLSRL 100
Cdd:cd19091 45 VDIALDAGINFFDTADVYSEgesEEILGKALKG-------RRDDVLIATKVRGRmgegpnDVGlsRHHIIRAVEASLKRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 101 GLKYLDLYLVHWPgTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAqVS-----IKPVINQVEYHP----Yl 171
Cdd:cd19091 118 GTDYIDLYQLHGF-DALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALG-ISerrglARFVALQAYYSLlgrdL- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 172 tQHKLKLYLAAQRIVMESWSPL------------------------------MNAQILND--ETIKDIAQELGKSPAQVV 219
Cdd:cd19091 195 -EHELMPLALDQGVGLLVWSPLaggllsgkyrrgqpapegsrlrrtgfdfppVDRERGYDvvDALREIAKETGATPAQVA 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446375467 220 LRWNVQHAVVTipkSV-----TPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19091 274 LAWLLSRPTVS---SViigarNEEQLEDNLGAAGLSLTPEEIARLD 316
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-252 |
1.86e-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: 104.22 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFRV---------ENDENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGAGIRAglestgiAREDLFITSKL- 79
Cdd:cd19088 2 SRLGYGAMRLtgpgiwgppADREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHP-------YPDDVVIATKGg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 -------YFEDFGR-ENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVmVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEA 151
Cdd:cd19088 75 lvrtgpgWWGPDGSpEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPF-EEQLGALAELQDEGLIRHIGLSNVTVAQIEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 152 LLAQVSIKPVINQveYHPYLTQH-KLKLYLAAQRIVMESWSPLMNAQIL-NDETIKDIAQELGKSPAQVVLRWNVQHA-- 227
Cdd:cd19088 154 ARAIVRIVSVQNR--YNLANRDDeGVLDYCEAAGIAFIPWFPLGGGDLAqPGGLLAEVAARLGATPAQVALAWLLARSpv 231
|
250 260
....*....|....*....|....*
gi 446375467 228 VVTIPKSVTPNRISENFQIFDFELS 252
Cdd:cd19088 232 MLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
32-255 |
2.09e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 104.85 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 32 VKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAglesTGIAREDLFITSKL--------------YFeDFGRENVAAAYE 94
Cdd:COG4989 37 IEAALELGITTFDHADIYGGytcEALFGEALKL----SPSLREKIELQTKCgirlpseardnrvkHY-DTSKEHIIASVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 95 ASLSRLGLKYLDLYLVHWPGTneavMVD---TWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQVEYHPY- 170
Cdd:COG4989 112 GSLRRLGTDYLDLLLLHRPDP----LMDpeeVAEAFDELKASGKVRHFGVSNFTPSQFELLQSALDQPLVTNQIELSLLh 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 171 --------LTQHKLKlylaaqRIVMESWSPLMNAQILNDET---------IKDIAQELGKSPAQVVLRWNVQH--AVVTI 231
Cdd:COG4989 188 tdafddgtLDYCQLN------GITPMAWSPLAGGRLFGGFDeqfprlraaLDELAEKYGVSPEAIALAWLLRHpaGIQPV 261
|
250 260
....*....|....*....|....
gi 446375467 232 PKSVTPNRISENFQIFDFELSDEQ 255
Cdd:COG4989 262 IGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
3-260 |
1.03e-23 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 97.65 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 3 VKTFYNGNTMPQIGLGTFR---------VENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaglesTGIAR 70
Cdd:cd19079 3 VRLGNSGLKVSRLCLGCMSfgdpkwrpwVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALK-----EFAPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 71 EDLFITSKLYF--------EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPgTNEAVMVDTWKGMEDLYKNNNVKNIGVS 142
Cdd:cd19079 78 DEVVIATKVYFpmgdgpngRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRW-DYETPIEETLEALHDVVKSGKVRYIGAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 143 NFEPEHLEALLAQ---------VSIKPVINQV------EYHPYLTQHKLKLYlaaqrivmeSWSPL-------------- 193
Cdd:cd19079 157 SMYAWQFAKALHLaekngwtkfVSMQNHYNLLyreeerEMIPLCEEEGIGVI---------PWSPLargrlarpwgdtte 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 194 ------------------MNAQILNDetIKDIAQELGKSPAQVVLRWNVQHAVVTIP--KSVTPNRISENFQIFDFELSD 253
Cdd:cd19079 228 rrrsttdtaklkydyfteADKEIVDR--VEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSE 305
|
....*..
gi 446375467 254 EQMTRID 260
Cdd:cd19079 306 EEIKYLE 312
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
36-260 |
2.25e-23 |
|
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: 96.90 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 36 IEQGYRSIDTAKVYGNEEQVGAG------IRAGLESTGiAREDLFITSKLYFE------DFGRENVAAAYEASLSRLGLK 103
Cdd:cd19081 36 VDAGGNFIDTADVYSAWVPGNAGgesetiIGRWLKSRG-KRDRVVIATKVGFPmgpngpGLSRKHIRRAVEASLRRLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 104 YLDLYLVHWPgtNEAVMVD-TWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQ---------VSIKPVINQV-------E 166
Cdd:cd19081 115 YIDLYQAHWD--DPATPLEeTLGALNDLIRQGKVRYIGASNYSAWRLQEALELsrqhglpryVSLQPEYNLVdresfegE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 167 YHPYLTQHKLKL--------------YLAAQRIVMESWSPLMNAQILNDETIK------DIAQELGKSPAQVVLRWNVQH 226
Cdd:cd19081 193 LLPLCREEGIGVipysplaggfltgkYRSEADLPGSTRRGEAAKRYLNERGLRildaldEVAAEHGATPAQVALAWLLAR 272
|
250 260 270
....*....|....*....|....*....|....*.
gi 446375467 227 AVVTIP--KSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19081 273 PGVTAPiaGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
14-254 |
4.85e-23 |
|
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: 95.74 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 14 QIGLGTFRV----ENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaglestGIAREDLFITSKLYF----- 81
Cdd:cd19074 6 ELSLGTWLTfggqVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK------GWPRESYVISTKVFWptgpg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 -EDFG--RENVAAAYEASLSRLGLKYLDLYLVHWPGTnEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEA---LLAQ 155
Cdd:cd19074 80 pNDRGlsRKHIFESIHASLKRLQLDYVDIYYCHRYDP-ETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEahdLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 156 VS-IKPVINQVEYHpYLTQHK---LKLYLAAQRIVMESWSPL-------------------------MNAQILNDET--- 203
Cdd:cd19074 159 FGlIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsrsratdedNRDKKRRLLTden 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446375467 204 ------IKDIAQELGKSPAQVVLRWNVQHAVVT--IPKSVTPNRISENFQIFDFELSDE 254
Cdd:cd19074 238 lekvkkLKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-262 |
8.06e-23 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 96.04 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 1 MEVKTFynGNT---MPQIGLGTFR--VENDENCMESVKYAIEQGYRSIDTAKVYGN-EEQVGAGIRAglestgiAREDLF 74
Cdd:COG1453 1 MQYRRL--GKTgleVSVLGFGGMRlpRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 75 ITSKLYFEDFGRENVAAAYEASLSRLGLKYLDLYLVHwpgtneavMVDTWKGMEDLYKNNN-------------VKNIGV 141
Cdd:COG1453 72 LATKLPPWVRDPEDMRKDLEESLKRLQTDYIDLYLIH--------GLNTEEDLEKVLKPGGalealekakaegkIRHIGF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 142 SNfepeH--LEALLAqvsikpVIN-------QVEYHPYLTQHK--LKLYLAAQR-----IVMEswsPLMNAQILND-ETI 204
Cdd:COG1453 144 ST----HgsLEVIKE------AIDtgdfdfvQLQYNYLDQDNQagEEALEAAAEkgigvIIMK---PLKGGRLANPpEKL 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446375467 205 KDIAqELGKSPAQVVLRWNVQHAVVTIPkSVTPNRIS---ENFQIFD-FE-LSDEQMTRIDGL 262
Cdd:COG1453 211 VELL-CPPLSPAEWALRFLLSHPEVTTV-LSGMSTPEqldENLKTADnLEpLTEEELAILERL 271
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
8-259 |
1.19e-22 |
|
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: 94.59 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGT------FRVENDENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGAGIRAGlestgiaREDLFITSK 78
Cdd:cd19076 8 QGLEVSALGLGCmgmsafYGPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 79 lyfedFG---------------RENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMvDTWKGMEDLYKNNNVKNIGVSN 143
Cdd:cd19076 81 -----FGivrdpgsgfrgvdgrPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIE-ETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 144 FEPEHLEALLAQVSIKPVinQVEYHPYlTQHKLKLYLAAQR---IVMESWSPL--------------------------- 193
Cdd:cd19076 155 ASADTIRRAHAVHPITAV--QSEYSLW-TRDIEDEVLPTCRelgIGFVAYSPLgrgfltgaikspedlpeddfrrnnprf 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446375467 194 ------MNAQILndETIKDIAQELGKSPAQVVLRWnVQHA---VVTIPKSVTPNRISENFQIFDFELSDEQMTRI 259
Cdd:cd19076 232 qgenfdKNLKLV--EKLEAIAAEKGCTPAQLALAW-VLAQgddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
43-260 |
2.71e-22 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 93.82 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 43 IDTAKVYGN---EEQVGAGIRAglestgiAREDLFITSKLYFEDF---------GRENVAAAYEASLSRLGLKYLDLYLV 110
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKYTMNRRpgdpnaggnHRKNLRRSVEASLRRLQTDYIDLLYV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 111 H-WPGTN--EAVMvdtwKGMEDLYKNNNVKNIGVSNFePEHLEA---LLAQVSIK--PVINQVEYH-----------PYL 171
Cdd:cd19080 121 HaWDFTTpvEEVM----RALDDLVRAGKVLYVGISDT-PAWVVAranTLAELRGWspFVALQIEYSllertperellPMA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 172 TQHKLKL--------------YLAAQRIVMESWSPLM---------NAQILndETIKDIAQELGKSPAQVVLRWNVQHAV 228
Cdd:cd19080 196 RALGLGVtpwsplggglltgkYQRGEEGRAGEAKGVTvgfgklterNWAIV--DVVAAVAEELGRSAAQVALAWVRQKPG 273
|
250 260 270
....*....|....*....|....*....|....*
gi 446375467 229 VTIPkSVTPNRIS---ENFQIFDFELSDEQMTRID 260
Cdd:cd19080 274 VVIP-IIGARTLEqlkDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
15-260 |
6.92e-22 |
|
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: 92.76 E-value: 6.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRV-------ENDENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGagiRAgLESTGIaREDLFITSKL----- 79
Cdd:cd19148 7 IALGTWAIggwmwggTDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVG---KA-LKEYGK-RDRVVIATKVglewd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 ----YFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMvDTWKGMEDLYKNNNVKNIGVSNFEPEHLE----- 150
Cdd:cd19148 82 eggeVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIE-ETAEALKELLDEGKIRAIGVSNFSPEQMEtfrkv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 151 ALLAqvSIKPVINQVEYH------PYLTQHKlklylaaqrIVMESWSPL--------MNAQIL--------ND------- 201
Cdd:cd19148 161 APLH--TVQPPYNLFEREiekdvlPYARKHN---------IVTLAYGALcrgllsgkMTKDTKfegddlrrTDpkfqepr 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 202 --------ETIKDIAQE-LGKSPAQVVLRWNVQHAVVTIP--KSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19148 230 fsqylaavEELDKLAQErYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-260 |
1.02e-21 |
|
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: 92.27 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 36 IEQGYRSIDTAKVYGN-EEQVGAgIRAGLESTGIAREDLFITSKLYFEDF----GRENVAAAYEASLSRLGLKYLDLYLV 110
Cdd:cd19101 33 VDAGLTTFDCADIYGPaEELIGE-FRKRLRRERDAADDVQIHTKWVPDPGeltmTRAYVEAAIDRSLKRLGVDRLDLVQF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 111 HWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVsIKPVINQVEYH-----------PYLTQHKLKL- 178
Cdd:cd19101 112 HWWDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG-VPIVSNQVQYSlldrrpengmaALCEDHGIKLl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 179 -------------YLAAQ---RIVMESWSPLMNAQILND-----------ETIKDIAQELGKSPAQVVLRWNVQHAVV-- 229
Cdd:cd19101 191 aygtlaggllsekYLGVPeptGPALETRSLQKYKLMIDEwggwdlfqellRTLKAIADKHGVSIANVAVRWVLDQPGVag 270
|
250 260 270
....*....|....*....|....*....|.
gi 446375467 230 TIPKSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19101 271 VIVGARNSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
13-243 |
2.63e-21 |
|
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: 89.99 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFR------VENDENCMESVKYAIEQGYRSIDTAKVYGN-EEQVGAGIRaglestGIAREDLFITSKL------ 79
Cdd:cd19095 1 SVLGLGTSGigrvwgVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVgthgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 --YFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWPG--TNEAVMVDTwkgMEDLYKNNNVKNIGVSNFEPEHLEAL-LA 154
Cdd:cd19095 75 grDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSddELTGEVLET---LEDLKAAGKVRYIGVSGDGEELEAAIaSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 155 QVSikpVInQVEYHPYLTQHKLKLYLAAQR----IVMEswsPLMNAQILNDET-----------IKDIAQELGKSPAQVV 219
Cdd:cd19095 152 VFD---VV-QLPYNVLDREEEELLPLAAEAglgvIVNR---PLANGRLRRRVRrrplyadyarrPEFAAEIGGATWAQAA 224
|
250 260
....*....|....*....|....*.
gi 446375467 220 LRWNVQHAVVT--IPKSVTPNRISEN 243
Cdd:cd19095 225 LRFVLSHPGVSsaIVGTTNPEHLEEN 250
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
13-230 |
3.31e-21 |
|
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: 89.93 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFR-------VENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAGLestgiaREDLFITSKL-YF 81
Cdd:cd19096 1 SVLGFGTMRlpesdddSIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKEGP------REKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNE----AVMVDTWKGMEDLYKNNNVKNIGVSnF--EPEHLEALLAq 155
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEwlekARKGGLLEFLEKAKKEGLIRHIGFS-FhdSPELLKEILD- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 156 vSIKPVINQVEYHP--YLTQHKLKLYLAAQR-----IVMEswsPLMNAQILND-ETIKDIAQELGKSPAQVVLRWNVQHA 227
Cdd:cd19096 153 -SYDFDFVQLQYNYldQENQAGRPGIEYAAKkgmgvIIME---PLKGGGLANNpPEALAILCGAPLSPAEWALRFLLSHP 228
|
...
gi 446375467 228 VVT 230
Cdd:cd19096 229 EVT 231
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
14-243 |
1.60e-20 |
|
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: 87.53 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 14 QIGLGTFRVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAGlestgiaREDLFITSKL---------YF 81
Cdd:cd19086 12 GLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFgnrfdggpeRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPV 161
Cdd:cd19086 85 QDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGIDVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 162 inQVEYHPyLTQHKLK--LYLAAQR----IVMeswSPLMNAqILNdetikdiaqelGKsPAQVVLRWNVQHAVVT--IPK 233
Cdd:cd19086 165 --QVIYNL-LDQRPEEelFPLAEEHgvgvIAR---VPLASG-LLT-----------GK-LAQAALRFILSHPAVStvIPG 225
|
250
....*....|
gi 446375467 234 SVTPNRISEN 243
Cdd:cd19086 226 ARSPEQVEEN 235
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
17-262 |
1.77e-20 |
|
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: 88.78 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 17 LGT--FRVENDENcmES---VKYAIEQGYRSIDTAKVYGN---EEQVGagiRAglestgIA--REDLFITSKLYFE---- 82
Cdd:cd19087 18 LGTmnFGGRTDEE--TSfaiMDRALDAGINFFDTADVYGGgrsEEIIG---RW------IAgrRDDIVLATKVFGPmgdd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 83 --DFG--RENVAAAYEASLSRLGLKYLDLYLVHWPGTNeAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHL-EALLAQ-- 155
Cdd:cd19087 87 pnDRGlsRRHIRRAVEASLRRLQTDYIDLYQMHHFDRD-TPLEETLRALDDLVRQGKIRYIGVSNFAAWQIaKAQGIAar 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 156 ------VSIKPVINQVEYHPyltqhKLKLYLAAQR--IVMESWSPL-------------------------MNAQILNDE 202
Cdd:cd19087 166 rgllrfVSEQPMYNLLKRQA-----ELEILPAARAygLGVIPYSPLagglltgkygkgkrpesgrlverarYQARYGLEE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446375467 203 T------IKDIAQELGKSPAQVVLRWNVQHAVVTIP--KSVTPNRISENFQIFDFELSDEQMTRIDGL 262
Cdd:cd19087 241 YrdiaerFEALAAEAGLTPASLALAWVLSHPAVTSPiiGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
15-262 |
2.89e-20 |
|
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: 88.24 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRVE--------NDENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGAGIRaglestGIAREDLFITSK--LYF 81
Cdd:cd19083 14 IGLGTNAVGghnlypnlDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLK------EYNRNEVVIATKgaHKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 --EDFGRENVAA----AYEASLSRLGLKYLDLYLVHWPG----TNEAVmvdtwKGMEDLYKNNNVKNIGVSNFEPEHLEA 151
Cdd:cd19083 88 ggDGSVLNNSPEflrsAVEKSLKRLNTDYIDLYYIHFPDgetpKAEAV-----GALQELKDEGKIRAIGVSNFSLEQLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 152 LLAQVSIKPVinQVEYHPYLTQHKLKL--YLAAQRIVMESWSPLMNAQI---------LNDETI---------------- 204
Cdd:cd19083 163 ANKDGYVDVL--QGEYNLLQREAEEDIlpYCVENNISFIPYFPLASGLLagkytkdtkFPDNDLrndkplfkgerfsenl 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 205 ------KDIAQELGKSPAQVVLRWNV-QHAV-VTIPKSVTPNRISENFQIFDFELSDEQMTRIDGL 262
Cdd:cd19083 241 dkvdklKSIADEKGVTVAHLALAWYLtRPAIdVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-260 |
1.02e-19 |
|
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: 86.94 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRVENDEN-CMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAglestgiAREDLFITSK-----------L 79
Cdd:cd19149 21 IGGGPWWGGSDDNeSIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVLATKcglrwdreggsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 YFEDFGR--------ENVAAAYEASLSRLGLKYLDLYLVHWPgTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEA 151
Cdd:cd19149 94 FFVRDGVtvyknlspESIREEVEQSLKRLGTDYIDLYQTHWQ-DVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 152 LLAQVSIKpvINQVEYH-----------PYLTQHK--------LKLYLAAQRIVME---------SWSPLMN----AQIL 199
Cdd:cd19149 173 YVKAGQLD--IIQEKYSmldrgiekellPYCKKNNiafqayspLEQGLLTGKITPDrefdagdarSGIPWFSpenrEKVL 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446375467 200 N-DETIKDIAQELGKSPAQVVLRWNVQHA--VVTIPKSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19149 251 AlLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-230 |
2.88e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 84.56 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNT---MPQIGLGTFRVENDENcmESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaglestGIAREDLFITSKLYFE 82
Cdd:cd19105 7 GKTglkVSRLGFGGGGLPRESP--ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKASPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 83 D--FGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTW--KGMEDLYKNNNVKNIGVSNFEPEHlEALLAQVSI 158
Cdd:cd19105 79 LdkKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEEllEALEKLKKEGKVRFIGFSTHDNMA-EVLQAAIES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 159 KP--VInQVEYHpYLTQHKLK---LYLAAQR----IVMESwsplMNAQILNDETIKDIaQELGKSPAQVVLRWNVQHAVV 229
Cdd:cd19105 158 GWfdVI-MVAYN-FLNQPAELeeaLAAAAEKgigvVAMKT----LAGGYLQPALLSVL-KAKGFSLPQAALKWVLSNPRV 230
|
.
gi 446375467 230 T 230
Cdd:cd19105 231 D 231
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
13-254 |
5.13e-19 |
|
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: 84.53 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFRVEN------DENCMESVKYAIEQGYRSIDTAKVYGN-EEQVGAGIRaglestGIAREDLFITSKL-----Y 80
Cdd:cd19090 1 SALGLGTAGLGGvfggvdDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 81 FEDFGRENVAAAYEASLSRLGLKYLDLYLVH---WPGTNEAVMVD-TWKGMEDLYKNNNVKNIGVSNFEPEHLEA----- 151
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHdpeRVPWVDILAPGgALEALLELKEEGLIKHIGLGGGPPDLLRRaietg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 152 ------------LLAQVSIKPVInqveyhPYLTQHKLKLYLAA-------------QRIVMESW-SPLMNAQIlndETIK 205
Cdd:cd19090 155 dfdvvltanrytLLDQSAADELL------PAAARHGVGVINASplgmgllagrppeRVRYTYRWlSPELLDRA---KRLY 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446375467 206 DIAQELGKSPAQVVLRWNVQHAVV--TIPKSVTPNRISENFQIFDFELSDE 254
Cdd:cd19090 226 ELCDEHGVPLPALALRFLLRDPRIstVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
8-259 |
5.91e-18 |
|
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: 82.11 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRV-------ENDENCMESVKYAIEQGYRSIDTAKVYG-NEEQVGAGIRAgleSTGiAREDLFITSKL 79
Cdd:cd19144 9 NGPSVPALGFGAMGLsafygppKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQ---NPG-KREKIFLATKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 YFE----------DFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAVMvDTWKGMEDLYKNNNVKNIGVSNFEPEHL 149
Cdd:cd19144 85 GIEknvetgeysvDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIE-KTVAAMAELVQEGKIKHIGLSECSAETL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 150 EALLAQVSIKPVinQVEYHPYLT---QHKLKLYLAAQR--IVMESWSPL---------------------MNAQILNDE- 202
Cdd:cd19144 164 RRAHAVHPIAAV--QIEYSPFSLdieRPEIGVLDTCRElgVAIVAYSPLgrgfltgairspddfeegdfrRMAPRFQAEn 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446375467 203 ---------TIKDIAQELGKSPAQVVLRWNVQHA--VVTIPKSVTPNRISENFQIFDFELSDEQMTRI 259
Cdd:cd19144 242 fpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
25-260 |
7.55e-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: 81.51 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 25 DENCM-ESVKYAIEQGYRSIDTAKVYG---NEEQVGagiraglESTGIAREDLFITSKLYFE-----------DFGRENV 89
Cdd:cd19078 23 DKEEMiELIRKAVELGITFFDTAEVYGpytNEELVG-------EALKPFRDQVVIATKFGFKidggkpgplglDSRPEHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 90 AAAYEASLSRLGLKYLDLYLVHWPGTN---EAVMvdtwKGMEDLYKNNNVKNIGVSnfepehlEALLAQV----SIKPVI 162
Cdd:cd19078 96 RKAVEGSLKRLQTDYIDLYYQHRVDPNvpiEEVA----GTMKELIKEGKIRHWGLS-------EAGVETIrrahAVCPVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 163 N-QVEYHPYLTQHKLKL--YLAAQRIVMESWSPLM---------------------------------NAQILndETIKD 206
Cdd:cd19078 165 AvQSEYSMMWREPEKEVlpTLEELGIGFVPFSPLGkgfltgkidentkfdegddraslprftpealeaNQALV--DLLKE 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446375467 207 IAQELGKSPAQVVLRW--NVQHAVVTIPKSVTPNRISENFQIFDFELSDEQMTRID 260
Cdd:cd19078 243 FAEEKGATPAQIALAWllAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
14-260 |
4.07e-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: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 14 QIGLGT--FRVENDE-NCMESVKYAIEQGYRSIDTAKVY---GNEEQVGAG---IRAGLESTGiAREDLFITSKL----- 79
Cdd:cd19094 3 EICLGTmtWGEQNTEaEAHEQLDYAFDEGVNFIDTAEMYpvpPSPETQGRTeeiIGSWLKKKG-NRDKVVLATKVagpge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 -------YFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWP-------GTNEAVMVDTW----------KGMEDLYKNNN 135
Cdd:cd19094 82 gitwprgGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPdrytplfGGGYYTEPSEEedsvsfeeqlEALGELVKAGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 136 VKNIGVSNFEP----------EHL-------------------EALLAQVSIKPVINQVEYHP---------YL------ 171
Cdd:cd19094 162 IRHIGLSNETPwgvmkflelaEQLglprivsiqnpysllnrnfEEGLAEACHRENVGLLAYSPlaggvltgkYLdgaarp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 172 TQHKLKLY-LAAQRIVmeswSPLMNAQILNdetIKDIAQELGKSPAQVVLRWNVQHAVV--TIPKSVTPNRISENFQIFD 248
Cdd:cd19094 242 EGGRLNLFpGYMARYR----SPQALEAVAE---YVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFD 314
|
330
....*....|..
gi 446375467 249 FELSDEQMTRID 260
Cdd:cd19094 315 VPLSDELLAEID 326
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-142 |
4.68e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 79.67 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 14 QIGLGTFRVENDENC----MESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAGLESTGIAREDLFITSK--LYFEDF 84
Cdd:cd19099 5 SLGLGTYRGDSDDETdeeyREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagYIPGDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAY-------------------------------EASLSRLGLKYLDLYLVHWP-------GTNE--AVMVDTW 124
Cdd:cd19099 85 DEPLRPLKYleeklgrglidvadsaglrhcispayledqiERSLKRLGLDTIDLYLLHNPeeqllelGEEEfyDRLEEAF 164
|
170
....*....|....*...
gi 446375467 125 KGMEDLYKNNNVKNIGVS 142
Cdd:cd19099 165 EALEEAVAEGKIRYYGIS 182
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-167 |
6.65e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 78.34 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 32 VKYAIEQGYRSIDTAKVYGNEEQVgagiragLESTGIAREDLFITSKL----YFEDFGRENVAAAYEASLSRLGLKYLDL 107
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGDSEKV-------LGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 108 YLVHWPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAqvSIKPVINQVEY 167
Cdd:cd19097 105 LLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE--SFKIDIIQLPF 162
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
13-232 |
4.95e-16 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 76.05 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGT---FRVENDENCMESVKYAIEQGYRSIDTAKVYGNEEQVGAG---IRAGLESTGIaREDLFITSK---LYFED 83
Cdd:cd19082 1 SRIVLGTadfGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServIGEWLKSRGN-RDKVVIATKgghPDLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 84 FG-----RENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAV--MVDTwkgMEDLYKNNNVKNIGVSNFEPEHLEAL---- 152
Cdd:cd19082 80 MSrsrlsPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVgeIVDT---LNELVRAGKIRAFGASNWSTERIAEAnaya 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 153 ----------------LAQVSIKPVINQV------EYHPYLTQHKLKLY------------------LAAQRIVMESWSP 192
Cdd:cd19082 157 kahglpgfaasspqwsLARPNEPPWPGPTlvamdeEMRAWHEENQLPVFayssqargffskraaggaEDDSELRRVYYSE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446375467 193 lMNAQILndETIKDIAQELGKSPAQVVLRWNVQHAVVTIP 232
Cdd:cd19082 237 -ENFERL--ERAKELAEEKGVSPTQIALAYVLNQPFPTVP 273
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-152 |
9.96e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 74.44 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFRV--ENDENCMESVKYAIEQGYRSIDTAKVYGN-EEQVGAGIRAGlestgiaREDLFITSKLYFEDfgRENV 89
Cdd:cd19100 12 SRLGFGGGPLgrLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARD--YEGA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446375467 90 AAAYEASLSRLGLKYLDLYLVHWPGTNEAVMVDTWKG-----MEDLYKNNNVKNIGVSNFEPE-HLEAL 152
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGPGgaleaLLEAKEEGKIRFIGISGHSPEvLLRAL 151
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-243 |
2.20e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 71.59 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGT--FRVENDENCMESV--KYaIEQGYRSIDTAKVY---------GNEEQVgagIRAGLESTGiAREDLFITSKL 79
Cdd:cd19752 1 SELCLGTmyFGTRTDEETSFAIldRY-VAAGGNFLDTANNYafwteggvgGESERL---IGRWLKDRG-NRDDVVIATKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 YF------------EDFGRENVAAAYEASLSRLGLKYLDLYLVHW--PGTNeavMVDTWKGMEDLYKNNNVKNIGVSNFE 145
Cdd:cd19752 76 GAgprdpdggpespEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVddRDTP---LEETLEAFNELVKAGKVRAIGASNFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 146 PEHLE---ALLAQVSIKPVINQVEYHPYLtQHKLKLYLAAQRIV---------------MESWSPLMNAQILNDE----- 202
Cdd:cd19752 153 AWRLErarQIARQQGWAEFSAIQQRHSYL-RPRPGADFGVQRIVtdelldyassrpdltLLAYSPLLSGAYTRPDrplpe 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446375467 203 ------------TIKDIAQELGKSPAQVVLRWNVQHAVVTIP--KSVTPNRISEN 243
Cdd:cd19752 232 qydgpdsdarlaVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEEN 286
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
8-260 |
1.74e-13 |
|
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: 69.19 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRV------ENDENCMESVKYAIEQGYRSIDTAKVYG------NEEQVGAGIRAGLEStgiaREDLFI 75
Cdd:cd19077 1 NGKLVGPIGLGLMGLtwrpnpTPDEEAFETMKAALDAGSNLWNGGEFYGppdphaNLKLLARFFRKYPEY----ADKVVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 76 TSK------LYFEDFGRENVAAAYEASLSRLG-LKYLDLYlvhwpgtnEAVMVD-------TWKGMEDLYKNNNVKNIGV 141
Cdd:cd19077 77 SVKggldpdTLRPDGSPEAVRKSIENILRALGgTKKIDIF--------EPARVDpnvpieeTIKALKELVKEGKIRGIGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 142 SNFEPEHLEALLAQVSIkpVINQVEYHPYLTQ----------HKLKLYLAAqrivmesWSPL----MNAQILNDETIKD- 206
Cdd:cd19077 149 SEVSAETIRRAHAVHPI--AAVEVEYSLFSREieengvletcAELGIPIIA-------YSPLgrglLTGRIKSLADIPEg 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 207 --------------------------IAQELGKSPAQVVLRWNV---QHAVVTIPKSVTPNRISENFQIFDFELSDEQMT 257
Cdd:cd19077 220 dfrrhldrfngenfeknlklvdalqeLAEKKGCTPAQLALAWILaqsGPKIIPIPGSTTLERVEENLKAANVELTDEELK 299
|
...
gi 446375467 258 RID 260
Cdd:cd19077 300 EIN 302
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
22-261 |
2.31e-13 |
|
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: 68.78 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 22 VENDENCMesvKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAGlestGIAREDLFITSKLYF-------EDFG--RENV 89
Cdd:cd19143 30 VDEAKECM---KAAYDAGVNFFDNAEVYANgqsEEIMGQAIKEL----GWPRSDYVVSTKIFWggggpppNDRGlsRKHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 90 AAAYEASLSRLGLKYLDLYLVHWPGTnEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHL-EALlaQVS-----IKPVIN 163
Cdd:cd19143 103 VEGTKASLKRLQLDYVDLVFCHRPDP-ATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIeEAH--EIAdrlglIPPVME 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 164 QVEYHpYLTQHKL-KLYLAAQRIV---MESWSPLM----------------------------NAQILNDETI------K 205
Cdd:cd19143 180 QPQYN-LFHRERVeVEYAPLYEKYglgTTTWSPLAsglltgkynngipegsrlalpgyewlkdRKEELGQEKIekvrklK 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 206 DIAQELGKSPAQVVLRWNV--QHAVVTIPKSVTPNRISENFQIFDF--ELSDEQMTRIDG 261
Cdd:cd19143 259 PIAEELGCSLAQLAIAWCLknPNVSTVITGATKVEQLEENLKALEVlpKLTPEVMEKIEA 318
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-226 |
3.05e-12 |
|
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: 65.66 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTF----RVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAgiraglesTGIAREDLFITSKLYF---EDF 84
Cdd:cd19075 5 LGTMTFgsqgRFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGE--------LGLGERGFKIDTKANPgvgGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 85 GRENVAAAYEASLSRLGLKYLDLYLVHWP--GTNeavMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALL----AQVSI 158
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPdrSTP---LEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVeickENGWV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 159 KPVINQVEYH-----------PYLTQHKLKLY----LAA-------QRIVME----------SWSPLMNAQILNDET--- 203
Cdd:cd19075 154 LPTVYQGMYNaitrqvetelfPCLRKLGIRFYayspLAGgfltgkyKYSEDKagggrfdpnnALGKLYRDRYWKPSYfea 233
|
250 260
....*....|....*....|....*.
gi 446375467 204 ---IKDIAQELGKSPAQVVLRWNVQH 226
Cdd:cd19075 234 lekVEEAAEKEGISLAEAALRWLYHH 259
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
13-230 |
3.82e-12 |
|
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: 65.36 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLG---TF-RVENDENCMESVKYAIEQGYRSIDTAKVYGN-----EEQVGAGIRAGLESTgiaREDLFITSKLYFE- 82
Cdd:cd19089 12 PAISLGlwhNFgDYTSPEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPY---RDELVISTKAGYGm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 83 ------DFG-RENVAAAYEASLSRLGLKYLDLYLVHWPgTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLE---AL 152
Cdd:cd19089 89 wpgpygDGGsRKYLLASLDQSLKRMGLDYVDIFYHHRY-DPDTPLEETMTALADAVRSGKALYVGISNYPGAKARraiAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 153 LAQVSIKPVINQVEYHpYLTQ---HKLKLYLAAQRIVMESWSPLmnAQ-ILNDETIKD---------------------- 206
Cdd:cd19089 168 LRELGVPLIIHQPRYS-LLDRwaeDGLLEVLEEAGIGFIAFSPL--AQgLLTDKYLNGippdsrraaeskflteealtpe 244
|
250 260 270
....*....|....*....|....*....|....
gi 446375467 207 ----------IAQELGKSPAQVVLRWNVQHAVVT 230
Cdd:cd19089 245 kleqlrklnkIAAKRGQSLAQLALSWVLRDPRVT 278
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
8-207 |
1.06e-11 |
|
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: 64.02 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRV----ENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAGlestGIAREDLFITSKLY 80
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 81 F----EDFG--RENVAAAYEASLSRLGLKYLDLYLVHwpgTNEAV--MVDTWKGMEDLYKNNNVKNIGVSNFEPEHL-EA 151
Cdd:cd19142 85 WsygsEERGlsRKHIIESVRASLRRLQLDYIDIVIIH---KADPMcpMEEVVRAMSYLIDNGLIMYWGTSRWSPVEImEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446375467 152 LLA--QVS-IKPVINQVEYHPyLTQHKLKLYLA----AQRIVMESWSPL-MNaqilNDETIKDI 207
Cdd:cd19142 162 FSIarQFNcPTPICEQSEYHM-FCREKMELYMPelynKVGVGLITWSPLsLG----LDPGISEE 220
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
13-142 |
2.23e-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: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGTFRVEN-----DENCMESVKYAIEQGYRSIDTAKVYG---NEEQVGAGIRaglestGIAREDLFITSKL--YFE 82
Cdd:cd19162 1 PRLGLGAASLGNlaragEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA------RHPRAEYVVSTKVgrLLE 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446375467 83 --------------DFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTN-EAVMVDTWKGMEDLYKNNNVKNIGVS 142
Cdd:cd19162 75 pgaagrpagadrrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHlLQALTDAFPALEELRAEGVVGAIGVG 149
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-264 |
2.42e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 63.33 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 14 QIGLG--TFRVENDE-NCMESVKYAIEQGYRSIDTAKVY---------GNEEQVgagIRAGLESTGiAREDLFITSKLYF 81
Cdd:PRK10625 15 TLGLGtmTFGEQNSEaDAHAQLDYAVAQGINLIDVAEMYpvpprpetqGLTETY---IGNWLAKRG-SREKLIIASKVSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFG------------RENVAAAYEASLSRLGLKYLDLYLVHWPG-------------TNEAVMV---DTWKGMEDLYKN 133
Cdd:PRK10625 91 PSRNndkgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswTDSAPAVsllETLDALAEQQRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 134 NNVKNIGVSNFEP----EHLEalLAQVSIKPVINQVEyHPY-LTQHKLKLYLAA----QRIVMESWSPL----MNAQILN 200
Cdd:PRK10625 171 GKIRYIGVSNETAfgvmRYLH--LAEKHDLPRIVTIQ-NPYsLLNRSFEVGLAEvsqyEGVELLAYSCLafgtLTGKYLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 201 --------------------DETIK------DIAQELGKSPAQVVLRWNVQHAVV--TIPKSVTPNRISENFQIFDFELS 252
Cdd:PRK10625 248 gakpagarntlfsrftrysgEQTQKavaayvDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLS 327
|
330
....*....|..
gi 446375467 253 DEQMTRIDGLNQ 264
Cdd:PRK10625 328 EEVLAEIEAVHQ 339
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
13-254 |
1.86e-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: 60.32 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 13 PQIGLGT------FRVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaglestGIAREDLFITSKL---- 79
Cdd:cd19152 1 PKLGFGTaplgnlYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR------ELGREDYVISTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 ---------------------YFEDFGRENVAAAYEASLSRLGLKYLDLYLVH----------WPGTNEAVMVDTWKGME 128
Cdd:cd19152 75 vplqeveptfepgfwnplpfdAVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHdpdedlagaeSDEHFAQAIKGAFRALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 129 DLYKNNNVKNIGV-SNFEPEHLEA----------------LLAQVSIKPVINQVEyhpyltQHKLKLYLAAQR----IVM 187
Cdd:cd19152 155 ELREEGVIKAIGLgVNDWEVILRIleeadldwvmlagrytLLDHSAARELLPECE------KRGVKVVNAGPFnsgfLAG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446375467 188 ESWSPLMNAQILNDE------TIKDIAQELGKSPAQVVLRWNVQHAVVT--IPKSVTPNRISENFQIFDFELSDE 254
Cdd:cd19152 229 GDNFDYYEYGPAPPEliarrdRIEALCEQHGVSLAAAALQFALAPPAVAsvAPGASSPERVEENVALLATEIPAA 303
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
35-263 |
2.39e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 59.98 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 35 AIEQGYRSIDTAKVYG----NeeQVgagIRAGLESTgiaREDLFITSKL---------YFEDFGRENVAAAYEASLSRLG 101
Cdd:PRK10376 49 AVALGVNHIDTSDFYGphvtN--QL---IREALHPY---PDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 102 LKYLDL------YLVHWPGTN---EAVMVdtwkgMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPVINQveyhpYLT 172
Cdd:PRK10376 121 LDVLDVvnlrlmGDGHGPAEGsieEPLTV-----LAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNH-----YNL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 173 QHK----LKLYLAAQRIVMESWSPLMNAQILNDETIKDIAQELGKSPAQVVLRWNVQHA--VVTIPKSVTPNRISENFQI 246
Cdd:PRK10376 191 AHRaddaLIDALARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAA 270
|
250
....*....|....*..
gi 446375467 247 FDFELSDEQMTRIDGLN 263
Cdd:PRK10376 271 AELVLSEEVLAELDGIA 287
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
32-259 |
2.43e-10 |
|
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: 60.14 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 32 VKYAIEQGYRSIDTAKVYG---NEEQVGAGIRAGLestgiaREDLFITSKL---YFEDFGRE------NVAAAYEASLSR 99
Cdd:cd19145 39 IHHAFNSGVTFLDTSDIYGpntNEVLLGKALKDGP------REKVQLATKFgihEIGGSGVEvrgdpaYVRAACEASLKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 100 LGLKYLDLYLVHWPGTNEAVMVdTWKGMEDLYKNNNVKNIGVSNFEPE--------------HLEALL----AQVSIKPV 161
Cdd:cd19145 113 LDVDYIDLYYQHRIDTTVPIEI-TMGELKKLVEEGKIKYIGLSEASADtirrahavhpitavQLEWSLwtrdIEEEIIPT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 162 -----INQVEYHPYltqhkLKLYLAAQRIVMESWS--------PLMNAQILND-----ETIKDIAQELGKSPAQVVLRWn 223
Cdd:cd19145 192 crelgIGIVPYSPL-----GRGFFAGKAKLEELLEnsdvrkshPRFQGENLEKnkvlyERVEALAKKKGCTPAQLALAW- 265
|
250 260 270
....*....|....*....|....*....|....*....
gi 446375467 224 VQHA---VVTIPKSVTPNRISENFQIFDFELSDEQMTRI 259
Cdd:cd19145 266 VLHQgedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
30-161 |
3.57e-10 |
|
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: 59.47 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 30 ESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRAglesTGIAREDLFITSKL--YFE---DFGRENVAAAYEASLSRLG 101
Cdd:cd19153 37 AIVAEAFAAGINHFDTSPYYGAessEAVLGKALAA----LQVPRSSYTVATKVgrYRDsefDYSAERVRASVATSLERLH 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446375467 102 LKYLDLYLVH--WPGTNEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLEALLAQVSIKPV 161
Cdd:cd19153 113 TTYLDVVYLHdiEFVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSL 174
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-163 |
6.04e-10 |
|
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: 58.88 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 35 AIEQGYRSIDTAKVYG---NEEQVGAGIRAglestgIAREDLFITSKlyF----EDFGRENVAAAYEASLSRLGLKYLDL 107
Cdd:cd19103 41 AMAAGLNLWDTAAVYGmgaSEKILGEFLKR------YPREDYIISTK--FtpqiAGQSADPVADMLEGSLARLGTDYIDI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446375467 108 YLVHWPgtneaVMVDTW-KGMEDLYKNNNVKNIGVSNF---EPEHLEALLAQ--VSIKPVIN 163
Cdd:cd19103 113 YWIHNP-----ADVERWtPELIPLLKSGKVKHVGVSNHnlaEIKRANEILAKagVSLSAVQN 169
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-257 |
1.06e-09 |
|
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: 58.18 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFR----VENDENCMESVKYAIEQGYRSIDTAKVYG-----NEEQVGAGIRAGLESTgiaREDLFITSKL 79
Cdd:cd19151 9 GLKLPAISLGLWHnfgdVDRYENSRAMLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKPY---RDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 YFE-------DFG-RENVAAAYEASLSRLGLKYLDLYLVHWPGTnEAVMVDTWKGMEDLYKNNNVKNIGVSNFEPEHLE- 150
Cdd:cd19151 86 GYTmwpgpygDWGsKKYLIASLDQSLKRMGLDYVDIFYHHRPDP-ETPLEETMGALDQIVRQGKALYVGISNYPPEEARe 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 151 --ALLAQVSIKPVINQVEYHPY-----------------------------LTQHKLKLYLAAQRiVMESWSPLMNAQIL 199
Cdd:cd19151 165 aaAILKDLGTPCLIHQPKYSMFnrwveeglldvleeegigciafsplaqglLTDRYLNGIPEDSR-AAKGSSFLKPEQIT 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446375467 200 NDETIK-----DIAQELGKSPAQVVLRWNVQHAVVT---IPKSvTPNRISENFQIFD-FELSDEQMT 257
Cdd:cd19151 244 EEKLAKvrrlnEIAQARGQKLAQMALAWVLRNKRVTsvlIGAS-KPSQIEDAVGALDnREFSEEELA 309
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-111 |
7.84e-09 |
|
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: 55.25 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNT---MPQIGLGT------FRVENDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaglestGIAREDLFIT 76
Cdd:cd19163 7 GKTglkVSKLGFGAsplggvFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK------GIPRDSYYLA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446375467 77 SKL--Y-------FeDFGRENVAAAYEASLSRLGLKYLDLYLVH 111
Cdd:cd19163 81 TKVgrYgldpdkmF-DFSAERITKSVEESLKRLGLDYIDIIQVH 123
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
8-260 |
1.60e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 54.61 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 8 NGNTMPQIGLGTFRVENDENCMES----VKYAIEQGYRSIDTAKVYG-----NEEQVGAGIRaglESTGIAREDLFITSK 78
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGHVNALESqraiLRKAFDLGITHFDLANNYGpppgsAEENFGRLLR---EDFAAYRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 79 L--------YFEDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAvMVDTWKGMEDLYKNNNVKNIGVSNFEPEH-- 148
Cdd:PRK09912 98 AgydmwpgpYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTP-MEETASALAHAVQSGKALYVGISSYSPERtq 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 149 -LEALLAQVSIKPVINQVEY---HPYLTQHKLKLYLAAQRIVMESWSP----LMNAQILND------------------- 201
Cdd:PRK09912 177 kMVELLREWKIPLLIHQPSYnllNRWVDKSGLLDTLQNNGVGCIAFTPlaqgLLTGKYLNGipqdsrmhregnkvrgltp 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446375467 202 -----------ETIKDIAQELGKSPAQVVLRWNVQHAVVT--IPKSVTPNRISENFQIF-DFELSDEQMTRID 260
Cdd:PRK09912 257 kmlteanlnslRLLNEMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVQALnNLTFSTEELAQID 329
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-111 |
5.19e-08 |
|
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: 53.04 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 24 NDENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGIRaGLestgiaREDLFITSKLYFEDFGRENVAAAY----EAS 96
Cdd:cd19104 30 TREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALK-GL------PAGPYITTKVRLDPDDLGDIGGQIersvEKS 102
|
90
....*....|....*
gi 446375467 97 LSRLGLKYLDLYLVH 111
Cdd:cd19104 103 LKRLKRDSVDLLQLH 117
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
15-244 |
1.07e-07 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 52.35 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRVE----NDENCMESVKYAIEQGYRSIDTAKVY--GNEEQVGAGIragLESTGIAREDLFITSKLYF------- 81
Cdd:cd19159 16 LGLGTWVTFggqiSDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSI---IKKKGWRRSSLVITTKLYWggkaete 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAvMVDTWKGMEDLYKNNNVKNIGVSNFEP-EHLEA--LLAQVS- 157
Cdd:cd19159 93 RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP-MEEIVRAMTHVINQGMAMYWGTSRWSAmEIMEAysVARQFNm 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 158 IKPVINQVEYHPYlTQHKLKLYLAA--QRIVM--ESWSPL--------------------------MNAQILNDE----- 202
Cdd:cd19159 172 IPPVCEQAEYHLF-QREKVEVQLPElyHKIGVgaMTWSPLacgiisgkygngvpessraslkcyqwLKERIVSEEgrkqq 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446375467 203 -TIKD---IAQELGKSPAQVVLRWNVQHAVVT--IPKSVTPNRISENF 244
Cdd:cd19159 251 nKLKDlspIAERLGCTLPQLAVAWCLRNEGVSsvLLGSSTPEQLIENL 298
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-256 |
4.24e-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: 50.15 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 9 GNTMPQIGLGTFRVENDENCMES----VKYAIEQGYRSIDTAKVYG-----NEEQVGAGIRAGLESTgiaREDLFITSKL 79
Cdd:cd19150 9 GLKLPALSLGLWHNFGDDTPLETqraiLRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAGY---RDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 80 --------YFEDFGRENVAAAYEASLSRLGLKYLDLYLVHW--PGTNeavMVDTWKGMEDLYKNNNVKNIGVSNFEPEHL 149
Cdd:cd19150 86 gydmwpgpYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRfdPDTP---LEETMGALDHAVRSGKALYVGISSYSPERT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 150 E---ALLAQVSIKPVINQVEY---HPYLTQHKLKLYLAAQRIVMESWSPL------------------------MNAQIL 199
Cdd:cd19150 163 ReaaAILRELGTPLLIHQPSYnmlNRWVEESGLLDTLQELGVGCIAFTPLaqglltdkylngipegsraskersLSPKML 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446375467 200 NDETIK------DIAQELGKSPAQVVLRWNVQHAVVT---IPKSvTPNRISENFQIFD-FELSDEQM 256
Cdd:cd19150 243 TEANLNsiralnEIAQKRGQSLAQMALAWVLRDGRVTsalIGAS-RPEQLEENVGALDnLTFSADEL 308
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
15-194 |
5.13e-07 |
|
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: 50.14 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRV----ENDENCMESVKYAIEQGYRSIDTAKVY--GNEEQVGAGIragLESTGIAREDLFITSKLYF------- 81
Cdd:cd19141 15 LGLGTWVTfgsqISDEVAEELVTLAYENGINLFDTAEVYaaGKAEIVLGKI---LKKKGWRRSSYVITTKIFWggkaete 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAvMVDTWKGMEDLYKNNNVKNIGVSNFEP-EHLEA--LLAQVS- 157
Cdd:cd19141 92 RGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTP-MEEIVRAFTHVINQGMAMYWGTSRWSAmEIMEAysVARQFNl 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446375467 158 IKPVINQVEYHpYLTQHKLKLYLAA--QRIVMES--WSPLM 194
Cdd:cd19141 171 IPPIVEQAEYH-LFQREKVEMQLPElfHKIGVGAmtWSPLA 210
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
25-142 |
1.29e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.01 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 25 DENCMESVKYAIEQGYRSIDTAKVYGN---EEQVGAGiragLESTGIAREDLFITSKL--YFE--DFGRENVAAAYEASL 97
Cdd:PLN02587 30 EEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKA----LKALGIPREKYVVSTKCgrYGEgfDFSAERVTKSVDESL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446375467 98 SRLGLKYLDLYLVH--WPGTNEAVMVDTWKGMEDLYKNNNVKNIGVS 142
Cdd:PLN02587 106 ARLQLDYVDILHCHdiEFGSLDQIVNETIPALQKLKESGKVRFIGIT 152
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
32-111 |
2.90e-06 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 47.66 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 32 VKYAIEQGYRSIDTAKVYGNEEQV-GAGIRAglESTGIAREDLFITSKL--Y-FEDF--GRENVAAAYEASLSRLGLKYL 105
Cdd:cd19164 40 VRRALELGIRAFDTSPYYGPSEIIlGRALKA--LRDEFPRDTYFIITKVgrYgPDDFdySPEWIRASVERSLRRLHTDYL 117
|
....*.
gi 446375467 106 DLYLVH 111
Cdd:cd19164 118 DLVYLH 123
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
15-193 |
3.34e-06 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 47.77 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRVE----NDENCMESVKYAIEQGYRSIDTAKVY--GNEEQVGAGIragLESTGIAREDLFITSKLYF------- 81
Cdd:cd19158 16 LGLGTWVTFggqiTDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNI---IKKKGWRRSSLVITTKIFWggkaete 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNEAvMVDTWKGMEDLYKNNNVKNIGVSNFEP-EHLEALLAQVS--- 157
Cdd:cd19158 93 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTP-MEETVRAMTHVINQGMAMYWGTSRWSSmEIMEAYSVARQfnl 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446375467 158 IKPVINQVEYHPYlTQHKLKLYLAAQ----RIVMESWSPL 193
Cdd:cd19158 172 IPPICEQAEYHMF-QREKVEVQLPELfhkiGVGAMTWSPL 210
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
15-193 |
8.43e-06 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 46.52 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 15 IGLGTFRVE----NDENCMESVKYAIEQGYRSIDTAKVY--GNEEQVGAGIragLESTGIAREDLFITSKLYF------- 81
Cdd:cd19160 18 LGLGTWVTFgsqiSDETAEDLLTVAYEHGVNLFDTAEVYaaGKAERTLGNI---LKSKGWRRSSYVVTTKIYWggqaete 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 82 EDFGRENVAAAYEASLSRLGLKYLDLYLVHWPGTNeAVMVDTWKGMEDLYKNNNVKNIGVSNFEP-EHLEA--LLAQVS- 157
Cdd:cd19160 95 RGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPN-SPMEEIVRAMTYVINQGMAMYWGTSRWSAmEIMEAysVARQFNl 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446375467 158 IKPVINQVEYHpYLTQHKLKLYLAA--QRIVMES--WSPL 193
Cdd:cd19160 174 IPPVCEQAEYH-LFQREKVEMQLPElyHKIGVGSvtWSPL 212
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
37-143 |
1.97e-04 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 42.03 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 37 EQGYRSIDTAKVY---GNEEQVGAGiragLESTGIaREDLFITSK--LYFEDFGRENVAAAY------------EASLSR 99
Cdd:cd19146 46 EQGGNFIDTANNYqgeESERWVGEW----MASRGN-RDEMVLATKytTGYRRGGPIKIKSNYqgnhakslrlsvEASLKK 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446375467 100 LGLKYLDLYLVHW---PGTNEAVMvdtwKGMEDLYKNNNVKNIGVSN 143
Cdd:cd19146 121 LQTSYIDILYVHWwdyTTSIPELM----QSLNHLVAAGKVLYLGVSD 163
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-111 |
1.60e-03 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 39.25 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446375467 35 AIEQGYRSIDTAKVYGNEEQVGAGIragLESTGIAREDLFITSKLYFE---------------DFGRENVAAAYEASLSR 99
Cdd:cd19098 44 AWAAGVRYFDAARSYGRAEEFLGSW---LRSRNIAPDAVFVGSKWGYTytadwqvdaavhevkDHSLARLLKQWEETRSL 120
|
90
....*....|..
gi 446375467 100 LGlKYLDLYLVH 111
Cdd:cd19098 121 LG-KHLDLYQIH 131
|
|
| |
