|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
20-282 |
1.32e-94 |
|
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: 279.75 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 20 MPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTlNENTVEETE 99
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEA-VLAALEAGYRHIDTAAAYGNEAEVGEAIRES----GVPREELFITTKLWP-TDHGYERVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 100 KQLANSLATLQTDYVDLLLIHYPRDrdtgndDDYEINKSRRKIVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIR 179
Cdd:cd19071 75 EALEESLKDLGLDYLDLYLIHWPVP------GKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 180 PVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSMIPKSATP 259
Cdd:cd19071 149 PAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNP 228
|
250 260
....*....|....*....|...
gi 17562292 260 SRIHDNLhNTIKIKLTEDELKSL 282
Cdd:cd19071 229 ERIKENL-DVFDFELSEEDMAAI 250
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
20-285 |
5.54e-88 |
|
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: 263.34 E-value: 5.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 20 MPKIGLGISRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTlNENTVEETE 99
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAP-KDQGYEKAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 100 KQLANSLATLQTDYVDLLLIHYPRDRDTGNDDdyEINKSRRKIVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIR 179
Cdd:cd19136 80 AACLGSLERLGTDYLDLYLIHWPGVQGLKPSD--PRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 180 PVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSMIPKSATP 259
Cdd:cd19136 158 PAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNP 237
|
250 260
....*....|....*....|....*.
gi 17562292 260 SRIHDNLHnTIKIKLTEDELKSLRSL 285
Cdd:cd19136 238 ERIAENIK-VFDFELSEEDMAELNAL 262
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
16-291 |
5.54e-79 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 240.34 E-value: 5.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 16 DGYEMPKIGLGISRIETQQDLDvSIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVrtLNEN-T 94
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAA-AVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKV--WNDNhG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 95 VEETEKQLANSLATLQTDYVDLLLIHYPrdrdtgNDDDY-EinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHLVEMF 173
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWP------GPGPYvE--------TWRALEELYEEGLIRAIGVSNFDPEHLEELL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 174 EYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLcwGDKEILQEKPLVDLCQKYNQTP-QAILyAFAHCSNTSM 252
Cdd:COG0656 140 AETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPL--GRGKLLDDPVLAEIAEKHGKTPaQVVL-RWHLQRGVVV 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 17562292 253 IPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKSF 291
Cdd:COG0656 217 IPKSVTPERIRENL-DAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
17-291 |
3.67e-66 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 207.86 E-value: 3.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGI-------SRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVRT 89
Cdd:cd19120 1 GSKIPAIAFGTgtawyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 90 LNENTVEETEKQLANslatLQTDYVDLLLIHYPRDRDTGNDDDYEinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHL 169
Cdd:cd19120 77 GIKDPREALRKSLAK----LGVDYVDLYLIHSPFFAKEGGPTLAE--------AWAELEALKDAGLVRSIGVSNFRIEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 170 VEMFEYAKIRPVLNQYEYQPYLTRPT--LKKFCDLNNIVVQSYSSLC--WGDKEILQEKPLVDLCQKYNQTPQAILYAFA 245
Cdd:cd19120 145 EELLDTAKIKPAVNQIEFHPYLYPQQpaLLEYCREHGIVVSAYSPLSplTRDAGGPLDPVLEKIAEKYGVTPAQVLLRWA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17562292 246 HCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKSF 291
Cdd:cd19120 225 LQKGIVVVTTSSKEERMKEYL-EAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
11-298 |
2.06e-63 |
|
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: 202.33 E-value: 2.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 11 AFKFSDGYEMPKIGLGISRIETQQDLDVSIEAaLKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTL 90
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRMEPGEIKELILNA-IKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 NENTVEETEKqlaNSLATLQTDYVDLLLIHYP----------RDRDTGNDDDYEINKSRRKI-VWQTLEKAKESGRVRSI 159
Cdd:cd19112 81 DHGHVIEACK---DSLKKLQLDYLDLYLVHFPvatkhtgvgtTGSALGEDGVLDIDVTISLEtTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 160 GVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL--------CWGDKEILQEKPLVDLCQ 231
Cdd:cd19112 158 GISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLggaaanaeWFGSVSPLDDPVLKDLAK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562292 232 KYNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKSFPQIGQTW 298
Cdd:cd19112 238 KYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENI-DVFDFQLSKEDMKLIKSLDRKYRTNQPAKFW 303
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
11-291 |
2.29e-63 |
|
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: 200.70 E-value: 2.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 11 AFKFSDGYEMPKIGLGISRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVRTl 90
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKVWN- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 NENTVEETEKQLANSLATLQTDYVDLLLIHYPRdrdtgndddyeinKSRRKIVWQTLEKAKESGRVRSIGVSNYEVYHLV 170
Cdd:cd19157 76 ADQGYDSTLKAFEASLERLGLDYLDLYLIHWPV-------------KGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 171 EMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGdkEILQEKPLVDLCQKYNQTPQAILYAFAHCSNT 250
Cdd:cd19157 143 DLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQG--QLLDNPVLKEIAEKYNKSVAQVILRWDLQNGV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17562292 251 SMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKSF 291
Cdd:cd19157 221 VTIPKSIKEHRIIENA-DVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
12-290 |
1.02e-62 |
|
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: 200.33 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 12 FKFSDGYEMPKIGLGISRIeTQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTlN 91
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQS-KGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT-H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 92 ENTVEETEKQLANSLATLQTDYVDLLLIHYP----------RDRDTGND--DDYEINKsrrkiVWQTLEKAKESGRVRSI 159
Cdd:cd19154 82 EHAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesGTMENGMSihDAVDVED-----VWRGMEKVYDEGLTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 160 GVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL-------------CWGDKEILQEKPL 226
Cdd:cd19154 157 GVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLgspgranftkstgVSPAPNLLQDPIV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17562292 227 VDLCQKYNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKS 290
Cdd:cd19154 237 KAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENF-NIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
13-291 |
2.83e-62 |
|
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: 198.13 E-value: 2.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVRTlNE 92
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR----ESGVPREEVFVTTKLWN-SD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTVEETEKQLANSLATLQTDYVDLLLIHYPRdrdtgndddyeinKSRRKIVWQTLEKAKESGRVRSIGVSNYEVYHLVEM 172
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPV-------------KGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 173 FEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLcwGDKEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSM 252
Cdd:cd19156 144 LKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPL--GQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIIT 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 17562292 253 IPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKSF 291
Cdd:cd19156 222 IPKSVHEERIQENF-DVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
12-288 |
6.60e-62 |
|
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: 197.89 E-value: 6.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 12 FKFSDGYEMPKIGLGISRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTLN 91
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 92 ENTvEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYEINKSRRKI----VWQTLEKAKESGRVRSIGVSNYEVY 167
Cdd:cd19116 83 HER-EQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSLSDIdyleTWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 168 HLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKP-------LVDLCQKYNQTPQAI 240
Cdd:cd19116 162 QINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPprlddptLVAIAKKYGKTTAQI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17562292 241 LYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKG 288
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENI-DIFDFQLTPEEVAALNSFNTN 288
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-288 |
3.12e-61 |
|
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: 196.48 E-value: 3.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 11 AFKFSDGYEMPKIGLGISRIETQQdLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTl 90
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKPGE-VGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 NENTVEETEKQLANSLATLQTDYVDLLLIHYP----RD--RDTGNDDDYEINKSRRKIVWQTLEKAKESGRVRSIGVSNY 164
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkKGvgFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 165 EVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDK----------EILQEKPLVDLCQKYN 234
Cdd:cd19123 161 SVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRpaamkaegepVLLEDPVINKIAEKHG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17562292 235 QTPQAILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKG 288
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNL-EAAEVELDASDMATIAALDRH 293
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
17-288 |
3.71e-61 |
|
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: 195.79 E-value: 3.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRIETQQdLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTLnENTVE 96
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEE-VRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPV-YLEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 97 ETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYEINKSRRKI-VWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEY 175
Cdd:cd19111 79 DTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGERELASSDVTsVWRAMEALVSEGKVKSIGLSNFNPRQINKILAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 176 AKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL---------CWGDK-EILQEKPLVDLCQKYNQTPQAILYAFA 245
Cdd:cd19111 159 AKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgspgranqsLWPDQpDLLEDPTVLAIAKELDKTPAQVLLRFV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17562292 246 HCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKG 288
Cdd:cd19111 239 LQRGTGVLPKSTNKERIEENF-EVFDFELTEEHFKKLKTLDRN 280
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
12-287 |
9.53e-61 |
|
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: 194.64 E-value: 9.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 12 FKFSDGYEMPKIGLGISRiETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTLN 91
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQ-SKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDS----GVPREEIFITTKLWCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 92 ENTVEETekqLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYEINKSRRKIV---------WQTLEKAKESGRVRSIGVS 162
Cdd:cd19117 81 HRRVEEA---LDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHepdwdfiktWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 163 NYEVYHLVEMF--EYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLVDLCQKYNQTPQAI 240
Cdd:cd19117 158 NFSIKNLEKLLasPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTPAQV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17562292 241 LYAFAHCSNTSMIPKSATPSRIHDNLHntiKIKLTEDELKSLRSLDK 287
Cdd:cd19117 238 IISWGLQRGYSVLPKSVTPSRIESNFK---LFTLSDEEFKEIDELHK 281
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
13-286 |
9.66e-61 |
|
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: 193.74 E-value: 9.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTlNE 92
Cdd:cd19131 3 TLNDGNTIPQLGLGVWQVSNDEAASA-VREALEVGYRSIDTAAIYGNEEGVGKAIRAS----GVPREELFITTKLWN-SD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTVEETEKQLANSLATLQTDYVDLLLIHYPRdrdtgndddyeinKSRRKIV--WQTLEKAKESGRVRSIGVSNYEVYHLV 170
Cdd:cd19131 77 QGYDSTLRAFDESLRKLGLDYVDLYLIHWPV-------------PAQDKYVetWKALIELKKEGRVKSIGVSNFTIEHLQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 171 EMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLcwGDKEILQEKPLVDLCQKYNQTPQAILYAFAHCSNT 250
Cdd:cd19131 144 RLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPL--GQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGL 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 17562292 251 SMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLD 286
Cdd:cd19131 222 VVIPKSVTPSRIAENF-DVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
13-286 |
1.36e-60 |
|
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: 193.17 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVrTLNE 92
Cdd:cd19133 2 TLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS----GIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTVEETEKQLANSLATLQTDYVDLLLIHYPRDrdtgndDDYEinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHLVEM 172
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG------DVYG--------AWRAMEELYKEGKIRAIGVSNFYPDRLVDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 173 FEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSM 252
Cdd:cd19133 143 ILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVV 222
|
250 260 270
....*....|....*....|....*....|....
gi 17562292 253 IPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLD 286
Cdd:cd19133 223 IPKSVRPERIAENF-DIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
13-286 |
2.11e-60 |
|
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: 192.65 E-value: 2.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVrtLNE 92
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES----GVPREELFVTTKL--WND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NT-VEETEKQLANSLATLQTDYVDLLLIHYPrdrdtgndddyeinkSRRKIV--WQTLEKAKESGRVRSIGVSNYEVYHL 169
Cdd:cd19126 76 DQrARRTEDAFQESLDRLGLDYVDLYLIHWP---------------GKDKFIdtWKALEKLYASGKVKAIGVSNFQEHHL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 170 VEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLcwGDKEILQEKPLVDLCQKYNQTPQAILYAFAHCSN 249
Cdd:cd19126 141 EELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPL--GQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHG 218
|
250 260 270
....*....|....*....|....*....|....*..
gi 17562292 250 TSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLD 286
Cdd:cd19126 219 VVTIPKSVHASRIKENA-DIFDFELSEDDMTAIDALN 254
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
15-285 |
4.94e-60 |
|
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: 192.15 E-value: 4.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLGISRIeTQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTLNENT 94
Cdd:cd19135 8 SNGVEMPILGLGTSHS-GGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKES----GVPREDLFLTTKLWPSDYGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 95 vEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDddyeiNKSRRKIVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFE 174
Cdd:cd19135 83 -ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN-----VKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 175 YAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGdkEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSMIP 254
Cdd:cd19135 157 DCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKG--KALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIP 234
|
250 260 270
....*....|....*....|....*....|.
gi 17562292 255 KSATPSRIHDNLhNTIKIKLTEDELKSLRSL 285
Cdd:cd19135 235 KSTKEERIKENC-QVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
20-283 |
1.46e-59 |
|
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: 190.17 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 20 MPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVRTLNENTvEETE 99
Cdd:cd19073 1 IPALGLGTWQLRGDDCANA-VKEALELGYRHIDTAEIYNNEAEVGEAIA----ESGVPREDLFITTKVWRDHLRP-EDLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 100 KQLANSLATLQTDYVDLLLIHYPrdrdtgnDDDYEINKSrrkivWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIR 179
Cdd:cd19073 75 KSVDRSLEKLGTDYVDLLLIHWP-------NPTVPLEET-----LGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 180 PVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGdkEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSMIPKSATP 259
Cdd:cd19073 143 IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARG--EVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSE 220
|
250 260
....*....|....*....|....
gi 17562292 260 SRIHDNLhNTIKIKLTEDELKSLR 283
Cdd:cd19073 221 DHLKENL-AIFDWELTSEDVAKID 243
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
12-285 |
9.20e-59 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 190.02 E-value: 9.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 12 FKFSDGYEMPKIGLGI-SRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTL 90
Cdd:cd19119 4 FKLNTGASIPALGLGTaSPHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 NENTVEETekqLANSLATLQTDYVDLLLIHYP----RDRDTGNDDDYEINKS---RRKI------VWQTLEKAKESGRVR 157
Cdd:cd19119 84 FYDEVERS---LDESLKALGLDYVDLLLVHWPvcfeKDSDDSGKPFTPVNDDgktRYAAsgdhitTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 158 SIGVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLVDLCQKYNQTP 237
Cdd:cd19119 161 AIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKYNVST 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17562292 238 QAILYAFAHCSNTSMIPKSATPSRIHDNLHntiKIKLTEDELKSLRSL 285
Cdd:cd19119 241 GDILISYHVRQGVIVLPKSLKPVRIVSNGK---IVSLTKEDLQKLDDI 285
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
21-285 |
2.46e-57 |
|
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: 185.80 E-value: 2.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRIETQQDlDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTLNENTvEETEK 100
Cdd:cd19128 2 PRLGFGTYKITESES-KEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQP-ENVKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 101 QLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYEINKSRRKI-------VWQTLEKAKESGRVRSIGVSNYEVYHLVEMF 173
Cdd:cd19128 80 QLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLskkpledTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 174 EYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL----CWGDKEILQEKPLVDLCQKYNQTPQAILYAF---AH 246
Cdd:cd19128 160 NYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLggsyGDGNLTFLNDSELKALATKYNTTPPQVIIAWhlqKW 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 17562292 247 CSNTSMIPKSATPSRIHDNLHNTiKIKLTEDELKSLRSL 285
Cdd:cd19128 240 PKNYSVIPKSANKSRCQQNFDIN-DLALTKEDMDAINTL 277
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
12-289 |
1.29e-55 |
|
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: 181.39 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 12 FKFSDGYEMPKIGLGISRIEtQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRtLN 91
Cdd:cd19125 3 FKLNTGAKIPAVGLGTWQAD-PGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLW-CT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 92 ENTVEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYEINKSRRKI--VWQTLEKAKESGRVRSIGVSNYEVYHL 169
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEEVLPPDIpsTWKAMEKLVDSGKVRAIGVSNFSVKKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 170 VEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL-----CWGDKEILQEKPLVDLCQKYNQTPQAILYAF 244
Cdd:cd19125 161 EDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLgspgtTWVKKNVLKDPIVTKVAEKLGKTPAQVALRW 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17562292 245 AHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGK 289
Cdd:cd19125 241 GLQRGTSVLPKSTNEERIKENI-DVFDWSIPEEDFAKFSSIEQQR 284
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
14-300 |
1.37e-55 |
|
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: 182.20 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 14 FSDGYEMPKIGLGISRIETQQdLDVSIEAALKSGYRQFDTANLYKNETFLGNSLK-KYLPQFGLTREDVFITTKVRtlne 92
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQ-VKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKeKVGPGKAVPREDLFVTSKLW---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTV---EETEKQLANSLATLQTDYVDLLLIHYPRDRDTG-----NDDDYEI--NKSRRKIVWQTLEKAKESGRVRSIGVS 162
Cdd:cd19106 76 NTKhhpEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGdnpfpKNPDGTIryDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 163 NYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL-----CW---GDKEILQEKPLVDLCQKYN 234
Cdd:cd19106 156 NFNSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrPWakpDEPVLLEEPKVKALAKKYN 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562292 235 QTPQAILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGksfpqigqtWRC 300
Cdd:cd19106 236 KSPAQILLRWQVQRGVVVIPKSVTPSRIKQNI-QVFDFTLSPEEMKQLDALNRN---------WRY 291
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
15-285 |
2.40e-55 |
|
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: 180.68 E-value: 2.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLGISRIETQQdLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLP-QFGLTREDVFITTKVRTlNEN 93
Cdd:cd19118 2 NTGNKIPAIGLGTWQAEPGE-VGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKeEPGVKREDLFITSKLWN-NSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 94 TVEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDD----YEINKSRRKI--------VWQTLEKAKESGRVRSIGV 161
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNpltaVPTNGGEVDLdlsvslvdTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 162 SNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL---CWGDKEILQEKPLVDLCQKYNQTPQ 238
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLPLLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17562292 239 AILYAFAHCSNTSMIPKSATPSRIHDNLHntiKIKLTEDELKSLRSL 285
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE---QVELSDDEFNAVTAL 283
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
13-289 |
2.84e-55 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 180.27 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVRTLNE 92
Cdd:PRK11565 8 KLQDGNVMPQLGLGVWQASNEEVITA-IHKALEVGYRSIDTAAIYKNEEGVGKALK----EASVAREELFITTKLWNDDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTVEETekqLANSLATLQTDYVDLLLIHYP---RDRDTGndddyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHL 169
Cdd:PRK11565 83 KRPREA---LEESLKKLQLDYVDLYLMHWPvpaIDHYVE--------------AWKGMIELQKEGLIKSIGVCNFQIHHL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 170 VEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLVDLCQKYNQTPQAILYAFAHCSN 249
Cdd:PRK11565 146 QRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 17562292 250 TSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGK 289
Cdd:PRK11565 226 LVVIPKSVTPSRIAENF-DVFDFRLDKDELGEIAKLDQGK 264
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
12-285 |
4.09e-54 |
|
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: 177.34 E-value: 4.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 12 FKFSDGYEMPKIGLGisrieTQQ----DLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQfGLTREDVFITTKV 87
Cdd:cd19121 4 FKLNTGASIPAVGLG-----TWQakagEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAG-GVKREDLFVTTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 RTLNENTVEETekqLANSLATLQTDYVDLLLIHYP-RDRDTGNDDDY-EINKSRRKIV--------WQTLEKAKESGRVR 157
Cdd:cd19121 78 WSTYHRRVELC---LDRSLKSLGLDYVDLYLVHWPvLLNPNGNHDLFpTLPDGSRDLDwdwnhvdtWKQMEKVLKTGKTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 158 SIGVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLVDLCQKYNQTP 237
Cdd:cd19121 155 AIGVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17562292 238 QAILYAFAHCSNTSMIPKSATPSRIHDNLHNtikIKLTEDELKSLRSL 285
Cdd:cd19121 235 GTVLISYQVARGAVVLPKSVTPDRIKSNLEI---IDLDDEDMNKLNDI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
14-288 |
8.74e-53 |
|
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: 175.02 E-value: 8.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 14 FSDGYEMPKIGLGISRIEtQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTLNeN 93
Cdd:cd19155 6 FNNGEKMPVVGLGTWQSS-PEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG-N 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 94 TVEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYEINKSRRKIV---------WQTLEKAKESGRVRSIGVSNY 164
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGKLDPTGEHKQdyttdlldiWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 165 EVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL----------CWGDKEILQEKPLVD-----L 229
Cdd:cd19155 164 NREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspGTGSPSGSSPDLLQDpvvkaI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17562292 230 CQKYNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKG 288
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENF-QVFDFELTEADMAKLSSLDKN 301
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
14-286 |
7.16e-52 |
|
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: 170.91 E-value: 7.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 14 FSDGYEMPKIGLGISRIETQQDLDvSIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVRTlNEN 93
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVE-AVVAALQAGYRLLDTAFNYENEGAVGEAVR----RSGVPREELFVTTKLPG-RHH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 94 TVEETEKQLANSLATLQTDYVDLLLIHYPrdrdtgndddyeiNKSRRKIV--WQTLEKAKESGRVRSIGVSNYEVYHLVE 171
Cdd:cd19132 75 GYEEALRTIEESLYRLGLDYVDLYLIHWP-------------NPSRDLYVeaWQALIEAREEGLVRSIGVSNFLPEHLDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 172 MFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDkEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTS 251
Cdd:cd19132 142 LIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS-GLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVV 220
|
250 260 270
....*....|....*....|....*....|....*
gi 17562292 252 MIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLD 286
Cdd:cd19132 221 PIPKSANPERQRENL-AIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
11-291 |
2.77e-51 |
|
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: 171.09 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 11 AFKFSDGYEMPKIGLGISRIETQQDLDvSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTl 90
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNATAAD-QIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 NENTVEETEKQLANSLATLQTDYVDLLLIH-------------YPRDRDTGNDDDYEINKSRRKIVWQTLEKAKESGRVR 157
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHfpiafkfvpieekYPPGFYCGDGDNFVYEDVPILDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 158 SIGVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSS------LCWGDKEILQEKPLVD--- 228
Cdd:cd19113 160 SIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSfgpqsfVELNQGRALNTPTLFEhdt 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562292 229 ---LCQKYNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLHnTIKIKLTEDELKSLRSLDKGKSF 291
Cdd:cd19113 240 iksIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLS-VNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
13-291 |
5.38e-51 |
|
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: 170.29 E-value: 5.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTLNE 92
Cdd:cd19115 6 KLNSGYDMPLVGFGLWKVNNDTCADQ-VYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTvEETEKQLANSLATLQTDYVDLLLIHYP----------RDRDTGNDDDYEINKSRRKI--VWQTLEKAKESGRVRSIG 160
Cdd:cd19115 85 DG-ERVEPICRKQLADWGIDYFDLFLIHFPialkyvdpavRYPPGWFYDGKKVEFSNAPIqeTWTAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 161 VSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLcwG-------------DKEILQEKPLV 227
Cdd:cd19115 164 VSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSF--GpqsfleldlpgakDTPPLFEHDVI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17562292 228 -DLCQKYNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLHNTiKIKLTEDELKSLRSLDKGKSF 291
Cdd:cd19115 242 kSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVT-GFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
17-285 |
8.26e-51 |
|
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: 168.21 E-value: 8.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTLNENTvE 96
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRA-VEHALELGYRHIDTAQMYGNEAQVGEAIAAS----GVPRDELFLTTKVWPDNYSP-D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 97 ETEKQLANSLATLQTDYVDLLLIHYPrdrdtgnDDDYEINKSRRkivwqTLEKAKESGRVRSIGVSNYEVYHLVEMFEYA 176
Cdd:cd19140 79 DFLASVEESLRKLRTDYVDLLLLHWP-------NKDVPLAETLG-----ALNEAQEAGLARHIGVSNFTVALLREAVELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 177 KIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLcwGDKEILQEKPLVDLCQKYNQTP-QAILYAFAHCSNTSMIPK 255
Cdd:cd19140 147 EAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPL--ARGEVLKDPVLQEIGRKHGKTPaQVALRWLLQQEGVAAIPK 224
|
250 260 270
....*....|....*....|....*....|
gi 17562292 256 SATPSRIHDNLhNTIKIKLTEDELKSLRSL 285
Cdd:cd19140 225 ATNPERLEENL-DIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
16-285 |
9.14e-51 |
|
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: 168.99 E-value: 9.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 16 DGYEMPKIGLGISriETQQDLDVSIEA---ALKSGYRQFDTANLYKNETFLGNSLKKYLpQFGL--TREDVFITTKVRtl 90
Cdd:cd19124 1 SGQTMPVIGMGTA--SDPPSPEDIKAAvleAIEVGYRHFDTAAAYGTEEALGEALAEAL-RLGLvkSRDELFVTSKLW-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 nentVEETEKQ-----LANSLATLQTDYVDLLLIHYPRDRDTGNdddYEINKSRRKI-------VWQTLEKAKESGRVRS 158
Cdd:cd19124 76 ----CSDAHPDlvlpaLKKSLRNLQLEYVDLYLIHWPVSLKPGK---FSFPIEEEDFlpfdikgVWEAMEECQRLGLTKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 159 IGVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL-----CWGDKEILQEKPLVDLCQKY 233
Cdd:cd19124 149 IGVSNFSCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgapgtKWGSNAVMESDVLKEIAAAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17562292 234 NQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLHnTIKIKLTEDELKSLRSL 285
Cdd:cd19124 229 GKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLD-IFDWELTEEDLEKISEI 279
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
13-286 |
9.43e-50 |
|
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: 166.04 E-value: 9.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVrTLNE 92
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPPEETADA-VATALADGYRLIDTAAAYGNEREVGEGIR----RSGVDRSDIFVTTKL-WISD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTVEETEKQLANSLATLQTDYVDLLLIHYPrdrdTGNDDDYEINKsrrkivWQTLEKAKESGRVRSIGVSNYEVYHLVEM 172
Cdd:cd19127 76 YGYDKALRGFDASLRRLGLDYVDLYLLHWP----VPNDFDRTIQA------YKALEKLLAEGRVRAIGVSNFTPEHLERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 173 FEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL----------CWGDKEILQEKPLVDLCQKYNQTPQAILY 242
Cdd:cd19127 146 IDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIggvmrygasgPTGPGDVLQDPTITGLAEKYGKTPAQIVL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17562292 243 AFaHCSN-TSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLD 286
Cdd:cd19127 226 RW-HLQNgVSAIPKSVHPERIAENI-DIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
15-291 |
4.73e-44 |
|
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: 151.16 E-value: 4.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLGISRIeTQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTlNENT 94
Cdd:cd19134 6 NDDNTMPVIGLGVGEL-SDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLAT-PDQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 95 VEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFE 174
Cdd:cd19134 80 FTASQAACRASLERLGLDYVDLYLIHWPAGREGKYVD-----------SWGGLMKLREEGLARSIGVSNFTAEHLENLID 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 175 YAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGdkEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSMIP 254
Cdd:cd19134 149 LTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG--RLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVIS 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 17562292 255 KSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKSF 291
Cdd:cd19134 227 RSSNPERIASNL-DVFDFELTADHMDALDGLDDGTRF 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
10-286 |
1.88e-43 |
|
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: 150.15 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 10 GAFKFSDGYEmpkiglGISRIETQQDLDvsieAALKSGYRQFDTANLY---KNETFLGNSLKKYLPQfgltREDVFITTK 86
Cdd:pfam00248 4 GTWQLGGGWG------PISKEEALEALR----AALEAGINFIDTAEVYgdgKSEELLGEALKDYPVK----RDKVVIATK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 87 VRTLNENTV-----EETEKQLANSLATLQTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGV 161
Cdd:pfam00248 70 VPDGDGPWPsggskENIRKSLEESLKRLGTDYIDLYYLHWP-DPDTPIEE-----------TWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 162 SNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPT--LKKFCDLNNIVVQSYSSLCWG--DKEILQEKP------------ 225
Cdd:pfam00248 138 SNFDAEQIEKALTKGKIPIVAVQVEYNLLRRRQEeeLLEYCKKNGIPLIAYSPLGGGllTGKYTRDPDkgpgerrrllkk 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17562292 226 -----------LVDLCQKYNQTPQ--AILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLD 286
Cdd:pfam00248 218 gtplnlealeaLEEIAKEHGVSPAqvALRWALSKPGVTIPIPGASNPEQLEDNL-GALEFPLSDEEVARIDELL 290
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
15-265 |
7.13e-43 |
|
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: 148.76 E-value: 7.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLGISrIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTLNENT 94
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 95 vEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYEiNKSRRKI---------VWQTLEKAKESGRVRSIGVSNYE 165
Cdd:cd19129 80 -ERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPR-DANGNVIyddgvtlldTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 166 VYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEKPLV-DLCQKYNQTPQAILYAF 244
Cdd:cd19129 158 LEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPKLLEDPVItAIARRVNKTPAQVLLAW 237
|
250 260
....*....|....*....|.
gi 17562292 245 AHCSNTSMIPKSATPSRIHDN 265
Cdd:cd19129 238 AIQRGTALLTTSKTPSRIREN 258
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
20-285 |
2.33e-42 |
|
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: 145.96 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 20 MPKIGLGISRIeTQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKkylpQFGLTREDVFITTKVRTLNENTvEETE 99
Cdd:cd19139 1 IPAFGLGTFRL-KDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLSK-DKLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 100 KQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYeinksrrkivWQTLEKAKESGRVRSIGVSNYEVYHL---VEMFEYA 176
Cdd:cd19139 75 PSLEESLEKLRTDYVDLTLIHWPSPNDEVPVEEY----------IGALAEAKEQGLTRHIGVSNFTIALLdeaIAVVGAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 177 KIrpVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGdkEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSMIPKS 256
Cdd:cd19139 145 AI--ATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYG--KVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSS 220
|
250 260
....*....|....*....|....*....
gi 17562292 257 ATPSRIHDNLhNTIKIKLTEDELKSLRSL 285
Cdd:cd19139 221 TKREHLRSNL-LALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
17-287 |
3.01e-41 |
|
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: 144.94 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGI---SRIETQQDLDVSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTLNEN 93
Cdd:cd19109 1 GNSIPIIGLGTysePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 94 TvEETEKQLANSLATLQTDYVDLLLIH-----------YPRDRDtgndDDYEINKSRRKIVWQTLEKAKESGRVRSIGVS 162
Cdd:cd19109 81 P-ELVRPTLERTLKVLQLDYVDLYIIEmpmafkpgdeiYPRDEN----GKWLYHKTNLCATWEALEACKDAGLVKSIGVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 163 NYEVYHLvEMF---EYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL------CWGDKE---ILQEKPLVDLC 230
Cdd:cd19109 156 NFNRRQL-ELIlnkPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLgtcrdpIWVNVSsppLLEDPLLNSIG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17562292 231 QKYNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLHnTIKIKLTEDELKSLRSLDK 287
Cdd:cd19109 235 KKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQ-IFDFSLTEEEMKDIEALNK 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
12-287 |
3.29e-41 |
|
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: 144.30 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 12 FKFSDGYEMPKIGLGI-----SRIETQQdldvSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQF-GLTREDVFITT 85
Cdd:cd19122 1 FTLNNGVKIPAVGFGTfanegAKGETYA----AVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KV-RTLNEntVEETEKQLANSLATLQTDYVDLLLIHYP--------RDRDTGNDDDYEINKSRRK---IVWQTLEKAKES 153
Cdd:cd19122 77 KVwNHLHE--PEDVKWSIDNSLKNLKLDYIDLFLVHWPiaaekndqRSPKLGPDGKYVILKDLTEnpePTWRAMEEIYES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 154 GRVRSIGVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSL-------CWGDKeILQEKPL 226
Cdd:cd19122 155 GKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgsqnqvpSTGER-VSENPTL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17562292 227 VDLCQKYNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLHNtikIKLTEDELKSLRSLDK 287
Cdd:cd19122 234 NEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS---IELSDEDFEAINQVAK 291
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
17-288 |
2.12e-40 |
|
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: 142.56 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKV-RTLNENTV 95
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEA-VKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLwCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 96 eeTEKQLANSLATLQTDYVDLLLIHYPRDRDTGN-----DDDYEINKSRRKIV--WQTLEKAKESGRVRSIGVSNYEVYH 168
Cdd:cd19107 80 --VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKelfplDESGNVIPSDTTFLdtWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 169 LVEMFEYA--KIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLC-----W---GDKEILQEKPLVDLCQKYNQTPQ 238
Cdd:cd19107 158 IERILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWakpEDPSLLEDPKIKEIAAKHNKTTA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17562292 239 AILYAFAHCSNTSMIPKSATPSRIHDNLHnTIKIKLTEDELKSLRSLDKG 288
Cdd:cd19107 238 QVLIRFPIQRNLVVIPKSVTPERIAENFK-VFDFELSSEDMATILSFNRN 286
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
19-292 |
1.01e-39 |
|
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: 140.86 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 19 EMPKIGLGISRIETQQDLDvSIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVR-TLNENTVEE 97
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTE-AVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWcTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 98 TekQLANSLATLQTDYVDLLLIHYPRDRDTGnDDDYEINKSRRKI--------VWQTLEKAKESGRVRSIGVSNYEVYHL 169
Cdd:cd19110 82 T--ACTRSLKALKLNYLDLYLIHWPMGFKPG-EPDLPLDRSGMVIpsdtdfldTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 170 VEMFEYA--KIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEI-LQEKPLVD-LCQKYNQTPQAILYAFA 245
Cdd:cd19110 159 ERLLNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVdLIDDPVIQrIAKKHGKSPAQILIRFQ 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17562292 246 HCSNTSMIPKSATPSRIHDNLHnTIKIKLTEDELKSLRSLDKG---KSFP 292
Cdd:cd19110 239 IQRNVIVIPKSVTPSRIKENIQ-VFDFELTEHDMDNLLSLDRNlrlATFP 287
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
16-286 |
3.97e-39 |
|
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: 138.12 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 16 DGYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTLNENTv 95
Cdd:cd19130 6 DGNSIPQLGYGVFKVPPADTQRA-VATALEVGYRHIDTAAIYGNEEGVGAAIAAS----GIPRDELFVTTKLWNDRHDG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 96 EETEKQLANSLATLQTDYVDLLLIHYPrdrdTGNDDDYeinksrrKIVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEY 175
Cdd:cd19130 80 DEPAAAFAESLAKLGLDQVDLYLVHWP----TPAAGNY-------VHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 176 AKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLcwGDKEILQEKPLVDLCQKYNQTP-QAILYafAHCSNT-SMI 253
Cdd:cd19130 149 TGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPL--GQGKLLGDPPVGAIAAAHGKTPaQIVLR--WHLQKGhVVF 224
|
250 260 270
....*....|....*....|....*....|...
gi 17562292 254 PKSATPSRIHDNLhNTIKIKLTEDELKSLRSLD 286
Cdd:cd19130 225 PKSVRRERMEDNL-DVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
13-287 |
1.08e-38 |
|
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: 138.13 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGisrieTQQDLDV----SIEA---ALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITT 85
Cdd:cd19108 4 KLNDGHFIPVLGFG-----TYAPEEVpkskALEAtklAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KVRTlNENTVEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGnDDDYEINKSRRKIV--------WQTLEKAKESGRVR 157
Cdd:cd19108 79 KLWC-TFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPG-EELFPKDENGKLIFdtvdlcatWEAMEKCKDAGLAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 158 SIGVSNYEVYHLvEMF---EYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLC------WGDKE--ILQEKP- 225
Cdd:cd19108 157 SIGVSNFNRRQL-EMIlnkPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGsqrdkeWVDQNspVLLEDPv 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17562292 226 LVDLCQKYNQTPQAIlyAFAHCSNTSMIP--KSATPSRIHDNLHnTIKIKLTEDELKSLRSLDK 287
Cdd:cd19108 236 LCALAKKHKRTPALI--ALRYQLQRGVVVlaKSFNEKRIKENLQ-VFEFQLTSEDMKALDGLNR 296
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
17-283 |
1.39e-38 |
|
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: 136.59 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRIETQQDLDVS--------IEAALKSGYRQFDTANLYKN---ETFLGNSLKKYLpqfgltREDVFITT 85
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSddkkaieaLRYAIELGINLIDTAEMYGGghaEELVGKAIKGFD------REDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KV--RTLNENTVEeteKQLANSLATLQTDYVDLLLIHYPrdrdtgnDDDYEINKSrrkivWQTLEKAKESGRVRSIGVSN 163
Cdd:cd19072 75 KVspDHLKYDDVI---KAAKESLKRLGTDYIDLYLIHWP-------NPSIPIEET-----LRAMEELVEEGKIRYIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 164 YEVYHLVEMFEYAK-IRPVLNQYEYQpYLTRPTLKK---FCDLNNIVVQSYSSLCWGDKEILQEKP-LVDLCQKYNQTPQ 238
Cdd:cd19072 140 FSLEELEEAQSYLKkGPIVANQVEYN-LFDREEESGllpYCQKNGIAIIAYSPLEKGKLSNAKGSPlLDEIAKKYGKTPA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17562292 239 AILYAF-AHCSNTSMIPKSATPSRIHDNLHNTiKIKLTEDELKSLR 283
Cdd:cd19072 219 QIALNWlISKPNVIAIPKASNIEHLEENAGAL-GWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
20-288 |
3.65e-38 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 135.54 E-value: 3.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 20 MPKIGLGISRIETQQDLDvSIEAALKSGYRQFDTANLYKNETFLGNSLKKYlpqfGLTREDVFITTKVRTLNENTvEETE 99
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVID-SVKTALELGYRAIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLAK-DKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 100 KQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYeinksrrkivWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIR 179
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPSPNDEVSVEEF----------MQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 180 PV-LNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGdkEILQEKPLVDLCQKYNQTPQAILYAFAHCSNTSMIPKSAT 258
Cdd:PRK11172 147 NIaTNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYG--KVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTK 224
|
250 260 270
....*....|....*....|....*....|
gi 17562292 259 PSRIHDNLhNTIKIKLTEDELKSLRSLDKG 288
Cdd:PRK11172 225 RENLASNL-LAQDLQLDAEDMAAIAALDRN 253
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
17-293 |
6.34e-36 |
|
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: 130.76 E-value: 6.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRIETQQDLDVsIEAALKSGYRQFDTANLYKNETFLGNSLKKYLPQFGLTREDVFITTKVRTlNENTVE 96
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEV-IYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWN-NFHGKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 97 ETEKQLANSLATLQTDYVDLLLIHYP---------RDRDTGNDD----DYEINKSRRKIVWQTLEKAKESGRVRSIGVSN 163
Cdd:cd19114 79 HVREAFDRQLKDYGLDYIDLYLIHFPipaayvdpaENYPFLWKDkelkKFPLEQSPMQECWREMEKLVDAGLVRNIGIAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 164 YEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDKEILQEK-----PLVD------LCQK 232
Cdd:cd19114 159 FNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHlkhftNLLEhpvvkkLADK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17562292 233 YNQTPQAILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLRSLDKGKSFPQ 293
Cdd:cd19114 239 HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNL-DITSYKLDEEDMEALYELEANARFND 298
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-285 |
7.60e-36 |
|
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: 131.07 E-value: 7.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLG---ISRIETQQDLDVSIE---AALKSGYRQFDTANLY---KNETFLGNSLKKYLpqfgltREDVFITTKV 87
Cdd:COG0667 10 GLKVSRLGLGtmtFGGPWGGVDEAEAIAildAALDAGINFFDTADVYgpgRSEELLGEALKGRP------RDDVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 -RTLNENTVEE------TEKQLANSLATLQTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIG 160
Cdd:COG0667 84 gRRMGPGPNGRglsrehIRRAVEASLRRLGTDYIDLYQLHRP-DPDTPIEE-----------TLGALDELVREGKIRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 161 VSNYEVYHLVEMFEYAK--IRPVLNQYEYQPyLTR-------PTLKKfcdlNNIVVQSYSSLCWG--------------- 216
Cdd:COG0667 152 VSNYSAEQLRRALAIAEglPPIVAVQNEYSL-LDRsaeeellPAARE----LGVGVLAYSPLAGGlltgkyrrgatfpeg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 217 ---------------DKEILQEkpLVDLCQKYNQTPQAILYAF--AHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDEL 279
Cdd:COG0667 227 draatnfvqgylterNLALVDA--LRAIAAEHGVTPAQLALAWllAQPGVTSVIPGARSPEQLEENL-AAADLELSAEDL 303
|
....*.
gi 17562292 280 KSLRSL 285
Cdd:COG0667 304 AALDAA 309
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-266 |
1.12e-32 |
|
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: 120.32 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRIETQQDLDVSIE---AALKSGYRQFDTANLY---KNETFLGNSLKKYLPqfgltREDVFITTKVRTLNENT 94
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFAlldAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-----RDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 95 V-------EETEKQLANSLATLQTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVY 167
Cdd:cd06660 76 PsrsrlspEHIRRDLEESLRRLGTDYIDLYYLHRD-DPSTPVEE-----------TLEALNELVREGKIRYIGVSNWSAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 168 HLVEMFEYAK----IRPVLNQYEY---QPYLTRPTLKKFCDLNNIVVQSYSSLCWGdkeilqekpLVDLcqkynqtpqAI 240
Cdd:cd06660 144 RLAEALAYAKahglPGFAAVQPQYsllDRSPMEEELLDWAEENGLPLLAYSPLARG---------PAQL---------AL 205
|
250 260
....*....|....*....|....*.
gi 17562292 241 LYAFAHCSNTSMIPKSATPSRIHDNL 266
Cdd:cd06660 206 AWLLSQPFVTVPIVGARSPEQLEENL 231
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
13-282 |
2.17e-32 |
|
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: 120.43 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 13 KFSDGYEMPKIGLGISRI-ETQQDLDVSIEA---ALKSGYRQFDTANLYKN---ETFLGNSLKKYlpqfgltREDVFITT 85
Cdd:cd19138 4 TLPDGTKVPALGQGTWYMgEDPAKRAQEIEAlraGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KVRTLN---ENTVEETEkqlaNSLATLQTDYVDLLLIHYPrdrdtGNDDDYEinksrrkiVWQTLEKAKESGRVRSIGVS 162
Cdd:cd19138 77 KVLPSNasrQGTVRACE----RSLRRLGTDYLDLYLLHWR-----GGVPLAE--------TVAAMEELKKEGKIRAWGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 163 NYEVYHLVEMFEYAKIRP-VLNQYEYqpYLTRP----TLKKFCDLNNIVVQSYSSLCWG---DKEILQEKPLVDLCQKYN 234
Cdd:cd19138 140 NFDTDDMEELWAVPGGGNcAANQVLY--NLGSRgieyDLLPWCREHGVPVMAYSPLAQGgllRRGLLENPTLKEIAARHG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17562292 235 QTPQAILYAFA-HCSNTSMIPKSATPSRIHDNLHnTIKIKLTEDELKSL 282
Cdd:cd19138 218 ATPAQVALAWVlRDGNVIAIPKSGSPEHARENAA-AADLELTEEDLAEL 265
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
34-283 |
2.81e-30 |
|
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: 115.70 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 34 QDLDVSIEA---ALKSGYRQFDTANLYKN---ETFLGNSLKKYlpqfgltREDVFITTKV--------RTLNENTVEETE 99
Cdd:cd19084 22 VDDQESIEAikaAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATKCglrwdggkGVTKDLSPESIR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 100 KQLANSLATLQTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIr 179
Cdd:cd19084 95 KEVEQSLRRLQTDYIDLYQIHWP-DPNTPIEE-----------TAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGPI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 180 pVLNQYEYQPyLTRPT---LKKFCDLNNIVVQSYSSLCWG---------------D----------------KEILQEkp 225
Cdd:cd19084 162 -VSLQPPYSM-LEREIeeeLLPYCRENGIGVLPYGPLAQGlltgkykkeptfppdDrrsrfpffrgenfeknLEIVDK-- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 226 LVDLCQKYNQTP-Q-AILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLR 283
Cdd:cd19084 238 LKEIAEKYGKSLaQlAIAWTLAQPGVTSAIVGAKNPEQLEENA-GALDWELTEEELKEID 296
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
17-282 |
5.03e-30 |
|
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: 114.20 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRI------ETQQDLDV--SIEAALKSGYRQFDTANLY---KNETFLGNSLKkYLPqfgltREDVFITT 85
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpDYSRDEEMveLLKTAIELGYTHIDTAEMYgggHTEELVGKAIK-DFP-----REDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KVrtLNEN-TVEETEKQLANSLATLQTDYVDLLLIHYPrdrdtgndddyeiNKS-RRKIVWQTLEKAKESGRVRSIGVSN 163
Cdd:cd19137 75 KV--WPTNlRYDDLLRSLQNSLRRLDTDYIDLYLIHWP-------------NPNiPLEETLSAMAEGVRQGLIRYIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 164 YEVYHLVEMFEYAKIRPVLNQYEYQPYLTRPT---LKKFCDLNNIVVQSYSSLcwgDKEILQEKPLVD-LCQKYNQTP-Q 238
Cdd:cd19137 140 FNRRLLEEAISKSQTPIVCNQVKYNLEDRDPErdgLLEYCQKNGITVVAYSPL---RRGLEKTNRTLEeIAKNYGKTIaQ 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17562292 239 AILYAFAHCSNTSMIPKSATPSRIHDNLHNTiKIKLTEDELKSL 282
Cdd:cd19137 217 IALAWLIQKPNVVAIPKAGRVEHLKENLKAT-EIKLSEEEMKLL 259
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
21-216 |
4.19e-29 |
|
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: 112.29 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGI-----SRIETQQDLDVS---IEAALKSGYRQFDTANLYKN---ETFLGNSLKKylpqfglTREDVFITTKVRt 89
Cdd:cd19085 2 SRLGLGCwqfggGYWWGDQDDEESiatIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVS- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 90 LNENTVEETEKQLANSLATLQTDYVDLLLIHYPrdrdtgnddDYEINkSRRKIvwQTLEKAKESGRVRSIGVSNYEVYHL 169
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP---------SSDVP-LEETM--EALEKLKEEGKIRAIGVSNFGPAQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17562292 170 VEMFEYAKIrpVLNQ-----------YEYQPYltrptlkkfCDLNNIVVQSYSSLCWG 216
Cdd:cd19085 142 EEALDAGRI--DSNQlpynllwraieYEILPF---------CREHGIGVLAYSPLAQG 188
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
40-283 |
2.12e-26 |
|
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: 105.00 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 40 IEAALKSGYRQFDTANLY---KNETFLGNSLKKYLPqfgltREDVFITTKV----RTLNENTVEETEKqlaNSLATLQTD 112
Cdd:cd19093 32 FDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIATKFaplpWRLTRRSVVKALK---ASLERLGLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 113 YVDLLLIHYPRDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAK---IRPVLNQYEYQp 189
Cdd:cd19093 104 SIDLYQLHWPGPWYSQIEA-----------LMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKergVPLASNQVEYS- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 190 yLTRPT-----LKKFCDLNNIVVQSYSSLCWG---------------------DKEILQEKPLVD----LCQKYNQTPQA 239
Cdd:cd19093 172 -LLYRDpeqngLLPACDELGITLIAYSPLAQGlltgkyspenpppggrrrlfgRKNLEKVQPLLDaleeIAEKYGKTPAQ 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17562292 240 ILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSLR 283
Cdd:cd19093 251 VALNWLIAKGVVPIPGAKNAEQAEENA-GALGWRLSEEEVAELD 293
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-267 |
2.92e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 103.33 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLG---ISRIeTQQDLDVSIEAALKSGYRQFDTANLYKN-ETFLGNSLKKYlpqfgltREDVFITTKVrtlNE 92
Cdd:cd19100 8 GLKVSRLGFGggpLGRL-SQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKT---GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTVEETEKQLANSLATLQTDYVDLLLIHYPRDrdtgnDDDYEINKSRRKiVWQTLEKAKESGRVRSIGVS--NYEVYH-L 169
Cdd:cd19100 77 RDYEGAKRDLERSLKRLGTDYIDLYQLHAVDT-----EEDLDQVFGPGG-ALEALLEAKEEGKIRFIGISghSPEVLLrA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 170 VEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWGDkeILQEKPLvdlcqkynQTPQAILYAFAHCSN 249
Cdd:cd19100 151 LETGEFDVVLFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGR--LLSGDPL--------DPEQALRYALSLPPV 220
|
250
....*....|....*...
gi 17562292 250 TSMIPKSATPSRIHDNLH 267
Cdd:cd19100 221 DVVIVGMDSPEELDENLA 238
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
17-162 |
8.20e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 104.90 E-value: 8.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRIET--QQDLDVSIEAALKSGYRQFDTANLY-KNETFLGNSLKKYlpqfgltREDVFITTKVrTLNEN 93
Cdd:COG1453 10 GLEVSVLGFGGMRLPRkdEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKL-PPWVR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 94 TVEETEKQLANSLATLQTDYVDLLLIHYPRDRDTgndddyeINKSRRKI-VWQTLEKAKESGRVRSIGVS 162
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEED-------LEKVLKPGgALEALEKAKAEGKIRHIGFS 144
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
21-164 |
6.44e-23 |
|
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: 94.99 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRI------ETQQDLDVSIEAALKSGYRQFDTANLYKN-ETFLGNSLKkylpqfGLTREDVFITTKVRTLNEN 93
Cdd:cd19095 1 SVLGLGTSGIgrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17562292 94 -------TVEETEKQLANSLATLQTDYVDLLLIHYPrDRDTGNDDDYEinksrrkivwqTLEKAKESGRVRSIGVSNY 164
Cdd:cd19095 75 grdrkdfSPAAIRASIERSLRRLGTDYIDLLQLHGP-SDDELTGEVLE-----------TLEDLKAAGKVRYIGVSGD 140
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
22-162 |
9.00e-23 |
|
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: 94.08 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 22 KIGLGISRIETQQDLDVS-------IEAALKSGYRQFDTANLY---KNETFLGNSLKKylpqfglTREDVFITTKV-RTL 90
Cdd:cd19086 5 EIGFGTWGLGGDWWGDVDdaeairaLRAALDLGINFFDTADVYgdgHSERLLGKALKG-------RRDKVVIATKFgNRF 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17562292 91 NENTVEET-------EKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVS 162
Cdd:cd19086 78 DGGPERPQdfspeyiREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDE-----------LFEALEKLKQEGKIRAYGVS 145
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
21-169 |
3.13e-22 |
|
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: 93.39 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLG---ISRIETQQDLDVS---IEAALKSGYRQFDTANLYKN-ETFLGNSLKkylpqfGLTREDVFITTKVRTLNEN 93
Cdd:cd19090 1 SALGLGtagLGGVFGGVDDDEAvatIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKVGRLPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 94 TV----EETEKQLANSLATLQTDYVDLLLIHYPrdrdtgnDDDYEINKSRRKIVWQTLEKAKESGRVRSIGVSNYEVYHL 169
Cdd:cd19090 75 TAdysaDRVRRSVEESLERLGRDRIDLLMIHDP-------ERVPWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLL 147
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-162 |
4.97e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 92.26 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRieTQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKkylpqfGLTREDVFITTKVR-TLNE 92
Cdd:cd19105 10 GLKVSRLGFGGGG--LPRESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALK------GLRRDKVFLATKASpRLDK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 93 NTVEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDYeinksrrkiVWQTLEKAKESGRVRSIGVS 162
Cdd:cd19105 82 KDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEE---------LLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
15-278 |
6.03e-22 |
|
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: 93.00 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLGISRI----ETQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKKylpQFGLtREDVFITTK- 86
Cdd:cd19092 1 PEGLEVSRLVLGCMRLadwgESAEELLSLIEAALELGITTFDHADIYgggKCEELFGEALAL---NPGL-REKIEIQTKc 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 87 -VRTLNENTVEETE----------KQLANSLATLQTDYVDLLLIHYPrdrDTGNDDDyEinksrrkiVWQTLEKAKESGR 155
Cdd:cd19092 77 gIRLGDDPRPGRIKhydtskehilASVEGSLKRLGTDYLDLLLLHRP---DPLMDPE-E--------VAEAFDELVKSGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 156 VRSIGVSNYEVYHLVEMFEYAKIRPVLNQYEYQPYLTRP----TLkKFCDLNNIVVQSYSSLCWG---------DKEILQ 222
Cdd:cd19092 145 VRYFGVSNFTPSQIELLQSYLDQPLVTNQIELSLLHTEAiddgTL-DYCQLLDITPMAWSPLGGGrlfggfderFQRLRA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 223 EkpLVDLCQKYNQTPQAILYAF--AHCSntSMIPKSAT--PSRIHDNLhNTIKIKLTEDE 278
Cdd:cd19092 224 A--LEELAEEYGVTIEAIALAWllRHPA--RIQPILGTtnPERIRSAV-KALDIELTREE 278
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
21-187 |
2.69e-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: 90.70 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRIETQQDLDVSIEA-------ALKSGYRQFDTANLY---KNETFLGNSLKKYLpqfgltREDVFITTKVRTL 90
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIDEEKaiemiryAIDAGINYFDTAYGYgggKSEEILGEALKEGP------REKFYLATKLPPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 NENTVEETEKQLANSLATLQTDYVDLLLIHyprdrdTGNDDDYEINKSRRKIvWQTLEKAKESGRVRSIGVS---NYEVy 167
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH------GLNSPEWLEKARKGGL-LEFLEKAKKEGLIRHIGFSfhdSPEL- 146
|
170 180
....*....|....*....|
gi 17562292 168 hLVEMFEYAKIRPVLNQYEY 187
Cdd:cd19096 147 -LKEILDSYDFDFVQLQYNY 165
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
15-278 |
4.63e-21 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 90.60 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLGISRIEtQQDLDVS-----IEAALKSGYRQFDTANLYKN---ETFLGNSLKKylpQFGLtREDVFITTK 86
Cdd:COG4989 8 ASGLSVSRIVLGCMRLG-EWDLSPAeaaalIEAALELGITTFDHADIYGGytcEALFGEALKL---SPSL-REKIELQTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 87 -----VRTLNENTV-------EETEKQLANSLATLQTDYVDLLLIHYPrdrdtgnddDY-----EINKsrrkivwqTLEK 149
Cdd:COG4989 83 cgirlPSEARDNRVkhydtskEHIIASVEGSLRRLGTDYLDLLLLHRP---------DPlmdpeEVAE--------AFDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 150 AKESGRVRSIGVSNYEVYHlVEMFE-YAKIRPVLNQYEYQPYLTRP----TLkKFCDLNNIVVQSYSSLCWG-------D 217
Cdd:COG4989 146 LKASGKVRHFGVSNFTPSQ-FELLQsALDQPLVTNQIELSLLHTDAfddgTL-DYCQLNGITPMAWSPLAGGrlfggfdE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562292 218 KEI-LQEKpLVDLCQKYNQTPQAILYAF--AHCSNtsMIP--KSATPSRIHDNLhNTIKIKLTEDE 278
Cdd:COG4989 224 QFPrLRAA-LDELAEKYGVSPEAIALAWllRHPAG--IQPviGTTNPERIKAAA-AALDIELTREE 285
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
40-282 |
2.31e-20 |
|
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: 89.18 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 40 IEAALKSGYRQFDTANLYKN---ETFLGNSLKKYLPqfgltREDVFITTKVR---TLNENTVEETEK----QLANSLATL 109
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgasEEILGRALKEFAP-----RDEVVIATKVYfpmGDGPNGRGLSRKhimaEVDASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 110 QTDYVDLLLIHYPrDRDTgndDDYEInksrrkivWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKI----RPVLNQY 185
Cdd:cd19079 116 GTDYIDLYQIHRW-DYET---PIEET--------LEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKngwtKFVSMQN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 186 EYQpYLTRPTLK---KFCDLNNIVVQSYSSLCWG------------------------------DKEILQEkpLVDLCQK 232
Cdd:cd19079 184 HYN-LLYREEERemiPLCEEEGIGVIPWSPLARGrlarpwgdtterrrsttdtaklkydyfteaDKEIVDR--VEEVAKE 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17562292 233 YNQTPQAILYA--FAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSL 282
Cdd:cd19079 261 RGVSMAQVALAwlLSKPGVTAPIVGATKLEHLEDAV-AALDIKLSEEEIKYL 311
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-284 |
2.79e-20 |
|
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: 88.87 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLGISRI--------ETQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfgltREDVFITT 85
Cdd:cd19149 8 GIEASVIGLGTWAIgggpwwggSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGR-------RDKVVLAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KV-----------------RTLNENTVEET-EKQLANSLATLQTDYVDLLLIHYPrdrdtgnDDDYEINKSrrkivWQTL 147
Cdd:cd19149 81 KCglrwdreggsfffvrdgVTVYKNLSPESiREEVEQSLKRLGTDYIDLYQTHWQ-------DVETPIEET-----MEAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 148 EKAKESGRVRSIGVSNYEVYHLVEMFEYAKIRPVLNQY---------EYQPYltrptlkkfCDLNNIVVQSYSSL----- 213
Cdd:cd19149 149 EELKRQGKIRAIGASNVSVEQIKEYVKAGQLDIIQEKYsmldrgiekELLPY---------CKKNNIAFQAYSPLeqgll 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 214 -------------------CWGDKEILQE-----KPLVDLCQKYNQT-PQ-AILYAFAHCSNTSMIPKSATPSRIHDNLH 267
Cdd:cd19149 220 tgkitpdrefdagdarsgiPWFSPENREKvlallEKWKPLCEKYGCTlAQlVIAWTLAQPGITSALCGARKPEQAEENAK 299
|
330
....*....|....*..
gi 17562292 268 nTIKIKLTEDELKSLRS 284
Cdd:cd19149 300 -AGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
5-285 |
7.12e-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: 87.47 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 5 TNVVGGAFKFSDGYEmpkiglgisriETQQDLdvsIEAALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfglTREDV 81
Cdd:cd19083 18 TNAVGGHNLYPNLDE-----------EEGKDL---VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 82 FITTKVRTLN-------ENTVEETEKQLANSLATLQTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESG 154
Cdd:cd19083 78 VIATKGAHKFggdgsvlNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFP-DGETPKAE-----------AVGALQELKDEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 155 RVRSIGVSNYEVYHLVEMFEYAKIRPVlnQYEYQpYLTRPTLKKF---CDLNNIVVQSYSSLCWG-------------DK 218
Cdd:cd19083 146 KIRAIGVSNFSLEQLKEANKDGYVDVL--QGEYN-LLQREAEEDIlpyCVENNISFIPYFPLASGllagkytkdtkfpDN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 219 EILQEKP----------------LVDLCQKYNQTPQ--AILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELK 280
Cdd:cd19083 223 DLRNDKPlfkgerfsenldkvdkLKSIADEKGVTVAhlALAWYLTRPAIDVVIPGAKRAEQVIDNL-KALDVTLTEEEIA 301
|
....*
gi 17562292 281 SLRSL 285
Cdd:cd19083 302 FIDAL 306
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-245 |
7.66e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 86.81 E-value: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 40 IEAALKSGYRQFDTANLYKN-ETFLGnslkkylpQFGLTREDVFITTKVRTLNENT---VEETEKQLANSLATLQTDYVD 115
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGDsEKVLG--------KFLKRLDKFKIITKLPPLKEDKkedEAAIEASVEASLKRLKVDSLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 116 LLLIHYPRDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSnyeVYHlVEMFEYAKIRP----------VLNQY 185
Cdd:cd19097 104 GLLLHNPDDLLKHGGK-----------LVEALLELKKEGLIRKIGVS---VYS-PEELEKALESFkidiiqlpfnILDQR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17562292 186 eyqpYLTRPTLKKFCDlNNIVVQSYSSLCWG----DKEILQEKP---------LVDLCQKYNQTPQAILYAFA 245
Cdd:cd19097 169 ----FLKSGLLAKLKK-KGIEIHARSVFLQGlllmEPDKLPAKFapakpllkkLHELAKKLGLSPLELALGFV 236
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
24-216 |
5.64e-18 |
|
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: 82.25 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 24 GLGISRI--------ETQQDLDVSIE---AALKSGYRQFDTANLYKN---ETFLGNSLKKYlpqfglTREDVFITTKV-- 87
Cdd:cd19074 1 GLKVSELslgtwltfGGQVDDEDAKAcvrKAYDLGINFFDTADVYAAgqaEEVLGKALKGW------PRESYVISTKVfw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 --------RTLNENTVEEtekQLANSLATLQTDYVDLLLIHYPrDRDTgndddyeinkSRRKIVWqTLEKAKESGRVRSI 159
Cdd:cd19074 75 ptgpgpndRGLSRKHIFE---SIHASLKRLQLDYVDIYYCHRY-DPET----------PLEETVR-AMDDLIRQGKILYW 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17562292 160 GVSNYEVYHLVEMFEYAK----IRPVLNQYEYQpYLTR---PTLKKFCDLNNIVVQSYSSLCWG 216
Cdd:cd19074 140 GTSEWSAEQIAEAHDLARqfglIPPVVEQPQYN-MLWReieEEVIPLCEKNGIGLVVWSPLAQG 202
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
39-216 |
5.71e-18 |
|
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: 82.35 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 39 SIEAALKSGYRQFDTANLY---KNETFLGNSLKKYLPqfgltREDVFITTKV--------RTLNENTVEETEKQLANSLA 107
Cdd:cd19148 30 TIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYGK-----RDRVVIATKVglewdeggEVVRNSSPARIRKEVEDSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 108 TLQTDYVDLLLIHYPrdrdtgnDDDYEINKSRRkivwqTLEKAKESGRVRSIGVSNYEVYhlvEMFEYAKIRPV-LNQYE 186
Cdd:cd19148 105 RLQTDYIDLYQVHWP-------DPLVPIEETAE-----ALKELLDEGKIRAIGVSNFSPE---QMETFRKVAPLhTVQPP 169
|
170 180 190
....*....|....*....|....*....|....
gi 17562292 187 YQpyLTRPTLKK----FCDLNNIVVQSYSSLCWG 216
Cdd:cd19148 170 YN--LFEREIEKdvlpYARKHNIVTLAYGALCRG 201
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
17-280 |
6.40e-18 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 81.83 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLG---ISRIETQQDLDVSIEA---ALKSGYRQFDTANLY---KNETFLGNSLKkylpqfGLTREDVFITTKV 87
Cdd:cd19163 10 GLKVSKLGFGaspLGGVFGPVDEEEAIRTvheALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 -R-TLNENTV-----EETEKQLANSLATLQTDYVDLLLIHyprdrdtgnddDYEINKSRRKIVWQT---LEKAKESGRVR 157
Cdd:cd19163 84 gRyGLDPDKMfdfsaERITKSVEESLKRLGLDYIDIIQVH-----------DIEFAPSLDQILNETlpaLQKLKEEGKVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 158 SIGVSNYEVYHLVEMFE--YAKIRPVLNqyeYQPY-LTRPTLKKFCDL---NNIVVQSYSSLCWG-------------DK 218
Cdd:cd19163 153 FIGITGYPLDVLKEVLErsPVKIDTVLS---YCHYtLNDTSLLELLPFfkeKGVGVINASPLSMGlltergppdwhpaSP 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17562292 219 EILQE-KPLVDLCQKYNQ--TPQAILYAFAHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELK 280
Cdd:cd19163 230 EIKEAcAKAAAYCKSRGVdiSKLALQFALSNPDIATTLVGTASPENLRKNL-EAAEEPLDAHLLA 293
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
21-216 |
1.29e-17 |
|
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: 81.06 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLG------ISRIETQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGnslkkylpQFGLTREDVFITTKVRTLN 91
Cdd:cd19075 1 PKIILGtmtfgsQGRFTTAEAAAELLDAFLERGHTEIDTARVYpdgTSEELLG--------ELGLGERGFKIDTKANPGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 92 EN--TVEETEKQLANSLATLQTDYVDLLLIHYPrDRDTgnddDYEinksrrkivwQTLE---KAKESGRVRSIGVSNYEV 166
Cdd:cd19075 73 GGglSPENVRKQLETSLKRLKVDKVDVFYLHAP-DRST----PLE----------ETLAaidELYKEGKFKEFGLSNYSA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17562292 167 YHLVEMFEYAK----IRPVLNQYEYQPyLTR-------PTLKKFcdlnNIVVQSYSSLCWG 216
Cdd:cd19075 138 WEVAEIVEICKengwVLPTVYQGMYNA-ITRqvetelfPCLRKL----GIRFYAYSPLAGG 193
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-162 |
3.47e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 77.36 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 22 KIGLGISRIETQQDLDV----SIEAALKSGYRQFDTANLYKN---ETFLGNSLKKYLPQFGLTREDVFITTKV------- 87
Cdd:cd19099 5 SLGLGTYRGDSDDETDEeyreALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 --------------RTLNENTVEET-----------EKQLANSLATLQTDYVDLLLIHYP-RDRDtgnDDDYEINKSRRK 141
Cdd:cd19099 85 deplrplkyleeklGRGLIDVADSAglrhcispaylEDQIERSLKRLGLDTIDLYLLHNPeEQLL---ELGEEEFYDRLE 161
|
170 180
....*....|....*....|.
gi 17562292 142 IVWQTLEKAKESGRVRSIGVS 162
Cdd:cd19099 162 EAFEALEEAVAEGKIRYYGIS 182
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-279 |
4.49e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 76.94 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 40 IEAALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfgltREDVFITTKVRTLNENTVEETE--------KQLANSLAT 108
Cdd:cd19102 32 IRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKCGLLWDEEGRIRRslkpasirAECEASLRR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 109 LQTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVyhlVEMFEYAKIRPVlnQYEYQ 188
Cdd:cd19102 105 LGVDVIDLYQIHWP-DPDEPIEE-----------AWGALAELKEEGKVRAIGVSNFSV---DQMKRCQAIHPI--ASLQP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 189 PY--LTRPTLKK---FCDLNNIVVQSYSSLCWG------DKEILQEKP---------------------LVD----LCQK 232
Cdd:cd19102 168 PYslLRRGIEAEilpFCAEHGIGVIVYSPMQSGlltgkmTPERVASLPaddwrrrspffqepnlarnlaLVDalrpIAER 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17562292 233 YNQTPQ--AILYAFAHCSNTSMIPKSATPSRIHDNLHnTIKIKLTEDEL 279
Cdd:cd19102 248 HGRTVAqlAIAWVLRRPEVTSAIVGARRPDQIDETVG-AADLRLTPEEL 295
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-162 |
5.46e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 76.92 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 19 EMPKIGLGISRI-------------ETQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKkylpqfGLtREDVF 82
Cdd:cd19104 4 RFGRTGLKVSELtfggggigglmgrTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALK------GL-PAGPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 83 ITTKVRTLNENT---VEETEKQLANSLATLQTDYVDLLLIH--YPRDRDTGNDDDYEINKSRRKI-VWQTLEKAKESGRV 156
Cdd:cd19104 77 ITTKVRLDPDDLgdiGGQIERSVEKSLKRLKRDSVDLLQLHnrIGDERDKPVGGTLSTTDVLGLGgVADAFERLRSEGKI 156
|
....*.
gi 17562292 157 RSIGVS 162
Cdd:cd19104 157 RFIGIT 162
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
40-179 |
6.60e-15 |
|
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: 73.76 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 40 IEAALKSGYRQFDTANLY---KNETFLGNSLKKylpqfglTREDVFITTKV--RTLNENTVEETE-----KQLANSLATL 109
Cdd:cd19087 36 MDRALDAGINFFDTADVYgggRSEEIIGRWIAG-------RRDDIVLATKVfgPMGDDPNDRGLSrrhirRAVEASLRRL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 110 QTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIR 179
Cdd:cd19087 109 QTDYIDLYQMHHF-DRDTPLEE-----------TLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARR 166
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
21-244 |
1.18e-14 |
|
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: 72.59 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRIETQQDLDVSIE---AALKSGYRQFDTANLYKNETFLGNS---LKKYLPQFGLtREDVFITTK-----VRT 89
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFAlldAFVELGGNFIDTARVYGDWVERGAServIGEWLKSRGN-RDKVVIATKgghpdLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 90 LNENTV--EETEKQLANSLATLQTDYVDLLLIHYprdrdtgndDDYEINKSrrKIVwQTLEKAKESGRVRSIGVSNYEVY 167
Cdd:cd19082 80 MSRSRLspEDIRADLEESLERLGTDYIDLYFLHR---------DDPSVPVG--EIV-DTLNELVRAGKIRAFGASNWSTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 168 HLVEMFEYAKIR----PVLNQ------YEYQPYLTRPTL-------KKFCDLNNIVVQSYSSLCWG--------DKEILQ 222
Cdd:cd19082 148 RIAEANAYAKAHglpgFAASSpqwslaRPNEPPWPGPTLvamdeemRAWHEENQLPVFAYSSQARGffskraagGAEDDS 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 17562292 223 EKP--------------LVDLCQKYNQTPQAILYAF 244
Cdd:cd19082 228 ELRrvyyseenferlerAKELAEEKGVSPTQIALAY 263
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
10-187 |
3.12e-14 |
|
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: 71.88 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 10 GAFKFSDGYEMPKIGLGISrietQQDLDVSIEAALKSGYRQFDTANLYKN---ETFLGNSLKKYlpqfgltREDVFITTK 86
Cdd:cd19091 19 GTMTFGGGGGFFGAWGGVD----QEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR-------RDDVLIATK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 87 VRTLNENTVEETE-------KQLANSLATLQTDYVDLLLIHYpRDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSI 159
Cdd:cd19091 88 VRGRMGEGPNDVGlsrhhiiRAVEASLKRLGTDYIDLYQLHG-FDALTPLEE-----------TLRALDDLVRQGKVRYI 155
|
170 180 190
....*....|....*....|....*....|..
gi 17562292 160 GVSNYEVYHLVEMF----EYAKIRPVLNQYEY 187
Cdd:cd19091 156 GVSNFSAWQIMKALgiseRRGLARFVALQAYY 187
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
15-162 |
1.34e-13 |
|
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: 69.94 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLG---ISRIETQQDLDVSIE---AALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfgltREDVFITT 85
Cdd:cd19076 7 TQGLEVSALGLGcmgMSAFYGPADEEESIAtlhRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 K----------VRTLNeNTVEETEKQLANSLATLQTDYVDLLLIHYPrdrdtgnDDDYEINKSrrkivWQTLEKAKESGR 155
Cdd:cd19076 80 KfgivrdpgsgFRGVD-GRPEYVRAACEASLKRLGTDVIDLYYQHRV-------DPNVPIEET-----VGAMAELVEEGK 146
|
....*..
gi 17562292 156 VRSIGVS 162
Cdd:cd19076 147 VRYIGLS 153
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
22-216 |
1.76e-13 |
|
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: 69.52 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 22 KIGLGISRIETQQDLDVSIE---AALKSGYRQFDTANLY----------KNETFLGNSLKKylpqFGLtREDVFITTKV- 87
Cdd:cd19094 3 EICLGTMTWGEQNTEAEAHEqldYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKK----KGN-RDKVVLATKVa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 ------RTLNENTVEETEKQLAN----SLATLQTDYVDLLLIHYPrDRDT--GNDDDYEINKSRRKIV-----WQTLEKA 150
Cdd:cd19094 78 gpgegiTWPRGGGTRLDRENIREavegSLKRLGTDYIDLYQLHWP-DRYTplFGGGYYTEPSEEEDSVsfeeqLEALGEL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17562292 151 KESGRVRSIGVSNYEVYHLVEMFEYAKI----RPVLNQYEYQpYLTR---PTLKKFCDLNNIVVQSYSSLCWG 216
Cdd:cd19094 157 VKAGKIRHIGLSNETPWGVMKFLELAEQlglpRIVSIQNPYS-LLNRnfeEGLAEACHRENVGLLAYSPLAGG 228
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-285 |
3.93e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 68.51 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 32 TQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfglTREDVFITTK----VRTLNENTVEETekqLAN 104
Cdd:cd19103 30 DEDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKRY------PREDYIISTKftpqIAGQSADPVADM---LEG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 105 SLATLQTDYVDLLLIHYPRDrdtgndddyeINKSRRKIVwqTLEKakeSGRVRSIGVSNY---EVYHLVEMFEYA--KIR 179
Cdd:cd19103 101 SLARLGTDYIDIYWIHNPAD----------VERWTPELI--PLLK---SGKVKHVGVSNHnlaEIKRANEILAKAgvSLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 180 PVLNQYEyqpYLTRPTLK----KFCDLNNIVVQSYSSLCWG------DKE---------------ILQE-KPLVDLC--- 230
Cdd:cd19103 166 AVQNHYS---LLYRSSEEagilDYCKENGITFFAYMVLEQGalsgkyDTKhplpegsgraetynpLLPQlEELTAVMaei 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17562292 231 -QKYNQTPQAILYAFAHCSNTSMIPKSATPSRIhDNLHNTIKIKLTEDELKSLRSL 285
Cdd:cd19103 243 gAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHV-EDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
21-267 |
6.85e-13 |
|
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: 67.63 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLG------ISRIETQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKkylpqfGLTREDVFITTKV-RTL 90
Cdd:cd19152 1 PKLGFGtaplgnLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYgagLSEERLGAALR------ELGREDYVISTKVgRLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 91 -NENTVEET----------------------EKQLANSLATLQTDYVDLLLIHyprDRDTGNDDDYEINKSRRKIV--WQ 145
Cdd:cd19152 75 vPLQEVEPTfepgfwnplpfdavfdysydgiLRSIEDSLQRLGLSRIDLLSIH---DPDEDLAGAESDEHFAQAIKgaFR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 146 TLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIRPVL--NQYEyqpYLTRPTLKKF---CDLNNIVVQS---YSS-LCWG 216
Cdd:cd19152 152 ALEELREEGVIKAIGLGVNDWEVILRILEEADLDWVMlaGRYT---LLDHSAARELlpeCEKRGVKVVNagpFNSgFLAG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562292 217 ----DKEILQEKP--LVD-------LCQKYNQTPQ--AILYAFAHCSNTSMIPKSATPSRIHDNLH 267
Cdd:cd19152 229 gdnfDYYEYGPAPpeLIArrdrieaLCEQHGVSLAaaALQFALAPPAVASVAPGASSPERVEENVA 294
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
40-177 |
1.59e-12 |
|
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: 66.53 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 40 IEAALKSGYRQFDTANLY-KNETFLGNSLKKYLPQFglTREDVFITTKVRTLNENTVEET----EKQLANSLATLQTDYV 114
Cdd:cd19164 40 VRRALELGIRAFDTSPYYgPSEIILGRALKALRDEF--PRDTYFIITKVGRYGPDDFDYSpewiRASVERSLRRLHTDYL 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17562292 115 DLLLIHyprdrdtgnddDYEInKSRRKIV--WQTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAK 177
Cdd:cd19164 118 DLVYLH-----------DVEF-VADEEVLeaLKELFKLKDEGKIRNVGISGYPLPVLLRLAELAR 170
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
52-216 |
8.77e-12 |
|
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: 64.54 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 52 DTANLY----------KNETFLGNSLKKYLPqfgltREDVFITTKVR-TLNENTV----EETEKQLANSLATLQTDYVDL 116
Cdd:cd19081 44 DTADVYsawvpgnaggESETIIGRWLKSRGK-----RDRVVIATKVGfPMGPNGPglsrKHIRRAVEASLRRLQTDYIDL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 117 LLIHYPrdrdtgnDDDYEINKSRRkivwqTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAK----IRPVLNQYEYQPY-- 190
Cdd:cd19081 119 YQAHWD-------DPATPLEETLG-----ALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEYNLVdr 186
|
170 180
....*....|....*....|....*..
gi 17562292 191 -LTRPTLKKFCDLNNIVVQSYSSLCWG 216
Cdd:cd19081 187 eSFEGELLPLCREEGIGVIPYSPLAGG 213
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
21-266 |
1.01e-11 |
|
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: 63.78 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRIETQ------QDLDVSIE---AALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfgltREDVFITTK-- 86
Cdd:cd19088 2 SRLGYGAMRLTGPgiwgppADREEAIAvlrRALELGVNFIDTADSYgpdVNERLIAEALHPY-------PDDVVIATKgg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 87 -VRTLNENTV-----EETEKQLANSLATLQTDYVDLLLIHYPrdrdtgnDDDYEINKSrrkivWQTLEKAKESGRVRSIG 160
Cdd:cd19088 75 lVRTGPGWWGpdgspEYLRQAVEASLRRLGLDRIDLYQLHRI-------DPKVPFEEQ-----LGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 161 VSNYEVYHLVEMFEYAKIRPVLNQyeYQPYLTRPT-LKKFCDLNNIVVQSYSSLCWGDKeiLQEKPLVD-LCQKYNQTPQ 238
Cdd:cd19088 143 LSNVTVAQIEEARAIVRIVSVQNR--YNLANRDDEgVLDYCEAAGIAFIPWFPLGGGDL--AQPGGLLAeVAARLGATPA 218
|
250 260 270
....*....|....*....|....*....|
gi 17562292 239 AILYA--FAHCSNTSMIPKSATPSRIHDNL 266
Cdd:cd19088 219 QVALAwlLARSPVMLPIPGTSSVEHLEENL 248
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
31-181 |
2.79e-11 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 62.94 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 31 ETQQDLDVSIEAALKSGYRQFDTANLYKN---ETFLGNSLKKylpqFGLTREDVFITTKVRTLNENTVEET----EKQLA 103
Cdd:cd19153 30 LEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAA----LQVPRSSYTVATKVGRYRDSEFDYSaervRASVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 104 NSLATLQTDYVDLLLIHyprdrdtgnddDYEINKsRRKIVWQT---LEKAKESGRVRSIGVSNYEVYHLVEMFEYAKIRP 180
Cdd:cd19153 106 TSLERLHTTYLDVVYLH-----------DIEFVD-YDTLVDEAlpaLRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS 173
|
.
gi 17562292 181 V 181
Cdd:cd19153 174 L 174
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
21-162 |
5.28e-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: 61.99 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRI-----ETQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKKYLpqfgltREDVFITTKV-RTLN 91
Cdd:cd19162 1 PRLGLGAASLgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARHP------RAEYVVSTKVgRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 92 EN--------------TVEETEKQLANSLATLQTDYVDLLLIHYPRDRDTGNDDDyeinksrrkiVWQTLEKAKESGRVR 157
Cdd:cd19162 75 PGaagrpagadrrfdfSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTD----------AFPALEELRAEGVVG 144
|
....*
gi 17562292 158 SIGVS 162
Cdd:cd19162 145 AIGVG 149
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
32-127 |
1.25e-10 |
|
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: 61.07 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 32 TQQDLDVS---IEAALKSGYRQFDTANLYKN---ETFLGNSLKKylpqFGLTREDVFITTKV-----------RTLNENT 94
Cdd:cd19143 26 NQVDVDEAkecMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKE----LGWPRSDYVVSTKIfwggggpppndRGLSRKH 101
|
90 100 110
....*....|....*....|....*....|...
gi 17562292 95 VEETEKqlaNSLATLQTDYVDLLLIHYPrDRDT 127
Cdd:cd19143 102 IVEGTK---ASLKRLQLDYVDLVFCHRP-DPAT 130
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-266 |
1.14e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 58.11 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLG-------ISRIETQQDLDVSIEAalksGYRQFDTANLY----------KNETFLGNSLKkylpQFGLtREDVFI 83
Cdd:cd19752 1 SELCLGtmyfgtrTDEETSFAILDRYVAA----GGNFLDTANNYafwteggvggESERLIGRWLK----DRGN-RDDVVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 84 TTKVRTL-----NENTVEE------TEKQLANSLATLQTDYVDLLLIHYpRDRDTGNDDDYEinksrrkivwqTLEKAKE 152
Cdd:cd19752 72 ATKVGAGprdpdGGPESPEglsaetIEQEIDKSLRRLGTDYIDLYYAHV-DDRDTPLEETLE-----------AFNELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 153 SGRVRSIGVSNYEVYHLVEMFEYAK----------------IRPVLNQYEYQPYLTRPTLKKFCDLN-NIVVQSYSSLCW 215
Cdd:cd19752 140 AGKVRAIGASNFAAWRLERARQIARqqgwaefsaiqqrhsyLRPRPGADFGVQRIVTDELLDYASSRpDLTLLAYSPLLS 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17562292 216 G----DKEILQE-----------KPLVDLCQKYNQTPQAILYAFAHCSNTSMIP--KSATPSRIHDNL 266
Cdd:cd19752 220 GaytrPDRPLPEqydgpdsdarlAVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENL 287
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
24-187 |
1.63e-09 |
|
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: 57.61 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 24 GLGISRIETQQDLDVSIEAalksGYRQFDTANLYKN---ETFLGNSLKKylpqfglTREDVFITTK----VRTLNENTVE 96
Cdd:cd19080 25 GWGADREEARAMFDAYVEA----GGNFIDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKytmnRRPGDPNAGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 97 ETEK----QLANSLATLQTDYVDLLLIHYPrDRDTGNDDdyeinksrrkiVWQTLEKAKESGRVRSIGVSNYEVYHLVEM 172
Cdd:cd19080 94 NHRKnlrrSVEASLRRLQTDYIDLLYVHAW-DFTTPVEE-----------VMRALDDLVRAGKVLYVGISDTPAWVVARA 161
|
170
....*....|....*....
gi 17562292 173 FEYAKIR----PVLNQYEY 187
Cdd:cd19080 162 NTLAELRgwspFVALQIEY 180
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-162 |
1.79e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 57.87 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLGISRIE------TQQDLDVSIEAALKSGYRQFDTANLYKN---ETFLGNSLKkylpQFGLTREDVFITT 85
Cdd:PLN02587 6 STGLKVSSVGFGASPLGsvfgpvSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALK----ALGIPREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KVRTLNEN---TVEETEKQLANSLATLQTDYVDLLLIHyprDRDTGNDDdyeinksrrKIVWQT---LEKAKESGRVRSI 159
Cdd:PLN02587 82 KCGRYGEGfdfSAERVTKSVDESLARLQLDYVDILHCH---DIEFGSLD---------QIVNETipaLQKLKESGKVRFI 149
|
...
gi 17562292 160 GVS 162
Cdd:PLN02587 150 GIT 152
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
19-216 |
3.28e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 57.17 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 19 EMPKIGLGISRIETQQ---DLDVSIEAALKSGYRQFDTANLYK----------NETFLGNSLKKYLpqfglTREDVFITT 85
Cdd:PRK10625 12 EVSTLGLGTMTFGEQNseaDAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-----SREKLIIAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 86 KV--------------RTLNENTVEETekqLANSLATLQTDYVDLLLIHYP-RDRDTGNDDDYEINKSRRKI-VWQTLEK 149
Cdd:PRK10625 87 KVsgpsrnndkgirpnQALDRKNIREA---LHDSLKRLQTDYLDLYQVHWPqRPTNCFGKLGYSWTDSAPAVsLLETLDA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562292 150 AKE---SGRVRSIGVSNYEVY------HLVEMFEYAKIRPVLNQYEYQPYLTRPTLKKFCDLNNIVVQSYSSLCWG 216
Cdd:PRK10625 164 LAEqqrAGKIRYIGVSNETAFgvmrylHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFG 239
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
40-282 |
5.07e-09 |
|
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: 56.09 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 40 IEAALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfgltREDVFITTK---------VRTLNENTVEETEKQ-LANSL 106
Cdd:cd19078 31 IRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKfgfkidggkPGPLGLDSRPEHIRKaVEGSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 107 ATLQTDYVDLLLIHYPrdrdtgnDDDYEINKsrrkiVWQTLEKAKESGRVRSIGVSnyEVYhlVEMFEYA-KIRPVLN-Q 184
Cdd:cd19078 104 KRLQTDYIDLYYQHRV-------DPNVPIEE-----VAGTMKELIKEGKIRHWGLS--EAG--VETIRRAhAVCPVTAvQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 185 YEYQPYLTRP--TLKKFCDLNNIVVQSYSSLCWG-------------------------DKEILQEKPLVDLCQKY---- 233
Cdd:cd19078 168 SEYSMMWREPekEVLPTLEELGIGFVPFSPLGKGfltgkidentkfdegddraslprftPEALEANQALVDLLKEFaeek 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17562292 234 NQTPQAILYAF--AHCSNTSMIPKSATPSRIHDNLhNTIKIKLTEDELKSL 282
Cdd:cd19078 248 GATPAQIALAWllAKKPWIVPIPGTTKLSRLEENI-GAADIELTPEELREI 297
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
21-178 |
1.75e-08 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 54.64 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 21 PKIGLGISRIE------TQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKKYlpqfglTREDVFITTKV---- 87
Cdd:cd19161 1 SELGLGTAGLGnlytavSNADADATLDAAWDSGIRYFDTAPMYghgLAEHRLGDFLREK------PRDEFVLSTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 ------RTLNEN--------------TVEETEKQLANSLATLQTDYVDLLLIHyprdrdtgnDDDYEINKSRRKIVW--- 144
Cdd:cd19161 75 kparegSVPDPNgfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVH---------DIGVYTHGDRKERHHfaq 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17562292 145 ------QTLEKAKESGRVRSIGVSNYEVYHLVEMFEYAKI 178
Cdd:cd19161 146 lmsggfKALEELKKAGVIKAFGLGVNEVQICLEALDEADL 185
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
16-283 |
8.17e-08 |
|
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: 52.63 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 16 DGYEMPKIGLGISRI---ETQQDLDVSIE---AALKSGYRQFDTANLYKNETFLGN--SLKKYLPQFGLTREDVFITTKV 87
Cdd:cd19077 1 NGKLVGPIGLGLMGLtwrPNPTPDEEAFEtmkAALDAGSNLWNGGEFYGPPDPHANlkLLARFFRKYPEYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 88 RTLNEN-----TVEETEKQLANSLATL-QTDYVDlllIHYPRDRDTGNDDDYEInksrrkivwQTLEKAKESGRVRSIGV 161
Cdd:cd19077 81 GLDPDTlrpdgSPEAVRKSIENILRALgGTKKID---IFEPARVDPNVPIEETI---------KALKELVKEGKIRGIGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 162 SnyEVYHlvEMFEYA-KIRPVL-NQYEYQPYLTRPT---LKKFCDLNNIVVQSYSSLCWG-------------------- 216
Cdd:cd19077 149 S--EVSA--ETIRRAhAVHPIAaVEVEYSLFSREIEengVLETCAELGIPIIAYSPLGRGlltgriksladipegdfrrh 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17562292 217 ----DKEILQE-KPLVD----LCQKYNQTPQAILYAF-AHCSNTSM--IPKSATPSRIHDNLhNTIKIKLTEDELKSLR 283
Cdd:cd19077 225 ldrfNGENFEKnLKLVDalqeLAEKKGCTPAQLALAWiLAQSGPKIipIPGSTTLERVEENL-KAANVELTDEELKEIN 302
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-120 |
2.07e-06 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 48.61 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 17 GYEMPKIGLG----ISRIETQQDLDVSIEAALKSGYRQFDTANLYKN---ETFLGNSLKKYlpqfGLTREDVFITTKV-- 87
Cdd:cd19142 10 GLRVSNVGLGtwstFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyw 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 17562292 88 ------RTLNENTVEETekqLANSLATLQTDYVDLLLIH 120
Cdd:cd19142 86 sygseeRGLSRKHIIES---VRASLRRLQLDYIDIVIIH 121
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
15-162 |
3.03e-05 |
|
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: 44.73 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 15 SDGYEMPKIGLG-------ISRIETQQDLDVSIEAALKSGYRQFDTANLY---KNETFLGNSLKkylpqfGLTREDVFIT 84
Cdd:cd19145 7 SQGLEVSAQGLGcmglsgdYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK------DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 85 TK--VRTLNENTVEET------EKQLANSLATLQTDYVDLLLIHyprdR-DTgndddyeinKSRRKIVWQTLEKAKESGR 155
Cdd:cd19145 81 TKfgIHEIGGSGVEVRgdpayvRAACEASLKRLDVDYIDLYYQH----RiDT---------TVPIEITMGELKKLVEEGK 147
|
....*..
gi 17562292 156 VRSIGVS 162
Cdd:cd19145 148 IKYIGLS 154
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
52-177 |
1.54e-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: 42.80 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562292 52 DTANLYK---NETFLGNSLKKYLpqfglTREDVFITTKVRTLNENTVEETEK-------------QLANSLATLQTDYVD 115
Cdd:cd19146 53 DTANNYQgeeSERWVGEWMASRG-----NRDEMVLATKYTTGYRRGGPIKIKsnyqgnhakslrlSVEASLKKLQTSYID 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562292 116 LLLIHYPrdrdtgnddDY-----EINKSRRKIVwqtlekakESGRVRSIGVSNYEVYHLVEMFEYAK 177
Cdd:cd19146 128 ILYVHWW---------DYttsipELMQSLNHLV--------AAGKVLYLGVSDTPAWVVSKANAYAR 177
|
|
| |
