|
Name |
Accession |
Description |
Interval |
E-value |
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
15-336 |
5.61e-150 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 423.41 E-value: 5.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 15 KNIPLSNHLEGVGQIAYGCMGLGGgWNdnpvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELR 94
Cdd:COG4989 2 KRIKLGASGLSVSRIVLGCMRLGE-WD------LSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 95 DQMFIQSKCGIRFEGEGN---VGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDF 171
Cdd:COG4989 75 EKIELQTKCGIRLPSEARdnrVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 172 FGVSNMNSHQIQYLQSALGQPIVANQIEMSLVKLDWLNDgvminsqghhqsdfaaGTLEHCQMKGIQLQAWGCLAQGRFA 251
Cdd:COG4989 155 FGVSNFTPSQFELLQSALDQPLVTNQIELSLLHTDAFDD----------------GTLDYCQLNGITPMAWSPLAGGRLF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 252 EQglysEHENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEWYNLYVYSR 331
Cdd:COG4989 219 GG----FDEQFPRLRAALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTREEWYELYEAAR 294
|
....*
gi 1699063870 332 GQALP 336
Cdd:COG4989 295 GHEVP 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
26-331 |
1.05e-129 |
|
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: 371.89 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWndnpvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKCGI 105
Cdd:cd19092 6 VSRLVLGCMRLADWG-------ESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RF---EGEGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQI 182
Cdd:cd19092 79 RLgddPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 183 QYLQSALGQPIVANQIEMSLVKLDWLNDgvminsqghhqsdfaaGTLEHCQMKGIQLQAWGCLAQGRFAEqglySEHENV 262
Cdd:cd19092 159 ELLQSYLDQPLVTNQIELSLLHTEAIDD----------------GTLDYCQLLDITPMAWSPLGGGRLFG----GFDERF 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699063870 263 KKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEWYNLYVYSR 331
Cdd:cd19092 219 QRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWYEIYEAAR 287
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
26-323 |
2.49e-60 |
|
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: 195.78 E-value: 2.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDNpvtasDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCGI 105
Cdd:COG0667 13 VSRLGLGTMTFGGPWGGV-----DEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRP--RDDVVIATKVGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNvgRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQI-QY 184
Cdd:COG0667 86 RMGPGPN--GRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLrRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 185 LQSALG-QPIVANQIEMSLVkldwlndgvminsqghhQSDFAAGTLEHCQMKGIQLQAWGCLAQG--------------- 248
Cdd:COG0667 164 LAIAEGlPPIVAVQNEYSLL-----------------DRSAEEELLPAARELGVGVLAYSPLAGGlltgkyrrgatfpeg 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699063870 249 -RFAE--QGLYSEHENVKKTAHYvAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEW 323
Cdd:COG0667 227 dRAATnfVQGYLTERNLALVDAL-RAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDL 303
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
29-323 |
2.02e-55 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 182.51 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGGWNdnPVTASDVAQTcsvIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKCGIRFE 108
Cdd:pfam00248 1 IGLGTWQLGGGWG--PISKEEALEA---LRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 GegnvGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSA 188
Cdd:pfam00248 76 P----WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 189 LGQPIVANQIEMSLVKldwlndgvminsqghhqSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGLYSEHENVKKTAHY 268
Cdd:pfam00248 152 GKIPIVAVQVEYNLLR-----------------RRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699063870 269 --------------VAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEW 323
Cdd:pfam00248 215 lkkgtplnlealeaLEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEV 283
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
26-326 |
1.54e-53 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 177.72 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDNpvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQqapELRDQMFIQSKCGI 105
Cdd:cd19084 4 VSRIGLGTWAIGGTWWGE----VDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALK---GRRDDVVIATKCGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVgRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYL 185
Cdd:cd19084 77 RWDGGKGV-TKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 186 QSALgqPIVANQIEMSLVkldwlndgvminsqghhQSDFAAGTLEHCQMKGIQLQAWGCLAQG----RFAEQGLYSEH-- 259
Cdd:cd19084 156 RKYG--PIVSLQPPYSML-----------------EREIEEELLPYCRENGIGVLPYGPLAQGlltgKYKKEPTFPPDdr 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699063870 260 ------------ENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEWYNL 326
Cdd:cd19084 217 rsrfpffrgenfEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
28-311 |
1.01e-48 |
|
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: 163.07 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 28 QIAYGCMGLGGGWndnpvtasDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPeLRDQMFIQSKCGIRF 107
Cdd:cd06660 2 RLGLGTMTFGGDG--------DEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGGHPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 108 EGEGNVGRYdfSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQ---- 183
Cdd:cd06660 73 GGDPSRSRL--SPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAeala 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 184 YLQSALGQPIVANQIEMSLVkldwlndgvminsqghHQSDFAAGTLEHCQMKGIQLQAWGCLAQGrfaeqglysehenvk 263
Cdd:cd06660 151 YAKAHGLPGFAAVQPQYSLL----------------DRSPMEEELLDWAEENGLPLLAYSPLARG--------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1699063870 264 ktahyVAQLAkqygveseaivLAFLLRHPAGIQPVIGTTNLDRIKASA 311
Cdd:cd06660 200 -----PAQLA-----------LAWLLSQPFVTVPIVGARSPEQLEENL 231
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
32-322 |
1.45e-42 |
|
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: 148.15 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 32 GCMGLGGGWNDNPvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALqqAPELRDQMFIQSKcgirfegeg 111
Cdd:cd19072 10 GTWGIGGGMSKDY---SDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTK--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 112 nVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQ 191
Cdd:cd19072 76 -VSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 192 -PIVANQIEMSLVKLDWLNdgvminsqghhqsdfaaGTLEHCQMKGIQLQAWGCLAQGRFAEQGLYSEhenvkktahyVA 270
Cdd:cd19072 155 gPIVANQVEYNLFDREEES-----------------GLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL----------LD 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1699063870 271 QLAKQYGVESEAIVLAFLLRHPaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19072 208 EIAKKYGKTPAQIALNWLISKP-NVIAIPKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
26-319 |
4.00e-38 |
|
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: 136.19 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGL-GGGWNDNPvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelrDQMFIQSKCG 104
Cdd:cd19088 1 VSRLGYGAMRLtGPGIWGPP---ADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYP---DDVVIATKGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 105 IRFEGEGNVGRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQY 184
Cdd:cd19088 75 LVRTGPGWWGP-DGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 185 LQSALgqPIVANQIEMSLVkldwlndgvminsqghHQSDfaAGTLEHCQMKGIQLQAWGCLAQGRFAEQGlysehenvkk 264
Cdd:cd19088 154 ARAIV--RIVSVQNRYNLA----------------NRDD--EGVLDYCEAAGIAFIPWFPLGGGDLAQPG---------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1699063870 265 taHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLT 319
Cdd:cd19088 204 --GLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
26-323 |
4.47e-38 |
|
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: 137.36 E-value: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDNPvtasDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQapeLRDQMFIQSKCGI 105
Cdd:cd19078 4 VSAIGLGCMGMSHGYGPPP----DKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVGRY-DFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQY 184
Cdd:cd19078 77 KIDGGKPGPLGlDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 185 LQSAlgQPIVANQIEMSLVkldWlndgvminsqghhqSDFAAGTLEHCQMKGIQLQAWGCLAQG----------RFAEQG 254
Cdd:cd19078 157 AHAV--CPVTAVQSEYSMM---W--------------REPEKEVLPTLEELGIGFVPFSPLGKGfltgkidentKFDEGD 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699063870 255 LYS-----EHENVKKTAHYVA---QLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEW 323
Cdd:cd19078 218 DRAslprfTPEALEANQALVDllkEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEEL 294
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
26-175 |
2.13e-37 |
|
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: 133.76 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNdNPVTASDVAQTcsvIDTALESGINLFDHADIYTFSKAEQAFGQALQQApelRDQMFIQSKCGI 105
Cdd:cd19086 3 VSEIGFGTWGLGGDWW-GDVDDAEAIRA---LRAALDLGINFFDTADVYGDGHSERLLGKALKGR---RDKVVIATKFGN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699063870 106 RFeGEGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRP-DPLMELNELARTLENLKAQGKVDFFGVS 175
Cdd:cd19086 76 RF-DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYGVS 145
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
56-322 |
4.31e-36 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 130.95 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 56 VIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGILNRLN 135
Cdd:COG0656 23 AVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTK----------VWNDNHGYDDTLAAFEESLERLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 136 AEKLDVLLLHRP--DPLMElnelA-RTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEMSLvkldwlndgv 212
Cdd:COG0656 90 LDYLDLYLIHWPgpGPYVE----TwRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVELHP---------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 213 minsqGHHQSDFaagtLEHCQMKGIQLQAWGCLAQGRFAEQGLysehenvkktahyVAQLAKQYGVESEAIVLAFLLRHp 292
Cdd:COG0656 156 -----YLQQREL----LAFCREHGIVVEAYSPLGRGKLLDDPV-------------LAEIAEKHGKTPAQVVLRWHLQR- 212
|
250 260 270
....*....|....*....|....*....|
gi 1699063870 293 aGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:COG0656 213 -GVVVIPKSVTPERIRENLDAFDFELSDED 241
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
34-322 |
1.35e-35 |
|
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: 129.52 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGGWndnpvtaSDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgirfegegnV 113
Cdd:cd19071 4 IGLGTYK-------LKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTK----------L 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 114 GRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELA------RTLENLKAQGKVDFFGVSNMNSHQIQYLQS 187
Cdd:cd19071 64 WPTDHGYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEarletwRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 188 ALGQPIVANQIEMSLvkldwlndgvminsqGHHQSDfaagTLEHCQMKGIQLQAWGCLAQGRfaeqGLYSEHENVKKtah 267
Cdd:cd19071 144 AARIKPAVNQIELHP---------------YLQQKE----LVEFCKEHGIVVQAYSPLGRGR----RPLLDDPVLKE--- 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1699063870 268 yvaqLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19071 198 ----IAKKYGKTPAQVLLRWALQR--GVVVIPKSSNPERIKENLDVFDFELSEED 246
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
28-315 |
1.52e-35 |
|
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: 130.37 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 28 QIAYGCMGLGggwndnpvTASDVAQTCSVIDTALESGINLFDHADIY----TFSKAEQAFGQALQqAPELRDQMFIQSKC 103
Cdd:cd19082 2 RIVLGTADFG--------TRIDEEEAFALLDAFVELGGNFIDTARVYgdwvERGASERVIGEWLK-SRGNRDKVVIATKG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 104 GIRFEGEGNVGRydFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQ 183
Cdd:cd19082 73 GHPDLEDMSRSR--LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 184 ----YLQSALGQPIVANQIEMSLVKLD---WLNDG-VMINS---QGHHQSDFAagtlehcqmkgiqLQAWGCLAQGRFAE 252
Cdd:cd19082 151 eanaYAKAHGLPGFAASSPQWSLARPNeppWPGPTlVAMDEemrAWHEENQLP-------------VFAYSSQARGFFSK 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699063870 253 ---QGL----------YSEhENVKKtAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQ 315
Cdd:cd19082 218 raaGGAeddselrrvyYSE-ENFER-LERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
26-322 |
3.97e-35 |
|
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: 130.01 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLG----GGWNdnpvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQ-APelRDQMFIQ 100
Cdd:cd19079 12 VSRLCLGCMSFGdpkwRPWV------LDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEfAP--RDEVVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 101 SKCGIRFEGEGNVGRydFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSH 180
Cdd:cd19079 84 TKVYFPMGDGPNGRG--LSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 181 QI---QYLQSALGqpivanqiemsLVKldwlndgvMINSQGHH---QSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAeqG 254
Cdd:cd19079 162 QFakaLHLAEKNG-----------WTK--------FVSMQNHYnllYREEEREMIPLCEEEGIGVIPWSPLARGRLA--R 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 255 LYSEHENVKKT------AHY-------------VAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQ 315
Cdd:cd19079 221 PWGDTTERRRSttdtakLKYdyfteadkeivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALD 300
|
....*..
gi 1699063870 316 INLTREE 322
Cdd:cd19079 301 IKLSEEE 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
26-321 |
4.52e-35 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 129.24 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDNPVtasDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQapeLRDQMFIQSKCGI 105
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGDQ---DDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RfegegnvgryDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNmnsHQIQYL 185
Cdd:cd19085 75 D----------NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSN---FGPAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 186 QSALG-QPIVANQIEMSLVkldWLNDgvminsqghhqsdfAAGTLEHCQMKGIQLQAWGCLAQG---------------- 248
Cdd:cd19085 142 EEALDaGRIDSNQLPYNLL---WRAI--------------EYEILPFCREHGIGVLAYSPLAQGlltgkfssaedfppgd 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 249 ------RFAEQGLYSE-HENVKKtahyVAQLAKQYGVESEAIVLAFLLRHPaGIQPVI-GTTNLDRIKASAVATQINLTR 320
Cdd:cd19085 205 artrlfRHFEPGAEEEtFEALEK----LKEIADELGVTMAQLALAWVLQQP-GVTSVIvGARNPEQLEENAAAVDLELSP 279
|
.
gi 1699063870 321 E 321
Cdd:cd19085 280 S 280
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
26-322 |
5.40e-35 |
|
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: 129.66 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWN-DNPVTASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQqapELRDQMFIQSKCG 104
Cdd:cd19091 13 VSELALGTMTFGGGGGfFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALK---GRRDDVLIATKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 105 IRF-EGEGNVGrydFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQI- 182
Cdd:cd19091 90 GRMgEGPNDVG---LSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIm 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 183 --QYLQSALG-QPIVANQIEMSLVKLDwlndgvminsqghhqsdfaagtLEH-----CQMKGIQLQAWGCLAQG------ 248
Cdd:cd19091 167 kaLGISERRGlARFVALQAYYSLLGRD----------------------LEHelmplALDQGVGLLVWSPLAGGllsgky 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 249 -------------RFAEQGLYSEHENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQ 315
Cdd:cd19091 225 rrgqpapegsrlrRTGFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAG 304
|
....*..
gi 1699063870 316 INLTREE 322
Cdd:cd19091 305 LSLTPEE 311
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
26-321 |
2.40e-34 |
|
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: 127.69 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGgwndnpvtASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQApelRDQMFIQSKCGI 105
Cdd:cd19087 13 VSRLCLGTMNFGG--------RTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR---RDDIVLATKVFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVGRydFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQI--- 182
Cdd:cd19087 82 PMGDDPNDRG--LSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIaka 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 183 QYLQSALG-------QP---IVANQIEMSLvkldwlndgvminsqghhqsdfaagtLEHCQMKGIQLQAWGCLA------ 246
Cdd:cd19087 160 QGIAARRGllrfvseQPmynLLKRQAELEI--------------------------LPAARAYGLGVIPYSPLAgglltg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 247 ---------QGRFAEQGLYSE---HENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVAT 314
Cdd:cd19087 214 kygkgkrpeSGRLVERARYQArygLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAAL 293
|
....*..
gi 1699063870 315 QINLTRE 321
Cdd:cd19087 294 EITLTPE 300
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
29-311 |
2.52e-33 |
|
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: 123.50 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGGWNdnPVTASDVAQtcsVIDTALESGINLFDHADIYtfSKAEQAFGQALQQAPelRDQMFIQSKCGIRFE 108
Cdd:cd19095 3 LGLGTSGIGRVWG--VPSEAEAAR---LLNTALDLGINLIDTAPAY--GRSEERLGRALAGLR--RDDLFIATKVGTHGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 GEGNvgRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHqiqyLQSA 188
Cdd:cd19095 74 GGRD--RKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEE----LEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 189 LGQPIVanqiemslvkldwlnDGVMINSQGHHQSdfAAGTLEHCQMKGIQLQAWGCLAQGRFAEQglySEHENVKKTAHY 268
Cdd:cd19095 148 IASGVF---------------DVVQLPYNVLDRE--EEELLPLAAEAGLGVIVNRPLANGRLRRR---VRRRPLYADYAR 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1699063870 269 VAQLAKQYGVESEA-IVLAFLLRHPAGIQPVIGTTNLDRIKASA 311
Cdd:cd19095 208 RPEFAAEIGGATWAqAALRFVLSHPGVSSAIVGTTNPEHLEENL 251
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
26-323 |
3.82e-33 |
|
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: 124.26 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCM--GLGGGWNDNPVTASDVAQtcsVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPElRDQMFIQSKc 103
Cdd:cd19093 2 VSPLGLGTWqwGDRLWWGYGEYGDEDLQA---AFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGD-RDEVVIATK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 104 girFEGEgnvgRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDP-LMELNELARTLENLKAQGKVDFFGVSNMNSHQI 182
Cdd:cd19093 77 ---FAPL----PWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 183 QYLQSAL---GQPIVANQIEMSLVKLDWLNDGVminsqghhqsdfaagtLEHCQMKGIQLQAWGCLAQGRFAeqGLYSE- 258
Cdd:cd19093 150 RRAHKALkerGVPLASNQVEYSLLYRDPEQNGL----------------LPACDELGITLIAYSPLAQGLLT--GKYSPe 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 259 ------------HENVKKTAHYVA---QLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIKASAVATQINLTREEW 323
Cdd:cd19093 212 npppggrrrlfgRKNLEKVQPLLDaleEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQAEENAGALGWRLSEEEV 289
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
26-322 |
6.26e-33 |
|
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: 123.87 E-value: 6.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNdnpvtASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQApelRDQMFIQSKCGI 105
Cdd:cd19076 12 VSALGLGCMGMSAFYG-----PADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDR---RDEVVIATKFGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQyl 185
Cdd:cd19076 84 VRDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIR-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 186 QSALGQPIVANQIEMSLVKLDwLNDGVMinsqghhqsdfaaGTlehCQMKGIQLQAW-----GCLAqGRFAEQGLYSEH- 259
Cdd:cd19076 162 RAHAVHPITAVQSEYSLWTRD-IEDEVL-------------PT---CRELGIGFVAYsplgrGFLT-GAIKSPEDLPEDd 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699063870 260 ----------ENVKKTAHYVAQL---AKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19076 224 frrnnprfqgENFDKNLKLVEKLeaiAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEE 299
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
26-309 |
3.47e-32 |
|
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: 121.50 E-value: 3.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGgwNDNPVTASDVAQTcsvIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCGi 105
Cdd:cd19163 13 VSKLGFGASPLGG--VFGPVDEEEAIRT---VHEALDSGINYIDTAPWYGQGRSETVLGKALKGIP--RDSYYLATKVG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNvGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPD--PLME--LNELARTLENLKAQGKVDFFGVSNMNSHQ 181
Cdd:cd19163 85 RYGLDPD-KMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIEfaPSLDqiLNETLPALQKLKEEGKVRFIGITGYPLDV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 182 IQYLqsalgqpivanqIEMSLVKLDwlndgvMINSQGHH--QSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGLYSEH 259
Cdd:cd19163 164 LKEV------------LERSPVKID------TVLSYCHYtlNDTSLLELLPFFKEKGVGVINASPLSMGLLTERGPPDWH 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1699063870 260 ---ENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKA 309
Cdd:cd19163 226 pasPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRK 278
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
38-321 |
1.55e-31 |
|
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: 120.00 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 38 GGW-NDNPVTASDVAQTCsvIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCgiRFEGEGNVGRY 116
Cdd:cd19074 10 GTWlTFGGQVDDEDAKAC--VRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWP--RESYVISTKV--FWPTGPGPNDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 117 DFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQ----P 192
Cdd:cd19074 84 GLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQfgliP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 193 IVANQIEMSLVKLDWLNDgvminsqghhqsdfaagTLEHCQMKGIQLQAWGCLAQG----------------RFAEQGLY 256
Cdd:cd19074 164 PVVEQPQYNMLWREIEEE-----------------VIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsRATDEDNR 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 257 -----SEHENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTRE 321
Cdd:cd19074 227 dkkrrLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
19-322 |
2.07e-31 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 120.24 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 19 LSNHLEGVGQIAYGCMGLGGGWNdnpvTASDVAQTCSVIDTALESGINLFDHADIYTFSkaEQAFGQALQQAPELRDQMF 98
Cdd:cd19144 6 LGRNGPSVPALGFGAMGLSAFYG----PPKPDEERFAVLDAAFELGCTFWDTADIYGDS--EELIGRWFKQNPGKREKIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 99 IQSKCGIRFEGEGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMN 178
Cdd:cd19144 80 LATKFGIEKNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 179 SHQIQylQSALGQPIVANQIEMSLVKLDwlndgvminsqghhQSDFAAGTLEHCQMKGIQLQAWGCLAQG---------- 248
Cdd:cd19144 160 AETLR--RAHAVHPIAAVQIEYSPFSLD--------------IERPEIGVLDTCRELGVAIVAYSPLGRGfltgairspd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 249 ------------RFAEQGLYSEHENVKKtahyVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQI 316
Cdd:cd19144 224 dfeegdfrrmapRFQAENFPKNLELVDK----IKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV 299
|
....*.
gi 1699063870 317 NLTREE 322
Cdd:cd19144 300 KLTEEE 305
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
29-322 |
1.43e-30 |
|
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: 117.76 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGGWNDNPvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQqapELRDQMFIQSKCGIRFE 108
Cdd:cd19149 14 IGLGTWAIGGGPWWGG---SDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIK---GRRDKVVLATKCGLRWD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 GEGNVGRY---------DFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNS 179
Cdd:cd19149 88 REGGSFFFvrdgvtvykNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 180 HQIQYLQSAlGQpIVANQIEMSLVKLDwlndgvminsqghHQSDFaagtLEHCQMKGIQLQAWGCLAQG----------R 249
Cdd:cd19149 168 EQIKEYVKA-GQ-LDIIQEKYSMLDRG-------------IEKEL----LPYCKKNNIAFQAYSPLEQGlltgkitpdrE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 250 FAEQGLYSEH-----ENVKKTAHYVAQ---LAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTRE 321
Cdd:cd19149 229 FDAGDARSGIpwfspENREKVLALLEKwkpLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAE 308
|
.
gi 1699063870 322 E 322
Cdd:cd19149 309 D 309
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
24-322 |
8.43e-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: 114.59 E-value: 8.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 24 EGVGQIAYGCMGLGGgwNDNPVTASDvAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKc 103
Cdd:cd19137 2 EKIPALGLGTWGIGG--FLTPDYSRD-EEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFP--REDLFIVTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 104 girfegegnVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQ 183
Cdd:cd19137 76 ---------VWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 184 YLQSALGQPIVANQIEMSLVKLDWLNDGVminsqghhqsdfaagtLEHCQMKGIQLQAWGCLAQGrfaeqglysehenVK 263
Cdd:cd19137 147 EAISKSQTPIVCNQVKYNLEDRDPERDGL----------------LEYCQKNGITVVAYSPLRRG-------------LE 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1699063870 264 KTAHYVAQLAKQYGVESEAIVLAFLLRHPaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19137 198 KTNRTLEEIAKNYGKTIAQIALAWLIQKP-NVVAIPKAGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
28-326 |
2.72e-29 |
|
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: 113.61 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 28 QIAYGCMGLGggwNDNPVTASDVAqtcSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCG--I 105
Cdd:cd19162 2 RLGLGAASLG---NLARAGEDEAA---ATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHP--RAEYVVSTKVGrlL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVG----RYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLME--LNELARTLENLKAQGKVDFFGVSNMNS 179
Cdd:cd19162 74 EPGAAGRPAgadrRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLqaLTDAFPALEELRAEGVVGAIGVGVTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 180 hqiqylqsalgqPIVANQIEMSLVkldwlnDGVMInsQGHH---QSDFAAGTLEHCQMKGIQLQAW-----GCLAQGRfA 251
Cdd:cd19162 154 ------------AALLRAARRADV------DVVMV--AGRYtllDRRAATELLPLCAAKGVAVVAAgvfnsGILATDD-P 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699063870 252 EQGLYSEH---ENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEWYNL 326
Cdd:cd19162 213 AGDRYDYRpatPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAEFWAEL 290
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
55-322 |
4.47e-29 |
|
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: 111.98 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 55 SVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGILNRL 134
Cdd:cd19073 18 NAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTK----------VWRDHLRPEDLKKSVDRSLEKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 135 NAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEMSlvklDWLNdgvmi 214
Cdd:cd19073 85 GTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEFH----PFLY----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 215 nsqghhQSDFaagtLEHCQMKGIQLQAWGCLAQGRFAeqglysEHENVKKtahyvaqLAKQYGVESEAIVLAFLLRHpaG 294
Cdd:cd19073 156 ------QAEL----LEYCRENDIVITAYSPLARGEVL------RDPVIQE-------IAEKYDKTPAQVALRWLVQK--G 210
|
250 260
....*....|....*....|....*...
gi 1699063870 295 IQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19073 211 IVVIPKASSEDHLKENLAIFDWELTSED 238
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
29-323 |
5.19e-29 |
|
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: 112.65 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGGWNDNPVTASDvaqtcSVIDTALESGINLFDHADIYTFSkaEQAFGQALQQAPelRDQMFIQSKCGIRFE 108
Cdd:cd19090 3 LGLGTAGLGGVFGGVDDDEAV-----ATIRAALDLGINYIDTAPAYGDS--EERLGLALAELP--REPLVLSTKVGRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 GEgnvgrYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELAR-----TLENLKAQGKVDFFGVSnMNSHQI- 182
Cdd:cd19090 74 DT-----ADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggaleALLELKEEGLIKHIGLG-GGPPDLl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 183 -QYLQSalgqpivaNQIEMSLVKLDW-LNDgvminsqghhqSDFAAGTLEHCQMKGIQLQAWGCLAQG----RFAEQGLY 256
Cdd:cd19090 148 rRAIET--------GDFDVVLTANRYtLLD-----------QSAADELLPAAARHGVGVINASPLGMGllagRPPERVRY 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 257 SEH---ENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEW 323
Cdd:cd19090 209 TYRwlsPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
33-322 |
9.48e-28 |
|
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: 110.20 E-value: 9.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 33 CMGLG----GGWNDNPvtASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQapELRDQMFIQSKCGIRFE 108
Cdd:cd19083 13 PIGLGtnavGGHNLYP--NLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKE--YNRNEVVIATKGAHKFG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 GEGNVgrYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQiqyLQSA 188
Cdd:cd19083 89 GDGSV--LNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQ---LKEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 189 LGQPIV-ANQIEMSLVkldwlndgvminsqghhQSDFAAGTLEHCQMKGIQLQAWGCLAQ----GRFAEQGLYSEHENVK 263
Cdd:cd19083 164 NKDGYVdVLQGEYNLL-----------------QREAEEDILPYCVENNISFIPYFPLASgllaGKYTKDTKFPDNDLRN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1699063870 264 KTAHY--------------VAQLAKQYGVESEAIVLAFLLRHPAgIQPVI-GTTNLDRIKASAVATQINLTREE 322
Cdd:cd19083 227 DKPLFkgerfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPA-IDVVIpGAKRAEQVIDNLKALDVTLTEEE 299
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
26-322 |
2.09e-27 |
|
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: 108.87 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGggWNDNPVTasdVAQTCSVIDTALESGINLFDHADIYTFSKAE---QAFGQALQQAPELRDQMFIQSK 102
Cdd:cd19077 5 VGPIGLGLMGLT--WRPNPTP---DEEAFETMKAALDAGSNLWNGGEFYGPPDPHanlKLLARFFRKYPEYADKVVLSVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 103 CGIRFEGEGNVGRYDFsadwVSQSVEGILNRLNA-EKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQ 181
Cdd:cd19077 80 GGLDPDTLRPDGSPEA----VRKSIENILRALGGtKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 182 IQylQSALGQPIVANQIEMSLVKLDWLNDGVminsqghhqsdfaagtLEHCQMKGIQLQAWGCLAQG------------- 248
Cdd:cd19077 156 IR--RAHAVHPIAAVEVEYSLFSREIEENGV----------------LETCAELGIPIIAYSPLGRGlltgriksladip 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 249 ---------RFAEQGLysehENVKKTAHYVAQLAKQYGVESEAIVLAFLLR-HPAGIQPVIGTTNLDRIKASAVATQINL 318
Cdd:cd19077 218 egdfrrhldRFNGENF----EKNLKLVDALQELAEKKGCTPAQLALAWILAqSGPKIIPIPGSTTLERVEENLKAANVEL 293
|
....
gi 1699063870 319 TREE 322
Cdd:cd19077 294 TDEE 297
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-323 |
1.22e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 106.99 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGGWNDNPVTASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQqapELRDQMFIQSKCGIRFE 108
Cdd:cd19102 4 IGLGTWAIGGGGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK---GLRDRPIVATKCGLLWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 GEGNVGRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSA 188
Cdd:cd19102 81 EEGRIRR-SLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 189 lgQPIVANQIEMSLVKldwlndgvminsqghhqSDFAAGTLEHCQMKGIQLQAWGCLAQG----RFAEQGLYS------- 257
Cdd:cd19102 160 --HPIASLQPPYSLLR-----------------RGIEAEILPFCAEHGIGVIVYSPMQSGlltgKMTPERVASlpaddwr 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699063870 258 ------EHENVKKTAHYVAQL---AKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEW 323
Cdd:cd19102 221 rrspffQEPNLARNLALVDALrpiAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEEL 295
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
51-322 |
2.14e-26 |
|
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: 105.03 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 51 AQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKCGIRfegegnvgryDFSADWVSQSVEGI 130
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMY---GNEAQVGEAIAASGVPRDELFLTTKVWPD----------NYSPDDFLASVEES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 131 LNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEMSlvkldwlnd 210
Cdd:cd19140 88 LRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEYH--------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 211 gVMINsqghhQSDFaagtLEHCQMKGIQLQAWGCLAQGRFAEqglysehenvkktaHYVAQ-LAKQYGVESEAIVLAFLL 289
Cdd:cd19140 159 -PYLD-----QRKL----LDAAREHGIALTAYSPLARGEVLK--------------DPVLQeIGRKHGKTPAQVALRWLL 214
|
250 260 270
....*....|....*....|....*....|...
gi 1699063870 290 RHPaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19140 215 QQE-GVAAIPKATNPERLEENLDIFDFTLSDEE 246
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
38-326 |
6.83e-26 |
|
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: 103.87 E-value: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 38 GGWN--DNPVTAsdvAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQqapELRDQMFIQSKcgirfegegnVGR 115
Cdd:cd19138 17 GTWYmgEDPAKR---AQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIR---GRRDKVFLVSK----------VLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 116 YDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPlMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSAL-GQPIV 194
Cdd:cd19138 81 SNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG-VPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPgGGNCA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 195 ANQIEMSLvkldwlndgvminsqGHHQSDFaaGTLEHCQMKGIQLQAWGCLAQGRFAEQGLYSEHEnvkktahyVAQLAK 274
Cdd:cd19138 160 ANQVLYNL---------------GSRGIEY--DLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPT--------LKEIAA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1699063870 275 QYGVESEAIVLAFLLRHPAgiqpVIG---TTNLDRIKASAVATQINLTREEWYNL 326
Cdd:cd19138 215 RHGATPAQVALAWVLRDGN----VIAipkSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
35-197 |
7.72e-26 |
|
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: 104.70 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 35 GLG----GGWNDNPvtaSDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPElRDQMFIQSKCGIRFEGE 110
Cdd:cd19148 8 ALGtwaiGGWMWGG---TDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGK-RDRVVIATKVGLEWDEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 111 GNVGRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSAlg 190
Cdd:cd19148 84 GEVVR-NSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRKV-- 160
|
....*..
gi 1699063870 191 QPIVANQ 197
Cdd:cd19148 161 APLHTVQ 167
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
26-323 |
1.37e-25 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 104.22 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGggWNdnpvtaSDVAQTCSVIDTALESGINLFDHADIYTFS-------KAEQAFGQALQQAPElRDQMF 98
Cdd:cd19081 9 VSPLCLGTMVFG--WT------ADEETSFALLDAFVDAGGNFIDTADVYSAWvpgnaggESETIIGRWLKSRGK-RDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 99 IQSKCGirfeGEGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMN 178
Cdd:cd19081 80 IATKVG----FPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 179 SHQiqyLQSALG-------QPIVANQIEMSLVkldwlndgvminsqghHQSDFAAGTLEHCQMKGIQLQAWGCLAQGrF- 250
Cdd:cd19081 156 AWR---LQEALElsrqhglPRYVSLQPEYNLV----------------DRESFEGELLPLCREEGIGVIPYSPLAGG-Fl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 251 -----AEQGLYSEHENVKKTAHY-----------VAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVAT 314
Cdd:cd19081 216 tgkyrSEADLPGSTRRGEAAKRYlnerglrildaLDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAA 295
|
....*....
gi 1699063870 315 QINLTREEW 323
Cdd:cd19081 296 GLRLTDEEV 304
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-313 |
5.88e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 101.12 E-value: 5.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGgwnDNPvtasdvaqtcSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCGIRFE 108
Cdd:cd19105 16 LGFGGGGLPR---ESP----------ELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLR--RDKVFLATKASPRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 GegnvgrydFSADWVSQSVEGILNRLNAEKLDVLLLH---RPDPLMELNELARTLENLKAQGKVDFFGVSnmnSHqiqyl 185
Cdd:cd19105 81 K--------KDKAELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELLEALEKLKKEGKVRFIGFS---TH----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 186 qsalgqpivANQIEM--SLVKLDWLnDGVMINSQGHHQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGLYsehENVK 263
Cdd:cd19105 145 ---------DNMAEVlqAAIESGWF-DVIMVAYNFLNQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLS---VLKA 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1699063870 264 KTAHYvAQLAkqygveseaivLAFLLRHP--AGIqpVIGTTNLDRIKASAVA 313
Cdd:cd19105 212 KGFSL-PQAA-----------LKWVLSNPrvDTV--VPGMRNFAELEENLAA 249
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
28-322 |
2.31e-24 |
|
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: 100.00 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 28 QIAYGCmglGGGWNDNPVTASDVAQTCSVIdTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgiRF 107
Cdd:cd19120 6 AIAFGT---GTAWYKSGDDDIQRDLVDSVK-LALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTK---VS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 108 EGEGNVgrydfsadwvSQSVEGILNRLNAEKLDVLLLHRP----DPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQ 183
Cdd:cd19120 76 PGIKDP----------REALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 184 YLQSALGQPIVANQIEmslvkldwlndgvmINSQGHHQSDfaaGTLEHCQMKGIQLQAWGCLA-QGRFAeqglyseHENV 262
Cdd:cd19120 146 ELLDTAKIKPAVNQIE--------------FHPYLYPQQP---ALLEYCREHGIVVSAYSPLSpLTRDA-------GGPL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 263 KKTahyVAQLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19120 202 DPV---LEKIAEKYGVTPAQVLLRWALQK--GIVVVTTSSKEERMKEYLEAFDFELTEEE 256
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
56-322 |
9.56e-24 |
|
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: 98.09 E-value: 9.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 56 VIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPEL----RDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGIL 131
Cdd:cd19136 20 AVDAALKAGYRLIDTASVY---RNEADIGKALRDLLPKyglsREDIFITSK----------LAPKDQGYEKARAACLGSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 132 NRLNAEKLDVLLLHRP-----DPLMELNELAR-----TLENLKAQGKVDFFGVSNMN-SHQIQYLQSALGQPIVaNQIEm 200
Cdd:cd19136 87 ERLGTDYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYTvRHLEELLKYCEVPPAV-NQVE- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 201 slvkldwlndgvminsqgHH----QSDFaagtLEHCQMKGIQLQAWGCLAQGrfaeQGLYSEHENVKktahyvaQLAKQY 276
Cdd:cd19136 165 ------------------FHphlvQKEL----LKFCKDHGIHLQAYSSLGSG----DLRLLEDPTVL-------AIAKKY 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1699063870 277 GVESEAIVLAFLLRHPAGIQPviGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19136 212 GRTPAQVLLRWALQQGIGVIP--KSTNPERIAENIKVFDFELSEED 255
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
55-322 |
9.85e-24 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 98.87 E-value: 9.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 55 SVIDTALESGINLFDHADIYTFSK--AEQAFGQALQQA-PELRDQMFIQSKCGIRFeGEGNVGRYDfSADWVSQSVEGIL 131
Cdd:cd19089 33 ELLRTAFDLGITHFDLANNYGPPPgsAEENFGRILKRDlRPYRDELVISTKAGYGM-WPGPYGDGG-SRKYLLASLDQSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 132 NRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQY---LQSALGQPIVANQIEMSLvkLD-W 207
Cdd:cd19089 111 KRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRaiaLLRELGVPLIIHQPRYSL--LDrW 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 208 LNDGVminsqghhqsdfaagtLEHCQMKGIQLQAWGCLAQG---------------RFAEQGLYSEH---ENVKKTAHYV 269
Cdd:cd19089 189 AEDGL----------------LEVLEEAGIGFIAFSPLAQGlltdkylngippdsrRAAESKFLTEEaltPEKLEQLRKL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1699063870 270 AQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRI-KASAVATQINLTREE 322
Cdd:cd19089 253 NKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLeDNVAALKNLDFSEEE 306
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
26-322 |
1.10e-22 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 96.13 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWndnpVTASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQqapELRDQMFIQSKCGI 105
Cdd:cd19080 10 VSPLALGTMTFGTEW----GWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIA---GNRDRIVLATKYTM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGE-----GNvGRYDfsadwVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNS- 179
Cdd:cd19080 83 NRRPGdpnagGN-HRKN-----LRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAw 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 180 --HQIQYLQSALG-QPIVANQIEMSLVkldwlndgvminsqghhQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFaeQGLY 256
Cdd:cd19080 157 vvARANTLAELRGwSPFVALQIEYSLL-----------------ERTPERELLPMARALGLGVTPWSPLGGGLL--TGKY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 257 SEHEN-------------VKKTAH------YVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQIN 317
Cdd:cd19080 218 QRGEEgrageakgvtvgfGKLTERnwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLT 297
|
....*
gi 1699063870 318 LTREE 322
Cdd:cd19080 298 LSPEQ 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
26-322 |
2.20e-22 |
|
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: 95.19 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDnPVTASDVaqtCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCGI 105
Cdd:cd19145 12 VSAQGLGCMGLSGDYGA-PKPEEEG---IALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGP--REKVQLATKFGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVgRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYL 185
Cdd:cd19145 86 HEIGGSGV-EVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 186 QSAlgQPIVANQIEMSLvkldWLNDgvmINSQghhqsdfaagTLEHCQMKGIQLQAWGCLAQGRFAEQGLYSE------- 258
Cdd:cd19145 165 HAV--HPITAVQLEWSL----WTRD---IEEE----------IIPTCRELGIGIVPYSPLGRGFFAGKAKLEEllensdv 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699063870 259 --------HENVKKTA---HYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19145 226 rkshprfqGENLEKNKvlyERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKED 300
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-175 |
1.82e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 93.10 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWndnpVTASDVAQtCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQqapELRDQMFIQSKCGI 105
Cdd:cd19104 12 VSELTFGGGGIGGLM----GRTTREEQ-IAAVRRALDLGINFFDTAPSYGDGKSEENLGRALK---GLPAGPYITTKVRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVGrydfsaDWVSQSVEGILNRLNAEKLDVLLLH------RPDPL---------MELNELARTLENLKAQGKVD 170
Cdd:cd19104 84 DPDDLGDIG------GQIERSVEKSLKRLKRDSVDLLQLHnrigdeRDKPVggtlsttdvLGLGGVADAFERLRSEGKIR 157
|
....*
gi 1699063870 171 FFGVS 175
Cdd:cd19104 158 FIGIT 162
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
29-323 |
2.86e-21 |
|
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: 92.39 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGGWNdnPVTASDVAQTcsvIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCG---- 104
Cdd:cd19161 3 LGLGTAGLGNLYT--AVSNADADAT---LDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKVGrllk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 105 -----IRFEGEGNVG------RYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLM-----ELNELA-------RTLE 161
Cdd:cd19161 76 paregSVPDPNGFVDplpfeiVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYThgdrkERHHFAqlmsggfKALE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 162 NLKAQGKVDFFGvsnmnshqiqylqsaLGqpivANQIEMSLVKLDWLN-DGVMInsQGHH---QSDFAAGTLEHCQMKGI 237
Cdd:cd19161 156 ELKKAGVIKAFG---------------LG----VNEVQICLEALDEADlDCFLL--AGRYsllDQSAEEEFLPRCEQRGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 238 QLQAWGCLAQGRFAEQGLYSEH-------ENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKAS 310
Cdd:cd19161 215 SLVIGGVFNSGILATGTKSGAKfnygdapAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQN 294
|
330
....*....|...
gi 1699063870 311 AVATQINLTREEW 323
Cdd:cd19161 295 VEAFQTDIPEELW 307
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
49-322 |
3.67e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 91.63 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 49 DVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKcgirFEGEGNvgryDFSADWVSQSVE 128
Cdd:cd19103 30 DEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYP--REDYIISTK----FTPQIA----GQSADPVADMLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 129 GILNRLNAEKLDVLLLHRP-DPLMELNELARTLEnlkaQGKVDFFGVSNMNSHQIQYLQSALGQ---PIVANQIEMSLVk 204
Cdd:cd19103 100 GSLARLGTDYIDIYWIHNPaDVERWTPELIPLLK----SGKVKHVGVSNHNLAEIKRANEILAKagvSLSAVQNHYSLL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 205 ldwlndgvminsqghHQSDFAAGTLEHCQMKGIQLQAWGCLAQGrfAEQGLYSEH----ENVKKTAHY------------ 268
Cdd:cd19103 175 ---------------YRSSEEAGILDYCKENGITFFAYMVLEQG--ALSGKYDTKhplpEGSGRAETYnpllpqleelta 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1699063870 269 -VAQLAKQYGVESEAIVLAFLLrhPAGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19103 238 vMAEIGAKHGASIAQVAIAWAI--AKGTTPIIGVTKPHHVEDAARAASITLTDDE 290
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
27-323 |
1.09e-20 |
|
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: 90.75 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 27 GQIAYGCMGLGGGWNdnPVTASDVAQTcsvIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCG-- 104
Cdd:cd19152 1 PKLGFGTAPLGNLYE--AVSDEEAKAT---LVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGrl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 105 -------------IRFEGEGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNEL-----------ARTL 160
Cdd:cd19152 74 lvplqeveptfepGFWNPLPFDAVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgaFRAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 161 ENLKAQGKVDFFGVSnMNSHQI--QYLQSAlgqpivanqiemslvKLDWlndgVMINSQGH--HQSDfAAGTLEHCQMKG 236
Cdd:cd19152 154 EELREEGVIKAIGLG-VNDWEVilRILEEA---------------DLDW----VMLAGRYTllDHSA-ARELLPECEKRG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 237 IQLQ-----AWGCLAQGRFAEQGLYSE-HENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKAS 310
Cdd:cd19152 213 VKVVnagpfNSGFLAGGDNFDYYEYGPaPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEEN 292
|
330
....*....|...
gi 1699063870 311 AVATQINLTREEW 323
Cdd:cd19152 293 VALLATEIPAAFW 305
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-272 |
1.83e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 88.69 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGggwndnPVTASDVAQtcsVIDTALESGINLFDHADIYtfSKAEQAFGQALQQapeLRDQMFIQSKCGI 105
Cdd:cd19100 11 VSRLGFGGGPLG------RLSQEEAAA---IIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATKTGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RfegegnvgrydfSADWVSQSVEGILNRLNAEKLDVLLLH------RPDPLMELNELARTLENLKAQGKVDFFGVSnmnS 179
Cdd:cd19100 77 R------------DYEGAKRDLERSLKRLGTDYIDLYQLHavdteeDLDQVFGPGGALEALLEAKEEGKIRFIGIS---G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 180 HQIQYLQSALGQPIVanqiemslvkldwlnDGVM--INSQGHHQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGlys 257
Cdd:cd19100 142 HSPEVLLRALETGEF---------------DVVLfpINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGD--- 203
|
250
....*....|....*
gi 1699063870 258 eHENVKKTAHYVAQL 272
Cdd:cd19100 204 -PLDPEQALRYALSL 217
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
19-175 |
1.39e-18 |
|
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: 84.51 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 19 LSNHLEGVGQIAYGCMGLGGGWNDNPvtASDVAQtcSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMF 98
Cdd:cd19153 5 LEIALGNVSPVGLGTAALGGVYGDGL--EQDEAV--AIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 99 IQSKCGiRFEGEGnvgrYDFSADWVSQSVEGILNRLNAEKLDVLLLH-----RPDPLmeLNELARTLENLKAQGKVDFFG 173
Cdd:cd19153 81 VATKVG-RYRDSE----FDYSAERVRASVATSLERLHTTYLDVVYLHdiefvDYDTL--VDEALPALRTLKDEGVIKRIG 153
|
..
gi 1699063870 174 VS 175
Cdd:cd19153 154 IA 155
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
26-321 |
1.76e-18 |
|
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: 84.54 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGgwndnpvtASDVAQTCSVIDTALESGINLFDHADIY-------TFSKAEQAFGQALQQAPElRDQMF 98
Cdd:cd19094 1 VSEICLGTMTWGE--------QNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLKKKGN-RDKVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 99 IQSK-CG----IRFEGeGNVGRYDfsADWVSQSVEGILNRLNAEKLDVLLLHRPD---PLMELN---------------E 155
Cdd:cd19094 72 LATKvAGpgegITWPR-GGGTRLD--RENIREAVEGSLKRLGTDYIDLYQLHWPDrytPLFGGGyytepseeedsvsfeE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 156 LARTLENLKAQGKVDFFGVSNMNSHQI-QYLQSA--LGQP-IVANQIEMSLVkldwlndgvminsqghHQSDFaAGTLEH 231
Cdd:cd19094 149 QLEALGELVKAGKIRHIGLSNETPWGVmKFLELAeqLGLPrIVSIQNPYSLL----------------NRNFE-EGLAEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 232 CQMKGIQLQAWGCLAQG----------RFAEQG---LYS------EHENVKK-TAHYVAqLAKQYGVESEAIVLAFLLRH 291
Cdd:cd19094 212 CHRENVGLLAYSPLAGGvltgkyldgaARPEGGrlnLFPgymaryRSPQALEaVAEYVK-LARKHGLSPAQLALAWVRSR 290
|
330 340 350
....*....|....*....|....*....|
gi 1699063870 292 PAGIQPVIGTTNLDRIKASAVATQINLTRE 321
Cdd:cd19094 291 PFVTSTIIGATTLEQLKENIDAFDVPLSDE 320
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
57-305 |
2.07e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 84.29 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 57 IDTALESGINLFDHADIYTFSKAEQAFGQALQQAPEL----RDQMFIQSKCGIRFEG----------------------- 109
Cdd:cd19099 27 LKAALDSGINVIDTAINYRGGRSERLIGKALRELIEKggikRDEVVIVTKAGYIPGDgdeplrplkyleeklgrglidva 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 110 EGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHrpDPLMELNELART------------LENLKAQGKVDFFGVSNM 177
Cdd:cd19099 107 DSAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLH--NPEEQLLELGEEefydrleeafeaLEEAVAEGKIRYYGISTW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 178 NSHQI-----QYLQSALGQPIVAN-----------QIEMSLvkldWLNDGVMINSQGHHQsdfAAGTLEHCQMKGIQLQA 241
Cdd:cd19099 185 DGFRAppalpGHLSLEKLVAAAEEvggdnhhfkviQLPLNL----LEPEALTEKNTVKGE---ALSLLEAAKELGLGVIA 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1699063870 242 WGCLAQGRFAEQGLYSEHENVKKTAHyVAQLAkqygveseaivLAFLLRHPAGIQPVIGTTNLD 305
Cdd:cd19099 258 SRPLNQGQLLGELRLADLLALPGGAT-LAQRA-----------LQFARSTPGVDSALVGMRRPE 309
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
52-322 |
2.54e-18 |
|
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: 83.21 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 52 QTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGIL 131
Cdd:cd19157 25 EVVNAVKTALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSK----------VWNADQGYDSTLKAFEASL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 132 NRLNAEKLDVLLLHRPDPlmELN-ELARTLENLKAQGKVDFFGVSNMNSHQIQ-YLQSALGQPIVaNQIEMslvkldwln 209
Cdd:cd19157 92 ERLGLDYLDLYLIHWPVK--GKYkETWKALEKLYKDGRVRAIGVSNFQVHHLEdLLADAEIVPMV-NQVEF--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 210 dgvminsqghHQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGLysehenvkktahyVAQLAKQYGVESEAIVLAFLL 289
Cdd:cd19157 160 ----------HPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPV-------------LKEIAEKYNKSVAQVILRWDL 216
|
250 260 270
....*....|....*....|....*....|...
gi 1699063870 290 RHpaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19157 217 QN--GVVTIPKSIKEHRIIENADVFDFELSQED 247
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
35-322 |
6.51e-18 |
|
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: 81.63 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 35 GLG-GGWNDNPVTASdvaqtcsvIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgIRFEgegnv 113
Cdd:cd19139 5 GLGtFRLKDDVVIDS--------VRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTK--IWID----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 114 gryDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDP--LMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALG- 190
Cdd:cd19139 67 ---NLSKDKLLPSLEESLEKLRTDYVDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 191 QPIVANQIEMSlvkldwlndGVMINSqghhqsdfaaGTLEHCQMKGIQLQAWGCLAQGRFAEQGLysehenvkktahyVA 270
Cdd:cd19139 144 GAIATNQIELS---------PYLQNR----------KLVAHCKQHGIHVTSYMTLAYGKVLDDPV-------------LA 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1699063870 271 QLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19139 192 AIAERHGATPAQIALAWAMAR--GYAVIPSSTKREHLRSNLLALDLTLDADD 241
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
26-326 |
6.85e-18 |
|
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: 82.86 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDNpVTASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQApELRDQMFIQSKCGI 105
Cdd:cd19146 11 VSPLCLGAMSFGEAWKSM-MGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASR-GNRDEMVLATKYTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFEGEGNVG-RYDF---SADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSN----M 177
Cdd:cd19146 89 GYRRGGPIKiKSNYqgnHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDtpawV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 178 NSHQIQYLQSALGQPIVANQIEMSLVKldwlndgvminsqghhqSDFAAGTLEHCQMKGIQLQAWGCLAQGRF--AEQ-- 253
Cdd:cd19146 169 VSKANAYARAHGLTQFVVYQGHWSAAF-----------------RDFERDILPMCEAEGMALAPWGVLGQGQFrtEEEfk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 254 ---------GLYSEHEnvKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREEWY 324
Cdd:cd19146 232 rrgrsgrkgGPQTEKE--RKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQ 309
|
..
gi 1699063870 325 NL 326
Cdd:cd19146 310 EI 311
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
52-322 |
1.44e-17 |
|
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: 80.94 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 52 QTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGIL 131
Cdd:cd19126 24 ETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTK----------LWNDDQRARRTEDAFQESL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 132 NRLNAEKLDVLLLHRPDPlMELNELARTLENLKAQGKVDFFGVSNMNSHQI-QYLQSALGQPIVaNQIEMSlvklDWLNd 210
Cdd:cd19126 91 DRLGLDYVDLYLIHWPGK-DKFIDTWKALEKLYASGKVKAIGVSNFQEHHLeELLAHADVVPAV-NQVEFH----PYLT- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 211 gvminsqghhQSDFaagtLEHCQMKGIQLQAWGCLAQGRFAEQGLysehenvkktahyVAQLAKQYGVESEAIVLAFLLR 290
Cdd:cd19126 164 ----------QKEL----RGYCKSKGIVVEAWSPLGQGGLLSNPV-------------LAAIGEKYGKSAAQVVLRWDIQ 216
|
250 260 270
....*....|....*....|....*....|..
gi 1699063870 291 HpaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19126 217 H--GVVTIPKSVHASRIKENADIFDFELSEDD 246
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
28-185 |
2.62e-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: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 28 QIAYGCMGLGggWNDNPVTASDVAQtcsVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRdqmfIQSKCGIRF 107
Cdd:cd19075 2 KIILGTMTFG--SQGRFTTAEAAAE---LLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERGFK----IDTKANPGV 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699063870 108 EGegnvgryDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYL 185
Cdd:cd19075 73 GG-------GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEI 143
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-308 |
6.07e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 79.68 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 28 QIAYGCMGLGggwndnpvTASDVAQTCSVIDTALESGINLFDHADIYTF-------SKAEQAFGQALQQApELRDQMFIQ 100
Cdd:cd19752 2 ELCLGTMYFG--------TRTDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDR-GNRDDVVIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 101 SKCGIRF--EGEGNVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMN 178
Cdd:cd19752 73 TKVGAGPrdPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 179 SHQIQYLQSALGQ----PIVANQIEMSLVKLD-WLNDGVMINSQGHHqsdfaagtLEHCQMKG-IQLQAWGCLAQGRF-- 250
Cdd:cd19752 153 AWRLERARQIARQqgwaEFSAIQQRHSYLRPRpGADFGVQRIVTDEL--------LDYASSRPdLTLLAYSPLLSGAYtr 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699063870 251 ---AEQGLYsEHENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIK 308
Cdd:cd19752 225 pdrPLPEQY-DGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLE 284
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
48-308 |
8.04e-17 |
|
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: 78.77 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 48 SDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKCGIRfegegnvgryDFSADWVSQSV 127
Cdd:cd19133 20 PDPEECERAVLEAIKAGYRLIDTAAAY---GNEEAVGRAIKKSGIPREELFITTKLWIQ----------DAGYEKAKKAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 128 EGILNRLNAEKLDVLLLHRP--DPLMELnelaRTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEMslvkl 205
Cdd:cd19133 87 ERSLKRLGLDYLDLYLIHQPfgDVYGAW----RAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAVNQIET----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 206 dwlndgvminsqgH--HQSDFAAGTLEHcqmKGIQLQAWGCLAQGRfaeQGLYSEHEnvkktahyVAQLAKQYGVESEAI 283
Cdd:cd19133 158 -------------HpfNQQIEAVEFLKK---YGVQIEAWGPFAEGR---NNLFENPV--------LTEIAEKYGKSVAQV 210
|
250 260
....*....|....*....|....*
gi 1699063870 284 VLAFLLRHpaGIQPVIGTTNLDRIK 308
Cdd:cd19133 211 ILRWLIQR--GIVVIPKSVRPERIA 233
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
15-322 |
1.32e-16 |
|
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: 78.99 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 15 KNIPLSNhleGVGQIAYGCmglgGGWNDNPVTASdvaqtcSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPEL- 93
Cdd:cd19154 2 ASITLSN---GVKMPLIGL----GTWQSKGAEGI------TAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELLEEg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 94 ---RDQMFIQSKCGIRFEGEGNVGRydfsadwvsqSVEGILNRLNAEKLDVLLLHRPDPL-------------------M 151
Cdd:cd19154 66 vvkREDLFITTKLWTHEHAPEDVEE----------ALRESLKKLQLEYVDLYLIHAPAAFkddegesgtmengmsihdaV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 152 ELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEMSLvkldWLndgvminSQGHHQsdfaagtlEH 231
Cdd:cd19154 136 DVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHL----YF-------PQKELV--------EF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 232 CQMKGIQLQAWGCLAQ-GR--FAEQGLYSEHENVKKTAHyVAQLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIK 308
Cdd:cd19154 197 CKKHNISVTSYATLGSpGRanFTKSTGVSPAPNLLQDPI-VKAIAEKHGKTPAQVLLRYLLQR--GIAVIPKSATPSRIK 273
|
330
....*....|....
gi 1699063870 309 ASAVATQINLTREE 322
Cdd:cd19154 274 ENFNIFDFSLSEED 287
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-322 |
1.50e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 78.79 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 32 GCMGLGGGWNDNPVTASDVaqtcSVIDTALESGINLFDHADIYTfsKAEQAFGQALQQAP---ELRDQMFIQSK-CGIRf 107
Cdd:cd19101 8 GMWQLSGGHGGIRDEDAAV----RAMAAYVDAGLTTFDCADIYG--PAEELIGEFRKRLRrerDAADDVQIHTKwVPDP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 108 egegnvGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLME-LNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQ 186
Cdd:cd19101 81 ------GELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 187 SAlGQPIVANQIEMSLvkLDWLNDGVMinsqghhqSDFaagtlehCQMKGIQLQAWGCLAQGRFAEQGL------YSEHE 260
Cdd:cd19101 155 DA-GVPIVSNQVQYSL--LDRRPENGM--------AAL-------CEDHGIKLLAYGTLAGGLLSEKYLgvpeptGPALE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 261 NVKKTAHYV------------------AQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19101 217 TRSLQKYKLmidewggwdlfqellrtlKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDED 296
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
34-277 |
3.80e-16 |
|
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: 77.03 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGggwndnpVTASDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgIRFEGEGnv 113
Cdd:cd19131 13 LGLG-------VWQVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTK--LWNSDQG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 114 grYDFSADWVSQSvegiLNRLNAEKLDVLLLHRPDPLMELN-ELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQP 192
Cdd:cd19131 79 --YDSTLRAFDES----LRKLGLDYVDLYLIHWPVPAQDKYvETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 193 IVANQIEMslvkldwlndgvminsqghHQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGLysehenvkktahyVAQL 272
Cdd:cd19131 153 PVVNQIEL-------------------HPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPV-------------IGEI 200
|
....*
gi 1699063870 273 AKQYG 277
Cdd:cd19131 201 AEKHG 205
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
25-310 |
4.61e-16 |
|
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: 77.32 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 25 GVGQIAYGCMGLGGGWNDNPvTASDVAQTCSVidtALESGINLFDHADIYtfSKAEQAFGQALQQ-APEL-RDQMFIQSK 102
Cdd:cd19164 12 GLPPLIFGAATFSYQYTTDP-ESIPPVDIVRR---ALELGIRAFDTSPYY--GPSEIILGRALKAlRDEFpRDTYFIITK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 103 CGirfegegnvgRY-----DFSADWVSQSVEGILNRLNAEKLDVLLLH------RPDPLmelnELARTLENLKAQGKVDF 171
Cdd:cd19164 86 VG----------RYgpddfDYSPEWIRASVERSLRRLHTDYLDLVYLHdvefvaDEEVL----EALKELFKLKDEGKIRN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 172 FGVSNMN----SHQIQYLQSALGQPIvanqiemslvkldwlnDGVMinSQGHH--QSDFAAGTLE--HCQMKGIQLQAWG 243
Cdd:cd19164 152 VGISGYPlpvlLRLAELARTTAGRPL----------------DAVL--SYCHYtlQNTTLLAYIPkfLAAAGVKVVLNAS 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699063870 244 CLAQGRFAEQGLYSEH---ENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQP-VIGTTNLDRIKAS 310
Cdd:cd19164 214 PLSMGLLRSQGPPEWHpasPELRAAAAKAAEYCQAKGTDLADVALRYALREWGGEGPtVVGCSNVDELEEA 284
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
34-285 |
7.55e-16 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 76.26 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGggwndnpVTASDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKCgirfegegnv 113
Cdd:PRK11565 18 LGLG-------VWQASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 114 grydfsadW------VSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELA-RTLENLKAQGKVDFFGVSNMNSHQIQYLQ 186
Cdd:PRK11565 78 --------WnddhkrPREALEESLKKLQLDYVDLYLMHWPVPAIDHYVEAwKGMIELQKEGLIKSIGVCNFQIHHLQRLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 187 SALGQPIVANQIEMslvkldwlndgvminsqgH---HQSDFAAGTLEHcqmkGIQLQAWGCLAQGrfaEQGLYsEHENVK 263
Cdd:PRK11565 150 DETGVTPVINQIEL------------------HplmQQRQLHAWNATH----KIQTESWSPLAQG---GKGVF-DQKVIR 203
|
250 260
....*....|....*....|..
gi 1699063870 264 ktahyvaQLAKQYGVESEAIVL 285
Cdd:PRK11565 204 -------DLADKYGKTPAQIVI 218
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
55-305 |
1.14e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 75.64 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 55 SVIDTALESGINLFDHADIYTFSkaEQAFGQALQQapelRDQMFIQSKCGIRFEGEGNVgrydfsADWVSQSVEGILNRL 134
Cdd:cd19097 30 KILEYALKAGINTLDTAPAYGDS--EKVLGKFLKR----LDKFKIITKLPPLKEDKKED------EAAIEASVEASLKRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 135 NAEKLDVLLLHRP-DPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLqSALGQP-IVanQIEMSLvkLDwlndgv 212
Cdd:cd19097 98 KVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKA-LESFKIdII--QLPFNI--LD------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 213 minsqghhQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFA--EQGLYSEHENVKKTAHYVAQLAKQYGVESEAIVLAFLLR 290
Cdd:cd19097 167 --------QRFLKSGLLAKLKKKGIEIHARSVFLQGLLLmePDKLPAKFAPAKPLLKKLHELAKKLGLSPLELALGFVLS 238
|
250
....*....|....*
gi 1699063870 291 HPAGIQPVIGTTNLD 305
Cdd:cd19097 239 LPEIDKIVVGVDSLE 253
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
57-322 |
2.03e-15 |
|
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: 74.61 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 57 IDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgIRfegegnvGRYDfSADWVSQSVEGILNRLNA 136
Cdd:cd19132 26 VVAALQAGYRLLDTAFNY---ENEGAVGEAVRRSGVPREELFVTTK--LP-------GRHH-GYEEALRTIEESLYRLGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 137 EKLDVLLLHRPDPLMELN-ELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEMSlvkldwlndgvmin 215
Cdd:cd19132 93 DYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVNQIELH-------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 216 sqghhqSDFA-AGTLEHCQMKGIQLQAWGCLAQGrfaeQGLYSEhenvkktaHYVAQLAKQYGVESEAIVLAFLLRHpaG 294
Cdd:cd19132 159 ------PYFPqAEQRAYHREHGIVTQSWSPLGRG----SGLLDE--------PVIKAIAEKHGKTPAQVVLRWHVQL--G 218
|
250 260
....*....|....*....|....*...
gi 1699063870 295 IQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19132 219 VVPIPKSANPERQRENLAIFDFELSDED 246
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
17-321 |
9.62e-15 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 74.12 E-value: 9.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 17 IPLSNhLEgVGQIAYGCMGLGggwnDNPVTASDVAQtcsvIDTALESGINLFDHADIY-------TFSKAEQAFGQALQQ 89
Cdd:PRK10625 6 IPHSS-LE-VSTLGLGTMTFG----EQNSEADAHAQ----LDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 90 APElRDQMFIQSKCGIRFEGEGNVGRYDFSADW--VSQSVEGILNRLNAEKLDVLLLHRPD-----------------PL 150
Cdd:PRK10625 76 RGS-REKLIIASKVSGPSRNNDKGIRPNQALDRknIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 151 MELNElarTLENLKAQ---GKVDFFGVSNMNSHQI-QYLQSALGQP---IVANQIEMSLvkldwLNDGvminsqghhqsd 223
Cdd:PRK10625 155 VSLLE---TLDALAEQqraGKIRYIGVSNETAFGVmRYLHLAEKHDlprIVTIQNPYSL-----LNRS------------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 224 FAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGL------------------YSEHENVKKTAHYVAqLAKQYGVESEAIVL 285
Cdd:PRK10625 215 FEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLngakpagarntlfsrftrYSGEQTQKAVAAYVD-IAKRHGLDPAQMAL 293
|
330 340 350
....*....|....*....|....*....|....*.
gi 1699063870 286 AFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTRE 321
Cdd:PRK10625 294 AFVRRQPFVASTLLGATTMEQLKTNIESLHLTLSEE 329
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
57-322 |
1.35e-14 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 73.21 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 57 IDTALESGINLFDHADIY--TFSKAEQAFGQALQQ--APeLRDQMFIQSKCGIrFEGEGNVGrydfsaDWVSQ-----SV 127
Cdd:cd19151 36 LRRAFDLGITHFDLANNYgpPPGSAEENFGRILKEdlKP-YRDELIISTKAGY-TMWPGPYG------DWGSKkyliaSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 128 EGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQ----IQYLQSaLGQPIVANQIEMSLV 203
Cdd:cd19151 108 DQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEareaAAILKD-LGTPCLIHQPKYSMF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 204 KlDWLNDGVminsqghhqsdfaagtLEHCQMKGIQLQAWGCLAQG--------------RFAEQGLYSEHENVkkTAHYV 269
Cdd:cd19151 187 N-RWVEEGL----------------LDVLEEEGIGCIAFSPLAQGlltdrylngipedsRAAKGSSFLKPEQI--TEEKL 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 270 AQ------LAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVAT-QINLTREE 322
Cdd:cd19151 248 AKvrrlneIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALdNREFSEEE 307
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
26-320 |
2.45e-14 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 72.50 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDnpvTASDVAQTCsvIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKCGi 105
Cdd:PLN02587 11 VSSVGFGASPLGSVFGP---VSEEDAIAS--VREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKCG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RFeGEGnvgrYDFSADWVSQSVEGILNRLNAEKLDVLLLHRpdplME-------LNELARTLENLKAQGKVDFFGVSNMN 178
Cdd:PLN02587 85 RY-GEG----FDFSAERVTKSVDESLARLQLDYVDILHCHD----IEfgsldqiVNETIPALQKLKESGKVRFIGITGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 179 SHQIQYlqsalgqpiVANQIEMSLVKLdwlndgvmINSQGHHQSDFAA--GTLEHCQMKGIQLQAWGCLAQGRFAEQGLY 256
Cdd:PLN02587 156 LAIFTY---------VLDRVPPGTVDV--------ILSYCHYSLNDSSleDLLPYLKSKGVGVISASPLAMGLLTENGPP 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699063870 257 SEH---ENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASaVATQINLTR 320
Cdd:PLN02587 219 EWHpapPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEEN-VAAATELET 284
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
38-183 |
1.20e-13 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 70.70 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 38 GGWndnpVT---ASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKCgirFEGEGNVG 114
Cdd:cd19143 19 GSW----VTfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKI---FWGGGGPP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699063870 115 RYD--FSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQ 183
Cdd:cd19143 92 PNDrgLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIE 162
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
33-316 |
1.28e-13 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 70.46 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 33 CMGLGGGWNDNPVTASDVAQTCSVIdtALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKcgIRFEGEGN 112
Cdd:cd19159 15 CLGLGTWVTFGGQISDEVAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK--LYWGGKAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 113 VGRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQ- 191
Cdd:cd19159 91 TER-GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQf 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 192 ---PIVANQIEMSL-------VKLDWLNDGVMINSQGhhQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGLYSEhEN 261
Cdd:cd19159 170 nmiPPVCEQAEYHLfqrekveVQLPELYHKIGVGAMT--WSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSE-EG 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1699063870 262 VKKTAHY--VAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQI 316
Cdd:cd19159 247 RKQQNKLkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 303
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
34-175 |
1.36e-13 |
|
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: 70.57 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGGWNDNPVTASDVAQtcSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKCgirFEGEGNV 113
Cdd:cd19142 16 VGLGTWSTFSTAISEEQAE--EIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTKI---YWSYGSE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699063870 114 GRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVS 175
Cdd:cd19142 91 ER-GLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTS 151
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
56-333 |
8.74e-13 |
|
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: 67.69 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 56 VIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPEL----RDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGIL 131
Cdd:cd19116 30 AVKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKIAEgvvkREDLFITTK----------LWNSYHEREQVEPALRESL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 132 NRLNAEKLDVLLLHRP-------DPLMELN---------ELARTLENLKAQGKVDFFGVSNMNSHQIQ-YLQSALGQPIV 194
Cdd:cd19116 97 KRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSEQINrLLSNCNIKPAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 195 aNQIEMSLvkldwlndgvminsqGHHQSDFaagtLEHCQMKGIQLQAWGCLAQ-----GRFAEQGLYSEHenvkktahyV 269
Cdd:cd19116 177 -NQIEVHP---------------TLTQEKL----VAYCQSNGIVVMAYSPFGRlvprgQTNPPPRLDDPT---------L 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1699063870 270 AQLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIKASAVATQINLTREEWYNLYVYSRGQ 333
Cdd:cd19116 228 VAIAKKYGKTTAQIVLRYLIDR--GVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQ 289
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
33-206 |
1.29e-12 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 67.70 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 33 CMGLGGGWNDNPVTASDVAQtcSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKcgIRFEGEGN 112
Cdd:cd19160 17 CLGLGTWVTFGSQISDETAE--DLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTK--IYWGGQAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 113 VGRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQ- 191
Cdd:cd19160 93 TER-GLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQf 171
|
170
....*....|....*...
gi 1699063870 192 ---PIVANQIEMSLVKLD 206
Cdd:cd19160 172 nliPPVCEQAEYHLFQRE 189
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
33-316 |
1.88e-12 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 67.03 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 33 CMGLGGGWNDNPVTASDVAQtcSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKcgIRFEGEGN 112
Cdd:cd19158 15 CLGLGTWVTFGGQITDEMAE--HLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK--IFWGGKAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 113 VGRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQ- 191
Cdd:cd19158 91 TER-GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQf 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 192 ---PIVANQIEMSL-------VKLDWLNDGVMINSQGhhQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQGLYSEhEN 261
Cdd:cd19158 170 nliPPICEQAEYHMfqrekveVQLPELFHKIGVGAMT--WSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSE-EG 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1699063870 262 VKKTAHY--VAQLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQI 316
Cdd:cd19158 247 RRQQAKLkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 303
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
29-180 |
1.94e-12 |
|
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: 66.05 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 29 IAYGCMGLGGGWNDNPvtasDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelRDQMFIQSKCGIRFe 108
Cdd:cd19096 3 LGFGTMRLPESDDDSI----DEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGP--REKFYLATKLPPWS- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699063870 109 gegnvgryDFSADWVSQSVEGILNRLNAEKLDVLLLH---RPD--PLMELNELARTLENLKAQGKVDFFGVSnmnSH 180
Cdd:cd19096 76 --------VKSAEDFRRILEESLKRLGVDYIDFYLLHglnSPEwlEKARKGGLLEFLEKAKKEGLIRHIGFS---FH 141
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
26-322 |
2.20e-12 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 66.77 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDNpVTASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQApELRDQMFIQSKCGI 105
Cdd:cd19147 10 VSPLILGAMSIGDAWSGF-MGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSR-KNRDQIVIATKFTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RF----EGEGNVGRY-DFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSh 180
Cdd:cd19147 88 DYkayeVGKGKAVNYcGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 181 qiqYLQSALGQPIVAN-QIEMSLVKLDWlndGVMinsqghhQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAE------- 252
Cdd:cd19147 167 ---WVVSAANYYATAHgKTPFSVYQGRW---NVL-------NRDFERDIIPMARHFGMALAPWDVLGGGKFQSkkaveer 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 253 ----QGLYSEHENVKKTAHYVA------QLAKQYGVES-EAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVATQINLTRE 321
Cdd:cd19147 234 kkngEGLRSFVGGTEQTPEEVKisealeKVAEEHGTESvTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPE 313
|
.
gi 1699063870 322 E 322
Cdd:cd19147 314 E 314
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
33-204 |
2.66e-12 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 66.32 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 33 CMGLGGGWNDNPVTASDVAQtcSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKcgIRFEGEGN 112
Cdd:cd19141 14 CLGLGTWVTFGSQISDEVAE--ELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK--IFWGGKAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 113 VGRyDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQ- 191
Cdd:cd19141 90 TER-GLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQf 168
|
170
....*....|....*.
gi 1699063870 192 ---PIVANQIEMSLVK 204
Cdd:cd19141 169 nliPPIVEQAEYHLFQ 184
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
34-305 |
3.16e-12 |
|
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: 65.89 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGggwndnpVTASDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKCGIRfegegnv 113
Cdd:cd19127 12 LGLG-------VFQTPPEETADAVATALADGYRLIDTAAAY---GNEREVGEGIRRSGVDRSDIFVTTKLWIS------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 114 gryDFSADWVSQSVEGILNRLNAEKLDVLLLHRPDPlmelNELART------LENLKAQGKVDFFGVSNMNSHQIQYLQS 187
Cdd:cd19127 75 ---DYGYDKALRGFDASLRRLGLDYVDLYLLHWPVP----NDFDRTiqaykaLEKLLAEGRVRAIGVSNFTPEHLERLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 188 ALGQPIVANQIEMSLVkldwlndgvminsqgHHQSDFAAGTLEHcqmkGIQLQAWGCLAQGRFAEQGLYSEHENVkkTAH 267
Cdd:cd19127 148 ATTVVPAVNQVELHPY---------------FSQKDLRAFHRRL----GIVTQAWSPIGGVMRYGASGPTGPGDV--LQD 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1699063870 268 YV-AQLAKQYGVESEAIVLAFLLRH-----PAGIQPVIGTTNLD 305
Cdd:cd19127 207 PTiTGLAEKYGKTPAQIVLRWHLQNgvsaiPKSVHPERIAENID 250
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
34-335 |
8.01e-12 |
|
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: 64.83 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGgWNDNPvtasdvAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPEL----RDQMFIQSKcgirfeg 109
Cdd:cd19111 7 IGLGT-YQSPP------EEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKWWLKNgklkREEVFITTK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 110 egnVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRP--------DPLME-----LNELARTLENLKAQGKVDFFGVSN 176
Cdd:cd19111 70 ---LPPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPcgfvnkkdKGERElassdVTSVWRAMEALVSEGKVKSIGLSN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 177 MNSHQIQYLQsALGQPIVAN-QIEMSLVkldwlndgvminSQGHHQSDFaagtlehCQMKGIQLQAWGCLAQGRFAEQGL 255
Cdd:cd19111 147 FNPRQINKIL-AYAKVKPSNlQLECHAY------------LQQRELRKF-------CNKKNIVVTAYAPLGSPGRANQSL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 256 YSEHENVKKTAHyVAQLAKQYGVESEAIVLAFLLRHPAGIQPviGTTNLDRIKASAVATQINLTREEWYNLYVYSRGQAL 335
Cdd:cd19111 207 WPDQPDLLEDPT-VLAIAKELDKTPAQVLLRFVLQRGTGVLP--KSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
47-322 |
8.44e-12 |
|
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: 64.46 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 47 ASDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKCGIRFEG-EGNVGRYDFSadwvsq 125
Cdd:cd19156 19 VQDGAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKLWNSDQGyESTLAAFEES------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 126 svegiLNRLNAEKLDVLLLHRPDPlMELNELARTLENLKAQGKVDFFGVSNMNSHQIQ-YLQSALGQPIVaNQIEMslvk 204
Cdd:cd19156 90 -----LEKLGLDYVDLYLIHWPVK-GKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEeLLKSCKVAPMV-NQIEL---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 205 ldwlndgvminsqghHQSDFAAGTLEHCQMKGIQLQAWGCLAQGRFAEQglysehenvkktaHYVAQLAKQYGVESEAIV 284
Cdd:cd19156 159 ---------------HPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSN-------------PVLKAIGKKYGKSAAQVI 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 1699063870 285 LAFLLRHpaGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19156 211 IRWDIQH--GIITIPKSVHEERIQENFDVFDFELTAEE 246
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
56-249 |
2.16e-11 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 63.50 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 56 VID---TALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKCGIRfegegnvgryDFSADWVSQSVEGILN 132
Cdd:PRK11172 18 VIDsvkTALELGYRAIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWID----------NLAKDKLIPSLKESLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 133 RLNAEKLDVLLLHRPDPLMELnELARTLENL---KAQGKVDFFGVSNMNSHQIQYLQSALGQ-PIVANQIEMSlvklDWL 208
Cdd:PRK11172 85 KLRTDYVDLTLIHWPSPNDEV-SVEEFMQALleaKKQGLTREIGISNFTIALMKQAIAAVGAeNIATNQIELS----PYL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1699063870 209 ndgvminsQGHHQSDFaagtlehCQMKGIQLQAWGCLAQGR 249
Cdd:PRK11172 160 --------QNRKVVAF-------AKEHGIHVTSYMTLAYGK 185
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
34-322 |
1.01e-10 |
|
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: 61.66 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGgWNDNPvtasdvAQTCSVIDTALESGINLFDHADIYTfSKAE--QAFGQALQQAPELRDQMFIQSKcgirfegeg 111
Cdd:cd19123 15 LGLGT-WKSKP------GEVGQAVKQALEAGYRHIDCAAIYG-NEAEigAALAEVFKEGKVKREDLWITSK--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 112 nVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRP-------------DPLMELNELA-----RTLENLKAQGKVDFFG 173
Cdd:cd19123 78 -LWNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgEDLLSLSPIPledtwRAMEELVDKGLCRHIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 174 VSNMNSHQIQYLQSALGQPIVANQIEMSlvklDWLndgvminsqghHQSDFaagtLEHCQMKGIQLQAWGCLAQGRFAeQ 253
Cdd:cd19123 157 VSNFSVKKLEDLLATARIKPAVNQVELH----PYL-----------QQPEL----LAFCRDNGIHLTAYSPLGSGDRP-A 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699063870 254 GLYSEHENVKKTAHYVAQLAKQYGVESEAIVLAFLLRHPAGIQPviGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19123 217 AMKAEGEPVLLEDPVINKIAEKHGASPAQVLIAWAIQRGTVVIP--KSVNPERIQQNLEAAEVELDASD 283
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
51-322 |
2.17e-10 |
|
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: 60.31 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 51 AQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGI 130
Cdd:cd19130 23 ADTQRAVATALEVGYRHIDTAAIY---GNEEGVGAAIAASGIPRDELFVTTK----------LWNDRHDGDEPAAAFAES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 131 LNRLNAEKLDVLLLHRPDPLMELN-ELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEmslvkldwln 209
Cdd:cd19130 90 LAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIE---------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 210 dgVMINSQGHHQSDFAagtlehcQMKGIQLQAWGCLAQGRFAEQGLysehenvkktahyVAQLAKQYGVESEAIVLAFLL 289
Cdd:cd19130 160 --LHPAYQQRTIRDWA-------QAHDVKIEAWSPLGQGKLLGDPP-------------VGAIAAAHGKTPAQIVLRWHL 217
|
250 260 270
....*....|....*....|....*....|...
gi 1699063870 290 RHPAGIQPviGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19130 218 QKGHVVFP--KSVRRERMEDNLDVFDFDLTDTE 248
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
56-322 |
4.48e-10 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 59.78 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 56 VIDTALESGINLFDHADIY--TFSKAEQAFGQALQQ--APeLRDQMFIQSKCGIRF----EGEGNVGRYDFSAdwVSQSv 127
Cdd:cd19150 35 ILRTAFDLGITHFDLANNYgpPPGSAEENFGRILREdfAG-YRDELIISTKAGYDMwpgpYGEWGSRKYLLAS--LDQS- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 128 egiLNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQY---LQSALGQPIVANQIEMSLVK 204
Cdd:cd19150 111 ---LKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREaaaILRELGTPLLIHQPSYNMLN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 205 lDWLNDgvminsqghhqsdfaAGTLEHCQMKGIQLQAWGCLAQGRFA---------------EQGLYSEHENVKKTAHYV 269
Cdd:cd19150 188 -RWVEE---------------SGLLDTLQELGVGCIAFTPLAQGLLTdkylngipegsraskERSLSPKMLTEANLNSIR 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1699063870 270 A--QLAKQYGVESEAIVLAFLLRHPAGIQPVIGTTNLDRIKASAVA-TQINLTREE 322
Cdd:cd19150 252 AlnEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGAlDNLTFSADE 307
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
46-242 |
1.03e-08 |
|
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: 55.35 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 46 TASDVA---QTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPEL-----RDQMFIQSK--CGirfegegnvgr 115
Cdd:cd19124 12 TASDPPspeDIKAAVLEAIEVGYRHFDTAAAY---GTEEALGEALAEALRLglvksRDELFVTSKlwCS----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 116 yDFSADWVSQSVEGILNRLNAEKLDVLLLHRP---------------DPL-MELNELARTLENLKAQGKVDFFGVSNMNS 179
Cdd:cd19124 78 -DAHPDLVLPALKKSLRNLQLEYVDLYLIHWPvslkpgkfsfpieeeDFLpFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1699063870 180 HQIQYLQSALGQPIVANQIEMSLvkldwlndgvminsqGHHQsdfaaGTL-EHCQMKGIQLQAW 242
Cdd:cd19124 157 KKLQELLSFATIPPAVNQVEMNP---------------AWQQ-----KKLrEFCKANGIHVTAY 200
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
62-322 |
1.11e-08 |
|
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: 55.41 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 62 ESGINLFDHADIYtfsKAEQAFGQALQQAPELRDQMFIQSK--CGirfegegnvgryDFSADWVSQSVEGILNRLNAEKL 139
Cdd:cd19135 37 ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKlwPS------------DYGYESTKQAFEASLKRLGVDYL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 140 DVLLLHRPD-PLMELN------ELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEmslvkldwlndgv 212
Cdd:cd19135 102 DLYLLHWPDcPSSGKNvketraETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHVNQVE------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 213 minsqgHHQSDFAAGTLEHCQMKGIQLQAWGCLAQGRfaeqglYSEHENvkktahyVAQLAKQYGVESEAIVLAFLLRHP 292
Cdd:cd19135 169 ------FHPFQNPVELIEYCRDNNIVFEGYCPLAKGK------ALEEPT-------VTELAKKYQKTPAQILIRWSIQNG 229
|
250 260 270
....*....|....*....|....*....|
gi 1699063870 293 AGIQPviGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19135 230 VVTIP--KSTKEERIKENCQVFDFSLSEED 257
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
34-309 |
2.06e-08 |
|
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: 54.81 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGgWNDNPvtaSDVAQTcsvIDTALESGinlFDHADIYTFSKAEQAFGQALQQAPELRDQMFIQSKcgirfegegnv 113
Cdd:cd19117 17 VGLGT-WQSKP---NEVAKA---VEAALKAG---YRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTK----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 114 grydFSADWVSQSVEGI---LNRLNAEKLDVLLLHRPDPL-------MELNELA--------------RTLENLKAQGKV 169
Cdd:cd19117 76 ----LWCTWHRRVEEALdqsLKKLGLDYVDLYLMHWPVPLdpdgndfLFKKDDGtkdhepdwdfiktwELMQKLPATGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 170 DFFGVSNMNSHQIQYLQSALGQPIV--ANQIEMSlvkldwlndgvMINSQgHHQSDFaagtlehCQMKGIQLQAWGCLAQ 247
Cdd:cd19117 152 KAIGVSNFSIKNLEKLLASPSAKIVpaVNQIELH-----------PLLPQ-PKLVDF-------CKSKGIHATAYSPLGS 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699063870 248 grfAEQGLYSEhenvkktaHYVAQLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIKA 309
Cdd:cd19117 213 ---TNAPLLKE--------PVIIKIAKKHGKTPAQVIISWGLQR--GYSVLPKSVTPSRIES 261
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
33-309 |
4.71e-08 |
|
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: 53.50 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 33 CMGLGGgWndnpvtASDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPE----LRDQMFIQSKcgirfe 108
Cdd:cd19125 13 AVGLGT-W------QADPGVVGNAVKTAIKEGYRHIDCAAIY---GNEKEIGKALKKLFEdgvvKREDLFITSK------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 109 gegnVGRYDFSADWVSQSVEGILNRLNAEKLDVLLLHRP----------DPLMELN----ELARTLENLKAQGKVDFFGV 174
Cdd:cd19125 77 ----LWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpEPEEVLPpdipSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 175 SNMNSHQIQYLQSALGQPIVANQIEMSLVkldWLNDGVminsqghhqsdfaagtLEHCQMKGIQLQAWGCLaqGRfaeQG 254
Cdd:cd19125 153 SNFSVKKLEDLLAVARVPPAVNQVECHPG---WQQDKL----------------HEFCKSKGIHLSAYSPL--GS---PG 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699063870 255 LYSEHENVKKTAhYVAQLAKQYGvESEAIVlafLLRHpaGIQpvIGT------TNLDRIKA 309
Cdd:cd19125 209 TTWVKKNVLKDP-IVTKVAEKLG-KTPAQV---ALRW--GLQ--RGTsvlpksTNEERIKE 260
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
55-248 |
6.21e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 53.45 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 55 SVIDTALESGINLFDHADIY--TFSKAEQAFGQALQQ--APeLRDQMFIQSKCGIRF----EGEGNVGRYDFSadwvsqS 126
Cdd:PRK09912 47 AILRKAFDLGITHFDLANNYgpPPGSAEENFGRLLREdfAA-YRDELIISTKAGYDMwpgpYGSGGSRKYLLA------S 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 127 VEGILNRLNAEKLDVLLLHRPDPLMELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQ---PIVANQIEMSLV 203
Cdd:PRK09912 120 LDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREwkiPLLIHQPSYNLL 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1699063870 204 KlDWLNDgvminsqghhqsdfaAGTLEHCQMKGIQLQAWGCLAQG 248
Cdd:PRK09912 200 N-RWVDK---------------SGLLDTLQNNGVGCIAFTPLAQG 228
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
34-322 |
3.02e-07 |
|
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: 51.34 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGgWNDNpvtaSDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPE----LRDQMFIQSKCGIRFEg 109
Cdd:cd19119 15 LGLGT-ASPH----EDRAEVKEAVEAAIKEGYRHIDTAYAY---ETEDFVGEAIKRAIDdgsiKREELFITTKVWPTFY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 110 egnvgrydfsaDWVSQSVEGILNRLNAEKLDVLLLHRPDPLMELNE-------------------------LARTLENLK 164
Cdd:cd19119 86 -----------DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDdsgkpftpvnddgktryaasgdhitTYKQLEKIY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 165 AQGKVDFFGVSNMNshqIQYLQSALGQ----PIVaNQIEMS--LVKLDwlndgvminsqghhqsdfaagTLEHCQMKGIQ 238
Cdd:cd19119 155 LDGRAKAIGVSNYS---IVYLERLIKEckvvPAV-NQVELHphLPQMD---------------------LRDFCFKHGIL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 239 LQAWGCLAQGRfaeqglyseHENVKKTAhyVAQLAKQYGVESEAIVLAFLLRHPAGIQPviGTTNLDRIKASavATQINL 318
Cdd:cd19119 210 VTAYSPLGSHG---------APNLKNPL--VKKIAEKYNVSTGDILISYHVRQGVIVLP--KSLKPVRIVSN--GKIVSL 274
|
....
gi 1699063870 319 TREE 322
Cdd:cd19119 275 TKED 278
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
60-322 |
6.83e-07 |
|
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: 49.85 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 60 ALESGINLFDHADIYTfskAEQAFGQALQQAPELRDQMFIQSKCGIRFEGegnvgrYDFSADWVSQSvegiLNRLNAEKL 139
Cdd:cd19134 33 ALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKLATPDQG------FTASQAACRAS----LERLGLDYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 140 DVLLLHRPDPLM-ELNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQSALGQPIVANQIEMSLVkldwLNDGVMINSQG 218
Cdd:cd19134 100 DLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIELHPL----LNQAELRKVNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 219 HHqsdfaagtlehcqmkGIQLQAWGCLAQGRFAEqglysehenvkktAHYVAQLAKQYGVESEAIVLAFLLRHpaGIQPV 298
Cdd:cd19134 176 QH---------------GIVTQAYSPLGVGRLLD-------------NPAVTAIAAAHGRTPAQVLLRWSLQL--GNVVI 225
|
250 260
....*....|....*....|....
gi 1699063870 299 IGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19134 226 SRSSNPERIASNLDVFDFELTADH 249
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
17-266 |
2.76e-06 |
|
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: 48.21 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 17 IPLSNHLEgVGQIAYGCmglgggWNDNPVTASDVaqtcsvIDTALESGINLFDHADIYTfskAEQAFGQALQQAPE---- 92
Cdd:cd19113 3 IKLNSGYK-MPSVGFGC------WKLDNATAADQ------IYQAIKAGYRLFDGAEDYG---NEKEVGEGVNRAIDeglv 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 93 LRDQMFIQSKCGIRFEGEGNVGRydfsadwvsqSVEGILNRLNAEKLDVLLLH-----RPDPLME--------------- 152
Cdd:cd19113 67 KREELFLTSKLWNNFHDPKNVET----------ALNKTLSDLKLDYVDLFLIHfpiafKFVPIEEkyppgfycgdgdnfv 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 153 -----LNELARTLENLKAQGKVDFFGVSNMNSHQIQ-YLQSALGQPIVAnQIEmslvkldwlndgvminsqgHHQSDFAA 226
Cdd:cd19113 137 yedvpILDTWKALEKLVDAGKIKSIGVSNFPGALILdLLRGATIKPAVL-QIE-------------------HHPYLQQP 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1699063870 227 GTLEHCQMKGIQLQAWGCLAQGRFAEQGLYS--------EHENVKKTA 266
Cdd:cd19113 197 KLIEYAQKAGITITAYSSFGPQSFVELNQGRalntptlfEHDTIKSIA 244
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
34-322 |
5.41e-06 |
|
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: 47.14 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGGWNDNPVTASDVAQtcsvidtALESGINLFDHADIYtfsKAEQAFGQALQQAPEL---RDQMFIQSKCgirfege 110
Cdd:cd19121 15 VGLGTWQAKAGEVKAAVAH-------ALKIGYRHIDGALCY---QNEDEVGEGIKEAIAGgvkREDLFVTTKL------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 111 gnvgrYDFSADWVSQSVEGILNRLNAEKLDVLLLHRP--------DPLM------------ELNELA--RTLENLKAQGK 168
Cdd:cd19121 78 -----WSTYHRRVELCLDRSLKSLGLDYVDLYLVHWPvllnpngnHDLFptlpdgsrdldwDWNHVDtwKQMEKVLKTGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 169 VDFFGVSNmnsHQIQYLQSALGQPIV---ANQIEMslvkldwlndgvminsqghHQSDFAAGTLEHCQMKGIQLQAWGCL 245
Cdd:cd19121 153 TKAIGVSN---YSIPYLEELLKHATVvpaVNQVEN-------------------HPYLPQQELVDFCKEKGILIEAYSPL 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699063870 246 AQgrfAEQGLYSEHEnvkktahyVAQLAKQYGVESEAIVLAFLLRHPAGIQPviGTTNLDRIKASavATQINLTREE 322
Cdd:cd19121 211 GS---TGSPLISDEP--------VVEIAKKHNVGPGTVLISYQVARGAVVLP--KSVTPDRIKSN--LEIIDLDDED 272
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
57-322 |
5.49e-06 |
|
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: 47.13 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 57 IDTALESGINLFDHADIYTFSKA-EQAFGQALQQAPELRDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGILNRLN 135
Cdd:cd19128 20 VKNAIKAGYRHIDCAYYYGNEAFiGIAFSEIFKDGGVKREDLFITSK----------LWPTMHQPENVKEQLLITLQDLQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 136 AEKLDVLLLHRP---------DPLME----------LNELARTLENLKAQGKVDFFGVSNMNSHQIQYLQS-ALGQPIVa 195
Cdd:cd19128 90 LEYLDLFLIHWPlafdmdtdgDPRDDnqiqslskkpLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNyCKIKPFM- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 196 NQIEMSLvkldwlndgvminsqgHHQSDfaaGTLEHCQMKGIQLQAWGCLAqgrfaeqGLYSEHENVKKTAHYVAQLAKQ 275
Cdd:cd19128 169 NQIECHP----------------YFQND---KLIKFCIENNIHVTAYRPLG-------GSYGDGNLTFLNDSELKALATK 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1699063870 276 YGVESEAIVLAF-LLRHPAGIQPVIGTTNLDRIKASAVATQINLTREE 322
Cdd:cd19128 223 YNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDINDLALTKED 270
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
59-278 |
2.33e-05 |
|
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: 45.48 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 59 TALESGINLFDHADIYTfSKAE--QAFGQALQQAPEL-RDQMFIQSKcgirfegegnVGRYDFSADWVSQSVEGILNRLN 135
Cdd:cd19118 28 IALKAGYRHLDLAKVYQ-NQHEvgQALKELLKEEPGVkREDLFITSK----------LWNNSHRPEYVEPALDDTLKELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 136 AEKLDVLLLHRP------------------DPLMELNE---LARTLE---NLKAQGKVDFFGVSNMNSHQIQYLQSALGQ 191
Cdd:cd19118 97 LDYLDLYLIHWPvafkptgdlnpltavptnGGEVDLDLsvsLVDTWKamvELKKTGKVKSIGVSNFSIDHLQAIIEETGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 192 PIVANQIEM-SLVKLDWLndgvminsqghhqsdfaagtLEHCQMKGIQLQAWGCLAQGRFAEQgLYSEHENVKKTA---- 266
Cdd:cd19118 177 VPAVNQIEAhPLLLQDEL--------------------VDYCKSKNIHITAYSPLGNNLAGLP-LLVQHPEVKAIAaklg 235
|
250
....*....|..
gi 1699063870 267 HYVAQLAKQYGV 278
Cdd:cd19118 236 KTPAQVLIAWGI 247
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
26-204 |
5.04e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 44.19 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 26 VGQIAYGCMGLGGGWNDNPvtASDVAQTCSVIDTALESGINLFDHADIYTFSKAEQAFGQALQQAPelrDQMFIQSKCGI 105
Cdd:PRK10376 17 VNRLGYGAMQLAGPGVFGP--PKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYP---DDLTIVTKVGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 106 RfegEGNVGRY--DFSADWVSQSVEGILNRLNAEKLDVLLL------HRPDPlMELNELARTLENLKAQGKVDFFGVSNM 177
Cdd:PRK10376 92 R---RGEDGSWlpAFSPAELRRAVHDNLRNLGLDVLDVVNLrlmgdgHGPAE-GSIEEPLTVLAELQRQGLVRHIGLSNV 167
|
170 180
....*....|....*....|....*..
gi 1699063870 178 NSHQIQYLQSAlgQPIVANQIEMSLVK 204
Cdd:PRK10376 168 TPTQVAEARKI--AEIVCVQNHYNLAH 192
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
48-308 |
7.77e-05 |
|
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: 43.60 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 48 SDVAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPEL----RDQMFIQSKcgirfegegnVGRYDFSADWV 123
Cdd:cd19129 16 PDPSATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVFKAgkirREDLFVTTK----------LWNTNHRPERV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 124 SQSVEGILNRLNAEKLDVLLLHRP---------DPLME-----------LNELARTLENLKAQGKVDFFGVSNMNSHQIQ 183
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqDPRDAngnviyddgvtLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 184 YL-QSALGQPIVanqiemslvkldwlndgVMINSQGHH-QSDFaagtLEHCQMKGIQLQAWGCLAQGrfAEQGLYSEhen 261
Cdd:cd19129 163 EIfEAARIKPAV-----------------VQVESHPYLpEWEL----LDFCKNHGIVLQAFAPLGHG--MEPKLLED--- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1699063870 262 vkktaHYVAQLAKQYGVESEAIVLAFLLRHpaGIQPVIGTTNLDRIK 308
Cdd:cd19129 217 -----PVITAIARRVNKTPAQVLLAWAIQR--GTALLTTSKTPSRIR 256
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
51-292 |
4.47e-04 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 41.56 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 51 AQTCSVIDTALESGINLFDHADIYtfSKAEQAFGQALQQAPELRDQMFIQSKCGIRFEGEGNVG-----RYDFSADWVSQ 125
Cdd:cd19098 35 AHTHAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSKWGYTYTADWQVDaavheVKDHSLARLLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 126 SVEGILNRLnAEKLDVLLLHRP---DPLMELNELARTLENLKAQG-KVdffGVSNMNSHQIQYLQSALgqpivanQIEMS 201
Cdd:cd19098 113 QWEETRSLL-GKHLDLYQIHSAtleSGVLEDADVLAALAELKAEGvKI---GLSLSGPQQAETLRRAL-------EIEID 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 202 LVKldwLNDGVMINSQGHHQSdfAAGTLEHCQMKGIQLQAWGCLAQGRFAEQglySEHENVKKTAHYVAQLAKQYGVESE 281
Cdd:cd19098 182 GAR---LFDSVQATWNLLEQS--AGEALEEAHEAGMGVIVKEALANGRLTDR---NPSPELAPLMAVLKAVADRLGVTPD 253
|
250
....*....|.
gi 1699063870 282 AIVLAFLLRHP 292
Cdd:cd19098 254 ALALAAVLAQP 264
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
60-249 |
8.40e-04 |
|
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: 40.68 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 60 ALESGINLFDHADIYtfsKAEQAFGQALQQAPE----LRDQMFIQSKCGIRFegegnvgrydFSADWVSQSVEGILNRLN 135
Cdd:cd19108 36 AIDAGFRHIDSAYLY---QNEEEVGQAIRSKIAdgtvKREDIFYTSKLWCTF----------HRPELVRPALEKSLKKLQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 136 AEKLDVLLLHRPDPLMELNELART-------------------LENLKAQGKVDFFGVSNMNSHQiqyLQSALGQP---- 192
Cdd:cd19108 103 LDYVDLYLIHFPVALKPGEELFPKdengklifdtvdlcatweaMEKCKDAGLAKSIGVSNFNRRQ---LEMILNKPglky 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1699063870 193 -IVANQIEMSLvkldWLNdgvminsqghhQSDFaagtLEHCQMKGIQLQAWGCLAQGR 249
Cdd:cd19108 180 kPVCNQVECHP----YLN-----------QSKL----LDFCKSKDIVLVAYSALGSQR 218
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
34-245 |
9.66e-04 |
|
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: 40.48 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 34 MGLGGgWNDNPvtasdvAQTCSVIDTALESGINLFDHADIYtfsKAEQAFGQALQQAPE----LRDQMFIQSKCGIRFeg 109
Cdd:cd19107 7 LGLGT-WKSPP------GQVTEAVKVAIDAGYRHIDCAYVY---QNENEVGEAIQEKIKeqvvKREDLFIVSKLWCTF-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699063870 110 egnvgrydFSADWVSQSVEGILNRLNAEKLDVLLLHRP------DPLMELNELARTL-------------ENLKAQGKVD 170
Cdd:cd19107 75 --------HEKGLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgKELFPLDESGNVIpsdttfldtweamEELVDEGLVK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699063870 171 FFGVSNMNSHQIQYLQSALG---QPIVaNQIEMSlvklDWLNDGVMINsqghhqsdfaagtleHCQMKGIQLQAWGCL 245
Cdd:cd19107 147 AIGVSNFNHLQIERILNKPGlkyKPAV-NQIECH----PYLTQEKLIQ---------------YCQSKGIVVTAYSPL 204
|
|
| |
