|
Name |
Accession |
Description |
Interval |
E-value |
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-311 |
9.25e-148 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 416.86 E-value: 9.25e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGKGRD--EAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQ 78
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSpaEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 79 TKFGIYKGD---NGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNM 155
Cdd:COG4989 81 TKCGIRLPSearDNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 156 NPMQVEMLQSAVGQKLEVNQLQFGLGHTGMVqqeihvnmadaasvdhDGGLISYSRLKGMTIQAWSPFQFGFFEGVFidN 235
Cdd:COG4989 161 TPSQFELLQSALDQPLVTNQIELSLLHTDAF----------------DDGTLDYCQLNGITPMAWSPLAGGRLFGGF--D 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 236 PKFPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEWYDLYVAA-GNDLP 311
Cdd:COG4989 223 EQFPRLRAALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTREEWYELYEAArGHEVP 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-307 |
6.29e-125 |
|
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: 358.79 E-value: 6.29e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDGKGRD--EAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQTKFGIYK 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESaeELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 86 GD---NGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEM 162
Cdd:cd19092 81 GDdprPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 163 LQSAVGQKLEVNQLQFGLGHTGMVqqeihvnmadaasvdhDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIdnPKFPALN 242
Cdd:cd19092 161 LQSYLDQPLVTNQIELSLLHTEAI----------------DDGTLDYCQLLDITPMAWSPLGGGRLFGGFD--ERFQRLR 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 243 EAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEWYDLYVAAG 307
Cdd:cd19092 223 AALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWYEIYEAAR 287
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-299 |
3.31e-73 |
|
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: 228.14 E-value: 3.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGKG----RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvDRQSIF 76
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGPWggvdEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGR--PRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 77 VQTKFGIYKGDNGaiTRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMN 156
Cdd:COG0667 79 IATKVGRRMGPGP--NGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 157 PMQV-EMLQSAVG-QKLEVNQLQFGLghtgmVQQEIHVNMADAAsVDHDGGLISYS----------RLKGMTIQAWSPFQ 224
Cdd:COG0667 157 AEQLrRALAIAEGlPPIVAVQNEYSL-----LDRSAEEELLPAA-RELGVGVLAYSplagglltgkYRRGATFPEGDRAA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 225 FGFFEGVfiDNPKFPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEW 299
Cdd:COG0667 231 TNFVQGY--LTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDL 303
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-302 |
2.00e-65 |
|
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: 207.38 E-value: 2.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRLDGKG-----RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIFVQTKFGIY 84
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWwgevdDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR---RDDVVIATKCGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 85 kGDNGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQ 164
Cdd:cd19084 78 -WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 165 SAVgqKLEVNQLQFglghtgmvqqeihvNMADAASVDHdggLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKFP----- 239
Cdd:cd19084 157 KYG--PIVSLQPPY--------------SMLEREIEEE---LLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPpddrr 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456322 240 ---------------ALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19084 218 srfpffrgenfeknlEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-299 |
1.84e-58 |
|
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: 189.44 E-value: 1.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 16 VALGVMRLDGKG----RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQTKFGIYKGDNGAi 91
Cdd:pfam00248 1 IGLGTWQLGGGWgpisKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWPS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 92 tryNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKL 171
Cdd:pfam00248 80 ---GGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 172 EVNQLQFglghtgmvqqeihvNMADAasvDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKFP------------ 239
Cdd:pfam00248 157 VAVQVEY--------------NLLRR---RQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGpgerrrllkkgt 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456322 240 ----ALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEW 299
Cdd:pfam00248 220 plnlEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEV 283
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-288 |
2.12e-58 |
|
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: 187.34 E-value: 2.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKG-RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVdRQSIFVQTKFGIYKGDNGAIT 92
Cdd:cd06660 1 SRLGLGTMTFGGDGdEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 93 RYnfSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAV----G 168
Cdd:cd06660 80 RL--SPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAkahgL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 169 QKLEVNQLQFGLGHTGMVQQEIhvnmadaasvdhdgglISYSRLKGMTIQAWSPFQFGffegvfidnpkfpalneamqrv 248
Cdd:cd06660 158 PGFAAVQPQYSLLDRSPMEEEL----------------LDWAEENGLPLLAYSPLARG---------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 705456322 249 adkygvtKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMA 288
Cdd:cd06660 200 -------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-298 |
3.23e-52 |
|
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: 173.95 E-value: 3.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGKG----------RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDlkv 70
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGgffgawggvdQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 71 DRQSIFVQTKFGIYKGDNgaITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHF 150
Cdd:cd19091 78 RRDDVLIATKVRGRMGEG--PNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 151 GVSNMNPMQVEMLQSavgqklevnqLQFGLGHTGMVQQEIHVNMAdAASVDHDggLISYSRLKGMTIQAWSPFQFGF--- 227
Cdd:cd19091 156 GVSNFSAWQIMKALG----------ISERRGLARFVALQAYYSLL-GRDLEHE--LMPLALDQGVGLLVWSPLAGGLlsg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 228 ------------------FEGVFIDNPKFPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAG 289
Cdd:cd19091 223 kyrrgqpapegsrlrrtgFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGA 302
|
....*....
gi 705456322 290 ADVEISAQE 298
Cdd:cd19091 303 AGLSLTPEE 311
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-298 |
7.99e-52 |
|
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: 172.77 E-value: 7.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 2 KYSELGSSGVDASRVALGVMRLdGK--------GRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkVDRQ 73
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSF-GDpkwrpwvlDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEF-APRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 74 SIFVQTK--FGIYKGDNGAItrynFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFG 151
Cdd:cd19079 79 EVVIATKvyFPMGDGPNGRG----LSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 152 VSNMNPMQV-EMLQSAVGQ---KLEVNQlqfglGHTGMVQQEIHVNMADAAsVDHDGGLISYSRL-KGMTIQAWSPFQfg 226
Cdd:cd19079 155 ASSMYAWQFaKALHLAEKNgwtKFVSMQ-----NHYNLLYREEEREMIPLC-EEEGIGVIPWSPLaRGRLARPWGDTT-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 227 ffeGVFIDNPKFPAL------------NEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEI 294
Cdd:cd19079 227 ---ERRRSTTDTAKLkydyfteadkeiVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKL 303
|
....
gi 705456322 295 SAQE 298
Cdd:cd19079 304 SEEE 307
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
14-288 |
2.91e-48 |
|
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: 161.49 E-value: 2.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKG-----RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDlkvDRQSIFVQTKFGiYKGDN 88
Cdd:cd19086 4 SEIGFGTWGLGGDWwgdvdDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFG-NRFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 89 GAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDT-LVEFDELAEAFNELQNSGRVRHFGVSnMNPMQvEMLQSAV 167
Cdd:cd19086 80 GPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDeVLDNDELFEALEKLKQEGKIRAYGVS-VGDPE-EALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 168 GQKLEVNQLQFGLGHTGMVQQeihvnMADAASvDHDGGLIsysrlkgmtiqAWSPFQFGFFEGvfidnpKFPALneamqr 247
Cdd:cd19086 158 RGGIDVVQVIYNLLDQRPEEE-----LFPLAE-EHGVGVI-----------ARVPLASGLLTG------KLAQA------ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 705456322 248 vadkygvtknaiAVAWILRHPARMQVLLGSMTPSRLKEMMA 288
Cdd:cd19086 209 ------------ALRFILSHPAVSTVIPGARSPEQVEENAA 237
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-295 |
6.17e-48 |
|
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: 162.38 E-value: 6.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRLDGKGRDE--AQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvdRQSIFVQTKfgIYKGD 87
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDedAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWP--RESYVISTK--VFWPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 NGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAV 167
Cdd:cd19074 77 GPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 168 GQ----KLEVNQLQFglghtGMVQQEIhvnmadaasvdhDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKFPA--- 240
Cdd:cd19074 157 RQfgliPPVVEQPQY-----NMLWREI------------EEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSrsr 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 241 ---------LNEAM-----------QRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEIS 295
Cdd:cd19074 220 atdednrdkKRRLLtdenlekvkklKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLS 294
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-297 |
3.37e-47 |
|
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: 160.44 E-value: 3.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKG------RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIFVQTKFGIYkgd 87
Cdd:cd19085 2 SRLGLGCWQFGGGYwwgdqdDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGR---RDDVVIATKVSPD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 ngaitryNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQvemLQSA- 166
Cdd:cd19085 76 -------NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQ---LEEAl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 167 -VGqKLEVNQLQFGLghtgmVQQEIhvnmadaasvdhDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKFPA----- 240
Cdd:cd19085 146 dAG-RIDSNQLPYNL-----LWRAI------------EYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPgdart 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456322 241 ----------------LNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQ 297
Cdd:cd19085 208 rlfrhfepgaeeetfeALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPS 280
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-298 |
5.51e-46 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 155.98 E-value: 5.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 9 SGVDASRVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQDLKVDRQSIFVQTKfgiykgdn 88
Cdd:COG0656 1 NGVEIPALGLGTWQLPG---EEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTK-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 89 gaITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTlVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVG 168
Cdd:COG0656 67 --VWNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGP-GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 169 QKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQfgffEGVFIDNPkfpalneAMQRV 248
Cdd:COG0656 144 VKPAVNQVEL---HPYLQQRE----------------LLAFCREHGIVVEAYSPLG----RGKLLDDP-------VLAEI 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 705456322 249 ADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:COG0656 194 AEKHGKTPAQVVLRWHLQR--GVVVIPKSVTPERIRENLDAFDFELSDED 241
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
19-298 |
7.51e-46 |
|
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: 155.85 E-value: 7.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 19 GVMRLDGKGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQdlKVDRQSIFVQTKFgiykgdngaiTRYNFSK 98
Cdd:cd19072 16 GGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIK--GFDREDLFITTKV----------SPDHLKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 99 DHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQ-KLEVNQLQ 177
Cdd:cd19072 84 DDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKgPIVANQVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 178 FGLghtgMVQQEIHvnmadaasvdhdgGLISYSRLKGMTIQAWSPFQFGFFEGVFIdnpkFPALNEamqrVADKYGVTKN 257
Cdd:cd19072 164 YNL----FDREEES-------------GLLPYCQKNGIAIIAYSPLEKGKLSNAKG----SPLLDE----IAKKYGKTPA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 705456322 258 AIAVAWILRHPaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19072 219 QIALNWLISKP-NVIAIPKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-298 |
1.00e-45 |
|
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: 155.33 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 15 RVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKfgiykgdngaITRY 94
Cdd:cd19071 3 LIGLGTYKLKP---EETAEAVLAALEAGYRHIDTAAAYGNEAE---VGEAIRESGVPREELFITTK----------LWPT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 95 NFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELA------EAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVG 168
Cdd:cd19071 67 DHGYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEarletwRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 169 QKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPfqFGFFEGVFIDNPkfpalneAMQRV 248
Cdd:cd19071 147 IKPAVNQIEL---HPYLQQKE----------------LVEFCKEHGIVVQAYSP--LGRGRRPLLDDP-------VLKEI 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 705456322 249 ADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19071 199 AKKYGKTPAQVLLRWALQR--GVVVIPKSSNPERIKENLDVFDFELSEED 246
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-298 |
8.95e-45 |
|
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: 154.74 E-value: 8.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 3 YSELGSSGVDASRVALGVMRLDG----KGRDEAQNI--VRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIF 76
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGgpwwGGSDDNESIrtIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR---RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 77 VQTKFGI----------YKGDNGAITRyNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGR 146
Cdd:cd19149 78 LATKCGLrwdreggsffFVRDGVTVYK-NLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 147 VRHFGVSNMNPMQVEMLQSAvGQkLEVNQLQFglghtgmvqqeihvNMADAAsvdHDGGLISYSRLKGMTIQAWSPFQFG 226
Cdd:cd19149 157 IRAIGASNVSVEQIKEYVKA-GQ-LDIIQEKY--------------SMLDRG---IEKELLPYCKKNNIAFQAYSPLEQG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 227 FFEG------VFI------DNPKFP--------ALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEM 286
Cdd:cd19149 218 LLTGkitpdrEFDagdarsGIPWFSpenrekvlALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEEN 297
|
330
....*....|..
gi 705456322 287 MAGADVEISAQE 298
Cdd:cd19149 298 AKAGDIRLSAED 309
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-301 |
3.96e-44 |
|
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: 152.73 E-value: 3.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGK-GRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDlkvDRQSIFVQT 79
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRtDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 80 KFGIYKGDNgaITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQ 159
Cdd:cd19087 78 KVFGPMGDD--PNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 160 VEMLQSAVGQ----KLEVNQLQFGLghtgmVQQEIHVNMADAAsVDHDGGLISYSRL----------KGMTIQAWSPFQF 225
Cdd:cd19087 156 IAKAQGIAARrgllRFVSEQPMYNL-----LKRQAELEILPAA-RAYGLGVIPYSPLagglltgkygKGKRPESGRLVER 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456322 226 GFFEGVFIDNPKFPALnEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAqEWYD 301
Cdd:cd19087 230 ARYQARYGLEEYRDIA-ERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTP-ELLA 303
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-299 |
1.07e-43 |
|
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: 151.60 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 5 ELGSSGVDASRVALGVMRLdGKGRDEAQN--IVRTALDGGVNFFDTADCYSD-------GESSRRLGQALQDlKVDRQSI 75
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVF-GWTADEETSfaLLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKS-RGKRDRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 76 FVQTKFGIYKGDNGaitrYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNM 155
Cdd:cd19081 79 VIATKVGFPMGPNG----PGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 156 NPmqvEMLQSAvgqkLEVNQlQFGLGHTGMVQQeiHVNMADAASVdhDGGLISYSRLKGMTIQAWSPFQFGFFEGVF--- 232
Cdd:cd19081 155 SA---WRLQEA----LELSR-QHGLPRYVSLQP--EYNLVDRESF--EGELLPLCREEGIGVIPYSPLAGGFLTGKYrse 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 233 IDNPKFPA--------LNE-------AMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQ 297
Cdd:cd19081 223 ADLPGSTRrgeaakryLNErglrildALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDE 302
|
..
gi 705456322 298 EW 299
Cdd:cd19081 303 EV 304
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-295 |
1.26e-43 |
|
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: 150.06 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKG-------RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDlkvDRQSIFVQTKFGIYKG 86
Cdd:cd19088 2 SRLGYGAMRLTGPGiwgppadREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLVRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 87 DNGAITRyNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSA 166
Cdd:cd19088 79 GPGWWGP-DGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 167 VGqkLEVNQLQFGLGHTgmvqqeihvnmadaasvdHDGGLISYSRLKGMTIQAWSPFQFGffegvfidNPKFPAlnEAMQ 246
Cdd:cd19088 158 VR--IVSVQNRYNLANR------------------DDEGVLDYCEAAGIAFIPWFPLGGG--------DLAQPG--GLLA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 705456322 247 RVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEIS 295
Cdd:cd19088 208 EVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-302 |
4.63e-43 |
|
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: 149.69 E-value: 4.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 13 ASRVALGVM----RL----DGKGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvDRQSIFVQTKFgiy 84
Cdd:cd19093 2 VSPLGLGTWqwgdRLwwgyGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 85 kgdngAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDE-LAEAFNELQNSGRVRHFGVSNMNPMQVEML 163
Cdd:cd19093 78 -----APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEaLMDGLADAVEEGLVRAVGVSNYSADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 164 QSAVGQK---LEVNQLQFGLGHTGMVQQeihvnmadaasvdhdgGLISYSRLKGMTIQAWSPFQFGFFEG---------- 230
Cdd:cd19093 153 HKALKERgvpLASNQVEYSLLYRDPEQN----------------GLLPACDELGITLIAYSPLAQGLLTGkyspenpppg 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456322 231 ------VFIDNPKFPALNEAMQRVADKYGVTKNAIAVAWILRHPArmQVLLGSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19093 217 grrrlfGRKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGV--VPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-285 |
9.20e-43 |
|
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: 147.35 E-value: 9.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGkgrdEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvdRQSIFVQTK 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPR----ESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLR--RDKVFLATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 81 FGIYKGDNgaitrynfSKDHLIASLDRELENLQTDYVDFVLLHR---PDTLVEFDELAEAFNELQNSGRVRHFGVSNMNP 157
Cdd:cd19105 75 ASPRLDKK--------DKAELLKSVEESLKRLQTDYIDIYQLHGvdtPEERLLNEELLEALEKLKKEGKVRFIGFSTHDN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 158 MQvEMLQSAV-GQKLEVNQLQFGLGHTGMVQQEIhvnMADAASvdHDGGLIsysrlkGMTIQAWSPFQfgffegvfidnp 236
Cdd:cd19105 147 MA-EVLQAAIeSGWFDVIMVAYNFLNQPAELEEA---LAAAAE--KGIGVV------AMKTLAGGYLQ------------ 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 705456322 237 kfpalnEAMQRVADKYGVTKNAIAVAWILRHPaRMQVLLGSM-TPSRLKE 285
Cdd:cd19105 203 ------PALLSVLKAKGFSLPQAALKWVLSNP-RVDTVVPGMrNFAELEE 245
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-291 |
1.49e-42 |
|
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: 148.08 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGK-GRDEAQNIVRTALDGGVNFFDTADCYSD----GESSRRLGQALQDLKVdRQSIFVQTKFGIYKGDN 88
Cdd:cd19082 1 SRIVLGTADFGTRiDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGN-RDKVVIATKGGHPDLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 89 GAITRynFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNpmqVEMLQSAV- 167
Cdd:cd19082 80 MSRSR--LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWS---TERIAEANa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 168 ------GQKLEVNQLQFGLGHtgMVQQeihvNMADAASVDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVfiDNPKFPAL 241
Cdd:cd19082 155 yakahgLPGFAASSPQWSLAR--PNEP----PWPGPTLVAMDEEMRAWHEENQLPVFAYSSQARGFFSKR--AAGGAEDD 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 242 NEAMQR---------------VADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGAD 291
Cdd:cd19082 227 SELRRVyyseenferlerakeLAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-298 |
7.40e-42 |
|
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: 145.09 E-value: 7.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQDLKVDRQSIFVQTKfgiykgdng 89
Cdd:cd19140 5 GVRIPALGLGTYPLTG---EECTRAVEHALELGYRHIDTAQMY---GNEAQVGEAIAASGVPRDELFLTTK--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 90 aITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQ 169
Cdd:cd19140 70 -VWPDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 170 KLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQfgffEGVFIDNPkfpalneAMQRVA 249
Cdd:cd19140 149 PLFTNQVEY---HPYLDQRK----------------LLDAAREHGIALTAYSPLA----RGEVLKDP-------VLQEIG 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 705456322 250 DKYGVTKNAIAVAWILRHPaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19140 199 RKHGKTPAQVALRWLLQQE-GVAAIPKATNPERLEENLDIFDFTLSDEE 246
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-298 |
1.46e-41 |
|
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: 144.34 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 16 VALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQDLKVDRQSIFVQTKfgiykgdngaITRYN 95
Cdd:cd19073 4 LGLGTWQLRG---DDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTK----------VWRDH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 96 FSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQ 175
Cdd:cd19073 68 LRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 176 LQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQFGffeGVFIDnpkfpalnEAMQRVADKYGVT 255
Cdd:cd19073 148 VEF---HPFLYQAE----------------LLEYCRENDIVITAYSPLARG---EVLRD--------PVIQEIAEKYDKT 197
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 705456322 256 KNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19073 198 PAQVALRWLVQK--GIVVIPKASSEDHLKENLAIFDWELTSED 238
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
6-298 |
2.54e-41 |
|
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: 145.25 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 6 LGSSGVDASRVALGVMRLDGK----GRDEAQ--NIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvDRQSIFVQT 79
Cdd:cd19083 4 LGKSDIDVNPIGLGTNAVGGHnlypNLDEEEgkDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEY--NRNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 80 KFGIYKGDNGaiTRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNpmq 159
Cdd:cd19083 82 KGAHKFGGDG--SVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFS--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 160 VEMLQSAVGQ-KLEVNQLQFGLghtgmVQQeihvnmadaasvDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKF 238
Cdd:cd19083 157 LEQLKEANKDgYVDVLQGEYNL-----LQR------------EAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 239 P--------------ALNEAMQRV------ADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19083 220 PdndlrndkplfkgeRFSENLDKVdklksiADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-298 |
2.99e-40 |
|
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: 142.74 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 6 LGSSGVDASRVALGVMRLD-----GKGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDlkvDRQSIFVQTK 80
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGtewgwGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLATK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 81 FGIYKGDNGAitryNFSKDH---LIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMnP 157
Cdd:cd19080 80 YTMNRRPGDP----NAGGNHrknLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDT-P 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 158 MQVemlqsaVGQKLEVNQLQfglGHTGMVQQEIHVNMADaASVDHDggLISYSRLKGMTIQAWSPFQFGFFEGVF----- 232
Cdd:cd19080 155 AWV------VARANTLAELR---GWSPFVALQIEYSLLE-RTPERE--LLPMARALGLGVTPWSPLGGGLLTGKYqrgee 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 233 -------IDNPKFPALNE-------AMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19080 223 grageakGVTVGFGKLTErnwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQ 302
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
28-302 |
4.42e-40 |
|
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: 140.85 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 28 RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDlkvDRQSIFVQTKfgIYKGdngaitryNFSKDHLIASLDR 107
Cdd:cd19138 28 RAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSK--VLPS--------NASRQGTVRACER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 108 ELENLQTDYVDFVLLHRPDTlVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAV-GQKLEVNQLQFGLGHTGmv 186
Cdd:cd19138 95 SLRRLGTDYLDLYLLHWRGG-VPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPgGGNCAANQVLYNLGSRG-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 187 qqeihvnmadaasVDHDggLISYSRLKGMTIQAWSPF-QFGFFEGVFIDNPkfpalneAMQRVADKYGVTKNAIAVAWIL 265
Cdd:cd19138 172 -------------IEYD--LLPWCREHGVPVMAYSPLaQGGLLRRGLLENP-------TLKEIAARHGATPAQVALAWVL 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 705456322 266 RHPArmqVLL--GSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19138 230 RDGN---VIAipKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-285 |
3.20e-38 |
|
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: 135.83 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKG----RDEAQNIVRTALDGGVNFFDTADCYSDGEssRRLGQALQDLkvDRQSIFVQTKFGIykGDNG 89
Cdd:cd19095 1 SVLGLGTSGIGRVWgvpsEAEAARLLNTALDLGINLIDTAPAYGRSE--ERLGRALAGL--RRDDLFIATKVGT--HGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 90 AITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPmqveMLQSAVgq 169
Cdd:cd19095 75 GRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGE----ELEAAI-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 170 klevnqlqfGLGHTGMVQqeIHVNMADAASVDhdggLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPkFPALNEAMQRVA 249
Cdd:cd19095 149 ---------ASGVFDVVQ--LPYNVLDREEEE----LLPLAAEAGLGVIVNRPLANGRLRRRVRRRP-LYADYARRPEFA 212
|
250 260 270
....*....|....*....|....*....|....*..
gi 705456322 250 DKYGVTKNA-IAVAWILRHPARMQVLLGSMTPSRLKE 285
Cdd:cd19095 213 AEIGGATWAqAALRFVLSHPGVSSAIVGTTNPEHLEE 249
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-292 |
1.94e-37 |
|
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: 135.42 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALG--VMRLDGKGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQ 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGswVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 79 TK--FGiykGDNGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMN 156
Cdd:cd19143 81 TKifWG---GGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 157 PMQV-EMLQSAVGQKLE---VNQLQFGLGHTGMVQQEIhvnmadaASVDHDGGLisysrlkGMTIqaWSPFQFGFFEGVF 232
Cdd:cd19143 158 AQQIeEAHEIADRLGLIppvMEQPQYNLFHRERVEVEY-------APLYEKYGL-------GTTT--WSPLASGLLTGKY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 233 IDN--------------------PKFPALNEAMQR---VADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAG 289
Cdd:cd19143 222 NNGipegsrlalpgyewlkdrkeELGQEKIEKVRKlkpIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKA 301
|
...
gi 705456322 290 ADV 292
Cdd:cd19143 302 LEV 304
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-291 |
1.65e-36 |
|
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: 132.46 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGK-GRDEAQNIVRTALDGGVNFFDTADCYS-------DGESSRRLGQALQDLKVdRQSIFVQTKFGIYK 85
Cdd:cd19752 1 SELCLGTMYFGTRtDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRGN-RDDVVIATKVGAGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 86 GDNGA--ITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEML 163
Cdd:cd19752 80 RDPDGgpESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 164 QSAVGQK----LEVNQLQFGL-----GHTGMVQQEIHVNMADAASVDHDGGLISYS-RLKGMTIQAWSPFQFGFfegvfi 233
Cdd:cd19752 160 RQIARQQgwaeFSAIQQRHSYlrprpGADFGVQRIVTDELLDYASSRPDLTLLAYSpLLSGAYTRPDRPLPEQY------ 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456322 234 DNPKFPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGAD 291
Cdd:cd19752 234 DGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-302 |
1.69e-36 |
|
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: 132.36 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRL-DGKG----RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIFVQTKFGIY 84
Cdd:cd19078 1 GLEVSAIGLGCMGMsHGYGpppdKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF---RDQVVIATKFGFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 85 KGDNGAITRY-NFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNpmqVEML 163
Cdd:cd19078 78 IDGGKPGPLGlDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAG---VETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 164 QSAvgqklevnqlqfglgHT----GMVQQEIHVnMADaasvDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKFP 239
Cdd:cd19078 155 RRA---------------HAvcpvTAVQSEYSM-MWR----EPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 240 --------------------ALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEW 299
Cdd:cd19078 215 egddraslprftpealeanqALVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEEL 294
|
...
gi 705456322 300 YDL 302
Cdd:cd19078 295 REI 297
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-160 |
1.18e-35 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 131.87 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGKGRDEAQNIVRTALDGGVNFFDTADCYsdGESSRRLGQALQDlkvDRQSIFVQTK 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 81 FGIYKGDngaitrynfsKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFD------ELAEAFNELQNSGRVRHFGVSN 154
Cdd:COG1453 76 LPPWVRD----------PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEkvlkpgGALEALEKAKAEGKIRHIGFST 145
|
....*.
gi 705456322 155 MNPMQV 160
Cdd:COG1453 146 HGSLEV 151
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-219 |
1.65e-35 |
|
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: 128.37 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 3 YSELGSSGVDASRVALGVMRLDGKGRDEAQNIVRTALDGGVNFFDTADCYSDGEssRRLGQALQDlkvDRQSIFVQTKFG 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDSE--EKIGKALKG---RRDKVFLATKTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 83 iykgdngaitryNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELA------EAFNELQNSGRVRHFGVSNMN 156
Cdd:cd19100 76 ------------ARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFgpggalEALLEAKEEGKIRFIGISGHS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456322 157 PmqvEMLQSAVgQKLEVNQLQFglghtgmvqqeiHVNMADAASVDHDGGLISYSRLKGMTIQA 219
Cdd:cd19100 144 P---EVLLRAL-ETGEFDVVLF------------PINPAGDHIDSFREELLPLAREKGVGVIA 190
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-298 |
2.61e-35 |
|
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: 129.64 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 2 KYSELGSSGVDASRVALGVMRL--DGKGRDEAQNI--VRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIFV 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMsaFYGPADEEESIatLHRALELGVTFLDTADMYGPGTNEELLGKALKDR---RDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 78 QTKFGIYKGDNGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNP 157
Cdd:cd19076 78 ATKFGIVRDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 158 MQVEMLQ-----SAVgqklevnQLQFGLghtgmvqqeihvnmadaASVDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVF 232
Cdd:cd19076 158 DTIRRAHavhpiTAV-------QSEYSL-----------------WTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 233 ID------------NPKFP--------ALNEAMQRVADKYGVTKNAIAVAWILrhpARMQVLL---GSMTPSRLKEMMAG 289
Cdd:cd19076 214 KSpedlpeddfrrnNPRFQgenfdknlKLVEKLEAIAAEKGCTPAQLALAWVL---AQGDDIVpipGTKRIKYLEENVGA 290
|
....*....
gi 705456322 290 ADVEISAQE 298
Cdd:cd19076 291 LDVVLTPEE 299
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-285 |
5.96e-35 |
|
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: 128.58 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRLDG---KGRDEAQNI--VRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVdRQSIFVQTKFGIY 84
Cdd:cd19148 1 DLPVSRIALGTWAIGGwmwGGTDEKEAIetIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGK-RDRVVIATKVGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 85 KGDNGAITRyNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQ 164
Cdd:cd19148 80 WDEGGEVVR-NSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 165 SAVgqKLEVNQLQFGLghtgmVQQEIhvnmadaasvdhDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKFP----- 239
Cdd:cd19148 159 KVA--PLHTVQPPYNL-----FEREI------------EKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEgddlr 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456322 240 ---------------ALNEAMQRVA-DKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKE 285
Cdd:cd19148 220 rtdpkfqeprfsqylAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDA 281
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-302 |
5.33e-34 |
|
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: 125.55 E-value: 5.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALG---VMRLDGKGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvdRQSIFVQTKFGIYKGDNGA 90
Cdd:cd19162 1 PRLGLGaasLGNLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHP--RAEYVVSTKVGRLLEPGAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 91 IT------RYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDT--LVEFDELAEAFNELQNSGRVRHFGVSNmnpMQVEM 162
Cdd:cd19162 79 GRpagadrRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGV---TDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 163 LQSAVgQKLEVNQLQFGLGHTgmvqqeihvnMADAASVDhdgGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKF---P 239
Cdd:cd19162 156 LLRAA-RRADVDVVMVAGRYT----------LLDRRAAT---ELLPLCAAKGVAVVAAGVFNSGILATDDPAGDRYdyrP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456322 240 ALNE------AMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19162 222 ATPEvlararRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAEFWAEL 290
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
27-299 |
9.67e-34 |
|
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: 124.59 E-value: 9.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 27 GRDEAQNIVRTALDGGVNFFDTADCYsdGESSRRLGQALQdlKVDRQSIFVQTKFGIYKGDNgaitrYNFSKDHLIASLD 106
Cdd:cd19090 18 DDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKVGRLPEDT-----ADYSADRVRRSVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 107 RELENLQTDYVDFVLLHRPDTLVEFDELA-----EAFNELQNSGRVRHFGVSnMNPmqVEMLQSAVgqklEVNQLQFGLG 181
Cdd:cd19090 89 ESLERLGRDRIDLLMIHDPERVPWVDILApggalEALLELKEEGLIKHIGLG-GGP--PDLLRRAI----ETGDFDVVLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 182 HtgmvqqeihvNMADAASVDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVFIDNPKF------PALNE---AMQRVADKY 252
Cdd:cd19090 162 A----------NRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYtyrwlsPELLDrakRLYELCDEH 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 705456322 253 GVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEW 299
Cdd:cd19090 232 GVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-298 |
2.58e-33 |
|
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: 123.06 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRLDG------KGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvdRQSIFVQTKfgi 83
Cdd:cd19137 1 GEKIPALGLGTWGIGGfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFP--REDLFIVTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 84 ykgdngaITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEML 163
Cdd:cd19137 76 -------VWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 164 QSAVGQKLEVNQLQFGLghtgmvqqeihvnmadaasVDHD---GGLISYSRLKGMTIQAWSPFQFGFFEgvfidnpkfpa 240
Cdd:cd19137 149 ISKSQTPIVCNQVKYNL-------------------EDRDperDGLLEYCQKNGITVVAYSPLRRGLEK----------- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456322 241 LNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLgSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19137 199 TNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-298 |
3.32e-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: 121.12 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGKGRD----EAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDlkVDRQSIF 76
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVFGPvdeeEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKG--IPRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 77 VQTKFGIYKGDngAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHrpDtlVEFDELAE--------AFNELQNSGRVR 148
Cdd:cd19163 79 LATKVGRYGLD--PDKMFDFSAERITKSVEESLKRLGLDYIDIIQVH--D--IEFAPSLDqilnetlpALQKLKEEGKVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 149 HFGVS--NMNPMQVEMLQSAVgqklevnQLQFGLGHTgmvqqeiHVNMADAASVDHdgglISYSRLKGMTIQAWSPFQFG 226
Cdd:cd19163 153 FIGITgyPLDVLKEVLERSPV-------KIDTVLSYC-------HYTLNDTSLLEL----LPFFKEKGVGVINASPLSMG 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 227 FF--EGVFIDNPKFPALNEAMQRVAD---KYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19163 215 LLteRGPPDWHPASPEIKEACAKAAAyckSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPLDAHL 291
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-299 |
1.60e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 119.31 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKGR-------DEAQNI--VRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIFVQTKFGIY 84
Cdd:cd19102 2 TTIGLGTWAIGGGGWgggwgpqDDRDSIaaIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATKCGLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 85 KGDNGAITRYnFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQ 164
Cdd:cd19102 79 WDEEGRIRRS-LKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 165 sAVGQkLEVNQLQFGLGHTGmVQQEIHvnmadAASVDHDGGLISYSRL-KGM--------TIQAWSPFQFGFFEGVFIDn 235
Cdd:cd19102 158 -AIHP-IASLQPPYSLLRRG-IEAEIL-----PFCAEHGIGVIVYSPMqSGLltgkmtpeRVASLPADDWRRRSPFFQE- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 236 PKFP---ALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEW 299
Cdd:cd19102 229 PNLArnlALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEEL 295
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-285 |
4.37e-31 |
|
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: 118.32 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 2 KYSELGSSGVDASRVALGV-MRLDGKGRDE-AQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQT 79
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTwVTFGSQISDEvAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 80 KfgIYKGDNgAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQ 159
Cdd:cd19141 81 K--IFWGGK-AETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAME 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 160 VeMLQSAVGQklevnqlQFGLGHTGMVQQEIHVNMADAASVdHDGGLisYSRLkGMTIQAWSPFQFGFFEGVFIDN---- 235
Cdd:cd19141 158 I-MEAYSVAR-------QFNLIPPIVEQAEYHLFQREKVEM-QLPEL--FHKI-GVGAMTWSPLACGILSGKYDDGvpey 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 236 --------------------PKFPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKE 285
Cdd:cd19141 226 sraslkgyqwlkekilseegRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYE 295
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-291 |
7.33e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 118.14 E-value: 7.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 2 KYSELGSSGVDASRVALG---VMRLDGKGRDEAQ-NIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIFV 77
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggIGGLMGRTTREEQiAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PAGPYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 78 QTKFGIYKGDNGAItrynfsKDHLIASLDRELENLQTDYVDFVLLH---RPDTLVEF------------DELAEAFNELQ 142
Cdd:cd19104 78 TTKVRLDPDDLGDI------GGQIERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVggtlsttdvlglGGVADAFERLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 143 NSGRVRHFGVsnmnpmqvemlqSAVGQKLEVNQLQfGLGHTGMVQqeIHVNMAD--------AASVDHD-GGLISYSRLK 213
Cdd:cd19104 152 SEGKIRFIGI------------TGLGNPPAIRELL-DSGKFDAVQ--VYYNLLNpsaaearpRGWSAQDyGGIIDAAAEH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 214 GMTIQAWSPFQFGFF-----EGVFIDNPKFPALNEAMQR------VADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSR 282
Cdd:cd19104 217 GVGVMGIRVLAAGALttsldRGREAPPTSDSDVAIDFRRaaafraLAREWGETLAQLAHRFALSNPGVSTVLVGVKNREE 296
|
....*....
gi 705456322 283 LKEMMAGAD 291
Cdd:cd19104 297 LEEAVAAEA 305
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-291 |
9.21e-30 |
|
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: 113.43 E-value: 9.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKG-----RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvDRQSIFVQTKFGIYKGDn 88
Cdd:cd19096 1 SVLGFGTMRLPESDddsidEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEG--PREKFYLATKLPPWSVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 89 gaitrynfSKDHLIASLDRELENLQTDYVDFVLLH---RPDTLVEFDE--LAEAFNELQNSGRVRHFGVS-NMNPMQVEM 162
Cdd:cd19096 78 --------SAEDFRRILEESLKRLGVDYIDFYLLHglnSPEWLEKARKggLLEFLEKAKKEGLIRHIGFSfHDSPELLKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 163 LqsavgqkLEVNQLQFglghtgmVQqeIHVNMADAASVdHDGGLISYSRLKGMtiqawspfqfgffeGVFIDNP----KF 238
Cdd:cd19096 150 I-------LDSYDFDF-------VQ--LQYNYLDQENQ-AGRPGIEYAAKKGM--------------GVIIMEPlkggGL 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 705456322 239 PALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGAD 291
Cdd:cd19096 199 ANNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-285 |
2.66e-29 |
|
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: 113.51 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 3 YSELGSSGVDASRVALGVMRLDGKGRD--EAQNIVRTALDGGVNFFDTADCY--SDGESSRRLGQAL-QDLKVDRQSIFV 77
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSpeEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILkRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 78 QTKFGIYK-----GDNGaitrynfSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGV 152
Cdd:cd19089 81 STKAGYGMwpgpyGDGG-------SRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 153 SNMNPMQVEM---LQSAVGQKLEVNQLQFglghtGMVQQEIHVNMADAAsvDHDG-GLISYS----------RLKGMTIQ 218
Cdd:cd19089 154 SNYPGAKARRaiaLLRELGVPLIIHQPRY-----SLLDRWAEDGLLEVL--EEAGiGFIAFSplaqglltdkYLNGIPPD 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 219 AWSPFQFGFFEGVFIDNPKFPALnEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKE 285
Cdd:cd19089 227 SRRAAESKFLTEEALTPEKLEQL-RKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLED 292
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
15-298 |
5.10e-29 |
|
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: 111.29 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 15 RVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYsDGESSrrLGQALQDLKVDRQSIFVQTKfgiykgdngaITRY 94
Cdd:cd19139 3 AFGLGTFRLKD---DVVIDSVRTALELGYRHIDTAQIY-DNEAA--VGQAIAESGVPRDELFITTK----------IWID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 95 NFSKDHLIASLDRELENLQTDYVDFVLLH--RPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNpmqVEMLQSAVGqkle 172
Cdd:cd19139 67 NLSKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFT---IALLDEAIA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 173 vnqlQFGLGHTGMVQQEIHVNMADAASVDHdgglisySRLKGMTIQAWSPFQfgffEGVFIDNPkfpalneAMQRVADKY 252
Cdd:cd19139 140 ----VVGAGAIATNQIELSPYLQNRKLVAH-------CKQHGIHVTSYMTLA----YGKVLDDP-------VLAAIAERH 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 705456322 253 GVTKNAIAVAWILrhpAR-MQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19139 198 GATPAQIALAWAM---ARgYAVIPSSTKREHLRSNLLALDLTLDADD 241
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-153 |
1.27e-28 |
|
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: 112.03 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRL--DGKGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDL----KVDRQSIFVQTKFGIYKGD 87
Cdd:cd19099 4 SSLGLGTYRGdsDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDEVVIVTKAGYIPGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 NGAITR-----------------------YNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVE-------FDELAEA 137
Cdd:cd19099 84 GDEPLRplkyleeklgrglidvadsaglrHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefYDRLEEA 163
|
170
....*....|....*....
gi 705456322 138 F---NELQNSGRVRHFGVS 153
Cdd:cd19099 164 FealEEAVAEGKIRYYGIS 182
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-292 |
3.80e-28 |
|
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: 110.90 E-value: 3.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGV-MRLDGKGRDE-AQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQ 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEvAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 79 TKfgIYKGDNgAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPM 158
Cdd:cd19159 81 TK--LYWGGK-AETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 159 QVeMLQSAVGQklevnqlQFGLGHTGMVQQEIHVNMADAASVDhdggLISYSRLKGMTIQAWSPFQFGFFEGVF------ 232
Cdd:cd19159 158 EI-MEAYSVAR-------QFNMIPPVCEQAEYHLFQREKVEVQ----LPELYHKIGVGAMTWSPLACGIISGKYgngvpe 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456322 233 ------------------IDNPKFPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADV 292
Cdd:cd19159 226 ssraslkcyqwlkerivsEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 303
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-298 |
3.55e-27 |
|
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: 106.75 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRL-DGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKfgIYKG 86
Cdd:cd19126 4 NNGTRMPWLGLGVFQTpDG---DETERAVQTALENGYRSIDTAAIYKNEEG---VGEAIRESGVPREELFVTTK--LWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 87 DNgaitRYNFSKDHLIASLDRelenLQTDYVDFVLLHRPdTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSA 166
Cdd:cd19126 76 DQ----RARRTEDAFQESLDR----LGLDYVDLYLIHWP-GKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 167 VGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQfgffEGVFIDNPKFPALneamq 246
Cdd:cd19126 147 ADVVPAVNQVEF---HPYLTQKE----------------LRGYCKSKGIVVEAWSPLG----QGGLLSNPVLAAI----- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 705456322 247 rvADKYGVTKNAIAVAWILRHParMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19126 199 --GEKYGKSAAQVVLRWDIQHG--VVTIPKSVHASRIKENADIFDFELSEDD 246
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-298 |
5.29e-27 |
|
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: 106.30 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKfgIYKGDNG 89
Cdd:cd19131 7 GNTIPQLGLGVWQVSN---DEAASAVREALEVGYRSIDTAAIYGNEEG---VGKAIRASGVPREELFITTK--LWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 90 aitrynfsKDHLIASLDRELENLQTDYVDFVLLHRP----DTLVEfdeLAEAFNELQNSGRVRHFGVSNMNPMQVEMLQS 165
Cdd:cd19131 79 --------YDSTLRAFDESLRKLGLDYVDLYLIHWPvpaqDKYVE---TWKALIELKKEGRVKSIGVSNFTIEHLQRLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 166 AVGQKLEVNQLQFglgHTGMVQQEIHvnmadAASVDHdgglisysrlkGMTIQAWSPFQFGffeGVFIDnpkfpalnEAM 245
Cdd:cd19131 148 ETGVVPVVNQIEL---HPRFQQRELR-----AFHAKH-----------GIQTESWSPLGQG---GLLSD--------PVI 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 705456322 246 QRVADKYGVTKNAIAVAWILRhpARMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19131 198 GEIAEKHGKTPAQVVIRWHLQ--NGLVVIPKSVTPSRIAENFDVFDFELDADD 248
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-292 |
8.97e-27 |
|
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: 107.38 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGV-MRLDGKGRDE-AQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQ 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDEtAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 79 TKfgIYKGDNgAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPM 158
Cdd:cd19160 83 TK--IYWGGQ-AETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 159 QVeMLQSAVGQklevnqlQFGLGHTGMVQQEIHVNMADAASVDhdggLISYSRLKGMTIQAWSPFQFGFFEGVFIDN-PK 237
Cdd:cd19160 160 EI-MEAYSVAR-------QFNLIPPVCEQAEYHLFQREKVEMQ----LPELYHKIGVGSVTWSPLACGLITGKYDGRvPD 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456322 238 --------FPALNEAMQR---------------VADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADV 292
Cdd:cd19160 228 tcraavkgYQWLKEKVQSeegkkqqakvkelhpIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQV 305
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
14-295 |
9.22e-27 |
|
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: 107.27 E-value: 9.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGKG-RDEAQNIVRTALDGGVNFFDTADCYS-------DGESSRRLGQALQDlKVDRQSIFVQTKFGIYK 85
Cdd:cd19094 2 SEICLGTMTWGEQNtEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKK-KGNRDKVVLATKVAGPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 86 GDN----GAITRYNfsKDHLIASLDRELENLQTDYVDFVLLHRPD------------------TLVEFDELAEAFNELQN 143
Cdd:cd19094 81 EGItwprGGGTRLD--RENIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 144 SGRVRHFGVSNMNPMQV-EMLQSAVgqklevnqlQFGLGHTGMVQQE---IHVNmadaasvdHDGGLISYSRLKGMTIQA 219
Cdd:cd19094 159 AGKIRHIGLSNETPWGVmKFLELAE---------QLGLPRIVSIQNPyslLNRN--------FEEGLAEACHRENVGLLA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 220 WSPFQFGFFEGVFIDNPKFPA---LNE---AMQR---------------VADKYGVTKNAIAVAWILRHPARMQVLLGSM 278
Cdd:cd19094 222 YSPLAGGVLTGKYLDGAARPEggrLNLfpgYMARyrspqaleavaeyvkLARKHGLSPAQLALAWVRSRPFVTSTIIGAT 301
|
330
....*....|....*..
gi 705456322 279 TPSRLKEMMAGADVEIS 295
Cdd:cd19094 302 TLEQLKENIDAFDVPLS 318
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
18-285 |
1.12e-26 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 18 LGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKFgiykgdngaitrYNFS 97
Cdd:PRK11565 20 LGVWQASN---EEVITAIHKALEVGYRSIDTAAIYKNEEG---VGKALKEASVAREELFITTKL------------WNDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 98 KDHLIASLDRELENLQTDYVDFVLLHRPDTlvEFDELAEAFN---ELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLEVN 174
Cdd:PRK11565 82 HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKgmiELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 175 QLQFglgHTGMVQQEIHvnmadaasvdhdggliSYSRLKGMTIQAWSPF-QFGffEGVFiDNPkfpalneAMQRVADKYG 253
Cdd:PRK11565 160 QIEL---HPLMQQRQLH----------------AWNATHKIQTESWSPLaQGG--KGVF-DQK-------VIRDLADKYG 210
|
250 260 270
....*....|....*....|....*....|..
gi 705456322 254 VTKNAIAVAWILrhPARMQVLLGSMTPSRLKE 285
Cdd:PRK11565 211 KTPAQIVIRWHL--DSGLVVIPKSVTPSRIAE 240
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-298 |
1.37e-26 |
|
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: 106.76 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 6 LGSSGVDASRVALGVMRLDG-----KGRDEAQNIVRTALDGGVNFFDTADCYSDGESSrrLGQALQDLKVDRQSIFVQTK 80
Cdd:cd19144 6 LGRNGPSVPALGFGAMGLSAfygppKPDEERFAVLDAAFELGCTFWDTADIYGDSEEL--IGRWFKQNPGKREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 81 FGIYKGDNGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNpmqV 160
Cdd:cd19144 84 FGIEKNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECS---A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 161 EMLQSAvgqklevnqlqFGLGHTGMVQQEIHVNMADAAsvDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVF-------- 232
Cdd:cd19144 161 ETLRRA-----------HAVHPIAAVQIEYSPFSLDIE--RPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIrspddfee 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456322 233 ----IDNPKFPALN--------EAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19144 228 gdfrRMAPRFQAENfpknlelvDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEE 305
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-298 |
1.37e-26 |
|
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: 104.96 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLdgKGRDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKFGIYkgd 87
Cdd:cd19133 4 NNGVEMPILGFGVFQI--PDPEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKLWIQ--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 ngaitryNFSKDHLIASLDRELENLQTDYVDFVLLHRPdtlveF-DELA--EAFNELQNSGRVRHFGVSNMNPMQVEMLQ 164
Cdd:cd19133 76 -------DAGYEKAKKAFERSLKRLGLDYLDLYLIHQP-----FgDVYGawRAMEELYKEGKIRAIGVSNFYPDRLVDLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 165 SAVGQKLEVNQLQFglgHTGMVQQEIHVNMADaasvdhdgglisysrlKGMTIQAWSPF---QFGFFEgvfidnpkfpal 241
Cdd:cd19133 144 LHNEVKPAVNQIET---HPFNQQIEAVEFLKK----------------YGVQIEAWGPFaegRNNLFE------------ 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456322 242 NEAMQRVADKYGVTKNAIAVAWILrhparmQ----VLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19133 193 NPVLTEIAEKYGKSVAQVILRWLI------QrgivVIPKSVRPERIAENFDIFDFELSDED 247
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
24-298 |
3.74e-26 |
|
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: 104.24 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 24 DGKGRDEAQNIVRtALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKfgiykgdngaitrYNFSKDHLIA 103
Cdd:cd19120 21 DDIQRDLVDSVKL-ALKAGFRHIDTAEMYGNEKE---VGEALKESGVPREDLFITTK-------------VSPGIKDPRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 104 SLDRELENLQTDYVDFVLLHRP----DTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQLQFg 179
Cdd:cd19120 84 ALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKPAVNQIEF- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 180 lghtgmvqqeiHVNMAdaasvDHDGGLISYSRLKGMTIQAWSPFqfgffegvfidNP--KFP--ALNEAMQRVADKYGVT 255
Cdd:cd19120 163 -----------HPYLY-----PQQPALLEYCREHGIVVSAYSPL-----------SPltRDAggPLDPVLEKIAEKYGVT 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 705456322 256 KNAIAVAWIL-RHPArmqVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19120 216 PAQVLLRWALqKGIV---VVTTSSKEERMKEYLEAFDFELTEEE 256
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-292 |
4.38e-26 |
|
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: 105.17 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGV-MRLDGKGRDE-AQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQ 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGGQITDEmAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 79 TKfgIYKGDNgAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPM 158
Cdd:cd19158 81 TK--IFWGGK-AETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 159 QVeMLQSAVGQklevnqlQFGLGHTGMVQQEIHVNMADAASVDhdggLISYSRLKGMTIQAWSPFQFGFFEGVFidNPKF 238
Cdd:cd19158 158 EI-MEAYSVAR-------QFNLIPPICEQAEYHMFQREKVEVQ----LPELFHKIGVGAMTWSPLACGIVSGKY--DSGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 239 PALNEA--------------------------MQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADV 292
Cdd:cd19158 224 PPYSRAslkgyqwlkdkilseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 303
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-291 |
4.46e-26 |
|
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: 104.54 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 6 LGSSGVDASRVALGVMRLDGKGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQTKFGIYK 85
Cdd:cd19153 10 GNVSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 86 GDNgaitrYNFSKDHLIASLDRELENLQTDYVDFVLLH-----RPDTLVefDELAEAFNELQNSGRVRHFGVSNMnPMQV 160
Cdd:cd19153 90 DSE-----FDYSAERVRASVATSLERLHTTYLDVVYLHdiefvDYDTLV--DEALPALRTLKDEGVIKRIGIAGY-PLDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 161 --EMLQSAVGQKLEVnqlqfglghtgmVQQEIHVNMADAASVDhdggLISYSRLKG--MTIQAwSPFQFGFF--EGVFID 234
Cdd:cd19153 162 ltRATRRCSPGSLDA------------VLSYCHLTLQDARLES----DAPGLVRGAgpHVINA-SPLSMGLLtsQGPPPW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456322 235 NPKFPALNEAmQRVADKYGVTKNA----IAVAWIL-RHPARMQVLLGSMTPSRLKEMMAGAD 291
Cdd:cd19153 225 HPASGELRHY-AAAADAVCASVEAslpdLALQYSLaAHAGVGTVLLGPSSLAQLRSMLAAVD 285
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-291 |
5.08e-26 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 104.86 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 3 YSELGSSGVDASRVALGVMRLDGK----GRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQ 78
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSVfgpvSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 79 TKFGIYKGDngaitrYNFSKDHLIASLDRELENLQTDYVDFVLLHRpdtlVEFDELAEAFNE-------LQNSGRVRHFG 151
Cdd:PLN02587 81 TKCGRYGEG------FDFSAERVTKSVDESLARLQLDYVDILHCHD----IEFGSLDQIVNEtipalqkLKESGKVRFIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 152 VSNMnPMQV--EMLQSAVGQKLEVnqlqfglghtgmVQQEIHVNMADAASVDhdggLISYSRLKGMTIQAWSPFQFGFF- 228
Cdd:PLN02587 151 ITGL-PLAIftYVLDRVPPGTVDV------------ILSYCHYSLNDSSLED----LLPYLKSKGVGVISASPLAMGLLt 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 229 -EGVFIDNPKFPALNEAMQRVAD---KYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGAD 291
Cdd:PLN02587 214 eNGPPEWHPAPPELKSACAAAAThckEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAAT 280
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-298 |
9.60e-26 |
|
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: 103.24 E-value: 9.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLdgKGRDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKfgIYKGD 87
Cdd:cd19157 5 NNGVKMPWLGLGVFKV--EEGSEVVNAVKTALKNGYRSIDTAAIYGNEEG---VGKGIKESGIPREELFITSK--VWNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 NGaitrYnfskDHLIASLDRELENLQTDYVDFVLLHRPDTlVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAV 167
Cdd:cd19157 78 QG----Y----DSTLKAFEASLERLGLDYLDLYLIHWPVK-GKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 168 GQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPfqfgFFEGVFIDNPkfpalneAMQR 247
Cdd:cd19157 149 EIVPMVNQVEF---HPRLTQKE----------------LRDYCKKQGIQLEAWSP----LMQGQLLDNP-------VLKE 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 705456322 248 VADKYGVTKNAIAVAWILRHparmQVLL--GSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19157 199 IAEKYNKSVAQVILRWDLQN----GVVTipKSIKEHRIIENADVFDFELSQED 247
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-283 |
1.41e-25 |
|
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: 104.08 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGKGRDEAQN--IVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKVDRQSIFVQ 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAeeIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 79 TKFGIYKGDNGAitryNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPM 158
Cdd:cd19142 81 TKIYWSYGSEER----GLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 159 QV-EMLQSAvgqklevnqLQFGLGHTGMVQQEIHVNMADAASVDHdggLISYSRLkGMTIQAWSPFQFGFFEG-VFIDNP 236
Cdd:cd19142 157 EImEAFSIA---------RQFNCPTPICEQSEYHMFCREKMELYM---PELYNKV-GVGLITWSPLSLGLDPGiSEETRR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456322 237 KFPALNEA--------------------------MQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRL 283
Cdd:cd19142 224 LVTKLSFKsskykvgsdgngiheetrrashklreLSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQL 296
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-298 |
4.22e-25 |
|
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: 101.17 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 16 VALGVMRLdgKGRDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDL----KVDRQSIFVQTKFGiykgdngai 91
Cdd:cd19136 4 LGLGTFRL--RGEEEVRQAVDAALKAGYRLIDTASVYRNEAD---IGKALRDLlpkyGLSREDIFITSKLA--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 92 tRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDT--LVEFD--------ELAEAFNELQNSGRVRHFGVSNMNPMQVE 161
Cdd:cd19136 70 -PKDQGYEKARAACLGSLERLGTDYLDLYLIHWPGVqgLKPSDprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 162 MLQSAVGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPfqFGFFEGVFIDNPKFpal 241
Cdd:cd19136 149 ELLKYCEVPPAVNQVEF---HPHLVQKE----------------LLKFCKDHGIHLQAYSS--LGSGDLRLLEDPTV--- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 242 neamQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19136 205 ----LAIAKKYGRTPAQVLLRWALQQ--GIGVIPKSTNPERIAENIKVFDFELSEED 255
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
15-298 |
3.32e-24 |
|
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: 98.50 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 15 RVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQDLKVDRQSIFVQTKF-GIYKGdngaitr 93
Cdd:cd19132 9 AIGFGTYPLKG---DEGVEAVVAALQAGYRLLDTAFNY---ENEGAVGEAVRRSGVPREELFVTTKLpGRHHG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 94 ynfsKDHLIASLDRELENLQTDYVDFVLLHRP----DTLVEfdeLAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQ 169
Cdd:cd19132 76 ----YEEALRTIEESLYRLGLDYVDLYLIHWPnpsrDLYVE---AWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 170 KLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQFGffEGVfIDNPKFpalneamQRVA 249
Cdd:cd19132 149 TPAVNQIEL---HPYFPQAE----------------QRAYHREHGIVTQSWSPLGRG--SGL-LDEPVI-------KAIA 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 250 DKYGVTKNAIAVAWilrhparmQVLLG------SMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19132 200 EKHGKTPAQVVLRW--------HVQLGvvpipkSANPERQRENLAIFDFELSDED 246
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-289 |
5.76e-24 |
|
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: 99.17 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 15 RVALGVMRLDGKGR----DEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQAL---QDLKVDrqsifvqTKfgIYKGD 87
Cdd:cd19075 2 KIILGTMTFGSQGRfttaEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGlgeRGFKID-------TK--ANPGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 NGaitryNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEmlqsav 167
Cdd:cd19075 73 GG-----GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVA------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 168 gqklevnqlqfglghtgmvqqEIHvNMAD---------------AASVDHDGGLISYSRLKGMTIQAWSPFQFGFFEG-- 230
Cdd:cd19075 142 ---------------------EIV-EICKengwvlptvyqgmynAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGky 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 231 VFIDNPK--------------------FPALNEAM---QRVADKYGVTKNAIAVAWILRHPARM-----QVLLGSMTPSR 282
Cdd:cd19075 200 KYSEDKAgggrfdpnnalgklyrdrywKPSYFEALekvEEAAEKEGISLAEAALRWLYHHSALDgekgdGVILGASSLEQ 279
|
....*..
gi 705456322 283 LKEMMAG 289
Cdd:cd19075 280 LEENLAA 286
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-298 |
7.77e-24 |
|
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: 97.97 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRL-DGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKfgIYKG 86
Cdd:cd19156 4 ANGVEMPRLGLGVWRVqDG---AEAENAVKWAIEAGYRHIDTAAIYKNEEG---VGQGIRESGVPREEVFVTTK--LWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 87 DNGAitrynfskDHLIASLDRELENLQTDYVDFVLLHRPDTlVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSA 166
Cdd:cd19156 76 DQGY--------ESTLAAFEESLEKLGLDYVDLYLIHWPVK-GKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 167 VGQKLEVNQLqfglghtgmvqqEIHVNMADAAsvdhdggLISYSRLKGMTIQAWSPFQfgffEGVFIDNPKFPALneamq 246
Cdd:cd19156 147 CKVAPMVNQI------------ELHPLLTQEP-------LRKFCKEKNIAVEAWSPLG----QGKLLSNPVLKAI----- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 705456322 247 rvADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19156 199 --GKKYGKSAAQVIIRWDIQH--GIITIPKSVHEERIQENFDVFDFELTAEE 246
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
16-285 |
4.83e-23 |
|
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: 96.20 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 16 VALGVMRLdgKGRDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDL----KVDRQSIFVQTKFGIYKgdngai 91
Cdd:cd19116 14 IALGTWKL--KDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAE---VGEAIREKiaegVVKREDLFITTKLWNSY------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 92 trynFSKDHLIASLDRELENLQTDYVDFVLLHRP--------------DTLVEFD--ELAEAFNELQNSGRVRHFGVSNM 155
Cdd:cd19116 83 ----HEREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesngdGSLSDIDylETWRGMEDLVKLGLTRSIGVSNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 156 NPMQVEMLQSAVGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPfqFGFFEGVFIDN 235
Cdd:cd19116 159 NSEQINRLLSNCNIKPAVNQIEV---HPTLTQEK----------------LVAYCQSNGIVVMAYSP--FGRLVPRGQTN 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 705456322 236 PKFPALNEAMQRVADKYGVTKNAIAVawilrhpaRMQVLLG------SMTPSRLKE 285
Cdd:cd19116 218 PPPRLDDPTLVAIAKKYGKTTAQIVL--------RYLIDRGvvpipkSSNKKRIKE 265
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
5-265 |
1.59e-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: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 5 ELGSSGVDASRVALGVMRLDG-----KGRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvdRQSIFVQT 79
Cdd:cd19145 4 KLGSQGLEVSAQGLGCMGLSGdygapKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGP--REKVQLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 80 KFGIYKGDnGAITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQ 159
Cdd:cd19145 82 KFGIHEIG-GSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 160 VEMLQsAVGQKLEVnQLQFGLgHTGMVQQEIhvnmadaasvdhdgglISYSRLKGMTIQAWSPFQFGFFEG--VFIDN-- 235
Cdd:cd19145 161 IRRAH-AVHPITAV-QLEWSL-WTRDIEEEI----------------IPTCRELGIGIVPYSPLGRGFFAGkaKLEELle 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 705456322 236 --------PKFPALN--------EAMQRVADKYGVTKNAIAVAWIL 265
Cdd:cd19145 222 nsdvrkshPRFQGENleknkvlyERVEALAKKKGCTPAQLALAWVL 267
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
18-265 |
2.52e-22 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 93.93 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 18 LGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYsDGESSrrLGQALQDLKVDRQSIFVQTKfgiykgdngaITRYNFS 97
Cdd:PRK11172 8 LGTFRLKD---QVVIDSVKTALELGYRAIDTAQIY-DNEAA--VGQAIAESGVPRDELFITTK----------IWIDNLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 98 KDHLIASLDRELENLQTDYVDFVLLH--RPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNpmqVEMLQSAVGqklevnq 175
Cdd:PRK11172 72 KDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFT---IALMKQAIA------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 176 lQFGLGHTGMVQQEIHVNMADAASVDhdgglisYSRLKGMTIQAWSPFQFGffeGVFIDnpkfpalnEAMQRVADKYGVT 255
Cdd:PRK11172 142 -AVGAENIATNQIELSPYLQNRKVVA-------FAKEHGIHVTSYMTLAYG---KVLKD--------PVIARIAAKHNAT 202
|
250
....*....|
gi 705456322 256 KNAIAVAWIL 265
Cdd:PRK11172 203 PAQVILAWAM 212
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-298 |
3.41e-22 |
|
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: 93.63 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDgesSRRLGQALQDLKVDRQSIFVQTKFGIYkgd 87
Cdd:cd19127 4 NNGVEMPALGLGVFQTPP---EETADAVATALADGYRLIDTAAAYGN---EREVGEGIRRSGVDRSDIFVTTKLWIS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 ngaitryNFSKDHLIASLDRELENLQTDYVDFVLLHRPdTLVEFDELAEAFNELQN---SGRVRHFGVSNMNPMQVEMLQ 164
Cdd:cd19127 75 -------DYGYDKALRGFDASLRRLGLDYVDLYLLHWP-VPNDFDRTIQAYKALEKllaEGRVRAIGVSNFTPEHLERLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 165 SAVGQKLEVNQLqfglghtgmvqqEIHVNMADAAsvdhdggLISYSRLKGMTIQAWSPfqFG---FFEGVFIDNPKFPAL 241
Cdd:cd19127 147 DATTVVPAVNQV------------ELHPYFSQKD-------LRAFHRRLGIVTQAWSP--IGgvmRYGASGPTGPGDVLQ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 242 NEAMQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19127 206 DPTITGLAEKYGKTPAQIVLRWHLQN--GVSAIPKSVHPERIAENIDIFDFALSAED 260
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-285 |
1.16e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 91.82 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 27 GRDEAQNIVRTALDGGVNFFDTADCYsdGESSRRLGQALQDLKvdrqSIFVQTKFGIYKGDNGAItrynfsKDHLIASLD 106
Cdd:cd19097 24 SEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLD----KFKIITKLPPLKEDKKED------EAAIEASVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 107 RELENLQTDYVDFVLLHRPDTL-VEFDELAEAFNELQNSGRVRHFGVSNMNPmqvEMLQSAVG-QKLEVNQLQFGLghtg 184
Cdd:cd19097 92 ASLKRLKVDSLDGLLLHNPDDLlKHGGKLVEALLELKKEGLIRKIGVSVYSP---EELEKALEsFKIDIIQLPFNI---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 185 mvqqeihvnmadaasVDH---DGGLISYSRLKGMTIQAWSPfqfgFFEGVFIDNP-----KFPALN---EAMQRVADKYG 253
Cdd:cd19097 165 ---------------LDQrflKSGLLAKLKKKGIEIHARSV----FLQGLLLMEPdklpaKFAPAKpllKKLHELAKKLG 225
|
250 260 270
....*....|....*....|....*....|..
gi 705456322 254 VTKNAIAVAWILRHPARMQVLLGSMTPSRLKE 285
Cdd:cd19097 226 LSPLELALGFVLSLPEIDKIVVGVDSLEQLKE 257
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-263 |
2.96e-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: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 27 GRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvdRQSIFVQTKFGIYKGDNGAitrynfskDHLIASLD 106
Cdd:cd19103 30 DEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYP--REDYIISTKFTPQIAGQSA--------DPVADMLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 107 RELENLQTDYVDFVLLHRPDTlVE--FDELAeafnELQNSGRVRHFGVSNMNPMQVEMLQ---SAVGQKLEVNQLQFGLG 181
Cdd:cd19103 100 GSLARLGTDYIDIYWIHNPAD-VErwTPELI----PLLKSGKVKHVGVSNHNLAEIKRANeilAKAGVSLSAVQNHYSLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 182 HTGmvqqeihvnmadaasvDHDGGLISYSRLKGMTIQAWSPFQFGFFEGVFID--------------NPKFP---ALNEA 244
Cdd:cd19103 175 YRS----------------SEEAGILDYCKENGITFFAYMVLEQGALSGKYDTkhplpegsgraetyNPLLPqleELTAV 238
|
250
....*....|....*....
gi 705456322 245 MQRVADKYGVTKNAIAVAW 263
Cdd:cd19103 239 MAEIGAKHGASIAQVAIAW 257
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
34-173 |
4.67e-21 |
|
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: 90.80 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 34 IVRTALDGGVNFFDTADCYsdGESSRRLGQALQDL--KVDRQSIFVQTKFGIYKGDNgaitrYNFSKDHLIASLDRELEN 111
Cdd:cd19164 39 IVRRALELGIRAFDTSPYY--GPSEIILGRALKALrdEFPRDTYFIITKVGRYGPDD-----FDYSPEWIRASVERSLRR 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456322 112 LQTDYVDFVLLHrpDtlVEF---DELAEA---FNELQNSGRVRHFGVSNMnPMQV-----EMLQSAVGQKLEV 173
Cdd:cd19164 112 LHTDYLDLVYLH--D--VEFvadEEVLEAlkeLFKLKDEGKIRNVGISGY-PLPVllrlaELARTTAGRPLDA 179
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
29-298 |
6.30e-21 |
|
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: 90.16 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 29 DEAQNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQDLK-----VDRQSIFVQTKFgiykgdngaitrYNFS--KDHL 101
Cdd:cd19118 20 GEVGAAVKIALKAGYRHLDLAKVY---QNQHEVGQALKELLkeepgVKREDLFITSKL------------WNNShrPEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 102 IASLDRELENLQTDYVDFVLLHRP------------------------DTLVEFDELAEAFNELQNSGRVRHFGVSNMNP 157
Cdd:cd19118 85 EPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltavptnggevdlDLSVSLVDTWKAMVELKKTGKVKSIGVSNFSI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 158 MQVEMLQSAVGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPF---QFGffEGVFID 234
Cdd:cd19118 165 DHLQAIIEETGVVPAVNQIEA---HPLLLQDE----------------LVDYCKSKNIHITAYSPLgnnLAG--LPLLVQ 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456322 235 NPkfpalneAMQRVADKYGVTKNAIAVAWILRhpARMQVLLGSMTPSRLKEMMagADVEISAQE 298
Cdd:cd19118 224 HP-------EVKAIAAKLGKTPAQVLIAWGIQ--RGHSVIPKSVTPSRIRSNF--EQVELSDDE 276
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-298 |
1.36e-20 |
|
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: 89.77 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 2 KYSELGSSGVDASRVALGVMRLDGkGRDEAQN---IVRTALDGGVNFFDTADCYSD--GESSRRLGQAL-QDLKVDRQSI 75
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFG-DVDRYENsraMLRRAFDLGITHFDLANNYGPppGSAEENFGRILkEDLKPYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 76 FVQTKFGIYK-----GDNGaitrynfSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHF 150
Cdd:cd19151 80 IISTKAGYTMwpgpyGDWG-------SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 151 GVSNMNPMQVE----MLQSaVGQKLEVNQLQFglghtGMVQQEIhvnmadaasvdhDGGLISYSRLKGMTIQAWSPFQFG 226
Cdd:cd19151 153 GISNYPPEEAReaaaILKD-LGTPCLIHQPKY-----SMFNRWV------------EEGLLDVLEEEGIGCIAFSPLAQG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 227 -----FFEGVFIDN-------------------PKFPALNEamqrVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSR 282
Cdd:cd19151 215 lltdrYLNGIPEDSraakgssflkpeqiteeklAKVRRLNE----IAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQ 290
|
330
....*....|....*..
gi 705456322 283 LKEMMAGAD-VEISAQE 298
Cdd:cd19151 291 IEDAVGALDnREFSEEE 307
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
30-298 |
1.38e-20 |
|
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: 88.81 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 30 EAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKFGiykgdngaitRYNFSKDHLIASLDREL 109
Cdd:cd19130 24 DTQRAVATALEVGYRHIDTAAIYGNEEG---VGAAIAASGIPRDELFVTTKLW----------NDRHDGDEPAAAFAESL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 110 ENLQTDYVDFVLLHRP-DTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQLqfglghtgmvqq 188
Cdd:cd19130 91 AKLGLDQVDLYLVHWPtPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQI------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 189 EIHVNMADAASVDhdgglisYSRLKGMTIQAWSPFQfgffEGVFIDNPkfpalneAMQRVADKYGVTKNAIAVAWILRHP 268
Cdd:cd19130 159 ELHPAYQQRTIRD-------WAQAHDVKIEAWSPLG----QGKLLGDP-------PVGAIAAAHGKTPAQIVLRWHLQKG 220
|
250 260 270
....*....|....*....|....*....|
gi 705456322 269 arMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19130 221 --HVVFPKSVRRERMEDNLDVFDFDLTDTE 248
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
28-302 |
3.07e-20 |
|
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: 88.92 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 28 RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvDRQSIFVQTKFG-IYKGDNGAITR------------- 93
Cdd:cd19161 19 NADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK--PRDEFVLSTKVGrLLKPAREGSVPdpngfvdplpfei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 94 -YNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELA------------EAFNELQNSGRVRHFGvsnmnpmqv 160
Cdd:cd19161 97 vYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKErhhfaqlmsggfKALEELKKAGVIKAFG--------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 161 emlqsavgqkLEVNQLQfglghtgmvqqeIHVNMADAAsvDHDGGLI--SYSRL--------------KGMTIQAWSPFQ 224
Cdd:cd19161 168 ----------LGVNEVQ------------ICLEALDEA--DLDCFLLagRYSLLdqsaeeeflprceqRGTSLVIGGVFN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 225 FGFFEGVFIDNPKF---PALNE------AMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEIS 295
Cdd:cd19161 224 SGILATGTKSGAKFnygDAPAEiisrvmEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIP 303
|
....*..
gi 705456322 296 AQEWYDL 302
Cdd:cd19161 304 EELWQAL 310
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
29-284 |
3.81e-20 |
|
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: 88.32 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 29 DEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKFgiykgdngaitrYNFSKDHLIASLDRE 108
Cdd:cd19117 27 NEVAKAVEAALKAGYRHIDTAAIYGNEEE---VGQGIKDSGVPREEIFITTKL------------WCTWHRRVEEALDQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 109 LENLQTDYVDFVLLHRPDTLV---------------------EFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAV 167
Cdd:cd19117 92 LKKLGLDYVDLYLMHWPVPLDpdgndflfkkddgtkdhepdwDFIKTWELMQKLPATGKVKAIGVSNFSIKNLEKLLASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 168 GQKL--EVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFqfgffegvfiDNPKFPALNE-A 244
Cdd:cd19117 172 SAKIvpAVNQIEL---HPLLPQPK----------------LVDFCKSKGIHATAYSPL----------GSTNAPLLKEpV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 705456322 245 MQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLK 284
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQR--GYSVLPKSVTPSRIE 260
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-298 |
1.03e-19 |
|
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: 87.29 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 9 SGVDASRVALGVMRLDGKG----RDEAQNIVRTALDGGVNFFDTADCY--SDGESSRRL-GQALQDLKVDRQSIFVQTKF 81
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPnptpDEEAFETMKAALDAGSNLWNGGEFYgpPDPHANLKLlARFFRKYPEYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 82 GIykgdNGAITRYNFSKDHLIASLDRELENL-QTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNMNpmqV 160
Cdd:cd19077 81 GL----DPDTLRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVS---A 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 161 EMLQ--SAVGqKLEVNQLQFGLGHTgmvqqEIHVNmadaasvdhdgGLISYSRLKGMTIQAWSPFQFGFFEGVF------ 232
Cdd:cd19077 154 ETIRraHAVH-PIAAVEVEYSLFSR-----EIEEN-----------GVLETCAELGIPIIAYSPLGRGLLTGRIksladi 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 233 ------IDNPKFP--------ALNEAMQRVADKYGVTKNAIAVAWILR-HPARMQVLLGSMTPSRLKEMMAGADVEISAQ 297
Cdd:cd19077 217 pegdfrRHLDRFNgenfeknlKLVDALQELAEKKGCTPAQLALAWILAqSGPKIIPIPGSTTLERVEENLKAANVELTDE 296
|
.
gi 705456322 298 E 298
Cdd:cd19077 297 E 297
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
29-302 |
4.40e-19 |
|
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: 85.74 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 29 DEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvDRQSIFVQTKFG---------------IYKGDNGAITR 93
Cdd:cd19152 20 EEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALREL--GREDYVISTKVGrllvplqeveptfepGFWNPLPFDAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 94 YNFSKDHLIASLDRELENLQTDYVDFVLLHRPDT-------LVEFDELAE----AFNELQNSGRVRHFGVSnMNpmQVEM 162
Cdd:cd19152 98 FDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEdlagaesDEHFAQAIKgafrALEELREEGVIKAIGLG-VN--DWEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 163 LQSAvgqkLEVNQLQFGLghtgmvqqeihvnMADAASV-DHDGglisYSRL------KGMTIQAWSPFQFGF-----FEG 230
Cdd:cd19152 175 ILRI----LEEADLDWVM-------------LAGRYTLlDHSA----ARELlpecekRGVKVVNAGPFNSGFlaggdNFD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 231 VFIDNPKFPAL---NEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19152 234 YYEYGPAPPELiarRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAAFWEEL 308
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-298 |
1.76e-18 |
|
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: 84.00 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDL----KVDRQSIFVQTKFGI 83
Cdd:cd19154 7 SNGVKMPLIGLGTWQSKG---AEGITAVRTALKAGYRLIDTAFLYQNEEA---IGEALAELleegVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 84 YKGDNGAITRynfskdhliaSLDRELENLQTDYVDFVLLHRP-------------------DTLVEFDELAEAFNELQNS 144
Cdd:cd19154 81 HEHAPEDVEE----------ALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 145 GRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQLQFglgHTGMVQQEIHVNMAdaasvDHDGGLISYSRLKgmtiqawSPFQ 224
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQRILDNARVKPHNNQVEC---HLYFPQKELVEFCK-----KHNISVTSYATLG-------SPGR 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456322 225 FGFFEGVFIDNPKFPALNEAMQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19154 216 ANFTKSTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYLLQR--GIAVIPKSATPSRIKENFNIFDFSLSEED 287
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
15-297 |
4.55e-18 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 82.32 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 15 RVALGVMRLDGKG-------RDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLkvdRQSIFVQTKFGIYKGD 87
Cdd:PRK10376 19 RLGYGAMQLAGPGvfgppkdRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPY---PDDLTIVTKVGARRGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 NGAitrYN--FSKDHLIASLDRELENLQTDYVDFVLL------HRPDTlvefDELAEAFN---ELQNSGRVRHFGVSNMN 156
Cdd:PRK10376 96 DGS---WLpaFSPAELRRAVHDNLRNLGLDVLDVVNLrlmgdgHGPAE----GSIEEPLTvlaELQRQGLVRHIGLSNVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 157 PMQVemlqsAVGQKLevnqlqfglghTGMVQQEIHVNMADAasvdHDGGLISYSRLKGMtiqAWSPFqfgFFEGVFIdnp 236
Cdd:PRK10376 169 PTQV-----AEARKI-----------AEIVCVQNHYNLAHR----ADDALIDALARDGI---AYVPF---FPLGGFT--- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456322 237 kfPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQ 297
Cdd:PRK10376 220 --PLQSSTLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEE 278
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-307 |
8.55e-18 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 82.34 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDG--KGRDEAQNIVRTALDGGVNFFDTADCYSD--GESSRRLGQALQ-DLKVDRQSI 75
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGhvNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLReDFAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 76 FVQTKFG--IYKGDNGAitryNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVS 153
Cdd:PRK09912 93 IISTKAGydMWPGPYGS----GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 154 NMNPMQVEMLQSAVGQ---KLEVNQLQFGLGHTGMVQQeihvnmadaasvdhdgGLISYSRLKGMTIQAWSPFQFGFFEG 230
Cdd:PRK09912 169 SYSPERTQKMVELLREwkiPLLIHQPSYNLLNRWVDKS----------------GLLDTLQNNGVGCIAFTPLAQGLLTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 231 VFI-----------DNPKFPALNEAM------------QRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKE-M 286
Cdd:PRK09912 233 KYLngipqdsrmhrEGNKVRGLTPKMlteanlnslrllNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEEnV 312
|
330 340
....*....|....*....|...
gi 705456322 287 MAGADVEISAQEW--YDLYVAAG 307
Cdd:PRK09912 313 QALNNLTFSTEELaqIDQHIADG 335
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
16-299 |
1.90e-17 |
|
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: 80.85 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 16 VALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCY-SDGESSRRLGQALQDLKVDRQSIFVQTKFgiykgdngaitry 94
Cdd:cd19125 14 VGLGTWQADP---GVVGNAVKTAIKEGYRHIDCAAIYgNEKEIGKALKKLFEDGVVKREDLFITSKL------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 95 nFSKDHLIA----SLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQN--------------SGRVRHFGVSNMN 156
Cdd:cd19125 78 -WCTDHAPEdvppALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEEVLPPdipstwkameklvdSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 157 PMQVEMLQSAVGQKLEVNQLQFglgHTGMVQQEIHvnmadaasvdhdggliSYSRLKGMTIQAWSPFQFGFFEGVFIDNP 236
Cdd:cd19125 157 VKKLEDLLAVARVPPAVNQVEC---HPGWQQDKLH----------------EFCKSKGIHLSAYSPLGSPGTTWVKKNVL 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 237 KFPALNEamqrVADKYGVTKNAIAVAWILR--HparmQVLLGSMTPSRLKEMMAGADVEISAQEW 299
Cdd:cd19125 218 KDPIVTK----VAEKLGKTPAQVALRWGLQrgT----SVLPKSTNEERIKENIDVFDWSIPEEDF 274
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
30-298 |
3.54e-17 |
|
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: 80.15 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 30 EAQNIVRTALDGGVNFFDTADCYsDGESsrRLGQALQDL----KVDRQSIFVQTKFgiykgdngaitrYNFS--KDHLIA 103
Cdd:cd19123 26 EVGQAVKQALEAGYRHIDCAAIY-GNEA--EIGAALAEVfkegKVKREDLWITSKL------------WNNShaPEDVLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 104 SLDRELENLQTDYVDFVLLHRPDTL---VEFDELAE---------------AFNELQNSGRVRHFGVSNMNPMQVEMLQS 165
Cdd:cd19123 91 ALEKTLADLQLDYLDLYLMHWPVALkkgVGFPESGEdllslspipledtwrAMEELVDKGLCRHIGVSNFSVKKLEDLLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 166 AVGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQFG--------FFEGVFIDNPk 237
Cdd:cd19123 171 TARIKPAVNQVEL---HPYLQQPE----------------LLAFCRDNGIHLTAYSPLGSGdrpaamkaEGEPVLLEDP- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456322 238 fpalneAMQRVADKYGVTKNAIAVAW-ILRHPArmqVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19123 231 ------VINKIAEKHGASPAQVLIAWaIQRGTV---VIPKSVNPERIQQNLEAAEVELDASD 283
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
8-302 |
4.04e-17 |
|
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: 80.16 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDGK--------GRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQdLKVDRQSIFVQT 79
Cdd:cd19146 6 TAGVRVSPLCLGAMSFGEAwksmmgecDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMA-SRGNRDEMVLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 80 KFGI-YKGDNGAITRYNFSKDH---LIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSNM 155
Cdd:cd19146 85 KYTTgYRRGGPIKIKSNYQGNHaksLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 156 NPMQVemlqsavgqkleVNQLQFGLGHtGMVQQEIHVNMADAASVDHDGGLISYSRLKGMTIQAWSPFQFGFF------- 228
Cdd:cd19146 165 PAWVV------------SKANAYARAH-GLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFrteeefk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 229 --EGVFID----NPKFPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19146 232 rrGRSGRKggpqTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEI 311
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-276 |
1.66e-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: 78.41 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 14 SRVALGVMRLDGK-----GRDEAQNIVRTALDGGVNFFDTADCYSDGESSrrLGQALQDLKVDRQS---IFVQTKFGIYK 85
Cdd:cd19101 3 SRVINGMWQLSGGhggirDEDAAVRAMAAYVDAGLTTFDCADIYGPAEEL--IGEFRKRLRRERDAaddVQIHTKWVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 86 GDNGAitrynfSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVE-FDELAEAFNELQNSGRVRHFGVSNMNpmqVEMLQ 164
Cdd:cd19101 81 GELTM------TRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFD---TERLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 165 SAV--GQKLEVNQLQFGLghtgmVQQEIHVNMADAAsVDHDGGLISYSRLKGmtiqawspfqfGFFEGVFIDNPK----- 237
Cdd:cd19101 152 EILdaGVPIVSNQVQYSL-----LDRRPENGMAALC-EDHGIKLLAYGTLAG-----------GLLSEKYLGVPEptgpa 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 238 ---------------------FPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLG 276
Cdd:cd19101 215 letrslqkyklmidewggwdlFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVG 274
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-295 |
6.99e-16 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 76.82 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELGSSGVDASRVALGVMRLDGKGRD-EAQNIVRTALDGGVNFFDTADCY-------SDGESSRRLGQALQDlKVDR 72
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEaDAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAK-RGSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 73 QSIFVQTKF-GIYKGDNGAItRYNFSKD--HLIASLDRELENLQTDYVDFVLLHRPD-----------------TLVEFD 132
Cdd:PRK10625 80 EKLIIASKVsGPSRNNDKGI-RPNQALDrkNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPAVSLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 133 ELAEAFNELQNSGRVRHFGVSNMNPMQVeMLQSAVGQKLEVNQLqfglghtgmvqqeihVNMADAASV---DHDGGLISY 209
Cdd:PRK10625 159 ETLDALAEQQRAGKIRYIGVSNETAFGV-MRYLHLAEKHDLPRI---------------VTIQNPYSLlnrSFEVGLAEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 210 SRLKGMTIQAWSPFQFGFFEGVFIDNPKfP--ALNEAMQR------------------VADKYGVTKNAIAVAWILRHPA 269
Cdd:PRK10625 223 SQYEGVELLAYSCLAFGTLTGKYLNGAK-PagARNTLFSRftrysgeqtqkavaayvdIAKRHGLDPAQMALAFVRRQPF 301
|
330 340
....*....|....*....|....*.
gi 705456322 270 RMQVLLGSMTPSRLKEMMAGADVEIS 295
Cdd:PRK10625 302 VASTLLGATTMEQLKTNIESLHLTLS 327
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
16-298 |
2.03e-15 |
|
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: 74.51 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 16 VALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLKVDRQSIFVQTKfgIYKGDNGaitrYN 95
Cdd:cd19134 14 IGLGVGELSD---DEAERSVSAALEAGYRLIDTAAAYGNEAA---VGRAIAASGIPRGELFVTTK--LATPDQG----FT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 96 FSKDHLIASLDRelenLQTDYVDFVLLHRPdtLVEFDELAEAFN---ELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLE 172
Cdd:cd19134 82 ASQAACRASLER----LGLDYVDLYLIHWP--AGREGKYVDSWGglmKLREEGLARSIGVSNFTAEHLENLIDLTFFTPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 173 VNQLQFglgHTGMVQQEIHvnmadAASVDHdgglisysrlkGMTIQAWSPFQFgffeGVFIDNPkfpalneAMQRVADKY 252
Cdd:cd19134 156 VNQIEL---HPLLNQAELR-----KVNAQH-----------GIVTQAYSPLGV----GRLLDNP-------AVTAIAAAH 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 705456322 253 GVTKNAIAVAWILRHParMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19134 206 GRTPAQVLLRWSLQLG--NVVISRSSNPERIASNLDVFDFELTADH 249
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
30-298 |
4.04e-15 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 74.34 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 30 EAQNIVRTALDGGVNFFDTADCYSDgesSRRLGQALQ-----DLKVDRQSIFVQTKFgiykgdngaitrYNfSKDH---L 101
Cdd:cd19106 21 QVKAAVKYALDAGYRHIDCAAVYGN---EQEVGEALKekvgpGKAVPREDLFVTSKL------------WN-TKHHpedV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 102 IASLDRELENLQTDYVDFVLLHRP--------------DTLVEFD-----ELAEAFNELQNSGRVRHFGVSNMNPMQVEM 162
Cdd:cd19106 85 EPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpknpDGTIRYDsthykETWKAMEKLVDKGLVKAIGLSNFNSRQIDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 163 LQSAVGQKLEVNQLQfglGHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPF--------QFGffEGVFID 234
Cdd:cd19106 165 ILSVARIKPAVLQVE---CHPYLAQNE----------------LIAHCKARGLVVTAYSPLgspdrpwaKPD--EPVLLE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456322 235 NPKFPALneamqrvADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19106 224 EPKVKAL-------AKKYNKSPAQILLRWQVQR--GVVVIPKSVTPSRIKQNIQVFDFTLSPEE 278
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
2-298 |
5.04e-15 |
|
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: 74.03 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 2 KYSELGSSGVDASRVALGVMRLDGKGR--DEAQNIVRTALDGGVNFFDTADCYSD--GESSRRLGQAL-QDLKVDRQSIF 76
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTplETQRAILRTAFDLGITHFDLANNYGPppGSAEENFGRILrEDFAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 77 VQTKFG--IYKGDNGAITrynfSKDHLIASLDRELENLQTDYVDFVLLHR--PDTLVEfdELAEAFNELQNSGRVRHFGV 152
Cdd:cd19150 81 ISTKAGydMWPGPYGEWG----SRKYLLASLDQSLKRMGLDYVDIFYSHRfdPDTPLE--ETMGALDHAVRSGKALYVGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 153 SNMNPMQVEmlqsavgqklEVNQLQFGLGHTGMVQQEIHvNMADAAsVDHDGGLISYSRLkGMTIQAWSPFQFGFFEGVF 232
Cdd:cd19150 155 SSYSPERTR----------EAAAILRELGTPLLIHQPSY-NMLNRW-VEESGLLDTLQEL-GVGCIAFTPLAQGLLTDKY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 233 ID--------------NPKFpaLNE-------AMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGAD 291
Cdd:cd19150 222 LNgipegsraskerslSPKM--LTEanlnsirALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALD 299
|
....*...
gi 705456322 292 -VEISAQE 298
Cdd:cd19150 300 nLTFSADE 307
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-298 |
4.08e-14 |
|
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: 70.82 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDGkgrdEAQNIVRTAL-DGGVNFFDTADCYSDGEssrRLGQALQDLKVDRQSIFVQTKfgIYKG 86
Cdd:cd19135 8 SNGVEMPILGLGTSHSGG----YSHEAVVYALkECGYRHIDTAKRYGCEE---LLGKAIKESGVPREDLFLTTK--LWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 87 DNGaitrYNFSKDHLIASLDRelenLQTDYVDFVLLHRPDTLVEFDELAE-------AFNELQNSGRVRHFGVSNMNPMQ 159
Cdd:cd19135 79 DYG----YESTKQAFEASLKR----LGVDYLDLYLLHWPDCPSSGKNVKEtraetwrALEELYDEGLCRAIGVSNFLIEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 160 VEMLQSAVGQKLEVNQLQFglghtgmvqqeiHVnmadaasVDHDGGLISYSRLKGMTIQAWSPFQfgffegvfidnpKFP 239
Cdd:cd19135 151 LEQLLEDCSVVPHVNQVEF------------HP-------FQNPVELIEYCRDNNIVFEGYCPLA------------KGK 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 240 ALNE-AMQRVADKYGVTKNAIAVAWILRHPArmQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19135 200 ALEEpTVTELAKKYQKTPAQILIRWSIQNGV--VTIPKSTKEERIKENCQVFDFSLSEED 257
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
35-298 |
8.22e-14 |
|
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: 70.52 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 35 VRTALDGGVNFFDTADCY-SDGESSRRLGQALQDLKVDRQSIFVQTKFgiykgdngaitrYN--FSKDHLIASLDRELEN 111
Cdd:cd19107 23 VKVAIDAGYRHIDCAYVYqNENEVGEAIQEKIKEQVVKREDLFIVSKL------------WCtfHEKGLVKGACQKTLSD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 112 LQTDYVDFVLLHRP------DTLVEFDELA-------------EAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLE 172
Cdd:cd19107 91 LKLDYLDLYLIHWPtgfkpgKELFPLDESGnvipsdttfldtwEAMEELVDEGLVKAIGVSNFNHLQIERILNKPGLKYK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 173 --VNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPfqFGFFEGVFIdNPKFPALNE--AMQRV 248
Cdd:cd19107 171 paVNQIEC---HPYLTQEK----------------LIQYCQSKGIVVTAYSP--LGSPDRPWA-KPEDPSLLEdpKIKEI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 705456322 249 ADKYGVTknaIAVAWILRHPAR-MQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19107 229 AAKHNKT---TAQVLIRFPIQRnLVVIPKSVTPERIAENFKVFDFELSSED 276
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
8-154 |
8.46e-14 |
|
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: 70.62 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDGK--------GRDEAQNIVRTALDGGVNFFDTADCYSDGESSRRLGQALQDLKvDRQSIFVQT 79
Cdd:cd19147 5 TAGIRVSPLILGAMSIGDAwsgfmgsmDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 80 KFGI-YK-GDNGAITRYNFSKDH---LIASLDRELENLQTDYVDFVLLHRPDTLVEFDELAEAFNELQNSGRVRHFGVSN 154
Cdd:cd19147 84 KFTTdYKaYEVGKGKAVNYCGNHkrsLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSD 163
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
16-308 |
1.80e-13 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 69.51 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 16 VALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCY-SDGESSRRLGQALQDLKVDRQSIFVQTKFGiykgdngaitrY 94
Cdd:cd19114 7 VGFGTAKIKA---NETEEVIYNAIKVGYRLIDGALLYgNEAEVGRGIRKAIQEGLVKREDLFIVTKLW-----------N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 95 NF-SKDHLIASLDRELENLQTDYVDFVLLHRPDTL--------------------VEFDE--LAEAFNELQ---NSGRVR 148
Cdd:cd19114 73 NFhGKDHVREAFDRQLKDYGLDYIDLYLIHFPIPAayvdpaenypflwkdkelkkFPLEQspMQECWREMEklvDAGLVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 149 HFGVSNMNpmqVEMLqsavgqkleVNQLQFGLGHTGMVQQEIHVNMADAAsvdhdggLISYSRLKGMTIQAWSPFQFGFF 228
Cdd:cd19114 153 NIGIANFN---VQLI---------LDLLTYAKIKPAVLQIEHHPYLQQKR-------LIDWAKKQGIQITAYSSFGNAVY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 229 EGVFIDNPKFPAL--NEAMQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQEWYDLYVAA 306
Cdd:cd19114 214 TKVTKHLKHFTNLleHPVVKKLADKHKRDTGQVLLRWAVQR--NITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELE 291
|
..
gi 705456322 307 GN 308
Cdd:cd19114 292 AN 293
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-298 |
2.54e-13 |
|
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: 68.70 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 15 RVALGVMRLDgkgRDEAQNIVRTALDGGVNFFDTADCYSDGES-SRRLGQALQDLKVDRQSIFVQTKfgiykgdngaITR 93
Cdd:cd19128 3 RLGFGTYKIT---ESESKEAVKNAIKAGYRHIDCAYYYGNEAFiGIAFSEIFKDGGVKREDLFITSK----------LWP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 94 YNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTLVEFDELA-------------------EAFNELQNSGRVRHFGVSN 154
Cdd:cd19128 70 TMHQPENVKEQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDprddnqiqslskkpledtwRAMEQCVDEKLTKNIGVSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 155 MNPMQVEMLQSAVGQKLEVNQLQFGLGHtgmvQQEihvnmadaasvdhdgGLISYSRLKGMTIQAWSPFQfgffeGVFID 234
Cdd:cd19128 150 YSTKLLTDLLNYCKIKPFMNQIECHPYF----QND---------------KLIKFCIENNIHVTAYRPLG-----GSYGD 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456322 235 NPKFPALNEAMQRVADKYGVTKNAIAVAWIL-RHPARMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19128 206 GNLTFLNDSELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNFDINDLALTKED 270
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
28-284 |
2.71e-13 |
|
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: 69.06 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 28 RDEAQNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQDL----KVDRQSIFVQTKfgIYKgdngaiTRYnfskDHLIA 103
Cdd:cd19119 26 RAEVKEAVEAAIKEGYRHIDTAYAY---ETEDFVGEAIKRAiddgSIKREELFITTK--VWP------TFY----DEVER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 104 SLDRELENLQTDYVDFVLLHRPDTLV-EFDELAEAF------------------------NELQNSGRVRHFGVSNMNPM 158
Cdd:cd19119 91 SLDESLKALGLDYVDLLLVHWPVCFEkDSDDSGKPFtpvnddgktryaasgdhittykqlEKIYLDGRAKAIGVSNYSIV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 159 QVEMLQSAVGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQFGffegvfidnpKF 238
Cdd:cd19119 171 YLERLIKECKVVPAVNQVEL---HPHLPQMD----------------LRDFCFKHGILVTAYSPLGSH----------GA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 705456322 239 PAL-NEAMQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLK 284
Cdd:cd19119 222 PNLkNPLVKKIAEKYNVSTGDILISYHVRQ--GVIVLPKSLKPVRIV 266
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
32-285 |
4.24e-13 |
|
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: 68.25 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 32 QNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQDL----KVDRQSIFVQTKfgiykgdngaITRYNFSKDHLIASLDR 107
Cdd:cd19129 22 RNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagKIRREDLFVTTK----------LWNTNHRPERVKPAFEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 108 ELENLQTDYVDFVLLHRP--------------------DTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAV 167
Cdd:cd19129 89 SLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 168 GQKLEVNQLQfglGHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQFGFFEGVFIDnpkfPALNEAMQR 247
Cdd:cd19129 169 RIKPAVVQVE---SHPYLPEWE----------------LLDFCKNHGIVLQAFAPLGHGMEPKLLED----PVITAIARR 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 705456322 248 VadkyGVTKNAIAVAW-ILRHPArmqVLLGSMTPSRLKE 285
Cdd:cd19129 226 V----NKTPAQVLLAWaIQRGTA---LLTTSKTPSRIRE 257
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-298 |
4.29e-13 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 68.67 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDgkgRDEAQNIVRTALDGGVNFFDTADCY-SDGESSRRLGQALQDLKVDRQSIFVQTKfgIYKG 86
Cdd:cd19112 6 NSGHKMPVIGLGVWRME---PGEIKELILNAIKIGYRHFDCAADYkNEKEVGEALAEAFKTGLVKREDLFITTK--LWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 87 DNGaitrynfskdHLIASLDRELENLQTDYVDFVLLHRP-----------------------DTLVEFDELAEAFNELQN 143
Cdd:cd19112 81 DHG----------HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 144 SGRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQLqfglghtgmvqqEIHvnmadaASVDHDgGLISYSRLKGMTIQAWSPF 223
Cdd:cd19112 151 AGLVRSIGISNYDIFLTRDCLAYSKIKPAVNQI------------ETH------PYFQRD-SLVKFCQKHGISVTAHTPL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 224 --------QFGFFEGvfIDNPkfpalneAMQRVADKYGVTKNAIAVAW-ILRHPArmqVLLGSMTPSRLKEMMAGADVEI 294
Cdd:cd19112 212 ggaaanaeWFGSVSP--LDDP-------VLKDLAKKYGKSAAQIVLRWgIQRNTA---VIPKSSKPERLKENIDVFDFQL 279
|
....
gi 705456322 295 SAQE 298
Cdd:cd19112 280 SKED 283
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
30-302 |
5.49e-13 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 68.06 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 30 EAQNIVRTALDGGVNFFDTADCY-SDGESSRRLGQALQDLKVDRQSIFVQTKFGIykgdngaitryNFSKDHLIAS-LDR 107
Cdd:cd19110 18 EVTEAVKVAIDAGYRHFDCAYLYhNESEVGAGIREKIKEGVVRREDLFIVSKLWC-----------TCHKKSLVKTaCTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 108 ELENLQTDYVDFVLLHRP-------------------DTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVG 168
Cdd:cd19110 87 SLKALKLNYLDLYLIHWPmgfkpgepdlpldrsgmviPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLNKPG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 169 QKLE--VNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQfGFFEGV-FIDNPkfpalneAM 245
Cdd:cd19110 167 LRVKpvTNQIEC---HPYLTQKK----------------LISFCQSRNVSVTAYRPLG-GSCEGVdLIDDP-------VI 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456322 246 QRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19110 220 QRIAKKHGKSPAQILIRFQIQR--NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-303 |
8.54e-13 |
|
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: 67.52 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 10 GVDASRVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDL----KVDRQSIFVQTKFGIYk 85
Cdd:cd19111 1 GFPMPVIGLGTYQSPP---EEVRAAVDYALFVGYRHIDTALSYQNEKA---IGEALKWWlkngKLKREEVFITTKLPPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 86 gdngaitrYNFSKDhLIASLDRELENLQTDYVDFVLLHRP-----DTLVEFDELAE--------AFNELQNSGRVRHFGV 152
Cdd:cd19111 74 --------YLEFKD-TEKSLEKSLENLKLPYVDLYLIHHPcgfvnKKDKGERELASsdvtsvwrAMEALVSEGKVKSIGL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 153 SNMNPMQV-EMLQSAvgqKLEVNQLQFGLgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPFQFGFFEGV 231
Cdd:cd19111 145 SNFNPRQInKILAYA---KVKPSNLQLEC-HAYLQQRE----------------LRKFCNKKNIVVTAYAPLGSPGRANQ 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456322 232 FIDNPKFPALNE-AMQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISAQEWYDLY 303
Cdd:cd19111 205 SLWPDQPDLLEDpTVLAIAKELDKTPAQVLLRFVLQR--GTGVLPKSTNKERIEENFEVFDFELTEEHFKKLK 275
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-285 |
5.44e-12 |
|
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: 64.86 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 1 MKYSELgSSGVDASRVALGVMRLDGkgrDEAQNIVRTALDGGVNFFDTADCYSDGESsrrLGQALQDLK---VDRQSIFV 77
Cdd:cd19121 1 MTSFKL-NTGASIPAVGLGTWQAKA---GEVKAAVAHALKIGYRHIDGALCYQNEDE---VGEGIKEAIaggVKREDLFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 78 QTKFgiykgdngaitrYNFSKDHLIASLDRELENLQTDYVDFVLLH----------------RPDTLVEFD---ELAEAF 138
Cdd:cd19121 74 TTKL------------WSTYHRRVELCLDRSLKSLGLDYVDLYLVHwpvllnpngnhdlfptLPDGSRDLDwdwNHVDTW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 139 NELQN---SGRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGM 215
Cdd:cd19121 142 KQMEKvlkTGKTKAIGVSNYSIPYLEELLKHATVVPAVNQVEN---HPYLPQQE----------------LVDFCKEKGI 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456322 216 TIQAWSPFQfgffegvFIDNPKFPAlnEAMQRVADKYGVTKNAIAVAWilrHPAR-MQVLLGSMTPSRLKE 285
Cdd:cd19121 203 LIEAYSPLG-------STGSPLISD--EPVVEIAKKHNVGPGTVLISY---QVARgAVVLPKSVTPDRIKS 261
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-284 |
6.58e-12 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 64.95 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDGkGRDEAQNIVRTALDGGVNFFDTADCY-SDGEssrrLGQALQDL-----KVDRQSIFVQTKF 81
Cdd:cd19122 4 NNGVKIPAVGFGTFANEG-AKGETYAAVTKALDVGYRHLDCAWFYlNEDE----VGDAVRDFlkenpSVKREDLFICTKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 82 GIYkgdngaITRYnfskDHLIASLDRELENLQTDYVDFVLLHRP----------------DTLVEFDELAE-------AF 138
Cdd:cd19122 79 WNH------LHEP----EDVKWSIDNSLKNLKLDYIDLFLVHWPiaaekndqrspklgpdGKYVILKDLTEnpeptwrAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 139 NELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQLqfglghtgmvqqEIHVNMADAAsvdhdggLISYSRLKGMTIQ 218
Cdd:cd19122 149 EEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQI------------EIHPFLPNEE-------LVDYCFSNDILPE 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 219 AWSPfqFGFFEGVFIDNPKF---PALNEamqrVADKYGVTKNAIAVAWILRhpaRMQVLL-GSMTPSRLK 284
Cdd:cd19122 210 AYSP--LGSQNQVPSTGERVsenPTLNE----VAEKGGYSLAQVLIAWGLR---RGYVVLpKSSTPSRIE 270
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
24-298 |
8.33e-12 |
|
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: 64.60 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 24 DGKGRDEAQNIVRTALDGGVNFFDTADCYsdgESSRRLGQALQD-----LKVDRQSIFVQTKfgIYKGDNGAitrynfsk 98
Cdd:cd19124 15 DPPSPEDIKAAVLEAIEVGYRHFDTAAAY---GTEEALGEALAEalrlgLVKSRDELFVTSK--LWCSDAHP-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 99 DHLIASLDRELENLQTDYVDFVLLHRP--------------DTLVEFD--ELAEAFNELQNSGRVRHFGVSNMNPMQVEM 162
Cdd:cd19124 82 DLVLPALKKSLRNLQLEYVDLYLIHWPvslkpgkfsfpieeEDFLPFDikGVWEAMEECQRLGLTKAIGVSNFSCKKLQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 163 LQSAVGQKLEVNQLQFGLGHtgmvQQEihvnmadaasvdhdgGLISYSRLKGMTIQAWSPF-QFGFFEG--VFIDNPkfp 239
Cdd:cd19124 162 LLSFATIPPAVNQVEMNPAW----QQK---------------KLREFCKANGIHVTAYSPLgAPGTKWGsnAVMESD--- 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456322 240 alneAMQRVADKYGVTKNAIAVAWILRHPARMQVllGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19124 220 ----VLKEIAAAKGKTVAQVSLRWVYEQGVSLVV--KSFNKERMKQNLDIFDWELTEED 272
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-302 |
2.36e-10 |
|
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: 60.54 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 8 SSGVDASRVALGVMRLDgkgRDEAQNIVRTALDGGVNFFDTADCYSD----GESSRRlgqALQDLKVDRQSIFVQTKFGi 83
Cdd:cd19113 6 NSGYKMPSVGFGCWKLD---NATAADQIYQAIKAGYRLFDGAEDYGNekevGEGVNR---AIDEGLVKREELFLTSKLW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 84 ykgdngaitrYNF-SKDHLIASLDRELENLQTDYVDFVLLHRPDTL--VEFDE--------------------LAE---A 137
Cdd:cd19113 79 ----------NNFhDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFkfVPIEEkyppgfycgdgdnfvyedvpILDtwkA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 138 FNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQKLEVNQLQfglgHTGMVQQEihvnmadaasvdhdgGLISYSRLKGMTI 217
Cdd:cd19113 149 LEKLVDAGKIKSIGVSNFPGALILDLLRGATIKPAVLQIE----HHPYLQQP---------------KLIEYAQKAGITI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 218 QAWSpfQFGFFEGVFIDNPKF---PAL--NEAMQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADV 292
Cdd:cd19113 210 TAYS--SFGPQSFVELNQGRAlntPTLfeHDTIKSIAAKHNKTPAQVLLRWATQR--GIAVIPKSNLPERLLQNLSVNDF 285
|
330
....*....|
gi 705456322 293 EISAQEWYDL 302
Cdd:cd19113 286 DLTKEDFEEI 295
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
29-298 |
6.86e-10 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 59.08 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 29 DEAQNIVRTALDGGVNFFDTADCY-SDGESSRRLGQALQDLKVDRQSIFVQTKfgIYKGDNgaiTRYNFSKdhliaSLDR 107
Cdd:cd19155 25 EEIETAVDTALEAGYRHIDTAYVYrNEAAIGNVLKKWIDSGKVKREELFIVTK--LPPGGN---RREKVEK-----FLLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 108 ELENLQTDYVDFVLLHRP---------------------DTLVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEMLQSA 166
Cdd:cd19155 95 SLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 167 VGQKLEVNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPF----QFGFFEGVF---IDNPKfP 239
Cdd:cd19155 175 ARIKPANLQVEL---HVYLQQKD----------------LVDFCSTHSITVTAYAPLgspgAAHFSPGTGspsGSSPD-L 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456322 240 ALNEAMQRVADKYGVTKNAIAVAWILRHParMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19155 235 LQDPVVKAIAERHGKSPAQVLLRWLMQRG--VVVIPKSTNAARIKENFQVFDFELTEAD 291
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-298 |
3.46e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 56.97 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 28 RDEAQNIVRTALDGGVNFFDTADCYsdGESSRRLGQALQDLKVDRQSIFVQTKFG-IYKGD---NGAITRynfSKDHLIA 103
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSKWGyTYTADwqvDAAVHE---VKDHSLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 104 SLDRELENLQT---DYVDFVLLHR--PDTLV-EFDELAEAFNELQNSGRvrHFGVSNMNPMQVEMLQSAV-----GQKL- 171
Cdd:cd19098 109 RLLKQWEETRSllgKHLDLYQIHSatLESGVlEDADVLAALAELKAEGV--KIGLSLSGPQQAETLRRALeieidGARLf 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 172 -----EVNQLQFGLG-------HTGM--VQQEIHVNmadaasvdhdgglisySRLKGMtiqawspfqfgffegvfIDNPK 237
Cdd:cd19098 187 dsvqaTWNLLEQSAGealeeahEAGMgvIVKEALAN----------------GRLTDR-----------------NPSPE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456322 238 FPALNEAMQRVADKYGVTKNAIAVAWILRHPARMQVLLGSMTPSRLKEMMAGADVEISAQE 298
Cdd:cd19098 234 LAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLEL 294
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
30-163 |
5.89e-09 |
|
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: 56.08 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 30 EAQNIvrtALDGGVNFFDTADCYSDGEssrRLGQALQ----DLKVDRQSIFVQTKFGIykgdngaitryNFSKDHLI-AS 104
Cdd:cd19108 31 EATKL---AIDAGFRHIDSAYLYQNEE---EVGQAIRskiaDGTVKREDIFYTSKLWC-----------TFHRPELVrPA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456322 105 LDRELENLQTDYVDFVLLHRP--------------------DTlVEFDELAEAFNELQNSGRVRHFGVSNMNPMQVEML 163
Cdd:cd19108 94 LEKSLKKLQLDYVDLYLIHFPvalkpgeelfpkdengklifDT-VDLCATWEAMEKCKDAGLAKSIGVSNFNRRQLEMI 171
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
35-302 |
1.71e-07 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 51.72 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 35 VRTALDGGVNFFDTADCYSdgeSSRRLGQALQ----DLKVDRQSIFVQTKFgiykgdngaitrYN-FSKDHLI-ASLDRE 108
Cdd:cd19109 27 VKVAIDTGYRHIDGAYIYQ---NEHEVGQAIRekiaEGKVKREDIFYCGKL------------WNtCHPPELVrPTLERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 109 LENLQTDYVDFVLLHRP------DTLVEFDELA-------------EAFNELQNSGRVRHFGVSNMNPMQVEMLQSAVGQ 169
Cdd:cd19109 92 LKVLQLDYVDLYIIEMPmafkpgDEIYPRDENGkwlyhktnlcatwEALEACKDAGLVKSIGVSNFNRRQLELILNKPGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 170 KLE--VNQLQFglgHTGMVQQEihvnmadaasvdhdggLISYSRLKGMTIQAWSPfqFGFFEGVFIDNPKFPAL--NEAM 245
Cdd:cd19109 172 KHKpvSNQVEC---HPYFTQPK----------------LLEFCQQHDIVIVAYSP--LGTCRDPIWVNVSSPPLleDPLL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456322 246 QRVADKYgvTKNAIAVAwiLRHPARMQVLL--GSMTPSRLKEMMAGADVEISAQEWYDL 302
Cdd:cd19109 231 NSIGKKY--NKTAAQVV--LRFNIQRGVVVipKSFNPERIKENFQIFDFSLTEEEMKDI 285
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-298 |
8.15e-07 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 49.73 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 9 SGVDASRVALGVMRLDgkgRDEAQNIVRTALDGGVNFFDTADCY-SDGESSRRLGQALQDLKVDRQSIFVQTKfgiykgd 87
Cdd:cd19115 9 SGYDMPLVGFGLWKVN---NDTCADQVYNAIKAGYRLFDGACDYgNEVEAGQGVARAIKEGIVKREDLFIVSK------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 88 ngaITRYNFSKDHLIASLDRELENLQTDYVDFVLLHRPDTL-------------------VEF-----DELAEAFNELQN 143
Cdd:cd19115 79 ---LWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALkyvdpavryppgwfydgkkVEFsnapiQETWTAMEKLVD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 144 SGRVRHFGVSNMNPMQV-EMLQSAvgqKLEVNQLQfgLGHTGMVQQEihvnmadaasvdhdgGLISYSRLKGMTIQAWSP 222
Cdd:cd19115 156 KGLARSIGVSNFSAQLLmDLLRYA---RIRPATLQ--IEHHPYLTQP---------------RLVKYAQKEGIAVTAYSS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456322 223 F-QFGFFEgvfIDNPK---FPALNE--AMQRVADKYGVTKNAIAVAWILRHpaRMQVLLGSMTPSRLKEMMAGADVEISA 296
Cdd:cd19115 216 FgPQSFLE---LDLPGakdTPPLFEhdVIKSIAEKHGKTPAQVLLRWATQR--GIAVIPKSNNPKRLAQNLDVTGFDLEA 290
|
..
gi 705456322 297 QE 298
Cdd:cd19115 291 EE 292
|
|
| |
