|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
61-395 |
0e+00 |
|
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: 574.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPPRKETQGRTDLYIGSWMQSKP-RDKIILATKVSGYS 139
Cdd:cd19094 1 VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQGRTEEIIGSWLKKKGnRDKVVLATKVAGPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 140 ERSTFLRdnAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLFGEYCY-NPTKWRPSVPFEEQLKAFQELID 218
Cdd:cd19094 81 EGITWPR--GGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLFGGGYYtEPSEEEDSVSFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 219 EGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRChFEVDLVEVCHPnnCNVGLLAYSPLAGGVLTGKYI 298
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRN-FEEGLAEACHR--ENVGLLAYSPLAGGVLTGKYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 299 DtNPDISKKSRLNLFPGYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKENIDAFt 378
Cdd:cd19094 236 D-GAARPEGGRLNLFPGYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF- 313
|
330
....*....|....*..
gi 1002248734 379 saPRPLAPEVLDDIESL 395
Cdd:cd19094 314 --DVPLSDELLAEIDAV 328
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
49-402 |
3.06e-130 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 378.04 E-value: 3.06e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPPRKETQGRTDLYIGSWMQSK-PRD 127
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQGLTETYIGNWLAKRgSRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 128 KIILATKVSGYSerstflRDNAKVVR----VDAANIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLFGEYCYNPTKWRPS 203
Cdd:PRK10625 81 KLIIASKVSGPS------RNNDKGIRpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYSWTDSAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 204 VPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLL 283
Cdd:PRK10625 155 VSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNR-SFEVGLAEVSQYE--GVELL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 284 AYSPLAGGVLTGKYIdtNPDISKKSRLNLFPGYMeRYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIG 363
Cdd:PRK10625 232 AYSCLAFGTLTGKYL--NGAKPAGARNTLFSRFT-RYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLG 308
|
330 340 350
....*....|....*....|....*....|....*....
gi 1002248734 364 ATTMDQLKENIDAFTSAprpLAPEVLDDIESLFKRYRDP 402
Cdd:PRK10625 309 ATTMEQLKTNIESLHLT---LSEEVLAEIEAVHQVYTYP 344
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
49-402 |
3.06e-117 |
|
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: 344.08 E-value: 3.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGE---QNTEKEAHDILSYSFDQGVNILDTAEMYPvpprketQGRTDLYIGSWMQSKP 125
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYG-------PGRSEELLGEALKGRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 126 RDKIILATKVSGYserstfLRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVP 205
Cdd:COG0667 74 RDDVVIATKVGRR------MGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPD-----------------PDTP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 206 FEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKvqGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNNcnVGLLAY 285
Cdd:COG0667 131 IEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDR-SAEEELLPAARELG--VGVLAY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 286 SPLAGGVLTGKYiDTNPDISKKSRLNLFpgYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGAT 365
Cdd:COG0667 206 SPLAGGLLTGKY-RRGATFPEGDRAATN--FVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGAR 282
|
330 340 350
....*....|....*....|....*....|....*..
gi 1002248734 366 TMDQLKENIDAFTsapRPLAPEVLDDIESLFKRYRDP 402
Cdd:COG0667 283 SPEQLEENLAAAD---LELSAEDLAALDAALAAVPAP 316
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
49-396 |
4.56e-90 |
|
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: 274.45 E-value: 4.56e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPvpprketQGRTDLYIGSWMQSKpRDK 128
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYG-------GGRSEEIIGRWIAGR-RDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 129 IILATKVSGyserSTFLRDNAKvvRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLfgeycynptkwrpsvpfEE 208
Cdd:cd19087 73 IVLATKVFG----PMGDDPNDR--GLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPL-----------------EE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 209 QLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPL 288
Cdd:cd19087 130 TLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKR-QAELEILPAARAY--GLGVIPYSPL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 289 AGGVLTGKYIDTNPdiSKKSRLNLFPGYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMD 368
Cdd:cd19087 207 AGGLLTGKYGKGKR--PESGRLVERARYQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLE 284
|
330 340
....*....|....*....|....*...
gi 1002248734 369 QLKENIDAftsAPRPLAPEVLDDIESLF 396
Cdd:cd19087 285 QLEDSLAA---LEITLTPELLAEIDELF 309
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
53-376 |
1.42e-84 |
|
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: 260.22 E-value: 1.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 53 KLGDSDLVISEVTLGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPPRKETQGRTDLYIGSWM-QSKPRDKIIL 131
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGNAGGESETIIGRWLkSRGKRDRVVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 132 ATKVSGyserstflRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLK 211
Cdd:cd19081 81 ATKVGF--------PMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDD-----------------PATPLEETLG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 212 AFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHPNncNVGLLAYSPLAGG 291
Cdd:cd19081 136 ALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREE--GIGVIPYSPLAGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 292 VLTGKYiDTNPDISKKSRLNLF-PGYM-ERYNASLAkeATNEyvkLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQ 369
Cdd:cd19081 214 FLTGKY-RSEADLPGSTRRGEAaKRYLnERGLRILD--ALDE---VAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQ 287
|
....*..
gi 1002248734 370 LKENIDA 376
Cdd:cd19081 288 LEDLLAA 294
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
50-377 |
6.37e-74 |
|
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: 232.86 E-value: 6.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 50 QYRKLGDSDLVISEVTLGTMTFGEQNT------EKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQS 123
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVY-------SGGASEEILGRALKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 124 -KPRDKIILATKVSGYSerstflRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrP 202
Cdd:cd19079 74 fAPRDEVVIATKVYFPM------GDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWD-----------------Y 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 203 SVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGL 282
Cdd:cd19079 131 ETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYR-EEEREMIPLCEEE--GIGV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 283 LAYSPLAGGVLTGKYIDTNpdiSKKSRLNLFPGYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTII 362
Cdd:cd19079 208 IPWSPLARGRLARPWGDTT---ERRRSTTDTAKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIV 284
|
330
....*....|....*
gi 1002248734 363 GATTMDQLKENIDAF 377
Cdd:cd19079 285 GATKLEHLEDAVAAL 299
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
58-393 |
1.92e-73 |
|
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: 231.26 E-value: 1.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 58 DLVISEVTLGTMTFGEQN----TEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKpRDKIILAT 133
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWwgevDDQESIEAIKAAIDLGINFFDTAPVY-------GFGHSEEILGKALKGR-RDDVVIAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 134 KVSGYSERSTFLRDNAKvvrvdAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAF 213
Cdd:cd19084 73 KCGLRWDGGKGVTKDLS-----PESIRKEVEQSLRRLQTDYIDLYQIHWPD-----------------PNTPIEETAEAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 214 QELIDEGKVRYIGVSNetsYGVMEFVHAAKVQglpKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAGGVL 293
Cdd:cd19084 131 EKLKKEGKIRYIGVSN---FSVEQLEEARKYG---PIVSLQPPYSMLER-EIEEELLPYCREN--GIGVLPYGPLAQGLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 294 TGKYiDTNPDISKKSRLNLFPGYmERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKEN 373
Cdd:cd19084 202 TGKY-KKEPTFPPDDRRSRFPFF-RGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEEN 279
|
330 340
....*....|....*....|
gi 1002248734 374 IDAFTSAprpLAPEVLDDIE 393
Cdd:cd19084 280 AGALDWE---LTEEELKEID 296
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
49-376 |
3.16e-72 |
|
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: 229.04 E-value: 3.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGEQN---------TEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGS 119
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGgffgawggvDQEEADRLVDIALDAGINFFDTADVY-------SEGESEEILGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 120 WMQSKpRDKIILATKVSGyserstflRDNAKVVRVDAA--NIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLfgeycynp 197
Cdd:cd19091 74 ALKGR-RDDVLIATKVRG--------RMGEGPNDVGLSrhHIIRAVEASLKRLGTDYIDLYQLHGFDALTPL-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 198 tkwrpsvpfEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVChpNN 277
Cdd:cd19091 137 ---------EETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGR-DLEHELMPLA--LD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 278 CNVGLLAYSPLAGGVLTGKYIDTNPdISKKSRLNLFPGYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFT 357
Cdd:cd19091 205 QGVGLLVWSPLAGGLLSGKYRRGQP-APEGSRLRRTGFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTV 283
|
330
....*....|....*....
gi 1002248734 358 ASTIIGATTMDQLKENIDA 376
Cdd:cd19091 284 SSVIIGARNEEQLEDNLGA 302
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
62-375 |
1.25e-70 |
|
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: 221.62 E-value: 1.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP-RDKIILATKVSGYSE 140
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVY-------GDGRSERLLGRWLKGRGnRDDVVIATKGGHPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 141 rstflrDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAFQELIDEG 220
Cdd:cd06660 74 ------GDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDD-----------------PSTPVEETLEALNELVREG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 221 KVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHPNncNVGLLAYSPLAGGvltgkyidt 300
Cdd:cd06660 131 KIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEEELLDWAEEN--GLPLLAYSPLARG--------- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002248734 301 npdiskksrlnlfpgymerynaslakeatneyvklakkhgltPVQLALGFVRDRPFTASTIIGATTMDQLKENID 375
Cdd:cd06660 200 ------------------------------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
64-395 |
1.45e-69 |
|
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: 221.03 E-value: 1.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 64 VTLGTMTFG---EQNTEKEAHDILSYSFDQGVNILDTAEMYPvpprketQGRTDLYIGSWMQSKP--RDKIILATKVSGy 138
Cdd:pfam00248 1 IGLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYG-------DGKSEELLGEALKDYPvkRDKVVIATKVPD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 139 serstflRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAFQELID 218
Cdd:pfam00248 73 -------GDGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPD-----------------PDTPIEETWDALEELKK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 219 EGKVRYIGVSNETSyGVMEFVHAAKVqglPKIVSIQNSYSLiVRCHFEVDLVEVCHPNNcnVGLLAYSPLAGGVLTGKYI 298
Cdd:pfam00248 129 EGKIRAIGVSNFDA-EQIEKALTKGK---IPIVAVQVEYNL-LRRRQEEELLEYCKKNG--IPLIAYSPLGGGLLTGKYT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 299 DTNPDISKKSRLNLFPGYmerynaSLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKENIDAFT 378
Cdd:pfam00248 202 RDPDKGPGERRRLLKKGT------PLNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE 275
|
330
....*....|....*..
gi 1002248734 379 SaprPLAPEVLDDIESL 395
Cdd:pfam00248 276 F---PLSDEEVARIDEL 289
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
59-388 |
6.66e-69 |
|
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: 219.77 E-value: 6.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 59 LVISEVTLGT-MTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPvpprketQGRTDLYIGSWMQSKPRDKIILATKVS- 136
Cdd:cd19074 2 LKVSELSLGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYA-------AGQAEEVLGKALKGWPRESYVISTKVFw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 137 ---------GYSERstflrdnakvvrvdaaNIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFE 207
Cdd:cd19074 75 ptgpgpndrGLSRK----------------HIFESIHASLKRLQLDYVDIYYCHRYD-----------------PETPLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 208 EQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHpnNCNVGLLAYSP 287
Cdd:cd19074 122 ETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWR-EIEEEVIPLCE--KNGIGLVVWSP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 288 LAGGVLTGKYID-TNPDISKKSRLNLFPGYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATT 366
Cdd:cd19074 199 LAQGLLTGKYRDgIPPPSRSRATDEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASR 278
|
330 340
....*....|....*....|..
gi 1002248734 367 MDQLKENIDAftSAPRpLAPEV 388
Cdd:cd19074 279 PEQLEENVKA--SGVK-LSPEV 297
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
61-394 |
1.12e-64 |
|
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: 208.59 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFG-----EQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKpRDKIILATKV 135
Cdd:cd19085 1 VSRLGLGCWQFGggywwGDQDDEESIATIHAALDAGINFFDTAEAY-------GDGHSEEVLGKALKGR-RDDVVIATKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 136 SGyserstflrDNAKvvrvdAANIKESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeycynptkwrpSVPFEEQLKAFQE 215
Cdd:cd19085 73 SP---------DNLT-----PEDVRKSCERSLKRLGTDYIDLYQIHWPSS-----------------DVPLEETMEALEK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 216 LIDEGKVRYIGVSNetsYGV--MEFVHAAKvqglpKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAGGVL 293
Cdd:cd19085 122 LKEEGKIRAIGVSN---FGPaqLEEALDAG-----RIDSNQLPYNLLWR-AIEYEILPFCREH--GIGVLAYSPLAQGLL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 294 TGKY--IDTNPDISKKSRLNLF--PGYMERynaslAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQ 369
Cdd:cd19085 191 TGKFssAEDFPPGDARTRLFRHfePGAEEE-----TFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQ 265
|
330 340
....*....|....*....|....*
gi 1002248734 370 LKENIDAFTSaprPLAPEVLDDIES 394
Cdd:cd19085 266 LEENAAAVDL---ELSPSVLERLDE 287
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
52-376 |
5.61e-62 |
|
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: 202.06 E-value: 5.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 52 RKLGDSDLVISEVTLGTMTFGEQ----NTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKpRD 127
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNY-------TNGTSERLLGEFIAGN-RD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 128 KIILATKVSGYSER--STFLRDNAKvvrvdaaNIKESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeycynptkwrpSVP 205
Cdd:cd19080 73 RIVLATKYTMNRRPgdPNAGGNHRK-------NLRRSVEASLRRLQTDYIDLLYVHAWDF-----------------TTP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 206 FEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHpnNCNVGLLAY 285
Cdd:cd19080 129 VEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLER-TPERELLPMAR--ALGLGVTPW 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 286 SPLAGGVLTGKY-IDTNPDISKKSRLNLFPGYMERYNASLAKEAtneyVKLAKKHGLTPVQLALGFVRDRPFTASTIIGA 364
Cdd:cd19080 206 SPLGGGLLTGKYqRGEEGRAGEAKGVTVGFGKLTERNWAIVDVV----AAVAEELGRSAAQVALAWVRQKPGVVIPIIGA 281
|
330
....*....|..
gi 1002248734 365 TTMDQLKENIDA 376
Cdd:cd19080 282 RTLEQLKDNLGA 293
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
49-394 |
7.14e-55 |
|
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: 183.95 E-value: 7.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGT-MTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGS------Wm 121
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVY-------ANGQSEEIMGQaikelgW- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 122 qskPRDKIILATKV----SGYSERSTFLrdNAKvvrvdaaNIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynp 197
Cdd:cd19143 73 ---PRSDYVVSTKIfwggGGPPPNDRGL--SRK-------HIVEGTKASLKRLQLDYVDLVFCHRPD------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 198 tkwrPSVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHpnN 277
Cdd:cd19143 128 ----PATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYE--K 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 278 CNVGLLAYSPLAGGVLTGKYidtNPDISKKSRLNLfPGYM---ERYNASLAK--EATNEYVKLAKKHGLTPVQLALGFVR 352
Cdd:cd19143 202 YGLGTTTWSPLASGLLTGKY---NNGIPEGSRLAL-PGYEwlkDRKEELGQEkiEKVRKLKPIAEELGCSLAQLAIAWCL 277
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1002248734 353 DRPFTASTIIGATTMDQLKENIDAFTSAPRpLAPEVLDDIES 394
Cdd:cd19143 278 KNPNVSTVITGATKVEQLEENLKALEVLPK-LTPEVMEKIEA 318
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
61-377 |
2.61e-53 |
|
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: 178.19 E-value: 2.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFGEQNT-----EKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKPRDKIILATKV 135
Cdd:cd19072 4 VPVLGLGTWGIGGGMSkdysdDKKAIEALRYAIELGINLIDTAEMY-------GGGHAEELVGKAIKGFDREDLFITTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 136 SgyserSTFLRDNAkvvrvdaanIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAFQE 215
Cdd:cd19072 77 S-----PDHLKYDD---------VIKAAKESLKRLGTDYIDLYLIHWPN-----------------PSIPIEETLRAMEE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 216 LIDEGKVRYIGVSNetsYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAGGVLTG 295
Cdd:cd19072 126 LVEEGKIRYIGVSN---FSLEELEEAQSYLKKGPIVANQVEYNLFDR-EEESGLLPYCQKN--GIAIIAYSPLEKGKLSN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 296 KYIDtnpdiskksrlnlfpgymerynASLAkeatneyvKLAKKHGLTPVQLALGFVRDRPFTAsTIIGATTMDQLKENID 375
Cdd:cd19072 200 AKGS----------------------PLLD--------EIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAG 248
|
..
gi 1002248734 376 AF 377
Cdd:cd19072 249 AL 250
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
52-396 |
8.19e-52 |
|
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: 175.69 E-value: 8.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 52 RKLGDSDLVISEVTLGTMTFGEQN-----TEKEAHDILSYSFDQGVNILDTAEMYPVpprketqGRTDLYIGSWMQSKPR 126
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNlypnlDEEEGKDLVREALDNGVNLLDTAFIYGL-------GRSEELVGEVLKEYNR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 127 DKIILATKVSGYSERSTFLRDNakvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPF 206
Cdd:cd19083 75 NEVVIATKGAHKFGGDGSVLNN------SPEFLRSAVEKSLKRLNTDYIDLYYIHFPD-----------------GETPK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 207 EEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQglpkivSIQNSYSLIVRCHfEVDLVEVCHPNncNVGLLAYS 286
Cdd:cd19083 132 AEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVD------VLQGEYNLLQREA-EEDILPYCVEN--NISFIPYF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 287 PLAGGVLTGKYI-DTN-PDISKKSRLNLFPGymERYNASLakEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGA 364
Cdd:cd19083 203 PLASGLLAGKYTkDTKfPDNDLRNDKPLFKG--ERFSENL--DKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGA 278
|
330 340 350
....*....|....*....|....*....|..
gi 1002248734 365 TTMDQLKENIDAftsAPRPLAPEVLDDIESLF 396
Cdd:cd19083 279 KRAEQVIDNLKA---LDVTLTEEEIAFIDALF 307
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
51-376 |
3.56e-51 |
|
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: 174.00 E-value: 3.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 51 YRKLGDSDLVISEVTLGT------MTFGEqNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSK 124
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTwaigggPWWGG-SDDNESIRTIHAALDLGINLIDTAPAY-------GFGHSEEIVGKAIKGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 pRDKIILATKVSGYSERS----TFLRDNAKVVR-VDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptk 199
Cdd:cd19149 73 -RDKVVLATKCGLRWDREggsfFFVRDGVTVYKnLSPESIREEVEQSLKRLGTDYIDLYQTHWQD--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 200 wrPSVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQglpkivSIQNSYSLIVRCHfEVDLVEVCHPNncN 279
Cdd:cd19149 137 --VETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLD------IIQEKYSMLDRGI-EKELLPYCKKN--N 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 280 VGLLAYSPLAGGVLTGKYI-DTNPDIS-KKSRLNLF-PGYMERYNASLAKEAtneyvKLAKKHGLTPVQLALGFVRDRPF 356
Cdd:cd19149 206 IAFQAYSPLEQGLLTGKITpDREFDAGdARSGIPWFsPENREKVLALLEKWK-----PLCEKYGCTLAQLVIAWTLAQPG 280
|
330 340
....*....|....*....|
gi 1002248734 357 TASTIIGATTMDQLKENIDA 376
Cdd:cd19149 281 ITSALCGARKPEQAEENAKA 300
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
50-392 |
1.84e-49 |
|
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: 169.32 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 50 QYRKLGDSDLVISEVTLGTM---TFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpVPPRKETqgrtdlYIGSWMQsKPR 126
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmsAFYGPADEEESIATLHRALELGVTFLDTADMY-GPGTNEE------LLGKALK-DRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 127 DKIILATKVsGYSerstfLRDNAKVVRVDA--ANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSV 204
Cdd:cd19076 73 DEVVIATKF-GIV-----RDPGSGFRGVDGrpEYVRAACEASLKRLGTDVIDLYYQHRVD-----------------PNV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 205 PFEEQLKAFQELIDEGKVRYIGVSnETSYGVMEfvHAAKVQglpKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLA 284
Cdd:cd19076 130 PIEETVGAMAELVEEGKVRYIGLS-EASADTIR--RAHAVH---PITAVQSEYSLWTR-DIEDEVLPTCREL--GIGFVA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 285 YSPLAGGVLTGKYIDTNpDISKKSRLNLFPGYME---RYNASLAKEATneyvKLAKKHGLTPVQLALGFVRDR-----Pf 356
Cdd:cd19076 201 YSPLGRGFLTGAIKSPE-DLPEDDFRRNNPRFQGenfDKNLKLVEKLE----AIAAEKGCTPAQLALAWVLAQgddivP- 274
|
330 340 350
....*....|....*....|....*....|....*.
gi 1002248734 357 tastIIGATTMDQLKENIDAftsAPRPLAPEVLDDI 392
Cdd:cd19076 275 ----IPGTKRIKYLEENVGA---LDVVLTPEELAEI 303
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
63-395 |
2.54e-49 |
|
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: 168.89 E-value: 2.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 63 EVTLGTMTFGEQN---TEKEAHDILSYSFDQGVNILDTAEMYPvpprketQGRTDLYIGSwMQSKPRDkIILATKVSGYS 139
Cdd:cd19075 2 KIILGTMTFGSQGrftTAEAAAELLDAFLERGHTEIDTARVYP-------DGTSEELLGE-LGLGERG-FKIDTKANPGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 140 ERStflrdnakvvrVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeycynptkwrpSVPFEEQLKAFQELIDE 219
Cdd:cd19075 73 GGG-----------LSPENVRKQLETSLKRLKVDKVDVFYLHAPDR-----------------STPLEETLAAIDELYKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 220 GKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNNCNvgLLAYSPLAGGVLTGKYiD 299
Cdd:cd19075 125 GKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITR-QVETELFPCLRKLGIR--FYAYSPLAGGFLTGKY-K 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 300 TNPDISKKSRL--NLFPG--YMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVR----------DRpftasTIIGAT 365
Cdd:cd19075 201 YSEDKAGGGRFdpNNALGklYRDRYWKPSYFEALEKVEEAAEKEGISLAEAALRWLYhhsaldgekgDG-----VILGAS 275
|
330 340 350
....*....|....*....|....*....|
gi 1002248734 366 TMDQLKENIDAFTSAprPLAPEVLDDIESL 395
Cdd:cd19075 276 SLEQLEENLAALEKG--PLPEEVVKAIDEA 303
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
62-376 |
5.17e-49 |
|
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: 167.73 E-value: 5.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPvppRKETQGRTDLYIGSWMQS-KPRDKIILATKvSGYSE 140
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYG---DWVERGASERVIGEWLKSrGNRDKVVIATK-GGHPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 141 RSTFLRDnakvvRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAFQELIDEG 220
Cdd:cd19082 77 LEDMSRS-----RLSPEDIRADLEESLERLGTDYIDLYFLHRDD-----------------PSVPVGEIVDTLNELVRAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 221 KVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLivrchfeVDLVEVCHPNNCNV---------------GLLAY 285
Cdd:cd19082 135 KIRAFGASNWSTERIAEANAYAKAHGLPGFAASSPQWSL-------ARPNEPPWPGPTLVamdeemrawheenqlPVFAY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 286 SPLAGGVLTGKYIDTNPDISKKSRLNLFPGYMERYNAslAKEatneyvkLAKKHGLTPVQLALGFVRDRPFTASTIIGAT 365
Cdd:cd19082 208 SSQARGFFSKRAAGGAEDDSELRRVYYSEENFERLER--AKE-------LAEEKGVSPTQIALAYVLNQPFPTVPIIGPR 278
|
330
....*....|.
gi 1002248734 366 TMDQLKENIDA 376
Cdd:cd19082 279 TPEQLRDSLAA 289
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
61-395 |
6.19e-48 |
|
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: 165.15 E-value: 6.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGT---------MTFGEQNtEKEAHDILSYSFDQGVNILDTAEMYPVPPRKETQGRTDLyigswmqsKPRDKIIL 131
Cdd:cd19102 1 LTTIGLGTwaiggggwgGGWGPQD-DRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK--------GLRDRPIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 132 ATKVSGYSErstflrDNAKVVR-VDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQL 210
Cdd:cd19102 72 ATKCGLLWD------EEGRIRRsLKPASIRAECEASLRRLGVDVIDLYQIHWPD-----------------PDEPIEEAW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 211 KAFQELIDEGKVRYIGVSNetsYGVMEFVHAAKVQGlpkIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAG 290
Cdd:cd19102 129 GALAELKEEGKVRAIGVSN---FSVDQMKRCQAIHP---IASLQPPYSLLRR-GIEAEILPFCAEH--GIGVIVYSPMQS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 291 GVLTGKyidtnpdISKKSRLNLFPGYMERYNASLAKEATNEYVKL-------AKKHGLTPVQLALGFVRDRPFTASTIIG 363
Cdd:cd19102 200 GLLTGK-------MTPERVASLPADDWRRRSPFFQEPNLARNLALvdalrpiAERHGRTVAQLAIAWVLRRPEVTSAIVG 272
|
330 340 350
....*....|....*....|....*....|..
gi 1002248734 364 ATTMDQLKENIDAftsAPRPLAPEVLDDIESL 395
Cdd:cd19102 273 ARRPDQIDETVGA---ADLRLTPEELAEIEAL 301
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
61-376 |
4.38e-47 |
|
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: 162.78 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFGEQ-------NTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQ-SKPRDKIILA 132
Cdd:cd19093 2 VSPLGLGTWQWGDRlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVY-------GTGRSERLLGRFLKeLGDRDEVVIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 133 TKVSGYserstFLRDNAKVvrvdaanIKESVEKSLSRLSTDYIDLLQIHWPdryvplfgeycynpTKWRPSVpfEEQLKA 212
Cdd:cd19093 75 TKFAPL-----PWRLTRRS-------VVKALKASLERLGLDSIDLYQLHWP--------------GPWYSQI--EALMDG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 213 FQELIDEGKVRYIGVSNetsYGV--MEFVHAA-KVQGLPkIVSIQNSYSLIVRCHFEVDLVEVCHPNNcnVGLLAYSPLA 289
Cdd:cd19093 127 LADAVEEGLVRAVGVSN---YSAdqLRRAHKAlKERGVP-LASNQVEYSLLYRDPEQNGLLPACDELG--ITLIAYSPLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 290 GGVLTGKYIDTNPDISKKSRLNLfpgymeRYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRDRpfTASTIIGATTMDQ 369
Cdd:cd19093 201 QGLLTGKYSPENPPPGGRRRLFG------RKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQ 272
|
....*..
gi 1002248734 370 LKENIDA 376
Cdd:cd19093 273 AEENAGA 279
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
59-376 |
6.95e-47 |
|
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: 160.34 E-value: 6.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 59 LVISEVTLGTMTFGEQN----TEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQsKPRDKIILATK 134
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWwgdvDDAEAIRALRAALDLGINFFDTADVY-------GDGHSERLLGKALK-GRRDKVVIATK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 135 VsGYsersTFLRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIH-WPDRYVPLfgeycynptkwrpsvpfEEQLKAF 213
Cdd:cd19086 73 F-GN----RFDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDN-----------------DELFEAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 214 QELIDEGKVRYIGVSNETSYGVMEFVHAakvqglPKIVSIQNSYSLIVRcHFEVDLVEVCHpnNCNVGLLAYSPLAGGVL 293
Cdd:cd19086 131 EKLKQEGKIRAYGVSVGDPEEALAALRR------GGIDVVQVIYNLLDQ-RPEEELFPLAE--EHGVGVIARVPLASGLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 294 TGKyidtnpdiskksrlnlfpgymerynaslakeatneyvklakkhgltPVQLALGFVRDRPFTASTIIGATTMDQLKEN 373
Cdd:cd19086 202 TGK----------------------------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEEN 235
|
...
gi 1002248734 374 IDA 376
Cdd:cd19086 236 AAA 238
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
62-376 |
1.74e-45 |
|
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: 158.65 E-value: 1.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPPRKETQGRTDLYIGSWM-QSKPRDKIILATKVsGYSE 140
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGGESERLIGRWLkDRGNRDDVVIATKV-GAGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 141 RStFLRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLfgeycynptkwrpsvpfEEQLKAFQELIDEG 220
Cdd:cd19752 80 RD-PDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPL-----------------EETLEAFNELVKAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 221 KVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCH---FEV------DLVEVC--HPnncNVGLLAYSPLa 289
Cdd:cd19752 142 KVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLRPRPgadFGVqrivtdELLDYAssRP---DLTLLAYSPL- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 290 ggvLTGKYidTNPDiskksrlNLFPGYMERYNASLAKEATNEyvkLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQ 369
Cdd:cd19752 218 ---LSGAY--TRPD-------RPLPEQYDGPDSDARLAVLEE---VAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQ 282
|
....*..
gi 1002248734 370 LKENIDA 376
Cdd:cd19752 283 LEENLAA 289
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
49-401 |
1.86e-43 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 155.36 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGEQNtEKEAHDILSYSFDQGVNILDTAEMYpvpprketqGRTDLYIGSWMqSKPRDK 128
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRKD-EEEAEALIRRAIDNGINYIDTARGY---------GDSEEFLGKAL-KGPRDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 129 IILATKVSGYSErstflrdnakvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPDRYvplfgEYCYNPTKwrPSVPFEe 208
Cdd:COG1453 70 VILATKLPPWVR--------------DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTE-----EDLEKVLK--PGGALE- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 209 qlkAFQELIDEGKVRYIGVSNETSYGVM-EFVHAakvqGLPKIVSIQNSYsLIVRCHFEVDLVEVCHPNncNVGLLAYSP 287
Cdd:COG1453 128 ---ALEKAKAEGKIRHIGFSTHGSLEVIkEAIDT----GDFDFVQLQYNY-LDQDNQAGEEALEAAAEK--GIGVIIMKP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 288 LAGGVLtgkyidTNPdiskksrlnlfpgymerynaslakeatNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTM 367
Cdd:COG1453 198 LKGGRL------ANP---------------------------PEKLVELLCPPLSPAEWALRFLLSHPEVTTVLSGMSTP 244
|
330 340 350
....*....|....*....|....*....|....
gi 1002248734 368 DQLKENIDAFtSAPRPLAPEVLDDIESLFKRYRD 401
Cdd:COG1453 245 EQLDENLKTA-DNLEPLTEEELAILERLAEELGE 277
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
58-394 |
6.05e-43 |
|
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: 152.00 E-value: 6.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 58 DLVISEVTLGTM----TFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpVPPRKETQGRTDLyigswmqsKP-RDKIILA 132
Cdd:cd19078 1 GLEVSAIGLGCMgmshGYGPPPDKEEMIELIRKAVELGITFFDTAEVY-GPYTNEELVGEAL--------KPfRDQVVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 133 TK----VSGYSERSTFLRDNAkvvrvdaANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEE 208
Cdd:cd19078 72 TKfgfkIDGGKPGPLGLDSRP-------EHIRKAVEGSLKRLQTDYIDLYYQHRVD-----------------PNVPIEE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 209 QLKAFQELIDEGKVRYIGVSnETSYGVMEFVHAAkvqgLPkIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPL 288
Cdd:cd19078 128 VAGTMKELIKEGKIRHWGLS-EAGVETIRRAHAV----CP-VTAVQSEYSMMWR-EPEKEVLPTLEEL--GIGFVPFSPL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 289 AGGVLTGKyIDTNPDISKKSrlnlFPGYMERYNASlAKEATNEYVKL----AKKHGLTPVQLALGFV-RDRPFTAStIIG 363
Cdd:cd19078 199 GKGFLTGK-IDENTKFDEGD----DRASLPRFTPE-ALEANQALVDLlkefAEEKGATPAQIALAWLlAKKPWIVP-IPG 271
|
330 340 350
....*....|....*....|....*....|.
gi 1002248734 364 ATTMDQLKENIDAftsAPRPLAPEVLDDIES 394
Cdd:cd19078 272 TTKLSRLEENIGA---ADIELTPEELREIED 299
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
58-377 |
3.39e-42 |
|
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: 150.15 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 58 DLVISEVTLGTMTFGEQ----NTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSK-PRDKIILA 132
Cdd:cd19148 1 DLPVSRIALGTWAIGGWmwggTDEKEAIETIHKALDLGINLIDTAPVY-------GFGLSEEIVGKALKEYgKRDRVVIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 133 TKVS-GYSERSTFLRDNAKvvrvdaANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLK 211
Cdd:cd19148 74 TKVGlEWDEGGEVVRNSSP------ARIRKEVEDSLRRLQTDYIDLYQVHWPD-----------------PLVPIEETAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 212 AFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQglpkivSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAGG 291
Cdd:cd19148 131 ALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLH------TVQPPYNLFER-EIEKDVLPYARKH--NIVTLAYGALCRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 292 VLTGKyIDTNPDISKKSRLNLFPGYME-RYNASLAkeATNEYVKLAKKHGLTPV-QLALGFVRDRPFTASTIIGATTMDQ 369
Cdd:cd19148 202 LLSGK-MTKDTKFEGDDLRRTDPKFQEpRFSQYLA--AVEELDKLAQERYGKSViHLAVRWLLDQPGVSIALWGARKPEQ 278
|
....*...
gi 1002248734 370 LKENIDAF 377
Cdd:cd19148 279 LDAVDEVF 286
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
51-375 |
1.11e-41 |
|
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: 146.86 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 51 YRKLGDSDLVISEVTLGTMTFGEqNTEKEAHDILSYSFDQGVNILDTAEMYpvpprketqGRTDLYIGSWMQsKPRDKII 130
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR-LSQEEAAAIIRRALDLGINYFDTAPSY---------GDSEEKIGKALK-GRRDKVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 131 LATKVSGYserstflrdnakvvrvDAANIKESVEKSLSRLSTDYIDLLQIH------WPDRyvpLFGEycynptkwrpsv 204
Cdd:cd19100 70 LATKTGAR----------------DYEGAKRDLERSLKRLGTDYIDLYQLHavdteeDLDQ---VFGP------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 205 pfEEQLKAFQELIDEGKVRYIGVSNETSYGVMEfvhAAKVqglPKIVSIQNSYSLIVRCH--FEVDLVEVCHPNncNVGL 282
Cdd:cd19100 119 --GGALEALLEAKEEGKIRFIGISGHSPEVLLR---ALET---GEFDVVLFPINPAGDHIdsFREELLPLAREK--GVGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 283 LAYSPLAGGVLTGKYIDTnpdiskksrlnlfpgymerynaslakeatneyvklakkhgltpVQLALGFVRDRPFTASTII 362
Cdd:cd19100 189 IAMKVLAGGRLLSGDPLD-------------------------------------------PEQALRYALSLPPVDVVIV 225
|
330
....*....|...
gi 1002248734 363 GATTMDQLKENID 375
Cdd:cd19100 226 GMDSPEELDENLA 238
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
51-382 |
1.55e-41 |
|
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: 148.75 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 51 YRKLGDSDLVISEVTLGT-MTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP--RD 127
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTwVTFGSQISDEVAEELVTLAYENGINLFDTAEVY-------AAGKAEIVLGKILKKKGwrRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 128 KIILATKVS--GYSERSTFLrdnakvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVP 205
Cdd:cd19141 75 SYVITTKIFwgGKAETERGL---------SRKHIIEGLKASLERLQLEYVDIVFANRPD-----------------PNTP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 206 FEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHpnNCNVGLLAY 285
Cdd:cd19141 129 MEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFH--KIGVGAMTW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 286 SPLAGGVLTGKYIDTNPDISKKSrlnlFPGYMERYNASLAKEATNEYVKL------AKKHGLTPVQLALGFVRDRPFTAS 359
Cdd:cd19141 207 SPLACGILSGKYDDGVPEYSRAS----LKGYQWLKEKILSEEGRRQQAKLkelqiiADRLGCTLPQLAIAWCLKNEGVSS 282
|
330 340
....*....|....*....|...
gi 1002248734 360 TIIGATTMDQLKENIDAFTSAPR 382
Cdd:cd19141 283 VLLGASSTEQLYENLQAIQVLPK 305
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
49-381 |
3.24e-40 |
|
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: 144.62 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGE---QNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP 125
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGvfgPVDEEEAIRTVHEALDSGINYIDTAPWY-------GQGRSETVLGKALKGIP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 126 RDKIILATKVSGYSerstflRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDrYVPLFgeycynptkwrpSVP 205
Cdd:cd19163 74 RDSYYLATKVGRYG------LDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIE-FAPSL------------DQI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 206 FEEQLKAFQELIDEGKVRYIGVsneTSY--GVMEFVhAAKVQGlpKIVSIQnSYslivrCHFEV------DLVEVCHpnN 277
Cdd:cd19163 135 LNETLPALQKLKEEGKVRFIGI---TGYplDVLKEV-LERSPV--KIDTVL-SY-----CHYTLndtsllELLPFFK--E 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 278 CNVGLLAYSPLAGGVLTGKyidtnpdiskksrlnlfpGYMERYNASLA-KEATNEYVKLAKKHGLTPVQLALGFVRDRPF 356
Cdd:cd19163 201 KGVGVINASPLSMGLLTER------------------GPPDWHPASPEiKEACAKAAAYCKSRGVDISKLALQFALSNPD 262
|
330 340
....*....|....*....|....*
gi 1002248734 357 TASTIIGATTMDQLKENIDAFTSAP 381
Cdd:cd19163 263 IATTLVGTASPENLRKNLEAAEEPL 287
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
49-376 |
5.61e-40 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 142.72 E-value: 5.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGEQNTEkeahdILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKPRDK 128
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESPE-----LLRRALDLGINYFDTAEGY-------GNGNSEEIIGEALKGLRRDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 129 IILATKVSGYSERStflrdnakvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplFGEYCYNPtkwrpsvpfEE 208
Cdd:cd19105 69 VFLATKASPRLDKK------------DKAELLKSVEESLKRLQTDYIDIYQLHGVD-----TPEERLLN---------EE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 209 QLKAFQELIDEGKVRYIGVSneTSYGVMEFVHAAkVQGlPKIVSIQNSYSLIVRCHFEVDLVEVCHPNncNVGLLAYSPL 288
Cdd:cd19105 123 LLEALEKLKKEGKVRFIGFS--THDNMAEVLQAA-IES-GWFDVIMVAYNFLNQPAELEEALAAAAEK--GIGVVAMKTL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 289 AGGVLTGKYidtnpdiskksrlnlfpgymerynaslakeatnEYVKLAKkhGLTPVQLALGFVRDRPFTASTIIGATTMD 368
Cdd:cd19105 197 AGGYLQPAL---------------------------------LSVLKAK--GFSLPQAALKWVLSNPRVDTVVPGMRNFA 241
|
....*...
gi 1002248734 369 QLKENIDA 376
Cdd:cd19105 242 ELEENLAA 249
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
51-381 |
4.74e-39 |
|
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: 142.01 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 51 YRKLGDSDLVISEVTLGT-MTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPPrketqGRTDLYIGSWMQS---KPR 126
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLwHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPP-----GSAEENFGRILKRdlrPYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 127 DKIILATKVsGY----------SERSTFLrdnakvvrvdaanikESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycyn 196
Cdd:cd19089 76 DELVISTKA-GYgmwpgpygdgGSRKYLL---------------ASLDQSLKRMGLDYVDIFYHHRYD------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 197 ptkwrPSVPFEEQLKAFQELIDEGKVRYIGVSNetsYGVMEFVHAAKV---QGLPKIVSiQNSYSLIVRCHFEvDLVEVC 273
Cdd:cd19089 128 -----PDTPLEETMTALADAVRSGKALYVGISN---YPGAKARRAIALlreLGVPLIIH-QPRYSLLDRWAED-GLLEVL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 274 HpnNCNVGLLAYSPLAGGVLTGKYIDTNPDISkkSRLNLFPGYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFVRD 353
Cdd:cd19089 198 E--EAGIGFIAFSPLAQGLLTDKYLNGIPPDS--RRAAESKFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLR 273
|
330 340
....*....|....*....|....*...
gi 1002248734 354 RPFTASTIIGATTMDQLKENIDAFTSAP 381
Cdd:cd19089 274 DPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
52-392 |
2.21e-38 |
|
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: 140.26 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 52 RKLGDSDLVISEVTLGTM----TFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPvPPRKEtqgrtdLYIGSWMQSKPRD 127
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsgDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYG-PNTNE------VLLGKALKDGPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 128 KIILATKVSgyserSTFLRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeycynptkwrpSVPFE 207
Cdd:cd19145 76 KVQLATKFG-----IHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDT-----------------TVPIE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 208 EQLKAFQELIDEGKVRYIGVSnETSYGVMEFVHAAKvqglpKIVSIQNSYSLIVRcHFEVDLVEVCHpnNCNVGLLAYSP 287
Cdd:cd19145 134 ITMGELKKLVEEGKIKYIGLS-EASADTIRRAHAVH-----PITAVQLEWSLWTR-DIEEEIIPTCR--ELGIGIVPYSP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 288 LAGGVLTGKyidtnPDISKKSRLNLFPGYMERYNASLAKEATNEYVK---LAKKHGLTPVQLALGFVRDRPFTASTIIGA 364
Cdd:cd19145 205 LGRGFFAGK-----AKLEELLENSDVRKSHPRFQGENLEKNKVLYERveaLAKKKGCTPAQLALAWVLHQGEDVVPIPGT 279
|
330 340
....*....|....*....|....*...
gi 1002248734 365 TTMDQLKENIDAFTSAprpLAPEVLDDI 392
Cdd:cd19145 280 TKIKNLNQNIGALSVK---LTKEDLKEI 304
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
49-396 |
3.68e-38 |
|
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: 140.12 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGT-MTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP-- 125
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVY-------AAGKAERTLGNILKSKGwr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 126 RDKIILATKVsgyserstFLRDNAKVVR-VDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSV 204
Cdd:cd19160 76 RSSYVVTTKI--------YWGGQAETERgLSRKHIIEGLRGSLDRLQLEYVDIVFANRSD-----------------PNS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 205 PFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHpnNCNVGLLA 284
Cdd:cd19160 131 PMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYH--KIGVGSVT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 285 YSPLAGGVLTGKYIDTNPDISKKSrlnlFPGYMERYNASLAKEATNEYVK------LAKKHGLTPVQLALGFVRDRPFTA 358
Cdd:cd19160 209 WSPLACGLITGKYDGRVPDTCRAA----VKGYQWLKEKVQSEEGKKQQAKvkelhpIADRLGCTVAQLAIAWCLRSEGVS 284
|
330 340 350
....*....|....*....|....*....|....*...
gi 1002248734 359 STIIGATTMDQLKENIDAFTSAPRpLAPEVLDDIESLF 396
Cdd:cd19160 285 SVLLGVSSAEQLIENLGSIQVLSQ-LTPQTVMEIDALL 321
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
49-396 |
6.05e-38 |
|
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: 139.45 E-value: 6.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGT-MTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSK--P 125
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVY-------AAGKAEVVLGNIIKKKgwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 126 RDKIILATKVsgyserstFLRDNAKVVR-VDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSV 204
Cdd:cd19158 74 RSSLVITTKI--------FWGGKAETERgLSRKHIIEGLKASLERLQLEYVDVVFANRPD-----------------PNT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 205 PFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHpnNCNVGLLA 284
Cdd:cd19158 129 PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFH--KIGVGAMT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 285 YSPLAGGVLTGKYIDTNPDISKKSrlnlFPGYMERYNASLAKEATNEYVKL------AKKHGLTPVQLALGFVRDRPFTA 358
Cdd:cd19158 207 WSPLACGIVSGKYDSGIPPYSRAS----LKGYQWLKDKILSEEGRRQQAKLkelqaiAERLGCTLPQLAIAWCLRNEGVS 282
|
330 340 350
....*....|....*....|....*....|....*...
gi 1002248734 359 STIIGATTMDQLKENIDAFTSAPRpLAPEVLDDIESLF 396
Cdd:cd19158 283 SVLLGASNAEQLMENIGAIQVLPK-LSSSIVHEIDSIL 319
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
61-376 |
2.26e-37 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 136.19 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTF------GEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKPRDKIIlATK 134
Cdd:cd19088 1 VSRLGYGAMRLtgpgiwGPPADREEAIAVLRRALELGVNFIDTADSY-------GPDVNERLIAEALHPYPDDVVI-ATK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 135 VSgyserstFLRDNAKVVRVDA--ANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKA 212
Cdd:cd19088 73 GG-------LVRTGPGWWGPDGspEYLRQAVEASLRRLGLDRIDLYQLHRID-----------------PKVPFEEQLGA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 213 FQELIDEGKVRYIGVSNETSYGVmefvhaAKVQGLPKIVSIQNSYSLIVRCHFEVdlVEVCHPNncNVGLLAYSPLAGGV 292
Cdd:cd19088 129 LAELQDEGLIRHIGLSNVTVAQI------EEARAIVRIVSVQNRYNLANRDDEGV--LDYCEAA--GIAFIPWFPLGGGD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 293 LTGkyidtnpdiskksrlnlfpgymeryNASLAKEatneyvkLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKE 372
Cdd:cd19088 199 LAQ-------------------------PGGLLAE-------VAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEE 246
|
....
gi 1002248734 373 NIDA 376
Cdd:cd19088 247 NLAA 250
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
49-377 |
2.69e-37 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 137.20 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTFGEQN-TEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP-- 125
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDlSPAEAAALIEAALELGITTFDHADIY-------GGYTCEALFGEALKLSPsl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 126 RDKIILATKVSgysersTFLRDNAKVVRV-----DAANIKESVEKSLSRLSTDYIDLLQIHWPDryvPLFgeycyNPtkw 200
Cdd:COG4989 74 REKIELQTKCG------IRLPSEARDNRVkhydtSKEHIIASVEGSLRRLGTDYLDLLLLHRPD---PLM-----DP--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 201 rpsvpfEEQLKAFQELIDEGKVRYIGVSNETSYGvMEFVHAAKVQglpKIVSIQNSYSLIVRCHFEVDLVEVCHPNncNV 280
Cdd:COG4989 137 ------EEVAEAFDELKASGKVRHFGVSNFTPSQ-FELLQSALDQ---PLVTNQIELSLLHTDAFDDGTLDYCQLN--GI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 281 GLLAYSPLAGGVLTGkyiDTNPDIskksrlnlfpgymERYNASLAkeatneyvKLAKKHGLTPVQLALGFVRDRPFTAST 360
Cdd:COG4989 205 TPMAWSPLAGGRLFG---GFDEQF-------------PRLRAALD--------ELAEKYGVSPEAIALAWLLRHPAGIQP 260
|
330
....*....|....*..
gi 1002248734 361 IIGATTMDQLKENIDAF 377
Cdd:COG4989 261 VIGTTNPERIKAAAAAL 277
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
49-376 |
3.08e-37 |
|
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: 137.57 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTMTF----GEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprketQGRTDLyIGSWMQSK 124
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLsafyGPPKPDEERFAVLDAAFELGCTFWDTADIY--------GDSEEL-IGRWFKQN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 P--RDKIILATKVSGYSERSTflrdNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrP 202
Cdd:cd19144 72 PgkREKIFLATKFGIEKNVET----GEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVD-----------------G 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 203 SVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEfvhAAKVQglpKIVSIQNSYSlivrcHFEVD-------LVEVCHP 275
Cdd:cd19144 131 KTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRR---AHAVH---PIAAVQIEYS-----PFSLDierpeigVLDTCRE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 276 NncNVGLLAYSPLAGGVLTGKYidtnpdiskKSRLNLFPGYMERYNASLAKEA-------TNEYVKLAKKHGLTPVQLAL 348
Cdd:cd19144 200 L--GVAIVAYSPLGRGFLTGAI---------RSPDDFEEGDFRRMAPRFQAENfpknlelVDKIKAIAKKKNVTAGQLTL 268
|
330 340
....*....|....*....|....*...
gi 1002248734 349 GFVRDRPFTASTIIGATTMDQLKENIDA 376
Cdd:cd19144 269 AWLLAQGDDIIPIPGTTKLKRLEENLGA 296
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
59-393 |
3.82e-37 |
|
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: 136.60 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 59 LVISEVTLGTMTF---GEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPPRKETQGrtdlYIGSWMQSKP--RDKIILAT 133
Cdd:cd19077 3 KLVGPIGLGLMGLtwrPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLK----LLARFFRKYPeyADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 134 KvsGYSERSTFLRDnakvvrVDAANIKESVEKSLSRL-STDYIDLlqihwpdryvplfgeycYNPTKWRPSVPFEEQLKA 212
Cdd:cd19077 79 K--GGLDPDTLRPD------GSPEAVRKSIENILRALgGTKKIDI-----------------FEPARVDPNVPIEETIKA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 213 FQELIDEGKVRYIGVSnETSYGVMEFVHAAKvqglpKIVSIQNSYSLIVRCHFEVDLVEVCHPNncNVGLLAYSPLAGGV 292
Cdd:cd19077 134 LKELVKEGKIRGIGLS-EVSAETIRRAHAVH-----PIAAVEVEYSLFSREIEENGVLETCAEL--GIPIIAYSPLGRGL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 293 LTGKY--IDTNPDISKKSRLNLFPGymERYNASLAKeaTNEYVKLAKKHGLTPVQLALGFVRDRPFTasTII---GATTM 367
Cdd:cd19077 206 LTGRIksLADIPEGDFRRHLDRFNG--ENFEKNLKL--VDALQELAEKKGCTPAQLALAWILAQSGP--KIIpipGSTTL 279
|
330 340
....*....|....*....|....*.
gi 1002248734 368 DQLKENIDAFTSAprpLAPEVLDDIE 393
Cdd:cd19077 280 ERVEENLKAANVE---LTDEELKEIN 302
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
62-376 |
5.12e-37 |
|
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: 135.05 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTM-TFGEQN--TEKEAHDILSYSFDQGVNILDTAEMYpvpprketqGRTDLYIGSWMQSKPRDKIILATKVSGY 138
Cdd:cd19095 1 SVLGLGTSgIGRVWGvpSEAEAARLLNTALDLGINLIDTAPAY---------GRSEERLGRALAGLRRDDLFIATKVGTH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 139 SERSTFLRDnakvvrVDAANIKESVEKSLSRLSTDYIDLLQIHwpdryvplfgeycyNPTKWRPSvpfEEQLKAFQELID 218
Cdd:cd19095 72 GEGGRDRKD------FSPAAIRASIERSLRRLGTDYIDLLQLH--------------GPSDDELT---GEVLETLEDLKA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 219 EGKVRYIGVSNETSygvmefvHAAKVQGLPKIVSIQNSYSLIVRchFEVDLVEVCHpnNCNVGLLAYSPLAGGVLTgkyi 298
Cdd:cd19095 129 AGKVRYIGVSGDGE-------ELEAAIASGVFDVVQLPYNVLDR--EEEELLPLAA--EAGLGVIVNRPLANGRLR---- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002248734 299 dtnpdiSKKSRLNLFPGYMERYNASLAKEATneyvklakkhglTPVQLALGFVRDRPFTASTIIGATTMDQLKENIDA 376
Cdd:cd19095 194 ------RRVRRRPLYADYARRPEFAAEIGGA------------TWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
57-378 |
1.42e-36 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 134.61 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 57 SDLVISEVTLGTMTFGEQNTE-KEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP--RDKIILAT 133
Cdd:cd19092 2 EGLEVSRLVLGCMRLADWGESaEELLSLIEAALELGITTFDHADIY-------GGGKCEELFGEALALNPglREKIEIQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 134 KVSgysERSTFLRDNAKVVRVD--AANIKESVEKSLSRLSTDYIDLLQIHWPDryvPLFgeycyNPtkwrpsvpfEEQLK 211
Cdd:cd19092 75 KCG---IRLGDDPRPGRIKHYDtsKEHILASVEGSLKRLGTDYLDLLLLHRPD---PLM-----DP---------EEVAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 212 AFQELIDEGKVRYIGVSNETSyGVMEFVHAAkvqgLP-KIVSIQNSYSLIVRCHFEVDLVEVCHPNncNVGLLAYSPLAG 290
Cdd:cd19092 135 AFDELVKSGKVRYFGVSNFTP-SQIELLQSY----LDqPLVTNQIELSLLHTEAIDDGTLDYCQLL--DITPMAWSPLGG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 291 GVLTGKYIDTNPDIskksrlnlfpgymeryNASLAkeatneyvKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQL 370
Cdd:cd19092 208 GRLFGGFDERFQRL----------------RAALE--------ELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERI 263
|
....*...
gi 1002248734 371 KENIDAFT 378
Cdd:cd19092 264 RSAVKALD 271
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
62-389 |
4.27e-36 |
|
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: 133.06 E-value: 4.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTFG---EQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprketqGRTDLYIGSWMQSKPRDKIILATKVSgy 138
Cdd:cd19090 1 SALGLGTAGLGgvfGGVDDDEAVATIRAALDLGINYIDTAPAY---------GDSEERLGLALAELPREPLVLSTKVG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 139 serstflRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRyVPLFGEYCYNPTkwrpsvpfeeqLKAFQELID 218
Cdd:cd19090 70 -------RLPEDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPER-VPWVDILAPGGA-----------LEALLELKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 219 EGKVRYIGVsnetsyGVME-FVHAAKVQ-GLPKIVSIQNSYSLIVRCHFEvDLVEVCHPNncNVGLLAYSPLAGGVLTGK 296
Cdd:cd19090 131 EGLIKHIGL------GGGPpDLLRRAIEtGDFDVVLTANRYTLLDQSAAD-ELLPAAARH--GVGVINASPLGMGLLAGR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 297 YidtnpdiskksrlNLFPGYMERYNASLAKEATNEYVKLAKKHGLTPVQLALGFV-RDrPFTASTIIGATTMDQLKENId 375
Cdd:cd19090 202 P-------------PERVRYTYRWLSPELLDRAKRLYELCDEHGVPLPALALRFLlRD-PRISTVLVGASSPEELEQNV- 266
|
330
....*....|....
gi 1002248734 376 afTSAPRPLAPEVL 389
Cdd:cd19090 267 --AAAEGPLPEELW 278
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-396 |
1.05e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 133.54 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 50 QYRKLGDSDLVISEVTLGTMTFGE---QNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKPr 126
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGGlmgRTTREEQIAAVRRALDLGINFFDTAPSY-------GDGKSEENLGRALKGLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 127 DKIILATKVsgyserstflrdnakvvRVDAAN-------IKESVEKSLSRLSTDYIDLLQIH---WPDRYVPLFGEYcyn 196
Cdd:cd19104 73 AGPYITTKV-----------------RLDPDDlgdiggqIERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVGGTL--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 197 PTKWrpSVPFEEQLKAFQELIDEGKVRYIGVsneTSYGVMEFVHAAKVQGLPKivSIQNSYSLI--------VRCHFEVD 268
Cdd:cd19104 133 STTD--VLGLGGVADAFERLRSEGKIRFIGI---TGLGNPPAIRELLDSGKFD--AVQVYYNLLnpsaaearPRGWSAQD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 269 ---LVEVCHPNncNVGLLAYSPLAGGVLTGKyIDTNPDISKKSRLNLFPGYmerynaSLAKeatnEYVKLAKKHGLTPVQ 345
Cdd:cd19104 206 yggIIDAAAEH--GVGVMGIRVLAAGALTTS-LDRGREAPPTSDSDVAIDF------RRAA----AFRALAREWGETLAQ 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1002248734 346 LALGFVRDRPFTASTIIGATTMDQLKENIDAftSAPRPLAPEVLDDIESLF 396
Cdd:cd19104 273 LAHRFALSNPGVSTVLVGVKNREELEEAVAA--EAAGPLPAENLARLEALW 321
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
49-396 |
1.42e-35 |
|
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: 133.24 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGT-MTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP-- 125
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVY-------AAGKAEVILGSIIKKKGwr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 126 RDKIILATKV--SGYSERSTFLrdnakvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeycynptkwrpS 203
Cdd:cd19159 74 RSSLVITTKLywGGKAETERGL---------SRKHIIEGLKGSLQRLQLEYVDVVFANRPDS-----------------N 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 204 VPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHpnNCNVGLL 283
Cdd:cd19159 128 TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYH--KIGVGAM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 284 AYSPLAGGVLTGKYIDTNPDISKKSrLNLFPGYMERYNASLAKEATN---EYVKLAKKHGLTPVQLALGFVRDRPFTAST 360
Cdd:cd19159 206 TWSPLACGIISGKYGNGVPESSRAS-LKCYQWLKERIVSEEGRKQQNklkDLSPIAERLGCTLPQLAVAWCLRNEGVSSV 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 1002248734 361 IIGATTMDQLKENIDAFTSAPRpLAPEVLDDIESLF 396
Cdd:cd19159 285 LLGSSTPEQLIENLGAIQVLPK-MTSHVVNEIDNIL 319
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
61-394 |
4.63e-35 |
|
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: 131.78 E-value: 4.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFGEQNT-------EKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKP-RDKIILA 132
Cdd:cd19146 11 VSPLCLGAMSFGEAWKsmmgecdKETAFKLLDAFYEQGGNFIDTANNY-------QGEESERWVGEWMASRGnRDEMVLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 133 TKVS-GYSE------RSTFLRDNAKVVRVdaanikeSVEKSLSRLSTDYIDLLQIHWpdryvplfgeycynptkWRPSVP 205
Cdd:cd19146 84 TKYTtGYRRggpikiKSNYQGNHAKSLRL-------SVEASLKKLQTSYIDILYVHW-----------------WDYTTS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 206 FEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNNcnvglLAY 285
Cdd:cd19146 140 IPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFR-DFERDILPMCEAEG-----MAL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 286 SPLagGVLTGKYIDTNPDISKKSRLNLFPGYMERYNASLAKEATneyvKLAKKHGLTPVQLALGFVRDRPFTASTIIGAT 365
Cdd:cd19146 214 APW--GVLGQGQFRTEEEFKRRGRSGRKGGPQTEKERKVSEKLE----KVAEEKGTAITSVALAYVMHKAPYVFPIVGGR 287
|
330 340
....*....|....*....|....*....
gi 1002248734 366 TMDQLKENIDAFTSAprpLAPEVLDDIES 394
Cdd:cd19146 288 KVEHLKGNIEALGIS---LSDEEIQEIED 313
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
49-393 |
3.96e-34 |
|
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: 129.12 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 49 MQYRKLGDSDLVISEVTLGTM-TFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSK--P 125
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWsTFSTAISEEQAEEIVTLAYENGINYFDTSDAF-------TSGQAETELGRILKKKgwK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 126 RDKIILATKV---SGYSERStflrdnakvvrVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrP 202
Cdd:cd19142 74 RSSYIVSTKIywsYGSEERG-----------LSRKHIIESVRASLRRLQLDYIDIVIIHKAD-----------------P 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 203 SVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHpnNCNVGL 282
Cdd:cd19142 126 MCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYN--KVGVGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 283 LAYSPLAGGVLTGKYIDTNPDISKKSRL----------NLFPGYMERYNASLAkeatnEYVKLAKKHGLTPVQLALGFVR 352
Cdd:cd19142 204 ITWSPLSLGLDPGISEETRRLVTKLSFKsskykvgsdgNGIHEETRRASHKLR-----ELSLIAERLGCDLTQLLIAWSL 278
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002248734 353 DRPFTASTIIGATTMDQLKENIDAFTSAPRpLAPEVLDDIE 393
Cdd:cd19142 279 KNENVQCVLIGASSLEQLYSQLNSLQLLPK-LNSAVMEELE 318
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
72-394 |
4.24e-34 |
|
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: 128.48 E-value: 4.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 72 GEQNTEKEA-HDILSYsFDQGVNILDTAEMYpvpprketqGRTDLYIG----SWM-QSKPRDKIILATKVSGYSERSTfl 145
Cdd:cd19101 17 GGIRDEDAAvRAMAAY-VDAGLTTFDCADIY---------GPAEELIGefrkRLRrERDAADDVQIHTKWVPDPGELT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 146 rdnakvvrVDAANIKESVEKSLSRLSTDYIDLLQIHWpdryvplfgeycynptkWRPSVP-FEEQLKAFQELIDEGKVRY 224
Cdd:cd19101 85 --------MTRAYVEAAIDRSLKRLGVDRLDLVQFHW-----------------WDYSDPgYLDAAKHLAELQEEGKIRH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 225 IGVSNetsygvMEFVHAAK-VQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAGGVLTGKYIDTNPd 303
Cdd:cd19101 140 LGLTN------FDTERLREiLDAGVPIVSNQVQYSLLDR-RPENGMAALCEDH--GIKLLAYGTLAGGLLSEKYLGVPE- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 304 iskksrlnlfPGYMERYNASLAK-----------EATNEYVKL----AKKHGLTPVQLALGFVRDRPFTASTIIGATTMD 368
Cdd:cd19101 210 ----------PTGPALETRSLQKyklmidewggwDLFQELLRTlkaiADKHGVSIANVAVRWVLDQPGVAGVIVGARNSE 279
|
330 340
....*....|....*....|....*.
gi 1002248734 369 QLKENIDAFTSAprpLAPEVLDDIES 394
Cdd:cd19101 280 HIDDNVRAFSFR---LDDEDRAAIDA 302
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
66-403 |
2.60e-33 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 125.17 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 66 LGTMtfgeQNTEKEAHDILSYSFDQGVNILDTAEMYpvppRKETQ-GR----TDLyigswmqskPRDKIILATKVSGyse 140
Cdd:COG0656 10 LGTW----QLPGEEAAAAVRTALEAGYRHIDTAAMY----GNEEGvGEaiaaSGV---------PREELFVTTKVWN--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 141 rstflrDNAkvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPdryvplfgeycynptkwrPSVPFEEQLKAFQELIDEG 220
Cdd:COG0656 70 ------DNH-----GYDDTLAAFEESLERLGLDYLDLYLIHWP------------------GPGPYVETWRALEELYEEG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 221 KVRYIGVSNETSYGVMEFVHAAKVqglpKIVSIQnsysliVRCH--F-EVDLVEVCHPNncNVGLLAYSPLA-GGVLtgk 296
Cdd:COG0656 121 LIRAIGVSNFDPEHLEELLAETGV----KPAVNQ------VELHpyLqQRELLAFCREH--GIVVEAYSPLGrGKLL--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 297 yidTNPDIskksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRPFTAstIIGATTMDQLKENIDA 376
Cdd:COG0656 186 ---DDPVL----------------------------AEIAEKHGKTPAQVVLRWHLQRGVVV--IPKSVTPERIRENLDA 232
|
330 340 350
....*....|....*....|....*....|
gi 1002248734 377 FTSAprpLAPEVLDDIESLFKRYR---DPT 403
Cdd:COG0656 233 FDFE---LSDEDMAAIDALDRGERlgpDPD 259
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
66-376 |
3.36e-33 |
|
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: 125.05 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 66 LGTMTFGEQ----NTEKEAhdiLSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSkPRDKIILATKVsgyser 141
Cdd:cd19138 16 QGTWYMGEDpakrAQEIEA---LRAGIDLGMTLIDTAEMY-------GDGGSEELVGEAIRG-RRDKVFLVSKV------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 142 stfLRDNAkvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWpdryvplfgeycynptkwRPSVPFEEQLKAFQELIDEGK 221
Cdd:cd19138 79 ---LPSNA-----SRQGTVRACERSLRRLGTDYLDLYLLHW------------------RGGVPLAETVAAMEELKKEGK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 222 VRYIGVSNetsYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAGGVLTGKYIDTN 301
Cdd:cd19138 133 IRAWGVSN---FDTDDMEELWAVPGGGNCAANQVLYNLGSR-GIEYDLLPWCREH--GVPVMAYSPLAQGGLLRRGLLEN 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002248734 302 PDISkksrlnlfpgymerynaslakeatneyvKLAKKHGLTPVQLALGFVRDRPFTAStIIGATTMDQLKENIDA 376
Cdd:cd19138 207 PTLK----------------------------EIAARHGATPAQVALAWVLRDGNVIA-IPKSGSPEHARENAAA 252
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
62-381 |
4.86e-32 |
|
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: 121.87 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTFG---------EQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprketqGRTDLYIGSWMQSKPRDKIIla 132
Cdd:cd19097 1 SKLALGTAQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY---------GDSEKVLGKFLKRLDKFKII-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 133 TKvsgyserstfLRDNAKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRYvplfgeycynpTKWRPSVpfeeqLKA 212
Cdd:cd19097 70 TK----------LPPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDL-----------LKHGGKL-----VEA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 213 FQELIDEGKVRYIGVSnetsygVMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVchPNNCNVGLLAYSPLAGGV 292
Cdd:cd19097 124 LLELKKEGLIRKIGVS------VYSPEELEKALESFKIDIIQLPFNILDQRFLKSGLLAK--LKKKGIEIHARSVFLQGL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 293 LTgkyidtnpdiSKKSRLnlfPGYMERynaslAKEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKE 372
Cdd:cd19097 196 LL----------MEPDKL---PAKFAP-----AKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKE 257
|
....*....
gi 1002248734 373 NIDAFTSAP 381
Cdd:cd19097 258 IIAAFKKPP 266
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
66-377 |
6.53e-32 |
|
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: 121.22 E-value: 6.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 66 LGTMTFgeQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprketqgRTDLYIGSWMQ--SKPRDKIILATKVsgyserst 143
Cdd:cd19073 4 LGLGTW--QLRGDDCANAVKEALELGYRHIDTAEIY----------NNEAEVGEAIAesGVPREDLFITTKV-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 144 fLRDNakvvrVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAFQELIDEGKVR 223
Cdd:cd19073 64 -WRDH-----LRPEDLKKSVDRSLEKLGTDYVDLLLIHWPN-----------------PTVPLEETLGALKELKEAGKVK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 224 YIGVSNETSYGVMEfvhAAKVQGLPkIVSIQnsysliVRCH---FEVDLVEVCHPNncNVGLLAYSPLA-GGVLtgkyid 299
Cdd:cd19073 121 SIGVSNFTIELLEE---ALDISPLP-IAVNQ------VEFHpflYQAELLEYCREN--DIVITAYSPLArGEVL------ 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002248734 300 TNPDIskksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRPFTAstIIGATTMDQLKENIDAF 377
Cdd:cd19073 183 RDPVI----------------------------QEIAEKYDKTPAQVALRWLVQKGIVV--IPKASSEDHLKENLAIF 230
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
61-390 |
1.20e-30 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 118.06 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFG-----EQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKPRDKIILATKV 135
Cdd:cd19137 4 IPALGLGTWGIGgfltpDYSRDEEMVELLKTAIELGYTHIDTAEMY-------GGGHTEELVGKAIKDFPREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 136 sgyseRSTFLRDNakvvrvdaaNIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAFQE 215
Cdd:cd19137 77 -----WPTNLRYD---------DLLRSLQNSLRRLDTDYIDLYLIHWPN-----------------PNIPLEETLSAMAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 216 LIDEGKVRYIGVSNETsygvMEFVHAAKVQGLPKIVSIQNSYSLIVRCHFEVDLVEVCHPNncNVGLLAYSPLAGGVltg 295
Cdd:cd19137 126 GVRQGLIRYIGVSNFN----RRLLEEAISKSQTPIVCNQVKYNLEDRDPERDGLLEYCQKN--GITVVAYSPLRRGL--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 296 kyidtnpdiskksrlnlfpgymerynaslakEATNEYVK-LAKKHGLTPVQLALGFVRDRPfTASTIIGATTMDQLKENI 374
Cdd:cd19137 197 -------------------------------EKTNRTLEeIAKNYGKTIAQIALAWLIQKP-NVVAIPKAGRVEHLKENL 244
|
330
....*....|....*.
gi 1002248734 375 DAFTSAPRPLAPEVLD 390
Cdd:cd19137 245 KATEIKLSEEEMKLLD 260
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
50-376 |
4.66e-28 |
|
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: 112.16 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 50 QYRKLGDSDLVISEVTLGTM-TFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPP--RKETQGR---TDLyigswmqS 123
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWhNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPgsAEENFGRilrEDF-------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 124 KPRDKIILATKvSGYS----------ERSTFLrdnakvvrvdaanikESVEKSLSRLSTDYIDLLQIHWPDryvplfgey 193
Cdd:cd19150 74 GYRDELIISTK-AGYDmwpgpygewgSRKYLL---------------ASLDQSLKRMGLDYVDIFYSHRFD--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 194 cynptkwrPSVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSiQNSYSLIVRCHFEVDLVEVC 273
Cdd:cd19150 129 --------PDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELGTPLLIH-QPSYNMLNRWVEESGLLDTL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 274 HPNNcnVGLLAYSPLAGGVLTGKYIDTNPDISKKSRLNLFpgymeryNASLAKEATNEYVK----LAKKHGLTPVQLALG 349
Cdd:cd19150 200 QELG--VGCIAFTPLAQGLLTDKYLNGIPEGSRASKERSL-------SPKMLTEANLNSIRalneIAQKRGQSLAQMALA 270
|
330 340
....*....|....*....|....*..
gi 1002248734 350 FVRDRPFTASTIIGATTMDQLKENIDA 376
Cdd:cd19150 271 WVLRDGRVTSALIGASRPEQLEENVGA 297
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
50-376 |
4.78e-28 |
|
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: 112.11 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 50 QYRKLGDSDLVISEVTLGTM-TFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPP--RKETQGR---TDLyigswmqs 123
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWhNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPgsAEENFGRilkEDL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 124 KP-RDKIILATKvSGYSERSTFLRDNAKvvrvdAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrP 202
Cdd:cd19151 73 KPyRDELIISTK-AGYTMWPGPYGDWGS-----KKYLIASLDQSLKRMGLDYVDIFYHHRPD-----------------P 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 203 SVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSiQNSYSLIVRcHFEVDLVEVCHPNNcnVGL 282
Cdd:cd19151 130 ETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLGTPCLIH-QPKYSMFNR-WVEEGLLDVLEEEG--IGC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 283 LAYSPLAGGVLTGKYIDTNPDISKKSRLNLFpgymerynasLAKE-ATNEYV-------KLAKKHGLTPVQLALGFVRDR 354
Cdd:cd19151 206 IAFSPLAQGLLTDRYLNGIPEDSRAAKGSSF----------LKPEqITEEKLakvrrlnEIAQARGQKLAQMALAWVLRN 275
|
330 340
....*....|....*....|..
gi 1002248734 355 PFTASTIIGATTMDQLKENIDA 376
Cdd:cd19151 276 KRVTSVLIGASKPSQIEDAVGA 297
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
48-379 |
5.07e-28 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 113.16 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 48 QMQYRKLGDSDLVISEVTLGTM-TFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVPPrketqGRTDLYIGSWMQS--K 124
Cdd:PRK09912 12 QMQYRYCGKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPP-----GSAEENFGRLLREdfA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 P-RDKIILATKvSGY----------SERSTFLrdnakvvrvdaanikESVEKSLSRLSTDYIDLLQIHWPDRyvplfgey 193
Cdd:PRK09912 87 AyRDELIISTK-AGYdmwpgpygsgGSRKYLL---------------ASLDQSLKRMGLEYVDIFYSHRVDE-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 194 cynptkwrpSVPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSiQNSYSLIVRCHFEVDLVEVC 273
Cdd:PRK09912 143 ---------NTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIH-QPSYNLLNRWVDKSGLLDTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 274 HPNncNVGLLAYSPLAGGVLTGKYIDTNPDiskKSRLNLFPGYMERYNASLAKEATNEYVKL----AKKHGLTPVQLALG 349
Cdd:PRK09912 213 QNN--GVGCIAFTPLAQGLLTGKYLNGIPQ---DSRMHREGNKVRGLTPKMLTEANLNSLRLlnemAQQRGQSMAQMALS 287
|
330 340 350
....*....|....*....|....*....|
gi 1002248734 350 FVRDRPFTASTIIGATTMDQLKENIDAFTS 379
Cdd:PRK09912 288 WLLKDERVTSVLIGASRAEQLEENVQALNN 317
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
125-377 |
1.87e-27 |
|
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: 109.11 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 PRDKIILATKVSgyserSTFLrdnakvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPdryvplfgeycYNPTKWRPSV 204
Cdd:cd19071 53 PREELFITTKLW-----PTDH---------GYERVREALEESLKDLGLDYLDLYLIHWP-----------VPGKEGGSKE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 205 PFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVqglpKIVSIQnsysliVRCH---FEVDLVEVCHPNncNVG 281
Cdd:cd19071 108 ARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARI----KPAVNQ------IELHpylQQKELVEFCKEH--GIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 282 LLAYSPLAGGVLTGKyidTNPDIskksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRPFtaSTI 361
Cdd:cd19071 176 VQAYSPLGRGRRPLL---DDPVL----------------------------KEIAKKYGKTPAQVLLRWALQRGV--VVI 222
|
250
....*....|....*.
gi 1002248734 362 IGATTMDQLKENIDAF 377
Cdd:cd19071 223 PKSSNPERIKENLDVF 238
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
62-380 |
2.59e-27 |
|
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: 108.80 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTF----GEQNTEKEAHDILSYSFDQGVNILDTAEMYPvpprketQGRTDLYIGSWMQSKPRDKIILATKVSG 137
Cdd:cd19096 1 SVLGFGTMRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYG-------GGKSEEILGEALKEGPREKFYLATKLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 138 YSERStflrdnakvvrvdAANIKESVEKSLSRLSTDYIDLLQIHWPDRYvplfgeycYNPTKWRPSVPFEeqlkAFQELI 217
Cdd:cd19096 74 WSVKS-------------AEDFRRILEESLKRLGVDYIDFYLLHGLNSP--------EWLEKARKGGLLE----FLEKAK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 218 DEGKVRYIGVSNETSYGV-MEFVHAAKVQGlpkiVSIQnsYSLIVRCHFE-VDLVEVCHPNncNVGLLAYSPLAGGVLtg 295
Cdd:cd19096 129 KEGLIRHIGFSFHDSPELlKEILDSYDFDF----VQLQ--YNYLDQENQAgRPGIEYAAKK--GMGVIIMEPLKGGGL-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 296 kyidtnpdiskksrlnlfpgymerynASLAKEAtneyVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKENID 375
Cdd:cd19096 199 --------------------------ANNPPEA----LAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIA 248
|
....*
gi 1002248734 376 AFTSA 380
Cdd:cd19096 249 AADEF 253
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
66-395 |
8.07e-27 |
|
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: 107.34 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 66 LGTMtfgeQNTEKEAHDILSYSFDQGVNILDTAEMYpvppRKETQgrtdlyIGSWM-QSK-PRDKIILATKVsgyserst 143
Cdd:cd19140 13 LGTY----PLTGEECTRAVEHALELGYRHIDTAQMY----GNEAQ------VGEAIaASGvPRDELFLTTKV-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 144 fLRDNAKVVRVdaaniKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkwrPSVPFEEQLKAFQELIDEGKVR 223
Cdd:cd19140 71 -WPDNYSPDDF-----LASVEESLRKLRTDYVDLLLLHWPN-----------------KDVPLAETLGALNEAQEAGLAR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 224 YIGVSNETSYGVMEfvhAAKVQGLPkIVSIQnsysliVRCHF---EVDLVEVCHPNNCnvGLLAYSPLAGGvltgkyidt 300
Cdd:cd19140 128 HIGVSNFTVALLRE---AVELSEAP-LFTNQ------VEYHPyldQRKLLDAAREHGI--ALTAYSPLARG--------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 301 npdiskksrlnlfpgymerynaslakEATNEYV--KLAKKHGLTPVQLALGFVRDRPFTAStIIGATTMDQLKENIDAFT 378
Cdd:cd19140 187 --------------------------EVLKDPVlqEIGRKHGKTPAQVALRWLLQQEGVAA-IPKATNPERLEENLDIFD 239
|
330
....*....|....*..
gi 1002248734 379 SAprpLAPEVLDDIESL 395
Cdd:cd19140 240 FT---LSDEEMARIAAL 253
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
61-393 |
1.16e-25 |
|
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: 106.06 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFGEQNT-------EKEAHDILSYSFDQGVNILDTAEMYpvpprKETQGRTdlYIGSWMQS-KPRDKIILA 132
Cdd:cd19147 10 VSPLILGAMSIGDAWSgfmgsmdKEQAFELLDAFYEAGGNFIDTANNY-----QDEQSET--WIGEWMKSrKNRDQIVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 133 TKVSGYSERStflrDNAKVVRVD-AANIKE----SVEKSLSRLSTDYIDLLQIHWPDryvplfgeycynptkWRPSVpfE 207
Cdd:cd19147 83 TKFTTDYKAY----EVGKGKAVNyCGNHKRslhvSVRDSLRKLQTDWIDILYVHWWD---------------YTTSI--E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 208 EQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLIVRcHFEVDLVEVCHpnNCNVGLLAYSP 287
Cdd:cd19147 142 EVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNR-DFERDIIPMAR--HFGMALAPWDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 288 LAGGVLTGKyiDTNPDISKKSR-LNLFPGYMERYNASLAkeATNEYVKLAKKHGLTPVQ-LALGFVRDRPFTASTIIGAT 365
Cdd:cd19147 219 LGGGKFQSK--KAVEERKKNGEgLRSFVGGTEQTPEEVK--ISEALEKVAEEHGTESVTaIALAYVRSKAPNVFPLVGGR 294
|
330 340
....*....|....*....|....*...
gi 1002248734 366 TMDQLKENIDAFTSAprpLAPEVLDDIE 393
Cdd:cd19147 295 KIEHLKDNIEALSIK---LTPEEIEYLE 319
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
67-376 |
2.04e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 104.72 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 67 GTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYPVpprketqGRTDLYIGSWMQSKPRDKIILATKvsgYSERSTFLR 146
Cdd:cd19103 21 GDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGM-------GASEKILGEFLKRYPREDYIISTK---FTPQIAGQS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 147 DNAkvvrvdaanIKESVEKSLSRLSTDYIDLLQIHwpdryvplfgeycyNPT---KWRPsvpfeeqlkafqELID---EG 220
Cdd:cd19103 91 ADP---------VADMLEGSLARLGTDYIDIYWIH--------------NPAdveRWTP------------ELIPllkSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 221 KVRYIGVSN---ETSYGVMEFVHAAKVqglpKIVSIQNSYSLIVRCHFEVDLVEVCHPNncNVGLLAYSPLAGGVLTGKY 297
Cdd:cd19103 136 KVKHVGVSNhnlAEIKRANEILAKAGV----SLSAVQNHYSLLYRSSEEAGILDYCKEN--GITFFAYMVLEQGALSGKY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 298 IDTNPDISKKSRLnlfpgymERYNASLAK--EATNEYVKLAKKHGLTPVQLALGFVRDRPFTAstIIGATTMDQLKENID 375
Cdd:cd19103 210 DTKHPLPEGSGRA-------ETYNPLLPQleELTAVMAEIGAKHGASIAQVAIAWAIAKGTTP--IIGVTKPHHVEDAAR 280
|
.
gi 1002248734 376 A 376
Cdd:cd19103 281 A 281
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
62-392 |
1.58e-22 |
|
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: 96.66 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTFGEQN--TEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKPRDKIILATKVSGYS 139
Cdd:cd19162 1 PRLGLGAASLGNLAraGEDEAAATLDAAWDAGIRYFDTAPLY-------GLGLSERRLGAALARHPRAEYVVSTKVGRLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 140 ERSTFLRDNAKVVRVD--AANIKESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeycynptkwRPSVPFEEQLKAFQELI 217
Cdd:cd19162 74 EPGAAGRPAGADRRFDfsADGIRRSIEASLERLGLDRLDLVFLHDPDR---------------HLLQALTDAFPALEELR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 218 DEGKVRYIGVSNETSYGVMEFVHAAKVQglpkIVSIQNSYSLIVRcHFEVDLVEVCHPNncNVGLLAYSPLAGGVLTGKy 297
Cdd:cd19162 139 AEGVVGAIGVGVTDWAALLRAARRADVD----VVMVAGRYTLLDR-RAATELLPLCAAK--GVAVVAAGVFNSGILATD- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 298 iDTNPDiskksrlnlfpgymeRYNASLA----KEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKEN 373
Cdd:cd19162 211 -DPAGD---------------RYDYRPAtpevLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDN 274
|
330
....*....|....*....
gi 1002248734 374 IDAftsAPRPLAPEVLDDI 392
Cdd:cd19162 275 LAL---LRTPIPAEFWAEL 290
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
62-380 |
2.22e-22 |
|
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: 96.63 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 62 SEVTLGTMTFGEQN---TEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIGSWMQSKPRDKIILATKVSgy 138
Cdd:cd19161 1 SELGLGTAGLGNLYtavSNADADATLDAAWDSGIRYFDTAPMY-------GHGLAEHRLGDFLREKPRDEFVLSTKVG-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 139 sERSTFLRDNAKVVRVDAAN--------------IKESVEKSLSRLSTDYIDLLQIHWPDRYV-------PLFGEYCynp 197
Cdd:cd19161 72 -RLLKPAREGSVPDPNGFVDplpfeivydysydgIMRSFEDSLQRLGLNRIDILYVHDIGVYThgdrkerHHFAQLM--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 198 tkwrpsvpfEEQLKAFQELIDEGKVRYIGVsnetsyGVMEF--VHAAKVQGLPKIVSIQNSYSLIVRCHfEVDLVEVCHP 275
Cdd:cd19161 148 ---------SGGFKALEELKKAGVIKAFGL------GVNEVqiCLEALDEADLDCFLLAGRYSLLDQSA-EEEFLPRCEQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 276 NNcnVGLLAYSPLAGGVL-TGK-------YIDTNPDISKKsrlnlfpgymerynaslakeaTNEYVKLAKKHGLTPVQLA 347
Cdd:cd19161 212 RG--TSLVIGGVFNSGILaTGTksgakfnYGDAPAEIISR---------------------VMEIEKICDAYNVPLAAAA 268
|
330 340 350
....*....|....*....|....*....|...
gi 1002248734 348 LGFVRDRPFTASTIIGATTMDQLKENIDAFTSA 380
Cdd:cd19161 269 LQFPLRHPAVASVLTGARNPAQLRQNVEAFQTD 301
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
59-375 |
3.09e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 93.15 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 59 LVISEVTLGTMTFGEQ-NTEKEAHDILSYSFDQGVNILDTAEMYpvpprkeTQGRTDLYIG----SWMQSK--PRDKIIL 131
Cdd:cd19099 1 LTLSSLGLGTYRGDSDdETDEEYREALKAALDSGINVIDTAINY-------RGGRSERLIGkalrELIEKGgiKRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 132 ATKVsGY---------SERSTFLR--DNAKVVRVDAAN---------IKESVEKSLSRLSTDYIDLLQIHWPDRYVPlfg 191
Cdd:cd19099 74 VTKA-GYipgdgdeplRPLKYLEEklGRGLIDVADSAGlrhcispayLEDQIERSLKRLGLDTIDLYLLHNPEEQLL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 192 EYCYNPTKWRpsvpFEEQLKAFQELIDEGKVRYIGVSNETSYGVM----------EFVHAAKVQG--LPKIVSIQNSYSL 259
Cdd:cd19099 150 ELGEEEFYDR----LEEAFEALEEAVAEGKIRYYGISTWDGFRAPpalpghlsleKLVAAAEEVGgdNHHFKVIQLPLNL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 260 I-----VRCHFEVD----LVEVCHPNncNVGLLAYSPLAGGVLTGkyidtnpdiskKSRLNLFPgymerynaslakeatn 330
Cdd:cd19099 226 LepealTEKNTVKGealsLLEAAKEL--GLGVIASRPLNQGQLLG-----------ELRLADLL---------------- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1002248734 331 eyvklAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKENID 375
Cdd:cd19099 277 -----ALPGGATLAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
66-377 |
6.78e-21 |
|
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: 92.29 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 66 LGTMTFG---EQNTEKEAHDILSYSFDQGVNILDTAEMYPVpprketqGRTDLYIGSWMQSKPRDKIILATKV------- 135
Cdd:cd19152 5 FGTAPLGnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGA-------GLSEERLGAALRELGREDYVISTKVgrllvpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 136 SGYSERSTFLRDNAKVVRVD----AANIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLFGEYCYNPTKWRPSVPfeeqlk 211
Cdd:cd19152 78 QEVEPTFEPGFWNPLPFDAVfdysYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKGAFR------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 212 AFQELIDEGKVRYIGV-SNETSYgVMEFVHAAKvqglPKIVSIQNSYSLIvrcHF--EVDLVEVCHPNncNVGLLAYSPL 288
Cdd:cd19152 152 ALEELREEGVIKAIGLgVNDWEV-ILRILEEAD----LDWVMLAGRYTLL---DHsaARELLPECEKR--GVKVVNAGPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 289 AGGVLTG-------KYIDTNPDISKKSRlnlfpgymeRYNAslakeatneyvkLAKKHGLTPVQLALGFVRDRPFTASTI 361
Cdd:cd19152 222 NSGFLAGgdnfdyyEYGPAPPELIARRD---------RIEA------------LCEQHGVSLAAAALQFALAPPAVASVA 280
|
330
....*....|....*.
gi 1002248734 362 IGATTMDQLKENIDAF 377
Cdd:cd19152 281 PGASSPERVEENVALL 296
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
51-403 |
7.11e-19 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 86.37 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 51 YRKLGDSDLVISEVTLGTMTFGE---QNTEKEAHDILSYSFDQGVNILDTAEMYpvpprKETQGRTDLYIGSWMQSKPRD 127
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSvfgPVSEEDAIASVREAFRLGINFFDTSPYY-----GGTLSEKVLGKALKALGIPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 128 KIILATKVSGYSERSTFlrdnakvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplFGEYcynptkwrpSVPFE 207
Cdd:PLN02587 76 KYVVSTKCGRYGEGFDF----------SAERVTKSVDESLARLQLDYVDILHCHDIE-----FGSL---------DQIVN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 208 EQLKAFQELIDEGKVRYIGVSNETsYGVMEFVhAAKVQglPKIVSIQNSYslivrCHFEVD---LVE-VCHPNNCNVGLL 283
Cdd:PLN02587 132 ETIPALQKLKESGKVRFIGITGLP-LAIFTYV-LDRVP--PGTVDVILSY-----CHYSLNdssLEDlLPYLKSKGVGVI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 284 AYSPLAGGVLTGKyidtnpdiskksrlnlfpGYMERYNASLA-KEATNEYVKLAKKHGLTPVQLALGFVRDRPFTASTII 362
Cdd:PLN02587 203 SASPLAMGLLTEN------------------GPPEWHPAPPElKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLV 264
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1002248734 363 GATTMDQLKENIDAFTSAPRP-LAPEVLDDIESLFKRYRDPT 403
Cdd:PLN02587 265 GMNSVQQVEENVAAATELETSgIDEELLSEVEAILAPVKNKT 306
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
64-400 |
9.22e-19 |
|
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: 85.93 E-value: 9.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 64 VTLGTMtfgeQNTEKEAHDILSYSFDQGVNILDTAEMYpvppRKETQgrtdlyIGSWMQ------SKPRDKIILATKVSg 137
Cdd:cd19154 15 IGLGTW----QSKGAEGITAVRTALKAGYRLIDTAFLY----QNEEA------IGEALAelleegVVKREDLFITTKLW- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 138 yserSTFLRdnakvvrvdAANIKESVEKSLSRLSTDYIDLLQIHWP-------DRYVPLFGEYCYnptkwRPSVPFEEQL 210
Cdd:cd19154 80 ----THEHA---------PEDVEEALRESLKKLQLEYVDLYLIHAPaafkddeGESGTMENGMSI-----HDAVDVEDVW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 211 KAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVqglpKIVSIQnsysliVRCHF---EVDLVEVCHPNncNVGLLAYSP 287
Cdd:cd19154 142 RGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARV----KPHNNQ------VECHLyfpQKELVEFCKKH--NISVTSYAT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 288 LAGgvlTGKYIDTNPDISKKSRLNLfpgymeryNASLAKEatneyvkLAKKHGLTPVQLALGFVRDRpfTASTIIGATTM 367
Cdd:cd19154 210 LGS---PGRANFTKSTGVSPAPNLL--------QDPIVKA-------IAEKHGKTPAQVLLRYLLQR--GIAVIPKSATP 269
|
330 340 350
....*....|....*....|....*....|...
gi 1002248734 368 DQLKENIDAFTSAprpLAPEVLDDIESLFKRYR 400
Cdd:cd19154 270 SRIKENFNIFDFS---LSEEDMATLEEIEKSLR 299
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
56-387 |
5.22e-18 |
|
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: 83.87 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 56 DSDLVISEVTLGTMTFGEQ-NTEKEA---HDILSYSFDQGVNILDTAEMYpvpprketqGRTDLYIGSWMQS----KPRD 127
Cdd:cd19164 8 LSLAGLPPLIFGAATFSYQyTTDPESippVDIVRRALELGIRAFDTSPYY---------GPSEIILGRALKAlrdeFPRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 128 KIILATKVSGYSErSTFlrDNAKvvrvdaANIKESVEKSLSRLSTDYIDLLQIHwpDryVplfgEYcynptkwrpsVPFE 207
Cdd:cd19164 79 TYFIITKVGRYGP-DDF--DYSP------EWIRASVERSLRRLHTDYLDLVYLH--D--V----EF----------VADE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 208 EQLKAFQELI---DEGKVRYIGVSNETsygvmefvhaakvqgLPKIVSIQNsysLIVRCHFE-VDLV-EVCHPNNCNVGL 282
Cdd:cd19164 132 EVLEALKELFklkDEGKIRNVGISGYP---------------LPVLLRLAE---LARTTAGRpLDAVlSYCHYTLQNTTL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 283 LAY----------------SPLAGGVLTGKyidtnpdiskksrlnlfpGYMERYNASLA-KEATNEYVKLAKKHGLTPVQ 345
Cdd:cd19164 194 LAYipkflaaagvkvvlnaSPLSMGLLRSQ------------------GPPEWHPASPElRAAAAKAAEYCQAKGTDLAD 255
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1002248734 346 LALGFV-RDRPFTASTIIGATTMDQLKENIDAFTSAPRPLAPE 387
Cdd:cd19164 256 VALRYAlREWGGEGPTVVGCSNVDELEEAVEAYWSVLAGASEE 298
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
65-395 |
6.65e-18 |
|
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: 82.68 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 65 TLGTMTFGEQNTEkEAHDILSYSFDQGVNILDTAEMYpvpprketqgRTDLYIGSWMQ------SKPRDKIILATKVS-- 136
Cdd:cd19136 3 ILGLGTFRLRGEE-EVRQAVDAALKAGYRLIDTASVY----------RNEADIGKALRdllpkyGLSREDIFITSKLApk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 137 --GYsERSTflrdnakvvrvdaanikESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeycynpTKWRPSVPFEEQL---- 210
Cdd:cd19136 72 dqGY-EKAR-----------------AACLGSLERLGTDYLDLYLIHWPGV------------QGLKPSDPRNAELrres 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 211 -KAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQglPKIvsiqnsysLIVRCH---FEVDLVEVCHPNncNVGLLAYS 286
Cdd:cd19136 122 wRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVP--PAV--------NQVEFHphlVQKELLKFCKDH--GIHLQAYS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 287 PLagGVLTGKYIdTNPDIskksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRpfTASTIIGATT 366
Cdd:cd19136 190 SL--GSGDLRLL-EDPTV----------------------------LAIAKKYGRTPAQVLLRWALQQ--GIGVIPKSTN 236
|
330 340
....*....|....*....|....*....
gi 1002248734 367 MDQLKENIDAFTSaprPLAPEVLDDIESL 395
Cdd:cd19136 237 PERIAENIKVFDF---ELSEEDMAELNAL 262
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
51-377 |
1.41e-16 |
|
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: 79.63 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 51 YRKLGDSDLvISEVTLGTMTFGEQNTEKEAhdiLSYSFDQGVNILDTAEMYpvppRKETQgrtdlyIGSWMQSK------ 124
Cdd:cd19116 2 TIKLNDGNE-IPAIALGTWKLKDDEGVRQA---VKHAIEAGYRHIDTAYLY----GNEAE------VGEAIREKiaegvv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 PRDKIILATKVSG-YSERstflrdnAKVVRvdaanikeSVEKSLSRLSTDYIDLLQIHWPDRYVPLFGEYCYNPTKWRpS 203
Cdd:cd19116 68 KREDLFITTKLWNsYHER-------EQVEP--------ALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSLS-D 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 204 VPFEEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQglPKIVSIQNSYSLIvrchfEVDLVEVCHPNncNVGLL 283
Cdd:cd19116 132 IDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCNIK--PAVNQIEVHPTLT-----QEKLVAYCQSN--GIVVM 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 284 AYSPLaggvltGKYidtnpdisKKSRLNLFPGYMerYNASLakeatneyVKLAKKHGLTPVQLALGFVRDRPFTAstIIG 363
Cdd:cd19116 203 AYSPF------GRL--------VPRGQTNPPPRL--DDPTL--------VAIAKKYGKTTAQIVLRYLIDRGVVP--IPK 256
|
330
....*....|....
gi 1002248734 364 ATTMDQLKENIDAF 377
Cdd:cd19116 257 SSNKKRIKENIDIF 270
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
125-377 |
3.06e-16 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 78.00 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 PRDKIILATKV--SGYSERSTflrdnakvvrvdaaniKESVEKSLSRLSTDYIDLLQIHWPdryvplFGEYcynPTKWRp 202
Cdd:cd19133 62 PREELFITTKLwiQDAGYEKA----------------KKAFERSLKRLGLDYLDLYLIHQP------FGDV---YGAWR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 203 svpfeeqlkAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVqglpKIVSIQnsysliVRCH-F--EVDLVEVCHPNncN 279
Cdd:cd19133 116 ---------AMEELYKEGKIRAIGVSNFYPDRLVDLILHNEV----KPAVNQ------IETHpFnqQIEAVEFLKKY--G 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 280 VGLLAYSPLAGGvltgkyidtnpdiskksRLNLFpgymerynaslakeaTNE-YVKLAKKHGLTPVQLALGFVRDRPFta 358
Cdd:cd19133 175 VQIEAWGPFAEG-----------------RNNLF---------------ENPvLTEIAEKYGKSVAQVILRWLIQRGI-- 220
|
250
....*....|....*....
gi 1002248734 359 STIIGATTMDQLKENIDAF 377
Cdd:cd19133 221 VVIPKSVRPERIAENFDIF 239
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
159-377 |
1.02e-15 |
|
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: 77.00 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 159 IKESVEKSLSRLSTDYIDLLQIHWPDRY---VPLFGEYCYNPTkwrpsvPFEEQLKAFQELIDEGKVRYIGVSNETSYGV 235
Cdd:cd19125 87 VPPALEKTLKDLQLDYLDLYLIHWPVRLkkgAHMPEPEEVLPP------DIPSTWKAMEKLVDSGKVRAIGVSNFSVKKL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 236 MEFVHAAKVqglPKIVSiQnsysliVRCH---FEVDLVEVCHPNncNVGLLAYSPLAGGVLTGKYID--TNPDIskksrl 310
Cdd:cd19125 161 EDLLAVARV---PPAVN-Q------VECHpgwQQDKLHEFCKSK--GIHLSAYSPLGSPGTTWVKKNvlKDPIV------ 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002248734 311 nlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRpfTASTIIGATTMDQLKENIDAF 377
Cdd:cd19125 223 ----------------------TKVAEKLGKTPAQVALRWGLQR--GTSVLPKSTNEERIKENIDVF 265
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
158-400 |
1.10e-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: 77.04 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 158 NIKESVEKSLSRLSTDYIDLLQIHWPDRYVP---LF-----GEYCYNptkwrpSVPFEEQLKAFQELIDEGKVRYIGVSN 229
Cdd:cd19106 83 DVEPALRKTLKDLQLDYLDLYLIHWPYAFERgdnPFpknpdGTIRYD------STHYKETWKAMEKLVDKGLVKAIGLSN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 230 ETSYGVMEFVHAAKVQglPKIvsiqnsysLIVRCH---FEVDLVEVCHPNNCNVglLAYSPLAggvltgkyidtNPDisk 306
Cdd:cd19106 157 FNSRQIDDILSVARIK--PAV--------LQVECHpylAQNELIAHCKARGLVV--TAYSPLG-----------SPD--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 307 ksRLNLFPGymeryNASLAKEATneYVKLAKKHGLTPVQLALGFVRDRPFTasTIIGATTMDQLKENIDAFTSAprpLAP 386
Cdd:cd19106 211 --RPWAKPD-----EPVLLEEPK--VKALAKKYNKSPAQILLRWQVQRGVV--VIPKSVTPSRIKQNIQVFDFT---LSP 276
|
250
....*....|....
gi 1002248734 387 EVLDDIESLFKRYR 400
Cdd:cd19106 277 EEMKQLDALNRNWR 290
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
77-400 |
1.54e-15 |
|
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: 76.12 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 77 EKEAHDILSYSFDQGVNILDTAEMYpvpprketqgRTDLYIG-SWMQS-KPRDKIILATKVSGyserstflrdnakvvrv 154
Cdd:cd19120 24 QRDLVDSVKLALKAGFRHIDTAEMY----------GNEKEVGeALKESgVPREDLFITTKVSP----------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 155 DAANIKESVEKSLSRLSTDYIDLLQIHWPDRyvplfgeyCYNPTKwrpsvPFEEQLKAFQELIDEGKVRYIGVSNETSYG 234
Cdd:cd19120 77 GIKDPREALRKSLAKLGVDYVDLYLIHSPFF--------AKEGGP-----TLAEAWAELEALKDAGLVRSIGVSNFRIED 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 235 VMEFVHAAKVQglPKIVSIQ-NSYSLivrcHFEVDLVEVCHPNNCNVGllAYSPLAggvltgkyidtnpdiskksrlnlf 313
Cdd:cd19120 144 LEELLDTAKIK--PAVNQIEfHPYLY----PQQPALLEYCREHGIVVS--AYSPLS------------------------ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 314 PGYmeRYNASLAKEATNeyvKLAKKHGLTPVQLALGFVRDR---PFTAStiigaTTMDQLKENIDAFtsaPRPLAPEVLD 390
Cdd:cd19120 192 PLT--RDAGGPLDPVLE---KIAEKYGVTPAQVLLRWALQKgivVVTTS-----SKEERMKEYLEAF---DFELTEEEVE 258
|
330
....*....|
gi 1002248734 391 DIESLFKRYR 400
Cdd:cd19120 259 EIDKAGKQKH 268
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
125-399 |
2.20e-15 |
|
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: 76.00 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 PRDKIILATKVSGysersTFLRDnakvvrvdaanIKESVEKSLSRLSTDYIDLLQIHWPdryVPLFGEYCYNPTKWRPSV 204
Cdd:cd19117 66 PREEIFITTKLWC-----TWHRR-----------VEEALDQSLKKLGLDYVDLYLMHWP---VPLDPDGNDFLFKKDDGT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 205 P-------FEEQLKAFQELIDEGKVRYIGVSNetsYGVMEFVHAAKVQGlPKIVSIQNSYSLivrcH---FEVDLVEVCh 274
Cdd:cd19117 127 KdhepdwdFIKTWELMQKLPATGKVKAIGVSN---FSIKNLEKLLASPS-AKIVPAVNQIEL----HpllPQPKLVDFC- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 275 pNNCNVGLLAYSPLAGGvltgkyidtnpdiskksrlnlfpgymeryNASLAKEatNEYVKLAKKHGLTPVQLALGFVRDR 354
Cdd:cd19117 198 -KSKGIHATAYSPLGST-----------------------------NAPLLKE--PVIIKIAKKHGKTPAQVIISWGLQR 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002248734 355 PFtaSTIIGATTMDQLKENIDAFTsaprpLAPEVLDDIESLFKRY 399
Cdd:cd19117 246 GY--SVLPKSVTPSRIESNFKLFT-----LSDEEFKEIDELHKEY 283
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
52-378 |
3.12e-15 |
|
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: 75.65 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 52 RKLGDSDLVISEVTLGTMTFGEQNT----EKEAHDILSYSFDQGVNILDTAEMYPVPPRKETQGRTDLYIGSwmqskPRD 127
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYGdgleQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQV-----PRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 128 KIILATKVSGYSErSTFlrdnakvvRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDryvplFGEYcynptkwrpSVPFE 207
Cdd:cd19153 78 SYTVATKVGRYRD-SEF--------DYSAERVRASVATSLERLHTTYLDVVYLHDIE-----FVDY---------DTLVD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 208 EQLKAFQELIDEGKVRYIGVsneTSYGVMEFVHAAKvQGLPKIVSIQNSYslivrCHFEV-----DLVEVCHPNNCNVGL 282
Cdd:cd19153 135 EALPALRTLKDEGVIKRIGI---AGYPLDTLTRATR-RCSPGSLDAVLSY-----CHLTLqdarlESDAPGLVRGAGPHV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 283 LAYSPLAGGVLTGK----YIDTNPDISKKSRLNLfpGYMERYNASLAKEATneYVKLAKKHGLTPVqlalgfvrdrpfta 358
Cdd:cd19153 206 INASPLSMGLLTSQgpppWHPASGELRHYAAAAD--AVCASVEASLPDLAL--QYSLAAHAGVGTV-------------- 267
|
330 340
....*....|....*....|
gi 1002248734 359 stIIGATTMDQLKENIDAFT 378
Cdd:cd19153 268 --LLGPSSLAQLRSMLAAVD 285
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
155-402 |
1.70e-14 |
|
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: 73.63 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 155 DAANIKESVEKSLSRLSTDYIDLLQIHWP---------DRYVPLFgeYCYNPTKWR-PSVPFEEQLKAFQELIDEGKVRY 224
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieEKYPPGF--YCGDGDNFVyEDVPILDTWKALEKLVDAGKIKS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 225 IGVSNETSYGVMEFVHAAKVQglPKIVSIQNsyslivrchfevdlvevcHPNNCNVGLLAYSPLAGGVLTGkYIDTNPdi 304
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIK--PAVLQIEH------------------HPYLQQPKLIEYAQKAGITITA-YSSFGP-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 305 skKSRLNLfpgymeryNASLAKEAT----NEYVK-LAKKHGLTPVQLALGFVRDRPFtaSTIIGATTMDQLKEN--IDAF 377
Cdd:cd19113 218 --QSFVEL--------NQGRALNTPtlfeHDTIKsIAAKHNKTPAQVLLRWATQRGI--AVIPKSNLPERLLQNlsVNDF 285
|
250 260
....*....|....*....|....*..
gi 1002248734 378 TsaprpLAPEVLDDIESLFK--RYRDP 402
Cdd:cd19113 286 D-----LTKEDFEEIAKLDIglRFNDP 307
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
158-395 |
3.53e-14 |
|
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: 72.17 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 158 NIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLFGEYcYNPTKWRPS---VPFEEQLKAFQELIDEGKVRYIGVSNETSYG 234
Cdd:cd19128 76 NVKEQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGD-PRDDNQIQSlskKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 235 VMEFVHAAKVQGLPKIVSIQnsyslivrCHFEVD-LVEVCHPNncNVGLLAYSPLAggvltGKYIDTNPDISKKSRLNlf 313
Cdd:cd19128 155 LTDLLNYCKIKPFMNQIECH--------PYFQNDkLIKFCIEN--NIHVTAYRPLG-----GSYGDGNLTFLNDSELK-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 314 pgymerynaslakeatneyvKLAKKHGLTPVQLALGF-VRDRPFTASTIIGATTMDQLKENIDAFTSAprpLAPEVLDDI 392
Cdd:cd19128 218 --------------------ALATKYNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDINDLA---LTKEDMDAI 274
|
...
gi 1002248734 393 ESL 395
Cdd:cd19128 275 NTL 277
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
64-400 |
3.21e-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: 69.45 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 64 VTLGTMtfgeQNTEKEAHDILSYSFDQGVNILDTAEMYPvppRKETQGRTdlyIGSWMQSK--PRDKIILATKVSGYser 141
Cdd:cd19111 7 IGLGTY----QSPPEEVRAAVDYALFVGYRHIDTALSYQ---NEKAIGEA---LKWWLKNGklKREEVFITTKLPPV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 142 stFLRdnakvvrvdAANIKESVEKSLSRLSTDYIDLLQIHWP----DRYVPLFGEYCynptkwrpSVPFEEQLKAFQELI 217
Cdd:cd19111 74 --YLE---------FKDTEKSLEKSLENLKLPYVDLYLIHHPcgfvNKKDKGERELA--------SSDVTSVWRAMEALV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 218 DEGKVRYIGVSNETSYGVMEFVHAAKVQglpkivsiqnSYSLIVRCHF---EVDLVEVChpNNCNVGLLAYSPLAGGVLT 294
Cdd:cd19111 135 SEGKVKSIGLSNFNPRQINKILAYAKVK----------PSNLQLECHAylqQRELRKFC--NKKNIVVTAYAPLGSPGRA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 295 GKYIDTN-PDISKKSRLNlfpgymerynaslakeatneyvKLAKKHGLTPVQLALGFVRDRpfTASTIIGATTMDQLKEN 373
Cdd:cd19111 203 NQSLWPDqPDLLEDPTVL----------------------AIAKELDKTPAQVLLRFVLQR--GTGVLPKSTNKERIEEN 258
|
330 340
....*....|....*....|....*..
gi 1002248734 374 IDAFTSAprpLAPEVLDDIESLFKRYR 400
Cdd:cd19111 259 FEVFDFE---LTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
74-395 |
4.98e-13 |
|
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: 68.55 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 74 QNTEKEAHDILSYSFDQGVNILDTAEMYpvpprKETQGrtdlyIGSWMQSK--PRDKIILATKV----SGYserstflrd 147
Cdd:cd19131 19 QVSNDEAASAVREALEVGYRSIDTAAIY-----GNEEG-----VGKAIRASgvPREELFITTKLwnsdQGY--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 148 nakvvrvDAAniKESVEKSLSRLSTDYIDLLQIHWPdryVPLFGEYCynptkwrpsvpfeEQLKAFQELIDEGKVRYIGV 227
Cdd:cd19131 80 -------DST--LRAFDESLRKLGLDYVDLYLIHWP---VPAQDKYV-------------ETWKALIELKKEGRVKSIGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 228 SNETSYGVMEFVHAAKVqgLPKIVSIQnsyslivrCH--FEVDLVEVCHPNNcNVGLLAYSPLA-GGVLTGKYIDtnpdi 304
Cdd:cd19131 135 SNFTIEHLQRLIDETGV--VPVVNQIE--------LHprFQQRELRAFHAKH-GIQTESWSPLGqGGLLSDPVIG----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 305 skksrlnlfpgymerynaslakeatneyvKLAKKHGLTPVQ------LALGFVrdrpftasTIIGATTMDQLKENIDAFT 378
Cdd:cd19131 199 -----------------------------EIAEKHGKTPAQvvirwhLQNGLV--------VIPKSVTPSRIAENFDVFD 241
|
330
....*....|....*..
gi 1002248734 379 SAprpLAPEVLDDIESL 395
Cdd:cd19131 242 FE---LDADDMQAIAGL 255
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
125-376 |
8.80e-13 |
|
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: 67.76 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 PRDKIILATKVsgyserstflrdnaKVVRVDAANIKESVEKSLSRLSTDYIDLLQIHWPDRYVPlfgeycynptkwrpsV 204
Cdd:cd19139 53 PRDELFITTKI--------------WIDNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNDE---------------V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 205 PFEEQLKAFQELIDEGKVRYIGVSNETSyGVMEfvHAAKVQGLPKIVS--------IQNSyslivrchfevDLVEVCHPN 276
Cdd:cd19139 104 PVEEYIGALAEAKEQGLTRHIGVSNFTI-ALLD--EAIAVVGAGAIATnqielspyLQNR-----------KLVAHCKQH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 277 ncNVGLLAYSPLAggvlTGKYIDtNPDIskksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRPF 356
Cdd:cd19139 170 --GIHVTSYMTLA----YGKVLD-DPVL----------------------------AAIAERHGATPAQIALAWAMARGY 214
|
250 260
....*....|....*....|
gi 1002248734 357 taSTIIGATTMDQLKENIDA 376
Cdd:cd19139 215 --AVIPSSTKREHLRSNLLA 232
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
125-229 |
5.69e-12 |
|
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: 65.37 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 PRDKIILATKVSGyserstflRDNAkvvrvdAANIKESVEKSLSRLSTDYIDLLQIHWP----DRYVplfgeycynptkw 200
Cdd:cd19132 59 PREELFVTTKLPG--------RHHG------YEEALRTIEESLYRLGLDYVDLYLIHWPnpsrDLYV------------- 111
|
90 100
....*....|....*....|....*....
gi 1002248734 201 rpsvpfeEQLKAFQELIDEGKVRYIGVSN 229
Cdd:cd19132 112 -------EAWQALIEAREEGLVRSIGVSN 133
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
125-377 |
6.16e-12 |
|
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: 65.42 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 125 PRDKIILATKVS----GYSerstflrdnakvvrvdaaNIKESVEKSLSRLSTDYIDLLQIHWPDryvplfgeyCYNPTKW 200
Cdd:cd19135 65 PREDLFLTTKLWpsdyGYE------------------STKQAFEASLKRLGVDYLDLYLLHWPD---------CPSSGKN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 201 RPSVpFEEQLKAFQELIDEGKVRYIGVSNetsygvmeFvhaakvqGLPKIVSIQNSYSLI-----VRCH---FEVDLVEV 272
Cdd:cd19135 118 VKET-RAETWRALEELYDEGLCRAIGVSN--------F-------LIEHLEQLLEDCSVVphvnqVEFHpfqNPVELIEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 273 CHPNNCNVGllAYSPLAggvlTGKYIdTNPDIskksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQ------L 346
Cdd:cd19135 182 CRDNNIVFE--GYCPLA----KGKAL-EEPTV----------------------------TELAKKYQKTPAQilirwsI 226
|
250 260 270
....*....|....*....|....*....|.
gi 1002248734 347 ALGFVrdrpftasTIIGATTMDQLKENIDAF 377
Cdd:cd19135 227 QNGVV--------TIPKSTKEERIKENCQVF 249
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
157-378 |
1.09e-11 |
|
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: 65.12 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 157 ANIKESVEKSLSRLSTDYIDLLQIHWPDRYVPLFGEycyNPTKWRPSVPFEEQL----------KAFQELIDEGKVRYIG 226
Cdd:cd19118 82 EYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDL---NPLTAVPTNGGEVDLdlsvslvdtwKAMVELKKTGKVKSIG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 227 VSNETSYGVMEFVHAAKVqgLPKIVSIQNSYSLIVRchfevDLVEVChpNNCNVGLLAYSPLAGGVLTGKYIDTNPDIsk 306
Cdd:cd19118 159 VSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQD-----ELVDYC--KSKNIHITAYSPLGNNLAGLPLLVQHPEV-- 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002248734 307 ksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRPFtaSTIIGATTMDQLKENIDAFT 378
Cdd:cd19118 228 --------------------------KAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRIRSNFEQVE 271
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
79-377 |
1.46e-11 |
|
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: 64.00 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 79 EAHDILSYSFDQGVNILDTAEMYpvppRKETQgrtdlyIGSWMQSK--PRDKIILATKVSGYSERstflrdnakvvrvdA 156
Cdd:cd19126 24 ETERAVQTALENGYRSIDTAAIY----KNEEG------VGEAIRESgvPREELFVTTKLWNDDQR--------------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 157 ANIKESVEKSLSRLSTDYIDLLQIHWPdryvplfgeycyNPTKWRpsvpfeEQLKAFQELIDEGKVRYIGVSNETSYGVM 236
Cdd:cd19126 80 RRTEDAFQESLDRLGLDYVDLYLIHWP------------GKDKFI------DTWKALEKLYASGKVKAIGVSNFQEHHLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 237 EFVHAAKVqgLPKIVSIQNSYSLIVRchfevDLVEVCHPNncNVGLLAYSPLAGGVLTgkyidTNPDIskksrlnlfpgy 316
Cdd:cd19126 142 ELLAHADV--VPAVNQVEFHPYLTQK-----ELRGYCKSK--GIVVEAWSPLGQGGLL-----SNPVL------------ 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002248734 317 merynaslakeatneyVKLAKKHGLTPVQLAL------GFVrdrpftasTIIGATTMDQLKENIDAF 377
Cdd:cd19126 196 ----------------AAIGEKYGKSAAQVVLrwdiqhGVV--------TIPKSVHASRIKENADIF 238
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
159-400 |
3.25e-11 |
|
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: 63.82 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 159 IKESVEKSLSRLSTDYIDLLQIHWPDRYVPlfGEYCYNPTKWRPSVP----FEEQLKAFQELIDEGKVRYIGVSNetsyg 234
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHWPMGFKP--GEPDLPLDRSGMVIPsdtdFLDTWEAMEDLVIEGLVKNIGVSN----- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 235 vmeFVHAAKVQGLPK----IVSIQNSysliVRCH---FEVDLVEVCHPNncNVGLLAYSPLaGGVLTGKYIDTNPDISkk 307
Cdd:cd19110 153 ---FNHEQLERLLNKpglrVKPVTNQ----IECHpylTQKKLISFCQSR--NVSVTAYRPL-GGSCEGVDLIDDPVIQ-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 308 srlnlfpgymerynaslakeatneyvKLAKKHGLTPVQLALGFVRDRpfTASTIIGATTMDQLKENIDAFTSAprpLAPE 387
Cdd:cd19110 221 --------------------------RIAKKHGKSPAQILIRFQIQR--NVIVIPKSVTPSRIKENIQVFDFE---LTEH 269
|
250
....*....|...
gi 1002248734 388 VLDDIESLFKRYR 400
Cdd:cd19110 270 DMDNLLSLDRNLR 282
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
155-400 |
6.16e-11 |
|
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: 62.81 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 155 DAANIKESVEKSLSRLSTDYIDLLQIHWP-----DRYVPLFGE--YCYNPtkwrpsVPFEEQLKAFQELIDEGKVRYIGV 227
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPvalkkGVGFPESGEdlLSLSP------IPLEDTWRAMEELVDKGLCRHIGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 228 SNETSYGVMEFVHAAKVQglPKIVSIQNSYSLIVRchfevDLVEVCHPNncNVGLLAYSPLAGGvltgkyiDTNPDISKK 307
Cdd:cd19123 158 SNFSVKKLEDLLATARIK--PAVNQVELHPYLQQP-----ELLAFCRDN--GIHLTAYSPLGSG-------DRPAAMKAE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 308 SRLNLFpgymerynaslakeATNEYVKLAKKHGLTPVQLALGFVRDRpfTASTIIGATTMDQLKENidaFTSAPRPLAPE 387
Cdd:cd19123 222 GEPVLL--------------EDPVINKIAEKHGASPAQVLIAWAIQR--GTVVIPKSVNPERIQQN---LEAAEVELDAS 282
|
250
....*....|...
gi 1002248734 388 VLDDIESLFKRYR 400
Cdd:cd19123 283 DMATIAALDRHHR 295
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
61-374 |
6.64e-11 |
|
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: 62.55 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMtfgeQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprketQGRTDLYIG---SWMQSKPRDKIILATKV-S 136
Cdd:cd19121 12 IPAVGLGTW----QAKAGEVKAAVAHALKIGYRHIDGALCY--------QNEDEVGEGikeAIAGGVKREDLFVTTKLwS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 137 GYSERstflrdnakvvrvdaanIKESVEKSLSRLSTDYIDLLQIHWPDRYVPlFGEYCYNPTK------WRPSVPFEEQL 210
Cdd:cd19121 80 TYHRR-----------------VELCLDRSLKSLGLDYVDLYLVHWPVLLNP-NGNHDLFPTLpdgsrdLDWDWNHVDTW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 211 KAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVqgLPKIVSIQNSYSLIvrchfEVDLVEVCHPNncNVGLLAYSPLAG 290
Cdd:cd19121 142 KQMEKVLKTGKTKAIGVSNYSIPYLEELLKHATV--VPAVNQVENHPYLP-----QQELVDFCKEK--GILIEAYSPLGS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 291 gvlTGKYIDTNPDIskksrlnlfpgymerynaslakeatneyVKLAKKHGLTPVQLALGFVRDRpftASTIIGAT-TMDQ 369
Cdd:cd19121 213 ---TGSPLISDEPV----------------------------VEIAKKHNVGPGTVLISYQVAR---GAVVLPKSvTPDR 258
|
....*
gi 1002248734 370 LKENI 374
Cdd:cd19121 259 IKSNL 263
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
66-302 |
9.21e-11 |
|
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: 62.25 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 66 LGTMTFGEQNTEKEAHDILSYSFDQGVNILDTAEMYpvpprkETQGRTDLYIGSWMQSKP---RDKIILATKVSGYSERS 142
Cdd:cd19122 12 VGFGTFANEGAKGETYAAVTKALDVGYRHLDCAWFY------LNEDEVGDAVRDFLKENPsvkREDLFICTKVWNHLHEP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 143 TflrdnakvvrvdaaNIKESVEKSLSRLSTDYIDLLQIHWP------DRYVPLFGE---YCYN--------PTkWRpsvp 205
Cdd:cd19122 86 E--------------DVKWSIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKLGPdgkYVILkdltenpePT-WR---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 206 feeqlkAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQglPKIVSIQNSYSLIvrchfEVDLVEVCHPNncNVGLLAY 285
Cdd:cd19122 147 ------AMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVK--PHVNQIEIHPFLP-----NEELVDYCFSN--DILPEAY 211
|
250 260
....*....|....*....|
gi 1002248734 286 SPLAGG---VLTGKYIDTNP 302
Cdd:cd19122 212 SPLGSQnqvPSTGERVSENP 231
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
164-402 |
1.19e-10 |
|
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: 61.64 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 164 EKSLSRLSTDYIDLLQIHWP--DRYVplfgeycynptkwrpsvpfeEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHA 241
Cdd:cd19157 88 EASLERLGLDYLDLYLIHWPvkGKYK--------------------ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 242 AkvqglpKIVSIQNSysliVRCH---FEVDLVEVCHPNncNVGLLAYSPLaggvLTGKYIDtNPDIskksrlnlfpgyme 318
Cdd:cd19157 148 A------EIVPMVNQ----VEFHprlTQKELRDYCKKQ--GIQLEAWSPL----MQGQLLD-NPVL-------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 319 rynaslakeatneyVKLAKKHGLTPVQLAL------GFVrdrpftasTIIGATTMDQLKENIDAFTSAprpLAPEVLDDI 392
Cdd:cd19157 197 --------------KEIAEKYNKSVAQVILrwdlqnGVV--------TIPKSIKEHRIIENADVFDFE---LSQEDMDKI 251
|
250
....*....|...
gi 1002248734 393 ESLFKRYR---DP 402
Cdd:cd19157 252 DALNENLRvgpDP 264
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
64-377 |
1.69e-10 |
|
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: 61.27 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 64 VTLGTMTFGE-QNTEKEAHDILSYSFDQGVNILDTAEMYpvppRKETQgrtdlyIGSWMQSK--PRDKIILATKVsgyse 140
Cdd:cd19127 7 VEMPALGLGVfQTPPEETADAVATALADGYRLIDTAAAY----GNERE------VGEGIRRSgvDRSDIFVTTKL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 141 rstFLRDNAKvvrvDAAniKESVEKSLSRLSTDYIDLLQIHWPdryvplfgeycyNPTKWRPSVpfeEQLKAFQELIDEG 220
Cdd:cd19127 72 ---WISDYGY----DKA--LRGFDASLRRLGLDYVDLYLLHWP------------VPNDFDRTI---QAYKALEKLLAEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 221 KVRYIGVSNetsygvmefvhaakvqglpkiVSIQNSYSLIVRCHF--EVDLVEVcHPNNCNVGLL-----------AYSP 287
Cdd:cd19127 128 RVRAIGVSN---------------------FTPEHLERLIDATTVvpAVNQVEL-HPYFSQKDLRafhrrlgivtqAWSP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 288 LaGGVLtgkyidtnpdiskksrlnlfpgymeRYNASLAKEATN-----EYVKLAKKHGLTPVQLALGFVRDRPFTAstII 362
Cdd:cd19127 186 I-GGVM-------------------------RYGASGPTGPGDvlqdpTITGLAEKYGKTPAQIVLRWHLQNGVSA--IP 237
|
330
....*....|....*
gi 1002248734 363 GATTMDQLKENIDAF 377
Cdd:cd19127 238 KSVHPERIAENIDIF 252
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
159-288 |
2.88e-10 |
|
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: 60.89 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 159 IKESVEKSLSRLSTDYIDLLQIHWP------DRYVPLFGEYCYNPTKWRpsvpFEEQLKAFQELIDEGKVRYIGVSNets 232
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPtgfkpgKELFPLDESGNVIPSDTT----FLDTWEAMEELVDEGLVKAIGVSN--- 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002248734 233 ygvmeFVHAakvqglpKIVSIQNSYSLI-------VRCH---FEVDLVEVCHPNNCNVglLAYSPL 288
Cdd:cd19107 153 -----FNHL-------QIERILNKPGLKykpavnqIECHpylTQEKLIQYCQSKGIVV--TAYSPL 204
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
61-400 |
3.75e-10 |
|
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: 60.55 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 61 ISEVTLGTMTFGEQNTEKEAHDILSYSFDQgvniLDTAEMYpvpprketqgRTDLYIGSWMQSK------PRDKIILATK 134
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRH----FDCAERY----------RNEAEVGEAMQEVfkagkiRREDLFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 135 VSGYSERSTflrdnakvvRVDAAnikesVEKSLSRLSTDYIDLLQIHWPDRYVP--------LFGEYCYNPtkwrpSVPF 206
Cdd:cd19129 72 LWNTNHRPE---------RVKPA-----FEASLKRLQLDYLDLYLIHTPFAFQPgdeqdprdANGNVIYDD-----GVTL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 207 EEQLKAFQELIDEGKVRYIGVSNETSYGVMEFVHAAKVQglPKIVSIQ-NSYslivrcHFEVDLVEVCHPNncNVGLLAY 285
Cdd:cd19129 133 LDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAARIK--PAVVQVEsHPY------LPEWELLDFCKNH--GIVLQAF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 286 SPLaGGVLTGKYIDtNPDISkksrlnlfpgymerynaslakeatneyvKLAKKHGLTPVQLALGFVRDRpfTASTIIGAT 365
Cdd:cd19129 203 APL-GHGMEPKLLE-DPVIT----------------------------AIARRVNKTPAQVLLAWAIQR--GTALLTTSK 250
|
330 340 350
....*....|....*....|....*....|....*
gi 1002248734 366 TMDQLKENIDaFTSAPRPLAPEVLDDIESlfkRYR 400
Cdd:cd19129 251 TPSRIRENFD-ISTLPEDAMREINEGIKT---RYR 281
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
79-402 |
4.97e-10 |
|
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: 59.84 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 79 EAHDILSYSFDQGVNILDTAEMYPvppRKETQGRtdlyiGSWMQSKPRDKIILATKV----SGYSerSTFlrdnakvvrv 154
Cdd:cd19156 24 EAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQ-----GIRESGVPREEVFVTTKLwnsdQGYE--STL---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 155 daanikESVEKSLSRLSTDYIDLLQIHWP--DRYVplfgeycynptkwrpsvpfeEQLKAFQELIDEGKVRYIGVSNETS 232
Cdd:cd19156 84 ------AAFEESLEKLGLDYVDLYLIHWPvkGKFK--------------------DTWKAFEKLYKEKKVRAIGVSNFHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 233 YGVMEFVHAAKVQglPKIVSIQNSYSLIVRchfevDLVEVCHPNncNVGLLAYSPLAGGVLTgkyidTNPDIskksrlnl 312
Cdd:cd19156 138 HHLEELLKSCKVA--PMVNQIELHPLLTQE-----PLRKFCKEK--NIAVEAWSPLGQGKLL-----SNPVL-------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 313 fpgymerynaslakeatneyVKLAKKHGLTPVQLALGFvrDRPFTASTIIGATTMDQLKENIDAFTSAprpLAPEVLDDI 392
Cdd:cd19156 196 --------------------KAIGKKYGKSAAQVIIRW--DIQHGIITIPKSVHEERIQENFDVFDFE---LTAEEIRQI 250
|
330
....*....|...
gi 1002248734 393 ESLFKRYR---DP 402
Cdd:cd19156 251 DGLNTDHRygpDP 263
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
80-391 |
8.87e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 59.67 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 80 AHDILSYSFDQGVNILDTAEMYpvpprketqGRTDLYIGSWMQSKP--RDKIILATKvSGYsersTFLRDnakvVRVDAA 157
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY---------GRAEEFLGSWLRSRNiaPDAVFVGSK-WGY----TYTAD----WQVDAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 158 nIKESVEKSLSRLST----------DYIDLLQIHwpdryvplfgeycynptkwrpSVPFE-------EQLKAFQELIDEG 220
Cdd:cd19098 99 -VHEVKDHSLARLLKqweetrsllgKHLDLYQIH---------------------SATLEsgvledaDVLAALAELKAEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 221 KVRYIGVSNETSYGVMEFVHAAKVQGLPKIVSIQNSYSLivrchFEVDLVEVCH-PNNCNVGLLAYSPLAGGVLTgkyiD 299
Cdd:cd19098 157 VKIGLSLSGPQQAETLRRALEIEIDGARLFDSVQATWNL-----LEQSAGEALEeAHEAGMGVIVKEALANGRLT----D 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 300 TNPDISKKSRLNLFPgymerynaslakeatneyvKLAKKHGLTPVQLALGFVRDRPFTASTIIGATTMDQLKENIDAFTS 379
Cdd:cd19098 228 RNPSPELAPLMAVLK-------------------AVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
330
....*....|..
gi 1002248734 380 APRPLAPEVLDD 391
Cdd:cd19098 289 SLDLELLAALAD 300
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
162-395 |
1.56e-09 |
|
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: 58.43 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 162 SVEKSLSRLSTDYIDLLQIHWPDRYVPlfGEYCYNPTKWRPsVPF--EEQLKAFQELIDEGKVRYIGVSNETSYGVMEFV 239
Cdd:cd19124 87 ALKKSLRNLQLEYVDLYLIHWPVSLKP--GKFSFPIEEEDF-LPFdiKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 240 HAAKVqglPKIVSiQNSYSLIVRchfEVDLVEVCHPNncNVGLLAYSPLAGgvltgkyidtnpdiskksrlnlfPGYMER 319
Cdd:cd19124 164 SFATI---PPAVN-QVEMNPAWQ---QKKLREFCKAN--GIHVTAYSPLGA-----------------------PGTKWG 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002248734 320 YNASLAKEATNEyvkLAKKHGLTPVQLALGFVRDRpfTASTIIGATTMDQLKENIDAFTSAprpLAPEVLDDIESL 395
Cdd:cd19124 212 SNAVMESDVLKE---IAAAKGKTVAQVSLRWVYEQ--GVSLVVKSFNKERMKQNLDIFDWE---LTEEDLEKISEI 279
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
160-403 |
1.67e-09 |
|
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: 58.59 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 160 KESVE----KSLSRLSTDYIDLLQIHWP------D---RYVPlfgEYCYNPTKWRPS-VPFEEQLKAFQELIDEGKVRYI 225
Cdd:cd19115 86 GERVEpicrKQLADWGIDYFDLFLIHFPialkyvDpavRYPP---GWFYDGKKVEFSnAPIQETWTAMEKLVDKGLARSI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 226 GVSNETSYGVMEFVHAAKVQglPKIVSIQNsyslivrchfevdlvevcHPNNCNVGLLAYSPLAGGVLTGkYIDTNPDis 305
Cdd:cd19115 163 GVSNFSAQLLMDLLRYARIR--PATLQIEH------------------HPYLTQPRLVKYAQKEGIAVTA-YSSFGPQ-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 306 kksrlnlfpGYMErYNASLAKEAT-----NEYVKLAKKHGLTPVQLALGFVRDRpfTASTIIGATTMDQLKENIDA--FT 378
Cdd:cd19115 220 ---------SFLE-LDLPGAKDTPplfehDVIKSIAEKHGKTPAQVLLRWATQR--GIAVIPKSNNPKRLAQNLDVtgFD 287
|
250 260
....*....|....*....|....*..
gi 1002248734 379 saprpLAPEVLDDIESLFK--RYRDPT 403
Cdd:cd19115 288 -----LEAEEIKAISALDIglRFNNPL 309
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
64-400 |
2.06e-09 |
|
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: 58.31 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 64 VTLGTMtfgeQNTEKEAHDILSYSFDQGVNILDTAEMYpvppRKETQ-GRTdlyIGSWMQSK--PRDKIILATKVSGYSE 140
Cdd:cd19155 15 VGLGTW----QSSPEEIETAVDTALEAGYRHIDTAYVY----RNEAAiGNV---LKKWIDSGkvKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 141 RSTflrdnakvvrvdaaNIKESVEKSLSRLSTDYIDLLQIHWPdryVPLFGEYcYNPTKWRPSVPFEEQL--------KA 212
Cdd:cd19155 84 RRE--------------KVEKFLLKSLEKLQLDYVDLYLIHFP---VGSLSKE-DDSGKLDPTGEHKQDYttdlldiwKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 213 FQELIDEGKVRYIGVSNETSYGVMEFVHAAKVqglpKIVSIQnsysliVRCHFEV---DLVEVCHPNncNVGLLAYSPLA 289
Cdd:cd19155 146 MEAQVDQGLTRSIGLSNFNREQMARILKNARI----KPANLQ------VELHVYLqqkDLVDFCSTH--SITVTAYAPLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 290 GGVLTGKYIDTNPDISKKSRLNLFPgymerynaslakeatnEYVKLAKKHGLTPVQLALGFVRDRPFTAstIIGATTMDQ 369
Cdd:cd19155 214 SPGAAHFSPGTGSPSGSSPDLLQDP----------------VVKAIAERHGKSPAQVLLRWLMQRGVVV--IPKSTNAAR 275
|
330 340 350
....*....|....*....|....*....|.
gi 1002248734 370 LKENIDAFTSAprpLAPEVLDDIESLFKRYR 400
Cdd:cd19155 276 IKENFQVFDFE---LTEADMAKLSSLDKNIR 303
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
82-231 |
4.28e-08 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 53.87 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 82 DILSYSFDQGVNILDTAEMYpvppRKETQgrtdlyIGSWMQSK--PRDKIILATK--VSGYSErstflrdnAKVVrvdaa 157
Cdd:PRK11172 20 DSVKTALELGYRAIDTAQIY----DNEAA------VGQAIAESgvPRDELFITTKiwIDNLAK--------DKLI----- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002248734 158 nikESVEKSLSRLSTDYIDLLQIHWPdryvplfgeycyNPTKwrpSVPFEEQLKAFQELIDEGKVRYIGVSNET 231
Cdd:PRK11172 77 ---PSLKESLQKLRTDYVDLTLIHWP------------SPND---EVSVEEFMQALLEAKKQGLTREIGISNFT 132
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
53-229 |
8.18e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 53.15 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 53 KLGDSDlVISEVTLGTMTFGEQNTEKEAHDILsysfDQGVNILDTAEMYpvpprKETQGrtdlyIGSWMQSK--PRDKII 130
Cdd:PRK11565 8 KLQDGN-VMPQLGLGVWQASNEEVITAIHKAL----EVGYRSIDTAAIY-----KNEEG-----VGKALKEAsvAREELF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 131 LATKVSgyserstflrdNAkvvrvDAANIKESVEKSLSRLSTDYIDLLQIHWPdryVPLFGEYcynptkwrpsvpfeeqL 210
Cdd:PRK11565 73 ITTKLW-----------ND-----DHKRPREALEESLKKLQLDYVDLYLMHWP---VPAIDHY----------------V 117
|
170 180
....*....|....*....|..
gi 1002248734 211 KAFQELID---EGKVRYIGVSN 229
Cdd:PRK11565 118 EAWKGMIElqkEGLIKSIGVCN 139
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
158-402 |
1.00e-06 |
|
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: 50.25 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 158 NIKESVEKSLSRLSTDYIDLLQIHWP--DRYVPLFGEYcynPTKWR---------PSVPFEEQLKAFQELIDEGKVRYIG 226
Cdd:cd19114 79 HVREAFDRQLKDYGLDYIDLYLIHFPipAAYVDPAENY---PFLWKdkelkkfplEQSPMQECWREMEKLVDAGLVRNIG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 227 VSNETSYGVMEFVHAAKVQglPKIVSIQNsYSLIVRCHFeVDLVEvchpnNCNVGLLAYSPLAGGVLTgkyidtnpdisk 306
Cdd:cd19114 156 IANFNVQLILDLLTYAKIK--PAVLQIEH-HPYLQQKRL-IDWAK-----KQGIQITAYSSFGNAVYT------------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 307 ksrlnLFPGYMERYnASLAKEATNEyvKLAKKHGLTPVQLALGFVRDRPFTasTIIGATTMDQLKENIDAFTSAPRPLAP 386
Cdd:cd19114 215 -----KVTKHLKHF-TNLLEHPVVK--KLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTNLDITSYKLDEEDM 284
|
250
....*....|....*.
gi 1002248734 387 EVLDDIESlFKRYRDP 402
Cdd:cd19114 285 EALYELEA-NARFNDP 299
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
159-323 |
1.12e-06 |
|
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: 49.80 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 159 IKESVEKSLSRLSTDYIDLLQIHWP--------DRYVPLFGEYCYNPTKWRPSVPFEEQLKAFQELIDEGKVRYIGVSNE 230
Cdd:cd19119 88 VERSLDESLKALGLDYVDLLLVHWPvcfekdsdDSGKPFTPVNDDGKTRYAASGDHITTYKQLEKIYLDGRAKAIGVSNY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 231 TSYGVMEFVHAAKVqgLPKIVSIQNSYSLIVRchfevDLVEVCHPNncNVGLLAYSPLAGGvltGKYIDTNPDISKKSrl 310
Cdd:cd19119 168 SIVYLERLIKECKV--VPAVNQVELHPHLPQM-----DLRDFCFKH--GILVTAYSPLGSH---GAPNLKNPLVKKIA-- 233
|
170
....*....|...
gi 1002248734 311 nlfpgymERYNAS 323
Cdd:cd19119 234 -------EKYNVS 239
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
87-229 |
1.78e-06 |
|
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: 49.14 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 87 SFDQGVNILDTAEMYpvpprKETQGRTDLYIGSWMqskPRDKIILATKVSGyserstflrDNAKVVRVDAAnikesVEKS 166
Cdd:cd19130 32 ALEVGYRHIDTAAIY-----GNEEGVGAAIAASGI---PRDELFVTTKLWN---------DRHDGDEPAAA-----FAES 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002248734 167 LSRLSTDYIDLLQIHWPdryVPLFGEYCynptkwrpsvpfeEQLKAFQELIDEGKVRYIGVSN 229
Cdd:cd19130 90 LAKLGLDQVDLYLVHWP---TPAAGNYV-------------HTWEAMIELRAAGRTRSIGVSN 136
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
80-262 |
2.96e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.43 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 80 AHDILSYSFDQGVNILDTAEMYPvpPRKETQG-RTDLYigswmqskP-RDKIILATKVSGysERSTflrDNAKVVRVDAA 157
Cdd:PRK10376 42 AIAVLREAVALGVNHIDTSDFYG--PHVTNQLiREALH--------PyPDDLTIVTKVGA--RRGE---DGSWLPAFSPA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 158 NIKESVEKSLSRLSTDYIDLLQIH-WPDRYVPLFGeycynptkwrpsvPFEEQLKAFQELIDEGKVRYIGVSNETSYGVm 236
Cdd:PRK10376 107 ELRRAVHDNLRNLGLDVLDVVNLRlMGDGHGPAEG-------------SIEEPLTVLAELQRQGLVRHIGLSNVTPTQV- 172
|
170 180
....*....|....*....|....*.
gi 1002248734 237 efvhaAKVQGLPKIVSIQNSYSLIVR 262
Cdd:PRK10376 173 -----AEARKIAEIVCVQNHYNLAHR 193
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
74-239 |
9.18e-06 |
|
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: 46.77 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 74 QNTEKEAHDILSYSFDQGVNILDTAEMYPvppRKETQGRTDLYIGSwmqskPRDKIILATKVSGYSERSTFLRDNAKvvr 153
Cdd:cd19134 20 ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGI-----PRGELFVTTKLATPDQGFTASQAACR--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 154 vdaanikesveKSLSRLSTDYIDLLQIHWP----DRYVPLFGeycynptkwrpsvpfeeqlkAFQELIDEGKVRYIGVSN 229
Cdd:cd19134 89 -----------ASLERLGLDYVDLYLIHWPagreGKYVDSWG--------------------GLMKLREEGLARSIGVSN 137
|
170
....*....|
gi 1002248734 230 ETSYGVMEFV 239
Cdd:cd19134 138 FTAEHLENLI 147
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
117-400 |
1.41e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 43.37 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 117 IGSWMQSK------PRDKIILATKVSgyserSTFLRdnAKVVRVdaanikeSVEKSLSRLSTDYIDLLQIHWP------D 184
Cdd:cd19108 56 VGQAIRSKiadgtvKREDIFYTSKLW-----CTFHR--PELVRP-------ALEKSLKKLQLDYVDLYLIHFPvalkpgE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 185 RYVPL--FGEYCYNptkwrpSVPFEEQLKAFQELIDEGKVRYIGVSNetsygvmeFVHaakvQGLPKI----------VS 252
Cdd:cd19108 122 ELFPKdeNGKLIFD------TVDLCATWEAMEKCKDAGLAKSIGVSN--------FNR----RQLEMIlnkpglkykpVC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248734 253 IQnsysliVRCHFEVD---LVEVCHPNncNVGLLAYSPLaGGVLTGKYIDTN-PDISKKSRLNlfpgymerynaslakea 328
Cdd:cd19108 184 NQ------VECHPYLNqskLLDFCKSK--DIVLVAYSAL-GSQRDKEWVDQNsPVLLEDPVLC----------------- 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002248734 329 tneyvKLAKKHGLTPVQLALGFVRDR---PFTAStiigaTTMDQLKENIDAFTSAprpLAPEVLDDIESLFKRYR 400
Cdd:cd19108 238 -----ALAKKHKRTPALIALRYQLQRgvvVLAKS-----FNEKRIKENLQVFEFQ---LTSEDMKALDGLNRNLR 299
|
|
| |
