|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-336 |
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: 548.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVPPRGETYTKTESIIGEYFKKYADRNDWVLASKVAGPG 92
Cdd:cd19094 1 VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQGRTEEIIGSWLKKKGNRDKVVLATKVAGPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 93 -RMDHIRDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNFFGVLGYT-HDPDDQAVEIEETLSVLGDLVKAG 170
Cdd:cd19094 81 eGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLFGGGYYTePSEEEDSVSFEEQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 171 KIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKYLDGA-R 249
Cdd:cd19094 161 KIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAaR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 250 PADGRLTLFERFQ-RYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVTLSDE 328
Cdd:cd19094 241 PEGGRLNLFPGYMaRYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVPLSDE 320
|
....*...
gi 966352627 329 VIAGIEAI 336
Cdd:cd19094 321 LLAEIDAV 328
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-345 |
6.86e-171 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 478.96 E-value: 6.86e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVPPRGETYTKTESIIGEYFKKYADRN 80
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQGLTETYIGNWLAKRGSRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 81 DWVLASKVAGPGR-MDHIRDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNFFGVLGYTHDPDDQAVEIEET 159
Cdd:PRK10625 81 KLIIASKVSGPSRnNDKGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYSWTDSAPAVSLLET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 160 LSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGV 239
Cdd:PRK10625 161 LDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 240 LAGKYLDGARPADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLE 319
Cdd:PRK10625 241 LTGKYLNGAKPAGARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIE 320
|
330 340
....*....|....*....|....*.
gi 966352627 320 SIDVTLSDEVIAGIEAIHTAQPNPAP 345
Cdd:PRK10625 321 SLHLTLSEEVLAEIEAVHQVYTYPAP 346
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-343 |
6.56e-131 |
|
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: 376.44 E-value: 6.56e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMTWGE---QNTQDEAFEQIRMAKDAKVNFLDTAEMYPvppRGETytktESIIGEYFKKYa 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYG---PGRS----EELLGEALKGR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 78 DRNDWVLASKVAGPGRMDHIRDGnprLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIE 157
Cdd:COG0667 73 PRDDVVIATKVGRRMGPGPNGRG---LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDT-----------------PIE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 158 ETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAEtlDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAF 237
Cdd:COG0667 133 ETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 238 GVLAGKYLDGAR-PADGRLTLFeRFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKI 316
Cdd:COG0667 211 GLLTGKYRRGATfPEGDRAATN-FVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEE 289
|
330 340
....*....|....*....|....*..
gi 966352627 317 NLESIDVTLSDEVIAGIEAIHTAQPNP 343
Cdd:COG0667 290 NLAAADLELSAEDLAALDAALAAVPAP 316
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-336 |
5.24e-110 |
|
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: 322.98 E-value: 5.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVPprgetytKTESIIGEYFKKyaDRN 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGG-------RSEEIIGRWIAG--RRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 81 DWVLASKVAGPgrMDhirDGN--PRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIEE 158
Cdd:cd19087 72 DIVLATKVFGP--MG---DDPndRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDT-----------------PLEE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFG 238
Cdd:cd19087 130 TLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 239 VLAGKYLDGARPADGRLTLFERFQ-RYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKIN 317
Cdd:cd19087 210 LLTGKYGKGKRPESGRLVERARYQaRYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDS 289
|
330
....*....|....*....
gi 966352627 318 LESIDVTLSDEVIAGIEAI 336
Cdd:cd19087 290 LAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-331 |
3.77e-95 |
|
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: 285.26 E-value: 3.77e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 5 KLGKTDLSVSAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVPPRGETYTKTESIIGEYFKKYADRNDWVL 84
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGNAGGESETIIGRWLKSRGKRDRVVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 85 ASKVAGPgrmdhIRDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWpdrktnffgvlgythdpDDQAVEIEETLSVLG 164
Cdd:cd19081 81 ATKVGFP-----MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHW-----------------DDPATPLEETLGALN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 165 DLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRT-FEVGLAEIAIREQIGLLAYSPLAFGVLAGK 243
Cdd:cd19081 139 DLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 244 YLDGARPADGRLTlFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDV 323
Cdd:cd19081 219 YRSEADLPGSTRR-GEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL 297
|
....*...
gi 966352627 324 TLSDEVIA 331
Cdd:cd19081 298 RLTDEEVA 305
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
5-334 |
3.01e-91 |
|
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: 275.23 E-value: 3.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 5 KLGKTDLSVSAICLGTMTWGEQNTQ------DEAFEQIRMAKDAKVNFLDTAEMYPvppRGETytktESIIGEYFKKYAD 78
Cdd:cd19079 4 RLGNSGLKVSRLCLGCMSFGDPKWRpwvldeEESRPIIKRALDLGINFFDTANVYS---GGAS----EEILGRALKEFAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVAGPGRmdhiRDGNPR-LDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdPddqaveIE 157
Cdd:cd19079 77 RDEVVIATKVYFPMG----DGPNGRgLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYET-----------P------IE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 158 ETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAF 237
Cdd:cd19079 136 ETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLAR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 238 GVLAGKYLDGARPADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKIN 317
Cdd:cd19079 216 GRLARPWGDTTERRRSTTDTAKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDA 295
|
330
....*....|....*..
gi 966352627 318 LESIDVTLSDEVIAGIE 334
Cdd:cd19079 296 VAALDIKLSEEEIKYLE 312
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-336 |
4.99e-88 |
|
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: 267.17 E-value: 4.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMTWGEQN---------TQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGE 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGgffgawggvDQEEADRLVDIALDAGINFFDTADVY-------SEGESEEILGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 72 YFKkyADRNDWVLASKVAGpgRMDhiRDGNPR-LDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpd 150
Cdd:cd19091 74 ALK--GRRDDVLIATKVRG--RMG--EGPNDVgLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALT------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 151 dqavEIEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLL 230
Cdd:cd19091 135 ----PLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 231 AYSPLAFGVLAGKYLDGARPADG---RLTLFErFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIG 307
Cdd:cd19091 211 VWSPLAGGLLSGKYRRGQPAPEGsrlRRTGFD-FPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIG 289
|
330 340
....*....|....*....|....*....
gi 966352627 308 ATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19091 290 ARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-334 |
3.01e-84 |
|
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: 256.68 E-value: 3.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 10 DLSVSAICLGTM-----TWGEQNTQdEAFEQIRMAKDAKVNFLDTAEMYPvppRGETytktESIIGEYFKKYadRNDWVL 84
Cdd:cd19084 1 DLKVSRIGLGTWaiggtWWGEVDDQ-ESIEAIKAAIDLGINFFDTAPVYG---FGHS----EEILGKALKGR--RDDVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 85 ASKVAGPGRMDHIRDGNprLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdPddqaveIEETLSVLG 164
Cdd:cd19084 71 ATKCGLRWDGGKGVTKD--LSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNT-----------P------IEETAEALE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 165 DLVKAGKIRHFGLSNETPWGTQRFLHLAEtldlprAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKY 244
Cdd:cd19084 132 KLKKEGKIRYIGVSNFSVEQLEEARKYGP------IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 245 LDGAR-PADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDV 323
Cdd:cd19084 206 KKEPTfPPDDRRSRFPFFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW 285
|
330
....*....|.
gi 966352627 324 TLSDEVIAGIE 334
Cdd:cd19084 286 ELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-336 |
2.24e-81 |
|
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: 249.43 E-value: 2.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTM-----TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETYTktESIIGEYFKKyaDRNDWVLASK 87
Cdd:cd19085 1 VSRLGLGCWqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAY-----GDGHS--EEVLGKALKG--RRDDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 88 VAGpgrmDHIRdgnprldRKNITAALEASLKRLNTDYLDLYQLHWPDRKtnffgvlgythdpddqaVEIEETLSVLGDLV 167
Cdd:cd19085 72 VSP----DNLT-------PEDVRKSCERSLKRLGTDYIDLYQIHWPSSD-----------------VPLEETMEALEKLK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 168 KAGKIRHFGLSNETPWgtqrflHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKYLDG 247
Cdd:cd19085 124 EEGKIRAIGVSNFGPA------QLEEALDAGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 248 AR--PADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVTL 325
Cdd:cd19085 198 EDfpPGDARTRLFRHFEPGAEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLEL 277
|
330
....*....|.
gi 966352627 326 SDEVIAGIEAI 336
Cdd:cd19085 278 SPSVLERLDEI 288
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-336 |
2.48e-77 |
|
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: 239.14 E-value: 2.48e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 16 ICLGTMTWGEQNTQ---DEAFEQIRMAKDAKVNFLDTAEMYPVpprgetyTKTESIIGEYFKKYADRND-WVLASKVAGP 91
Cdd:pfam00248 1 IGLGTWQLGGGWGPiskEEALEALRAALEAGINFIDTAEVYGD-------GKSEELLGEALKDYPVKRDkVVIATKVPDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 92 grmdhIRDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRktnffgvlgythdpddqAVEIEETLSVLGDLVKAGK 171
Cdd:pfam00248 74 -----DGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-----------------DTPIEETWDALEELKKEGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 172 IRHFGLSNETPWGTQRflhlAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKYLDGARPA 251
Cdd:pfam00248 132 IRAIGVSNFDAEQIEK----ALTKGKIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 252 DGRLtlfERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVTLSDEVIA 331
Cdd:pfam00248 208 PGER---RRLLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVA 284
|
....*
gi 966352627 332 GIEAI 336
Cdd:pfam00248 285 RIDEL 289
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-319 |
2.51e-76 |
|
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: 234.34 E-value: 2.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYADRNDWVLASKVAGPGR 93
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVY-------GDGRSERLLGRWLKGRGNRDDVVIATKGGHPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 94 MDHIRdgnPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIEETLSVLGDLVKAGKIR 173
Cdd:cd06660 74 GDPSR---SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPST-----------------PVEETLEALNELVREGKIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 174 HFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTF-EVGLAEIAIREQIGLLAYSPLAFGvlagkyldgarpad 252
Cdd:cd06660 134 YIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG-------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966352627 253 grltlferfqrynnpqavsatakyvalarehgldPSQMALAYVTSRPFVTSNIIGATKLDQLKINLE 319
Cdd:cd06660 200 ----------------------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-331 |
8.32e-74 |
|
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: 230.57 E-value: 8.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 4 RKLGKTDLSVSAICLGTMTWGEQ----NTQDEAFEQIRMAKDAKVNFLDTAEMYpvppRGETytkTESIIGEYFKKyaDR 79
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNY----TNGT---SERLLGEFIAG--NR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 80 NDWVLASKVAGPGRMDHIR-DGNprlDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIEE 158
Cdd:cd19080 72 DRIVLATKYTMNRRPGDPNaGGN---HRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTT-----------------PVEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHFGLSNeTP-WGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAF 237
Cdd:cd19080 132 VMRALDDLVRAGKVLYVGISD-TPaWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 238 GVLAGKYLDGARPADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKIN 317
Cdd:cd19080 211 GLLTGKYQRGEEGRAGEAKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDN 290
|
330
....*....|....
gi 966352627 318 LESIDVTLSDEVIA 331
Cdd:cd19080 291 LGALDLTLSPEQLA 304
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-329 |
2.26e-73 |
|
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: 229.02 E-value: 2.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 11 LSVSAICLGT-MTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvpprgetYTKTESIIGEYFKKYaDRNDWVLASKVA 89
Cdd:cd19074 2 LKVSELSLGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYA-------AGQAEEVLGKALKGW-PRESYVISTKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 90 GPGRmDHIRD-GnprLDRKNITAALEASLKRLNTDYLDLYQLHWPDrktnffgvlgythdPDdqaVEIEETLSVLGDLVK 168
Cdd:cd19074 74 WPTG-PGPNDrG---LSRKHIFESIHASLKRLQLDYVDIYYCHRYD--------------PE---TPLEETVRAMDDLIR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 169 AGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKYLDGA 248
Cdd:cd19074 133 QGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 249 RPADGRLTLFERF----QRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVT 324
Cdd:cd19074 213 PPPSRSRATDEDNrdkkRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVK 292
|
....*
gi 966352627 325 LSDEV 329
Cdd:cd19074 293 LSPEV 297
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-336 |
4.66e-64 |
|
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: 205.91 E-value: 4.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGT-MTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvppRGETytktESIIGEYFKKYA-D 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYA---NGQS----EEIMGQAIKELGwP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVAGPGRMDhirDGNPR-LDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdPddqaveIE 157
Cdd:cd19143 74 RSDYVVSTKIFWGGGGP---PPNDRgLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPAT-----------P------IE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 158 ETLSVLGDLVKAGKIRHFGLSNetpWGTQRF---LHLAETLDLPRAVSIQNPYNLLNRT-FEVGLAEIAIREQIGLLAYS 233
Cdd:cd19143 134 ETVRAMNDLIDQGKAFYWGTSE---WSAQQIeeaHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 234 PLAFGVLAGKYLDGArPADGRLTLFE-----RFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19143 211 PLASGLLTGKYNNGI-PEGSRLALPGyewlkDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGA 289
|
330 340 350
....*....|....*....|....*....|
gi 966352627 309 TKLDQLKINLESIDV--TLSDEVIAGIEAI 336
Cdd:cd19143 290 TKVEQLEENLKALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-335 |
1.42e-59 |
|
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: 194.03 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 3 FRKLGKTDLSVSAICLGT------MTWGEqNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKY 76
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTwaigggPWWGG-SDDNESIRTIHAALDLGINLIDTAPAY-------GFGHSEEIVGKAIKGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 77 adRNDWVLASK---VAGPGRMDHIRDGNPRLDRKNITAA-----LEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythd 148
Cdd:cd19149 73 --RDKVVLATKcglRWDREGGSFFFVRDGVTVYKNLSPEsireeVEQSLKRLGTDYIDLYQTHWQDVET----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 149 PddqaveIEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAEtLDlpravSIQNPYNLLNRTFEVGLAEIAIREQIG 228
Cdd:cd19149 140 P------IEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQ-LD-----IIQEKYSMLDRGIEKELLPYCKKNNIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 229 LLAYSPLAFGVLAGKY-LDGARPADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIG 307
Cdd:cd19149 208 FQAYSPLEQGLLTGKItPDREFDAGDARSGIPWFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCG 287
|
330 340
....*....|....*....|....*...
gi 966352627 308 ATKLDQLKINLESIDVTLSDEVIAGIEA 335
Cdd:cd19149 288 ARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-320 |
2.57e-56 |
|
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: 183.06 E-value: 2.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 11 LSVSAICLGTMT----WGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvppRGetytKTESIIGEYFKKyaDRNDWVLAS 86
Cdd:cd19086 1 LEVSEIGFGTWGlggdWWGDVDDAEAIRALRAALDLGINFFDTADVYG---DG----HSERLLGKALKG--RRDKVVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 87 KVaGPGRMDHIRDGnPRLDRKNITAALEASLKRLNTDYLDLYQLhwpdrktnffgvlgytHDPDDQAVEIEETLSVLGDL 166
Cdd:cd19086 72 KF-GNRFDGGPERP-QDFSPEYIREAVEASLKRLGTDYIDLYQL----------------HNPPDEVLDNDELFEALEKL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 167 VKAGKIRHFGLSNETPWGtqrflhLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKyld 246
Cdd:cd19086 134 KQEGKIRAYGVSVGDPEE------ALAALRRGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK--- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966352627 247 garpadgrltlferfqrynnpqavsatakyvalarehgldPSQMALAYVTSRPFVTSNIIGATKLDQLKINLES 320
Cdd:cd19086 205 ----------------------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-336 |
1.88e-55 |
|
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: 183.39 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 4 RKLGKTDLSVSAICLGTMTWGEQN-----TQDEAFEQIRMAKDAKVNFLDTAEMYPVpprgetyTKTESIIGEYFKKYaD 78
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNlypnlDEEEGKDLVREALDNGVNLLDTAFIYGL-------GRSEELVGEVLKEY-N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVAGPGRMDHIRDGNprlDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdPDDQAVeiee 158
Cdd:cd19083 74 RNEVVIATKGAHKFGGDGSVLNN---SPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGET-----------PKAEAV---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 tlSVLGDLVKAGKIRHFGLSNETPWGTQRFLHlAETLDLpravsIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFG 238
Cdd:cd19083 136 --GALQELKDEGKIRAIGVSNFSLEQLKEANK-DGYVDV-----LQGEYNLLQREAEEDILPYCVENNISFIPYFPLASG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 239 VLAGKYLDGARPADG----RLTLF--ERFQRynNPQAVSataKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLD 312
Cdd:cd19083 208 LLAGKYTKDTKFPDNdlrnDKPLFkgERFSE--NLDKVD---KLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAE 282
|
330 340
....*....|....*....|....
gi 966352627 313 QLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19083 283 QVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-334 |
2.77e-55 |
|
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: 181.27 E-value: 2.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 12 SVSAICLGTMTWGEQNTQD-----EAFEQIRMAKDAKVNFLDTAEMYpvpprGETYTktESIIGEYFKKYaDRNDWVLAS 86
Cdd:cd19072 3 EVPVLGLGTWGIGGGMSKDysddkKAIEALRYAIELGINLIDTAEMY-----GGGHA--EELVGKAIKGF-DREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 87 KVagpgrmdhirdgNP-RLDRKNITAALEASLKRLNTDYLDLYQLHWPdrktNFFgvlgythdpddqaVEIEETLSVLGD 165
Cdd:cd19072 75 KV------------SPdHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP----NPS-------------IPIEETLRAMEE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 166 LVKAGKIRHFGLSNetpwgtqrfLHLAEtldLPRA---------VSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLA 236
Cdd:cd19072 126 LVEEGKIRYIGVSN---------FSLEE---LEEAqsylkkgpiVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 237 FGVLAGKyldgarpaDGRLTLFErfqrynnpqavsatakyvaLAREHGLDPSQMALAYVTSRPFVTSnIIGATKLDQLKI 316
Cdd:cd19072 194 KGKLSNA--------KGSPLLDE-------------------IAKKYGKTPAQIALNWLISKPNVIA-IPKASNIEHLEE 245
|
330
....*....|....*...
gi 966352627 317 NLESIDVTLSDEVIAGIE 334
Cdd:cd19072 246 NAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-322 |
3.73e-55 |
|
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: 181.98 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvppRGETYTKTESIIGEYFKKYADRNDWVLASKVAGPGR 93
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYG---DWVERGASERVIGEWLKSRGNRDKVVIATKGGHPDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 94 MDhirDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHwpdRktnffgvlgythdpDDQAVEIEETLSVLGDLVKAGKIR 173
Cdd:cd19082 78 ED---MSRSRLSPEDIRADLEESLERLGTDYIDLYFLH---R--------------DDPSVPVGEIVDTLNELVRAGKIR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 174 HFGLSNetpWGTQRFLHL---AETLDLPRAVSIQNPYNL--LNRTFEVGLAEIAI---------REQIGLLAYSPLAFGV 239
Cdd:cd19082 138 AFGASN---WSTERIAEAnayAKAHGLPGFAASSPQWSLarPNEPPWPGPTLVAMdeemrawheENQLPVFAYSSQARGF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 240 LAGKYLDGARPADgrltlfERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLE 319
Cdd:cd19082 215 FSKRAAGGAEDDS------ELRRVYYSEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLA 288
|
...
gi 966352627 320 SID 322
Cdd:cd19082 289 AAD 291
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-334 |
8.14e-53 |
|
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: 175.88 E-value: 8.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTMTWGEQ---NTQDEAFEQIR----MAKDAKVNFLDTAEMYpvpprGetYTKTESIIGEYFKKYADRNDWVLA 85
Cdd:cd19093 2 VSPLGLGTWQWGDRlwwGYGEYGDEDLQaafdAALEAGVNLFDTAEVY-----G--TGRSERLLGRFLKELGDRDEVVIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 86 SKVAGPGRmdhirdgnpRLDRKNITAALEASLKRLNTDYLDLYQLHWPdrkTNFFGvlgythdpddqavEIEETLSVLGD 165
Cdd:cd19093 75 TKFAPLPW---------RLTRRSVVKALKASLERLGLDSIDLYQLHWP---GPWYS-------------QIEALMDGLAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 166 LVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPrAVSIQNPYNLLNRTFEV-GLAEIAIREQIGLLAYSPLAFGVLAGKY 244
Cdd:cd19093 130 AVEEGLVRAVGVSNYSADQLRRAHKALKERGVP-LASNQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQGLLTGKY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 245 LDGARPADGRLTLFeRFQRYNNPQAVSATAKyvALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVT 324
Cdd:cd19093 209 SPENPPPGGRRRLF-GRKNLEKVQPLLDALE--EIAEKYGKTPAQVALNWLIAKGVVP--IPGAKNAEQAEENAGALGWR 283
|
330
....*....|
gi 966352627 325 LSDEVIAGIE 334
Cdd:cd19093 284 LSEEEVAELD 293
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-334 |
2.42e-52 |
|
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: 175.11 E-value: 2.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 10 DLSVSAICLGTM----TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGeTYTkTESIIGEYFKKYadRNDWVLA 85
Cdd:cd19078 1 GLEVSAIGLGCMgmshGYGPPPDKEEMIELIRKAVELGITFFDTAEVY-----G-PYT-NEELVGEALKPF--RDQVVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 86 SK----VAGPGRMDHIRDGNPrldrKNITAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTH--DPDdqaVEIEET 159
Cdd:cd19078 72 TKfgfkIDGGKPGPLGLDSRP----EHIRKAVEGSLKRLQTDYIDLY----------------YQHrvDPN---VPIEEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 160 LSVLGDLVKAGKIRHFGLSNETpwgtqrflhlAETLDLPRAV----SIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPL 235
Cdd:cd19078 129 AGTMKELIKEGKIRHWGLSEAG----------VETIRRAHAVcpvtAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 236 AFGVLAGKYLDGAR--PADGRLTLFeRFQrynnPQAVSATAKYVAL----AREHGLDPSQMALAYVTS-RPFVTSnIIGA 308
Cdd:cd19078 199 GKGFLTGKIDENTKfdEGDDRASLP-RFT----PEALEANQALVDLlkefAEEKGATPAQIALAWLLAkKPWIVP-IPGT 272
|
330 340
....*....|....*....|....*.
gi 966352627 309 TKLDQLKINLESIDVTLSDEVIAGIE 334
Cdd:cd19078 273 TKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-336 |
5.40e-52 |
|
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: 174.01 E-value: 5.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGT---------MTWGEQNTqDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYADRNdwV 83
Cdd:cd19102 1 LTTIGLGTwaiggggwgGGWGPQDD-RDSIAAIRAALDLGINWIDTAAVY-------GLGHSEEVVGRALKGLRDRP--I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 84 LASKVaGPGRMDhirDGNPR--LDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNffgvlgythdpddqaveIEETLS 161
Cdd:cd19102 71 VATKC-GLLWDE---EGRIRrsLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEP-----------------IEEAWG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 162 VLGDLVKAGKIRHFGLSNEtpWGTQrflhLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLA 241
Cdd:cd19102 130 ALAELKEEGKVRAIGVSNF--SVDQ----MKRCQAIHPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 GKyLDGAR----PADGRltlfERFQRYNNPQAVSATAKYV----ALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQ 313
Cdd:cd19102 204 GK-MTPERvaslPADDW----RRRSPFFQEPNLARNLALVdalrPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQ 278
|
330 340
....*....|....*....|...
gi 966352627 314 LKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19102 279 IDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-336 |
1.48e-51 |
|
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: 173.13 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 16 ICLGTMTWGEQN---TQDEAFEQIRMAKDAKVNFLDTAEMYPvpprgetYTKTESIIGEyfKKYADRnDWVLASKVAGpg 92
Cdd:cd19075 3 IILGTMTFGSQGrftTAEAAAELLDAFLERGHTEIDTARVYP-------DGTSEELLGE--LGLGER-GFKIDTKANP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 93 rmdhirDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNffgvlgythdpddqaveIEETLSVLGDLVKAGKI 172
Cdd:cd19075 71 ------GVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTP-----------------LEETLAAIDELYKEGKF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 173 RHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKYLDG-ARPA 251
Cdd:cd19075 128 KEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSeDKAG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 252 DGRLTLFERF-----QRYNNPQAVSATAKYVALAREHGLDPSQMALAYVT--SRPFVTSN---IIGATKLDQLKINLESI 321
Cdd:cd19075 208 GGRFDPNNALgklyrDRYWKPSYFEALEKVEEAAEKEGISLAEAALRWLYhhSALDGEKGdgvILGASSLEQLEENLAAL 287
|
330
....*....|....*.
gi 966352627 322 DV-TLSDEVIAGIEAI 336
Cdd:cd19075 288 EKgPLPEEVVKAIDEA 303
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-331 |
2.26e-51 |
|
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: 172.83 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 3 FRKLGKTDLSVSAICLGTmtW---GEQNTQDEAFEQIRMAKDAKVNFLDTAEMY-PVPPRgetytkTESIIGEYFK--KY 76
Cdd:cd19089 1 YRRCGRSGLHLPAISLGL--WhnfGDYTSPEEARELLRTAFDLGITHFDLANNYgPPPGS------AEENFGRILKrdLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 77 ADRNDWVLASKVA---GPGRMDhirDGNprlDRKNITAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTHDPDDQa 153
Cdd:cd19089 73 PYRDELVISTKAGygmWPGPYG---DGG---SRKYLLASLDQSLKRMGLDYVDIF----------------YHHRYDPD- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 154 VEIEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPrAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYS 233
Cdd:cd19089 130 TPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELGVP-LIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 234 PLAFGVLAGKYLDGaRPADGRLTLFERFQ--RYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKL 311
Cdd:cd19089 209 PLAQGLLTDKYLNG-IPPDSRRAAESKFLteEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSP 287
|
330 340
....*....|....*....|.
gi 966352627 312 DQLKINLESID-VTLSDEVIA 331
Cdd:cd19089 288 SQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-333 |
1.92e-48 |
|
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: 165.08 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 2 QFRKLGKTDLSVSAICLGTM----TWGEQNTqDEAFEQIRMAKDAKVNFLDTAEMYpVPPRGETytktesIIGEYFKKYa 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmsaFYGPADE-EESIATLHRALELGVTFLDTADMY-GPGTNEE------LLGKALKDR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 78 dRNDWVLASK---VAGPGRMDHIRDGNPrldrKNITAALEASLKRLNTDYLDLYQLHWPdrktnffgvlgythdpdDQAV 154
Cdd:cd19076 72 -RDEVVIATKfgiVRDPGSGFRGVDGRP----EYVRAACEASLKRLGTDVIDLYYQHRV-----------------DPNV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 155 EIEETLSVLGDLVKAGKIRHFGLSNETPwGTQRFLHlaetldlprAV----SIQNPYNLLNRTFEVGLAEiAIRE-QIGL 229
Cdd:cd19076 130 PIEETVGAMAELVEEGKVRYIGLSEASA-DTIRRAH---------AVhpitAVQSEYSLWTRDIEDEVLP-TCRElGIGF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 230 LAYSPLAFGVLAGKYLDGAR-PADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRpfvTSNII-- 306
Cdd:cd19076 199 VAYSPLGRGFLTGAIKSPEDlPEDDFRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQ---GDDIVpi 275
|
330 340
....*....|....*....|....*...
gi 966352627 307 -GATKLDQLKINLESIDVTLSDEVIAGI 333
Cdd:cd19076 276 pGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-336 |
2.02e-47 |
|
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: 162.09 E-value: 2.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 10 DLSVSAICLGTMT-----WGEQNtQDEAFEQIRMAKDAKVNFLDTAemyPVPPRGetytKTESIIGEYFKKYADRNDWVL 84
Cdd:cd19148 1 DLPVSRIALGTWAiggwmWGGTD-EKEAIETIHKALDLGINLIDTA---PVYGFG----LSEEIVGKALKEYGKRDRVVI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 85 ASKVAGPGRMDHIRDGNPRLDRknITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIEETLSVLG 164
Cdd:cd19148 73 ATKVGLEWDEGGEVVRNSSPAR--IRKEVEDSLRRLQTDYIDLYQVHWPDPLV-----------------PIEETAEALK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 165 DLVKAGKIRHFGLSNETPWGTQRFLHLAetldlPRAVsIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKY 244
Cdd:cd19148 134 ELLDEGKIRAIGVSNFSPEQMETFRKVA-----PLHT-VQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 245 -LDGARPADGRLTLFERFQRYNNPQAVSATAKYVALAREHGlDPSQMALA--YVTSRPFVTSNIIGATKLDQLKINLESI 321
Cdd:cd19148 208 tKDTKFEGDDLRRTDPKFQEPRFSQYLAAVEELDKLAQERY-GKSVIHLAvrWLLDQPGVSIALWGARKPEQLDAVDEVF 286
|
330
....*....|....*
gi 966352627 322 DVTLSDEVIAGIEAI 336
Cdd:cd19148 287 GWSLNDEDMKEIDAI 301
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-322 |
7.28e-44 |
|
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: 152.49 E-value: 7.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVPPRGETYTKTESIIGEYFKKYADRNDWVLASKVAGPGR 93
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGGESERLIGRWLKDRGNRDDVVIATKVGAGPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 94 MDHIRDGNPR-LDRKNITAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTHdPDDQAVEIEETLSVLGDLVKAGKI 172
Cdd:cd19752 81 DPDGGPESPEgLSAETIEQEIDKSLRRLGTDYIDLY----------------YAH-VDDRDTPLEETLEAFNELVKAGKV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 173 RHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLL--NRTFEVGLAEIAIREQI---------GLLAYSPLafgvLA 241
Cdd:cd19752 144 RAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLrpRPGADFGVQRIVTDELLdyassrpdlTLLAYSPL----LS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 GKYLDGARPadgrltlfeRFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESI 321
Cdd:cd19752 220 GAYTRPDRP---------LPEQYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
.
gi 966352627 322 D 322
Cdd:cd19752 291 D 291
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-339 |
1.14e-43 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 154.21 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMTWGEQNtQDEAFEQIRMAKDAKVNFLDTAemYPvpprgetYTKTESIIGEYFKKYadRN 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRKD-EEEAEALIRRAIDNGINYIDTA--RG-------YGDSEEFLGKALKGP--RD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 81 DWVLASKVAGPGRmdhirdgnprlDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNFfgvlgythdpdDQAVEIEETL 160
Cdd:COG1453 69 KVILATKLPPWVR-----------DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDL-----------EKVLKPGGAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 161 SVLGDLVKAGKIRHFGLSNETPwgTQRFLHLAETlDLPRAVSIQnpYNLLNRTFEVGLA--EIAIREQIGLLAYSPLafg 238
Cdd:COG1453 127 EALEKAKAEGKIRHIGFSTHGS--LEVIKEAIDT-GDFDFVQLQ--YNYLDQDNQAGEEalEAAAEKGIGVIIMKPL--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 239 vlagkyldgarpADGRLtlferfqrYNNPQAVSATAkyvalarEHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINL 318
Cdd:COG1453 199 ------------KGGRL--------ANPPEKLVELL-------CPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
|
330 340
....*....|....*....|...
gi 966352627 319 ESID--VTLSDEVIAGIEAIHTA 339
Cdd:COG1453 252 KTADnlEPLTEEELAILERLAEE 274
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-331 |
2.97e-43 |
|
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: 151.40 E-value: 2.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 2 QFRKLGKTDLSVSAICLGTmtW---GEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvPPRGETYTKTESIIGEYFKKYad 78
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGL--WhnfGDVDRYENSRAMLRRAFDLGITHFDLANNYG-PPPGSAEENFGRILKEDLKPY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKvAG----PGrmdhirdgnPRLD---RKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpdd 151
Cdd:cd19151 76 RDELIISTK-AGytmwPG---------PYGDwgsKKYLIASLDQSLKRMGLDYVDIFYHHRPDPET-------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 152 qavEIEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPraVSIQNP-YNLLNRTFEVGLAEIAIREQIGLL 230
Cdd:cd19151 132 ---PLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLGTP--CLIHQPkYSMFNRWVEEGLLDVLEEEGIGCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 231 AYSPLAFGVLAGKYLDGArPADGRLTLFERFQRYNN--PQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19151 207 AFSPLAQGLLTDRYLNGI-PEDSRAAKGSSFLKPEQitEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGA 285
|
330 340
....*....|....*....|....
gi 966352627 309 TKLDQLKINLESIDVT-LSDEVIA 331
Cdd:cd19151 286 SKPSQIEDAVGALDNReFSEEELA 309
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-336 |
8.66e-43 |
|
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: 150.67 E-value: 8.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTM----TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetyTKTESIIGEYFKK- 75
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsaFYGPPKPDEERFAVLDAAFELGCTFWDTADIY---------GDSEELIGRWFKQn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 76 YADRNDWVLASKVAG---PGRMDHIRDGNPRLDRKnitaALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddq 152
Cdd:cd19144 72 PGKREKIFLATKFGIeknVETGEYSVDGSPEYVKK----ACETSLKRLGVDYIDLYYQHRVDGKT--------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 153 avEIEETLSVLGDLVKAGKIRHFGLSnETPWGTQRFLHLAETLDlprAVSIQ-NPYNLLNRTFEVGLAEIAIREQIGLLA 231
Cdd:cd19144 133 --PIEKTVAAMAELVQEGKIKHIGLS-ECSAETLRRAHAVHPIA---AVQIEySPFSLDIERPEIGVLDTCRELGVAIVA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 232 YSPLAFGVLAGKYL--DGARPADGRLTLfERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGAT 309
Cdd:cd19144 207 YSPLGRGFLTGAIRspDDFEEGDFRRMA-PRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTT 285
|
330 340
....*....|....*....|....*..
gi 966352627 310 KLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19144 286 KLKRLEENLGALKVKLTEEEEKEIREI 312
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
13-334 |
2.29e-42 |
|
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: 148.93 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTM--TWGEQNTQDE-AFEQIRMAKDAKVNFLDTAEMYPVPPRgetyTKTESIIGEYFKKYADRNDWVLASKVA 89
Cdd:cd19077 5 VGPIGLGLMglTWRPNPTPDEeAFETMKAALDAGSNLWNGGEFYGPPDP----HANLKLLARFFRKYPEYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 90 GPGRMDHIRDGnprlDRKNITAALEASLKRLN-TDYLDLYQlhwPDRKtnffgvlgythdpdDQAVEIEETLSVLGDLVK 168
Cdd:cd19077 81 GLDPDTLRPDG----SPEAVRKSIENILRALGgTKKIDIFE---PARV--------------DPNVPIEETIKALKELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 169 AGKIRHFGLSNETpwgtqrflhlAETLDLPRAV----SIQNPYNLLNRT-FEVGLAEIAIREQIGLLAYSPLAFGVLAGK 243
Cdd:cd19077 140 EGKIRGIGLSEVS----------AETIRRAHAVhpiaAVEVEYSLFSREiEENGVLETCAELGIPIIAYSPLGRGLLTGR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 244 Y--LDGARPADGRLtLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTsnII---GATKLDQLKINL 318
Cdd:cd19077 210 IksLADIPEGDFRR-HLDRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPK--IIpipGSTTLERVEENL 286
|
330
....*....|....*.
gi 966352627 319 ESIDVTLSDEVIAGIE 334
Cdd:cd19077 287 KAANVELTDEELKEIN 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-329 |
1.02e-41 |
|
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: 146.55 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTMTWG---EQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETytktESIIGEYFKKYAdRNDWVLASKVag 90
Cdd:cd19090 1 SALGLGTAGLGgvfGGVDDDEAVATIRAALDLGINYIDTAPAY-----GDS----EERLGLALAELP-REPLVLSTKV-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 91 pGRMdhiRDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRktnffgvlgythDPDDQAVEIEETLSVLGDLVKAG 170
Cdd:cd19090 69 -GRL---PEDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPER------------VPWVDILAPGGALEALLELKEEG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 171 KIRHFGLSNeTPWGTQRflHLAETLDLPRAVSIQNpYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKYLDGARP 250
Cdd:cd19090 133 LIKHIGLGG-GPPDLLR--RAIETGDFDVVLTANR-YTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRY 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966352627 251 ADGRLTlferfqrynnPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVTLSDEV 329
Cdd:cd19090 209 TYRWLS----------PELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEEL 277
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-326 |
1.66e-41 |
|
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: 145.44 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTMT------WGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvpPRGetytkTESIIGEYFKKYADrnDWVLAS 86
Cdd:cd19088 1 VSRLGYGAMRltgpgiWGPPADREEAIAVLRRALELGVNFIDTADSYG--PDV-----NERLIAEALHPYPD--DVVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 87 KVA----GPGRMDhiRDGNPrldrKNITAALEASLKRLNTDYLDLYQLHWPDrktnffgvlgythdpddQAVEIEETLSV 162
Cdd:cd19088 72 KGGlvrtGPGWWG--PDGSP----EYLRQAVEASLRRLGLDRIDLYQLHRID-----------------PKVPFEEQLGA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 163 LGDLVKAGKIRHFGLSNETPwgtqrfLHLAETLDLPRAVSIQNPYNLLNRTFEvGLAEIAIREQIGLLAYSPLafgvlag 242
Cdd:cd19088 129 LAELQDEGLIRHIGLSNVTV------AQIEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPL------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 243 kyldGARPADGRLTLFErfqrynnpqavsatakyvALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESID 322
Cdd:cd19088 195 ----GGGDLAQPGGLLA------------------EVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAG 252
|
....
gi 966352627 323 VTLS 326
Cdd:cd19088 253 LRLS 256
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-328 |
4.06e-41 |
|
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: 145.39 E-value: 4.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 8 KTDLSVSAICLGTMTWGEQNTQDEAFEQ-IRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYAD-RNDWVLA 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSlIEAALELGITTFDHADIY-------GGGKCEELFGEALALNPGlREKIEIQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 86 SKvAGpgrmdhIRDGNPR---------LDRKNITAALEASLKRLNTDYLDLYQLHWPDrktnffgVLgythdpddqaVEI 156
Cdd:cd19092 74 TK-CG------IRLGDDPrpgrikhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPD-------PL----------MDP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 157 EETLSVLGDLVKAGKIRHFGLSNETPWgtqRFLHLAETLDLPRAVSiQNPYNLLNRT-FEVGLAEIAIREQIGLLAYSPL 235
Cdd:cd19092 130 EEVAEAFDELVKSGKVRYFGVSNFTPS---QIELLQSYLDQPLVTN-QIELSLLHTEaIDDGTLDYCQLLDITPMAWSPL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 236 AFGVLAGKYLdgarpadgrltlfERFQRYNnpqavsatAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLK 315
Cdd:cd19092 206 GGGRLFGGFD-------------ERFQRLR--------AALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIR 264
|
330
....*....|...
gi 966352627 316 INLESIDVTLSDE 328
Cdd:cd19092 265 SAVKALDIELTRE 277
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-321 |
1.86e-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: 142.34 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMtwgeqNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYaDRN 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGG-----GLPRESPELLRRALDLGINYFDTAEGY-------GNGNSEEIIGEALKGL-RRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 81 DWVLASKVAGPGRmdhirdgnpRLDRKNITAALEASLKRLNTDYLDLYQLHwpdrktnffGVlgythDPDDQAVEIEETL 160
Cdd:cd19105 68 KVFLATKASPRLD---------KKDKAELLKSVEESLKRLQTDYIDIYQLH---------GV-----DTPEERLLNEELL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 161 SVLGDLVKAGKIRHFGLSNETPwgtqrflhLAETLDlpRAV------SIQNPYNLLNRTFEVG--LAEiAIREQIGLLAY 232
Cdd:cd19105 125 EALEKLKKEGKVRFIGFSTHDN--------MAEVLQ--AAIesgwfdVIMVAYNFLNQPAELEeaLAA-AAEKGIGVVAM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 233 SPLAfgvlagkyldGARPADGRLTLFERfQRYNNPQAvsatakyvalarehgldpsqmALAYVTSRPFVTSNIIGATKLD 312
Cdd:cd19105 194 KTLA----------GGYLQPALLSVLKA-KGFSLPQA---------------------ALKWVLSNPRVDTVVPGMRNFA 241
|
....*....
gi 966352627 313 QLKINLESI 321
Cdd:cd19105 242 ELEENLAAA 250
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-334 |
1.68e-39 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 140.46 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 9 TDLSVSAICLGTMTWGEQ-NTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETytKTESIIGEYFKkyADRNDWVLASK 87
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDpAKRAQEIEALRAGIDLGMTLIDTAEMY-----GDG--GSEELVGEAIR--GRRDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 88 VAgpgrmdhirdgnPR-LDRKNITAALEASLKRLNTDYLDLYQLHWPDRktnffgvlgythdpddqaVEIEETLSVLGDL 166
Cdd:cd19138 78 VL------------PSnASRQGTVRACERSLRRLGTDYLDLYLLHWRGG------------------VPLAETVAAMEEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 167 VKAGKIRHFGLSNetpWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKyld 246
Cdd:cd19138 128 KKEGKIRAWGVSN---FDTDDMEELWAVPGGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRR--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 247 garpadgrltlferfQRYNNPqavsataKYVALAREHGLDPSQMALAYVTSRPFVTSnIIGATKLDQLKINLESIDVTLS 326
Cdd:cd19138 202 ---------------GLLENP-------TLKEIAARHGATPAQVALAWVLRDGNVIA-IPKSGSPEHARENAAAADLELT 258
|
....*...
gi 966352627 327 DEVIAGIE 334
Cdd:cd19138 259 EEDLAELD 266
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-336 |
3.26e-39 |
|
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: 141.25 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 2 QFRKLGKTDLSVSAICLG----TMTWGEQnTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETytKTESIIGEYFKkyA 77
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggiGGLMGRT-TREEQIAAVRRALDLGINFFDTAPSY-----GDG--KSEENLGRALK--G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 78 DRNDWVLASKVA-GPGRMDHIRDGnprldrknITAALEASLKRLNTDYLDLYQLH---WPDRKTNFFGVLGYTHDPDDQA 153
Cdd:cd19104 71 LPAGPYITTKVRlDPDDLGDIGGQ--------IERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVGGTLSTTDVLGLGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 154 VeieetLSVLGDLVKAGKIRHFGLsneTPWGTQRFLHlaETLDLPRAVSIQNPYNLLN--------RTFEV----GLAEI 221
Cdd:cd19104 143 V-----ADAFERLRSEGKIRFIGI---TGLGNPPAIR--ELLDSGKFDAVQVYYNLLNpsaaearpRGWSAqdygGIIDA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 222 AIREQIGLLAYSPLAFGVLAGKyLDGARPADG--RLTLFERFQRynnpqavsaTAKYVALAREHGLDPSQMALAYVTSRP 299
Cdd:cd19104 213 AAEHGVGVMGIRVLAAGALTTS-LDRGREAPPtsDSDVAIDFRR---------AAAFRALAREWGETLAQLAHRFALSNP 282
|
330 340 350
....*....|....*....|....*....|....*...
gi 966352627 300 FVTSNIIGATKLDQLKINLESIDV-TLSDEVIAGIEAI 336
Cdd:cd19104 283 GVSTVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-319 |
3.70e-39 |
|
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: 138.77 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 4 RKLGKTDLSVSAICLGTMTWGEqNTQDEAFEQIRMAKDAKVNFLDTAEMYPvpprgetytKTESIIGEYFKKYadRNDWV 83
Cdd:cd19100 2 RRLGRTGLKVSRLGFGGGPLGR-LSQEEAAAIIRRALDLGINYFDTAPSYG---------DSEEKIGKALKGR--RDKVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 84 LASKVAGPgrmdhirdgnprlDRKNITAALEASLKRLNTDYLDLYQLHWPDrktnffgvlgyTHDPDDQAVEIEETLSVL 163
Cdd:cd19100 70 LATKTGAR-------------DYEGAKRDLERSLKRLGTDYIDLYQLHAVD-----------TEEDLDQVFGPGGALEAL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 164 GDLVKAGKIRHFGLSNETPwgtQRFLHLAETLDLPravSIQNPYNLL---NRTFEVGLAEIAIREQIGLLAYSPLAFGVL 240
Cdd:cd19100 126 LEAKEEGKIRFIGISGHSP---EVLLRALETGEFD---VVLFPINPAgdhIDSFREELLPLAREKGVGVIAMKVLAGGRL 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966352627 241 AGKyldgarpadgrltlferfqrynnpqavsatakyvalareHGLDPSQmALAYVTSRPFVTSNIIGATKLDQLKINLE 319
Cdd:cd19100 200 LSG---------------------------------------DPLDPEQ-ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-336 |
1.42e-38 |
|
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: 138.88 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 23 WGEQNTQDEAFEQIRMAKDAKVNFLDTAEmypvpprgeTYTKTESIIGEYFKKYADRNDwvLASKVAGpgrmdH----IR 98
Cdd:cd19101 16 HGGIRDEDAAVRAMAAYVDAGLTTFDCAD---------IYGPAEELIGEFRKRLRRERD--AADDVQI-----HtkwvPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 99 DGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDrktnfFGVLGYthdpddqaveiEETLSVLGDLVKAGKIRHFGLS 178
Cdd:cd19101 80 PGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWD-----YSDPGY-----------LDAAKHLAELQEEGKIRHLGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 179 N-ETPwgtqrflHLAETLDL-PRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKYLDGARPADGRLT 256
Cdd:cd19101 144 NfDTE-------RLREILDAgVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYLGVPEPTGPALE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 257 ---------LFERFQRYNNPQAVSATAKyvALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVTLSD 327
Cdd:cd19101 217 trslqkyklMIDEWGGWDLFQELLRTLK--AIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDD 294
|
....*....
gi 966352627 328 EVIAGIEAI 336
Cdd:cd19101 295 EDRAAIDAV 303
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-331 |
4.86e-38 |
|
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: 137.30 E-value: 4.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMTWGE---QNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETytKTESIIGEYFKKyA 77
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGvfgPVDEEEAIRTVHEALDSGINYIDTAPWY-----GQG--RSETVLGKALKG-I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 78 DRNDWVLASKVagpGRMDhiRDGNPRLD--RKNITAALEASLKRLNTDYLDLYQLHWPDrktnfFGvlgythDPDDQAve 155
Cdd:cd19163 73 PRDSYYLATKV---GRYG--LDPDKMFDfsAERITKSVEESLKRLGLDYIDIIQVHDIE-----FA------PSLDQI-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 156 IEETLSVLGDLVKAGKIRHFGLSNeTPWGTQRFL--HLAETLDlprAVSIQNPYNLLNRTFEvGLAEIAIREQIGLLAYS 233
Cdd:cd19163 135 LNETLPALQKLKEEGKVRFIGITG-YPLDVLKEVleRSPVKID---TVLSYCHYTLNDTSLL-ELLPFFKEKGVGVINAS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 234 PLAFGVLAGKYLDGARPAdgrltlferfqrynNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQ 313
Cdd:cd19163 210 PLSMGLLTERGPPDWHPA--------------SPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPEN 275
|
330
....*....|....*...
gi 966352627 314 LKINLESIDVTLSDEVIA 331
Cdd:cd19163 276 LRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
13-336 |
9.19e-38 |
|
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: 137.56 E-value: 9.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTMTWGEQNT-------QDEAFEQIRMAKDAKVNFLDTAEMYpvppRGETytkTESIIGEYFKKYADRNDWVLA 85
Cdd:cd19146 11 VSPLCLGAMSFGEAWKsmmgecdKETAFKLLDAFYEQGGNFIDTANNY----QGEE---SERWVGEWMASRGNRDEMVLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 86 SK-VAGPGRMDHIR-----DGNprlDRKNITAALEASLKRLNTDYLDLYQLHWPDrktnffgvlgYThdpddqaVEIEET 159
Cdd:cd19146 84 TKyTTGYRRGGPIKiksnyQGN---HAKSLRLSVEASLKKLQTSYIDILYVHWWD----------YT-------TSIPEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 160 LSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLlaySPlaFGV 239
Cdd:cd19146 144 MQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMAL---AP--WGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 240 LA-GKYldgaRPADGRLTLfERFQRYNNPQA---VSATAKYVALAREHGLDPSQMALAYVTSR-PFVTSnIIGATKLDQL 314
Cdd:cd19146 219 LGqGQF----RTEEEFKRR-GRSGRKGGPQTekeRKVSEKLEKVAEEKGTAITSVALAYVMHKaPYVFP-IVGGRKVEHL 292
|
330 340
....*....|....*....|..
gi 966352627 315 KINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19146 293 KGNIEALGISLSDEEIQEIEDA 314
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-320 |
7.18e-36 |
|
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: 130.43 E-value: 7.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTM-TWGEQN--TQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETytktESIIGEYFKKYaDRNDWVLASKVAg 90
Cdd:cd19095 1 SVLGLGTSgIGRVWGvpSEAEAARLLNTALDLGINLIDTAPAY-----GRS----EERLGRALAGL-RRDDLFIATKVG- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 91 pgrmDHIRDGNPRLD--RKNITAALEASLKRLNTDYLDLYQLHWPDRktnffgvlgythdpddqAVEIEETLSVLGDLVK 168
Cdd:cd19095 70 ----THGEGGRDRKDfsPAAIRASIERSLRRLGTDYIDLLQLHGPSD-----------------DELTGEVLETLEDLKA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 169 AGKIRHFGLSNETPwgtqrflHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIReQIGLLAYSPLAFGVLAGKYLDGA 248
Cdd:cd19095 129 AGKVRYIGVSGDGE-------ELEAAIASGVFDVVQLPYNVLDREEEELLPLAAEA-GLGVIVNRPLANGRLRRRVRRRP 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966352627 249 RPADGRltlferfqrynnpqavsatAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLES 320
Cdd:cd19095 201 LYADYA-------------------RRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-334 |
5.55e-35 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 130.49 E-value: 5.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTM-TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvPPRGETYTKTESIIGEYFKKYadR 79
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNYG-PPPGSAEENFGRLLREDFAAY--R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 80 NDWVLASKvAG----PGRMDhirDGNprlDRKNITAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTHDPDDQAvE 155
Cdd:PRK09912 90 DELIISTK-AGydmwPGPYG---SGG---SRKYLLASLDQSLKRMGLEYVDIF----------------YSHRVDENT-P 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 156 IEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSiQNPYNLLNRTFE-VGLAEIAIREQIGLLAYSP 234
Cdd:PRK09912 146 MEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIH-QPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 235 LAFGVLAGKYLDGArPADGRLtlferfQRYNNpQAVSATAKYVA------------LAREHGLDPSQMALAYVTSRPFVT 302
Cdd:PRK09912 225 LAQGLLTGKYLNGI-PQDSRM------HREGN-KVRGLTPKMLTeanlnslrllneMAQQRGQSMAQMALSWLLKDERVT 296
|
330 340 350
....*....|....*....|....*....|...
gi 966352627 303 SNIIGATKLDQLKINLESI-DVTLSDEVIAGIE 334
Cdd:PRK09912 297 SVLIGASRAEQLEENVQALnNLTFSTEELAQID 329
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-333 |
3.98e-34 |
|
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: 127.16 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 4 RKLGKTDLSVSAICLGTM----TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETytKTESIIGEYFKKYAdR 79
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsgDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIY-----GPN--TNEVLLGKALKDGP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 80 NDWVLASK----VAGPGRMDhIRdGNPRLDRknitAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTHDPdDQAVE 155
Cdd:cd19145 75 EKVQLATKfgihEIGGSGVE-VR-GDPAYVR----AACEASLKRLDVDYIDLY----------------YQHRI-DTTVP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 156 IEETLSVLGDLVKAGKIRHFGLSNETPwGTQRFLHLAETLdlpraVSIQNPYNLLNRTFEvglAEI--AIRE-QIGLLAY 232
Cdd:cd19145 132 IEITMGELKKLVEEGKIKYIGLSEASA-DTIRRAHAVHPI-----TAVQLEWSLWTRDIE---EEIipTCRElGIGIVPY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 233 SPLAFGVLAGKYLDGARPADG-RLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKL 311
Cdd:cd19145 203 SPLGRGFFAGKAKLEELLENSdVRKSHPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKI 282
|
330 340
....*....|....*....|..
gi 966352627 312 DQLKINLESIDVTLSDEVIAGI 333
Cdd:cd19145 283 KNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
2-331 |
1.63e-33 |
|
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: 125.64 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 2 QFRKLGKTDLSVSAICLGTM-TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvPPRGETYTKTESIIGEYFKKYadRN 80
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWhNFGDDTPLETQRAILRTAFDLGITHFDLANNYG-PPPGSAEENFGRILREDFAGY--RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 81 DWVLASKV-----AGP----GrmdhirdgnprlDRKNITAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTH--DP 149
Cdd:cd19150 78 ELIISTKAgydmwPGPygewG------------SRKYLLASLDQSLKRMGLDYVDIF----------------YSHrfDP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 150 DdqaVEIEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPraVSIQNP-YNLLNRTFE-VGLAEIAIREQI 227
Cdd:cd19150 130 D---TPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELGTP--LLIHQPsYNMLNRWVEeSGLLDTLQELGV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 228 GLLAYSPLAFGVLAGKYLDGArPADGRLTLFERF-QRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNII 306
Cdd:cd19150 205 GCIAFTPLAQGLLTDKYLNGI-PEGSRASKERSLsPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALI 283
|
330 340
....*....|....*....|....*.
gi 966352627 307 GATKLDQLKINLESID-VTLSDEVIA 331
Cdd:cd19150 284 GASRPEQLEENVGALDnLTFSADELA 309
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
22-344 |
8.44e-33 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 122.47 E-value: 8.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 22 TWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKY-ADRNDWVLASKVAgpgrmdhirdg 100
Cdd:COG0656 12 TW--QLPGEEAAAAVRTALEAGYRHIDTAAMY----------GNEEGVGEAIAASgVPREELFVTTKVW----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 101 NPRLDRKNITAALEASLKRLNTDYLDLYQLHWPdrktnffgvlgythdpddQAVEIEETLSVLGDLVKAGKIRHFGLSNe 180
Cdd:COG0656 69 NDNHGYDDTLAAFEESLERLGLDYLDLYLIHWP------------------GPGPYVETWRALEELYEEGLIRAIGVSN- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 181 tpwgtqrFL--HLAETLDLPRA--VSIQNPYNLLNRTFEvgLAEIAIREQIGLLAYSPLAfgvlAGKYLDGArpadgrlT 256
Cdd:COG0656 130 -------FDpeHLEELLAETGVkpAVNQVELHPYLQQRE--LLAFCREHGIVVEAYSPLG----RGKLLDDP-------V 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 257 LferfqrynnpqavsatakyVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:COG0656 190 L-------------------AEIAEKHGKTPAQVVLRWHLQRGVVV--IPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
330
....*....|.
gi 966352627 337 HTAQ---PNPA 344
Cdd:COG0656 249 DRGErlgPDPD 259
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-322 |
2.31e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 118.78 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGT----MTWGEQNT-----QDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETytktESIIGEYFKKYadrNDWVL 84
Cdd:cd19097 1 SKLALGTaqfgLDYGIANKsgkpsEKEAKKILEYALKAGINTLDTAPAY-----GDS----EKVLGKFLKRL---DKFKI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 85 ASKVAGPgrmdhirDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHwpdrktnffgvlgythDPDDQAVEIEETLSVLG 164
Cdd:cd19097 69 ITKLPPL-------KEDKKEDEAAIEASVEASLKRLKVDSLDGLLLH----------------NPDDLLKHGGKLVEALL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 165 DLVKAGKIRHFGLSNETPWgtqrflHLAETLDLPRAVSIQNPYNLLNRTFEV-GLAEIAIREQIGLLAYSplAF--GVLa 241
Cdd:cd19097 126 ELKKEGLIRKIGVSVYSPE------ELEKALESFKIDIIQLPFNILDQRFLKsGLLAKLKKKGIEIHARS--VFlqGLL- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 gkyLDgarPADGRLTLFERFQRYNNpqavsataKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESI 321
Cdd:cd19097 197 ---LM---EPDKLPAKFAPAKPLLK--------KLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAF 262
|
.
gi 966352627 322 D 322
Cdd:cd19097 263 K 263
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-323 |
4.64e-31 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 119.09 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 3 FRKLGKTDLSVSAICLGT-MTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVpprgetyTKTESIIGEYFKKYA-DRN 80
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTwVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAA-------GKAEIVLGKILKKKGwRRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 81 DWVLASKVAGPGRMDHIRDgnprLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIEETL 160
Cdd:cd19141 75 SYVITTKIFWGGKAETERG----LSRKHIIEGLKASLERLQLEYVDIVFANRPDPNT-----------------PMEEIV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 161 SVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNR-TFEVGLAEIAIREQIGLLAYSPLAFGV 239
Cdd:cd19141 134 RAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 240 LAGKYLDGArPADGRLTL------FERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQ 313
Cdd:cd19141 214 LSGKYDDGV-PEYSRASLkgyqwlKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQ 292
|
330
....*....|
gi 966352627 314 LKINLESIDV 323
Cdd:cd19141 293 LYENLQAIQV 302
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-334 |
6.94e-31 |
|
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: 116.99 E-value: 6.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 18 LGTMTWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKY-ADRNDWVLASKVagpgrmdh 96
Cdd:cd19073 4 LGLGTW--QLRGDDCANAVKEALELGYRHIDTAEIY----------NNEAEVGEAIAESgVPREDLFITTKV-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 97 IRDgnpRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRktnffgvlgythdpddqAVEIEETLSVLGDLVKAGKIRHFG 176
Cdd:cd19073 64 WRD---HLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNP-----------------TVPLEETLGALKELKEAGKVKSIG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 177 LSNETPWgtqrflHLAETLDLPRAVSIQN-----PYnlLNRTfevGLAEIAIREQIGLLAYSPLAFGvlagkyldgarpa 251
Cdd:cd19073 124 VSNFTIE------LLEEALDISPLPIAVNqvefhPF--LYQA---ELLEYCRENDIVITAYSPLARG------------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 252 dgrltlferfQRYNNPQAVSatakyvaLAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIA 331
Cdd:cd19073 180 ----------EVLRDPVIQE-------IAEKYDKTPAQVALRWLVQKGIVV--IPKASSEDHLKENLAIFDWELTSEDVA 240
|
...
gi 966352627 332 GIE 334
Cdd:cd19073 241 KID 243
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-322 |
6.23e-30 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 114.97 E-value: 6.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTM----TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvppRGetytKTESIIGEYFKKYaDRNDWVLASKVa 89
Cdd:cd19096 1 SVLGFGTMrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYG---GG----KSEEILGEALKEG-PREKFYLATKL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 90 gPGRMDHIRDGNPRLdrknitaaLEASLKRLNTDYLDLYQLHWPDRKTNffgvlgythdpdDQAVEIEETLSVLGDLVKA 169
Cdd:cd19096 72 -PPWSVKSAEDFRRI--------LEESLKRLGVDYIDFYLLHGLNSPEW------------LEKARKGGLLEFLEKAKKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 170 GKIRHFGLSnetpwgtqrFlH-----LAETLDLPRAVSIQNPYNLLNRTFE--VGLAEIAIREQIGLLAYSPLAFGVLAg 242
Cdd:cd19096 131 GLIRHIGFS---------F-HdspelLKEILDSYDFDFVQLQYNYLDQENQagRPGIEYAAKKGMGVIIMEPLKGGGLA- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 243 kyldgarpadgrltlferfqrYNNPQAvsatakyVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESID 322
Cdd:cd19096 200 ---------------------NNPPEA-------LAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-341 |
1.63e-29 |
|
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: 115.57 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGT-MTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVpprgetyTKTESIIGEYFKKYA-D 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVAGPGRMDHIRDgnprLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIEE 158
Cdd:cd19158 74 RSSLVITTKIFWGGKAETERG----LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNT-----------------PMEE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNR-TFEVGLAEIAIREQIGLLAYSPLAF 237
Cdd:cd19158 133 TVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLAC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 238 GVLAGKYLDGARPAD-----GRLTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLD 312
Cdd:cd19158 213 GIVSGKYDSGIPPYSraslkGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAE 292
|
330 340 350
....*....|....*....|....*....|.
gi 966352627 313 QLKINLESIDV--TLSDEVIAGIEAIHTAQP 341
Cdd:cd19158 293 QLMENIGAIQVlpKLSSSIVHEIDSILGNKP 323
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-328 |
2.99e-29 |
|
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: 113.05 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTmtWG-------EQNTQDEAFEQIRMAKDAKVNFLDTAEMYPvppRGETytktESIIGEYFKKYAdRNDWVLA 85
Cdd:cd19137 4 IPALGLGT--WGiggfltpDYSRDEEMVELLKTAIELGYTHIDTAEMYG---GGHT----EELVGKAIKDFP-REDLFIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 86 SKVAgpgrmdhirdgNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNFfgvlgythdpddqaveiEETLSVLGD 165
Cdd:cd19137 74 TKVW-----------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPL-----------------EETLSAMAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 166 LVKAGKIRHFGLSNetpwGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEV-GLAEIAIREQIGLLAYSPLAFGVLAGKy 244
Cdd:cd19137 126 GVRQGLIRYIGVSN----FNRRLLEEAISKSQTPIVCNQVKYNLEDRDPERdGLLEYCQKNGITVVAYSPLRRGLEKTN- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 245 ldgarpadgrltlfERFQRynnpqavsatakyvaLAREHGLDPSQMALAYVTSRPFVTSnIIGATKLDQLKINLESIDVT 324
Cdd:cd19137 201 --------------RTLEE---------------IAKNYGKTIAQIALAWLIQKPNVVA-IPKAGRVEHLKENLKATEIK 250
|
....
gi 966352627 325 LSDE 328
Cdd:cd19137 251 LSEE 254
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-335 |
3.00e-29 |
|
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: 113.97 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 10 DLSVSAICLGTMTWG--------------EQNTQDEAFEQirmAKDAKVNFLDTAEMYpvpprGETytKTESIIGEYFKK 75
Cdd:cd19103 1 DKKLPKIALGTWSWGsggaggdqvfgnhlDEDTLKAVFDK---AMAAGLNLWDTAAVY-----GMG--ASEKILGEFLKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 76 YAdRNDWVLASK----VAGPGrmdhirdGNPrldrknITAALEASLKRLNTDYLDLYQLhwpdrktnffgvlgytHDPDD 151
Cdd:cd19103 71 YP-REDYIISTKftpqIAGQS-------ADP------VADMLEGSLARLGTDYIDIYWI----------------HNPAD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 152 qaveIEETLSVLGDLVKAGKIRHFGLSNETpwgtqrflhLAEtldLPRAVSI-----------QNPYNLLNRTFE-VGLA 219
Cdd:cd19103 121 ----VERWTPELIPLLKSGKVKHVGVSNHN---------LAE---IKRANEIlakagvslsavQNHYSLLYRSSEeAGIL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 220 EIAIREQIGLLAYSPLAFGVLAGKYLDGARPADGRLtlfeRFQRYNN--PQAVSATAKYVALAREHGLDPSQMALAYVTS 297
Cdd:cd19103 185 DYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSG----RAETYNPllPQLEELTAVMAEIGAKHGASIAQVAIAWAIA 260
|
330 340 350
....*....|....*....|....*....|....*...
gi 966352627 298 RPfvTSNIIGATKLDQLKINLESIDVTLSDEVIAGIEA 335
Cdd:cd19103 261 KG--TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQ 296
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-341 |
7.41e-29 |
|
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: 113.60 E-value: 7.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGT-MTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVpprgetyTKTESIIGEYFKKYA-D 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVAGPGRMDHIRDgnprLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTnffgvlgythdpddqavEIEE 158
Cdd:cd19159 74 RSSLVITTKLYWGGKAETERG----LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNT-----------------PMEE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNR-TFEVGLAEIAIREQIGLLAYSPLAF 237
Cdd:cd19159 133 IVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLAC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 238 GVLAGKYLDGArPADGRLT------LFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKL 311
Cdd:cd19159 213 GIISGKYGNGV-PESSRASlkcyqwLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTP 291
|
330 340 350
....*....|....*....|....*....|..
gi 966352627 312 DQLKINLESIDV--TLSDEVIAGIEAIHTAQP 341
Cdd:cd19159 292 EQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 323
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-341 |
1.64e-27 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 110.07 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGT-MTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYPVpprgetyTKTESIIGEYFKKYA-D 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA-------GKAERTLGNILKSKGwR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVAGPGRMDHIRDgnprLDRKNITAALEASLKRLNTDYLDLyqlhwpdrktnffgVLGYTHDPDDqavEIEE 158
Cdd:cd19160 76 RSSYVVTTKIYWGGQAETERG----LSRKHIIEGLRGSLDRLQLEYVDI--------------VFANRSDPNS---PMEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHFGLSNetpWGTQRFLH---LAETLDLPRAVSIQNPYNLLNR-TFEVGLAEIAIREQIGLLAYSP 234
Cdd:cd19160 135 IVRAMTYVINQGMAMYWGTSR---WSAMEIMEaysVARQFNLIPPVCEQAEYHLFQReKVEMQLPELYHKIGVGSVTWSP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 235 LAFGVLAGKYlDGARPADGRLT------LFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19160 212 LACGLITGKY-DGRVPDTCRAAvkgyqwLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGV 290
|
330 340 350
....*....|....*....|....*....|....*
gi 966352627 309 TKLDQLKINLESIDV--TLSDEVIAGIEAIHTAQP 341
Cdd:cd19160 291 SSAEQLIENLGSIQVlsQLTPQTVMEIDALLGNKP 325
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-336 |
2.33e-27 |
|
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: 109.48 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 1 MQFRKLGKTDLSVSAICLGTMTWGEQNTQDEAFEQI-RMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYA-D 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIvTLAYENGINYFDTSDAF-------TSGQAETELGRILKKKGwK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVAGpgrmdHIRDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDrktnffgvlgyTHDPddqaveIEE 158
Cdd:cd19142 74 RSSYIVSTKIYW-----SYGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKAD-----------PMCP------MEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHfglsnetpWGTQRF--LHLAETLDLPRAVSIQNP------YNLLNR-TFEVGLAEIAIREQIGL 229
Cdd:cd19142 132 VVRAMSYLIDNGLIMY--------WGTSRWspVEIMEAFSIARQFNCPTPiceqseYHMFCReKMELYMPELYNKVGVGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 230 LAYSPLAFGVLAGKYLDGARPADGRltlFERFQRYNNPQAVSATAKYV-----------ALAREHGLDPSQMALAYVTSR 298
Cdd:cd19142 204 ITWSPLSLGLDPGISEETRRLVTKL---SFKSSKYKVGSDGNGIHEETrrashklrelsLIAERLGCDLTQLLIAWSLKN 280
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 966352627 299 PFVTSNIIGATKLDQLKINLESIDV--TLSDEVIAGIEAI 336
Cdd:cd19142 281 ENVQCVLIGASSLEQLYSQLNSLQLlpKLNSAVMEELERI 320
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
13-334 |
2.22e-26 |
|
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: 106.83 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 13 VSAICLGTMTWGEQNT-------QDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYADRNDWVLA 85
Cdd:cd19147 10 VSPLILGAMSIGDAWSgfmgsmdKEQAFELLDAFYEAGGNFIDTANNY-------QDEQSETWIGEWMKSRKNRDQIVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 86 SKVAGPGRMDHIRDGNPRL----DRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNffgvlgythdpddqaveIEETLS 161
Cdd:cd19147 83 TKFTTDYKAYEVGKGKAVNycgnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTS-----------------IEEVMD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 162 VLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLA 241
Cdd:cd19147 146 SLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 GKYLDGARPADGRLTLFERFQRYNNPQAVSATAKYVALAREHGLDP-SQMALAYVTSRPFVTSNIIGATKLDQLKINLES 320
Cdd:cd19147 226 SKKAVEERKKNGEGLRSFVGGTEQTPEEVKISEALEKVAEEHGTESvTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEA 305
|
330
....*....|....
gi 966352627 321 IDVTLSDEVIAGIE 334
Cdd:cd19147 306 LSIKLTPEEIEYLE 319
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-334 |
1.10e-25 |
|
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: 103.33 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 15 AICLGTmtWGEQNtqDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASKVAgpgr 93
Cdd:cd19071 3 LIGLGT--YKLKP--EETAEAVLAALEAGYRHIDTAAAY----------GNEAEVGEAIRESGvPREELFITTKLW---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 94 mdhirdgNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPdrktnffgvlgYTHDPDDQAVEIEETLSVLGDLVKAGKIR 173
Cdd:cd19071 65 -------PTDHGYERVREALEESLKDLGLDYLDLYLIHWP-----------VPGKEGGSKEARLETWRALEELVDEGLVR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 174 HFGLSNETPWgtqrflHLAETLDLPR---AVsIQNPYNLLNRTFEvgLAEIAIREQIGLLAYSPLafgvlagkyldgarp 250
Cdd:cd19071 127 SIGVSNFNVE------HLEELLAAARikpAV-NQIELHPYLQQKE--LVEFCKEHGIVVQAYSPL--------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 251 ADGRLTLFErfqrynNPQAvsatakyVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVI 330
Cdd:cd19071 183 GRGRRPLLD------DPVL-------KEIAKKYGKTPAQVLLRWALQRGVVV--IPKSSNPERIKENLDVFDFELSEEDM 247
|
....
gi 966352627 331 AGIE 334
Cdd:cd19071 248 AAID 251
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
17-336 |
1.07e-22 |
|
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: 95.02 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 17 CLGTMTWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKY-ADRNDWVLASKVAgpgrMD 95
Cdd:cd19140 10 ALGLGTY--PLTGEECTRAVEHALELGYRHIDTAQMY----------GNEAQVGEAIAASgVPRDELFLTTKVW----PD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 96 HIRdgnprldRKNITAALEASLKRLNTDYLDLYQLHWPDRKtnffgvlgythdpddqaVEIEETLSVLGDLVKAGKIRHF 175
Cdd:cd19140 74 NYS-------PDDFLASVEESLRKLRTDYVDLLLLHWPNKD-----------------VPLAETLGALNEAQEAGLARHI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 176 GLSNETPwgtQRFLHLAETLDLPrAVSIQ---NPY----NLLNRTFEVGLAeiaireqigLLAYSPLafgvlagkyldga 248
Cdd:cd19140 130 GVSNFTV---ALLREAVELSEAP-LFTNQveyHPYldqrKLLDAAREHGIA---------LTAYSPL------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 249 rpADGRLTLFERFQRynnpqavsatakyvaLAREHGLDPSQMALAYVTSRPFVTSnIIGATKLDQLKINLESIDVTLSDE 328
Cdd:cd19140 184 --ARGEVLKDPVLQE---------------IGRKHGKTPAQVALRWLLQQEGVAA-IPKATNPERLEENLDIFDFTLSDE 245
|
....*...
gi 966352627 329 VIAGIEAI 336
Cdd:cd19140 246 EMARIAAL 253
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-319 |
7.07e-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: 91.23 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 11 LSVSAICLGTMTWGEQNTQDEAFEQ-IRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKY-----ADRNDWVL 84
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREaLKAALDSGINVIDTAINY-------RGGRSERLIGKALRELiekggIKRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 85 ASKV--------------------AGPGRMD-HIRDGNPR-LDRKNITAALEASLKRLNTDYLDLYQLHWPDRktnFFGV 142
Cdd:cd19099 74 VTKAgyipgdgdeplrplkyleekLGRGLIDvADSAGLRHcISPAYLEDQIERSLKRLGLDTIDLYLLHNPEE---QLLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 143 LGYTHDPDdqavEIEETLSVLGDLVKAGKIRHFGLSNET----PWGTQRFLHLAETLDLPRAVS--------IQNPYNLL 210
Cdd:cd19099 151 LGEEEFYD----RLEEAFEALEEAVAEGKIRYYGISTWDgfraPPALPGHLSLEKLVAAAEEVGgdnhhfkvIQLPLNLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 211 N------RTFEVG----LAEIAIREQIGLLAYSPLafgvLAGKYLDGARPADGRLTLferfqrynnpqavsatakyvala 280
Cdd:cd19099 227 EpealteKNTVKGealsLLEAAKELGLGVIASRPL----NQGQLLGELRLADLLALP----------------------- 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 966352627 281 reHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLE 319
Cdd:cd19099 280 --GGATLAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-329 |
8.47e-20 |
|
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: 87.80 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTMTWGEQN--TQDEAFEQIRMAKDAKVNFLDTAEMYPVpprGETytktESIIGEYFKKYAdRNDWVLASKV--- 88
Cdd:cd19162 1 PRLGLGAASLGNLAraGEDEAAATLDAAWDAGIRYFDTAPLYGL---GLS----ERRLGAALARHP-RAEYVVSTKVgrl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 89 --AGPGRMDHIRDGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKtnffgvlgythdpDDQAveIEETLSVLGDL 166
Cdd:cd19162 73 lePGAAGRPAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRH-------------LLQA--LTDAFPALEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 167 VKAGKIRHFGLsnetpwGTQRFLHLAETLDLPR--AVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAGKY 244
Cdd:cd19162 138 RAEGVVGAIGV------GVTDWAALLRAARRADvdVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 245 LDGARPADGRLTlferfqrynnPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVT 324
Cdd:cd19162 212 PAGDRYDYRPAT----------PEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTP 281
|
....*
gi 966352627 325 LSDEV 329
Cdd:cd19162 282 IPAEF 286
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-336 |
1.18e-19 |
|
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: 87.29 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 12 SVSAICLGTMTW----GEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKY-ADRNDWVLAS 86
Cdd:cd19120 3 KIPAIAFGTGTAwyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMY----------GNEKEVGEALKESgVPREDLFITT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 87 KVAGPGrmdhirdgnprldrKNITAALEASLKRLNTDYLDLYQLHWPdrktnFFGvlgythdpDDQAVEIEETLSVLGDL 166
Cdd:cd19120 73 KVSPGI--------------KDPREALRKSLAKLGVDYVDLYLIHSP-----FFA--------KEGGPTLAEAWAELEAL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 167 VKAGKIRHFGLSNetpWGTQrflHLAETLDLPR---AVS-IQ-NPYNLlnrTFEVGLAEIAIREQIGLLAYSPLAfgvla 241
Cdd:cd19120 126 KDAGLVRSIGVSN---FRIE---DLEELLDTAKikpAVNqIEfHPYLY---PQQPALLEYCREHGIVVSAYSPLS----- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 gkyldgarPadgrLTLFErfqrynnPQAVSATAKyvALAREHGLDPSQMALAYVTSR---PFVTSniigaTKLDQLKINL 318
Cdd:cd19120 192 --------P----LTRDA-------GGPLDPVLE--KIAEKYGVTPAQVLLRWALQKgivVVTTS-----SKEERMKEYL 245
|
330
....*....|....*...
gi 966352627 319 ESIDVTLSDEVIAGIEAI 336
Cdd:cd19120 246 EAFDFELTEEEVEEIDKA 263
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
10-336 |
7.60e-19 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 85.41 E-value: 7.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 10 DLSVSAICLGTM------TWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETYTKTesIIGEYFKKYADrnDWV 83
Cdd:PRK10376 14 GRSVNRLGYGAMqlagpgVFGPPKDRDAAIAVLREAVALGVNHIDTSDFY-----GPHVTNQ--LIREALHPYPD--DLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 84 LASKVaGPGRMDhirDG--NPRLDRKNITAALEASLKRLNTDYLDLYQLHwpdrktnffgVLGYTHDPDDQAveIEETLS 161
Cdd:PRK10376 85 IVTKV-GARRGE---DGswLPAFSPAELRRAVHDNLRNLGLDVLDVVNLR----------LMGDGHGPAEGS--IEEPLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 162 VLGDLVKAGKIRHFGLSNETPwgTQrflhLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAiREQIgllAYSPlaFGVLA 241
Cdd:PRK10376 149 VLAELQRQGLVRHIGLSNVTP--TQ----VAEARKIAEIVCVQNHYNLAHRADDALIDALA-RDGI---AYVP--FFPLG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 GkyldgarpadgrltlFERFQrynnpqavSATAKyvALAREHGLDPSQMALAYVTSRpfvTSNII---GATKLDQLKINL 318
Cdd:PRK10376 217 G---------------FTPLQ--------SSTLS--DVAASLGATPMQVALAWLLQR---SPNILlipGTSSVAHLRENL 268
|
330
....*....|....*...
gi 966352627 319 ESIDVTLSDEVIAGIEAI 336
Cdd:PRK10376 269 AAAELVLSEEVLAELDGI 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
113-336 |
1.23e-18 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 83.94 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 113 LEASLKRLNTDYLDLYQLHWPdrktnffgvlgythDPDDqAVEIEETLSVLGDLVKAGKIRHFGLSNETpwgtqrFLHLA 192
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWP--------------SPND-EVPVEEYIGALAEAKEQGLTRHIGVSNFT------IALLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 193 ETLDLPRAVSIQ------NPYnLLNRTfevgLAEIAIREQIGLLAYSPLAFgvlaGKYLDgarpadgrltlferfqrynN 266
Cdd:cd19139 136 EAIAVVGAGAIAtnqielSPY-LQNRK----LVAHCKQHGIHVTSYMTLAY----GKVLD-------------------D 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 267 PQavsatakYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19139 188 PV-------LAAIAERHGATPAQIALAWAMARGYAV--IPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-336 |
3.56e-18 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 83.67 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 3 FRKLGKTDLSVSAICLGTMTWGE---QNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGETYTktESIIGEYFKKYA-D 78
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSvfgPVSEEDAIASVREAFRLGINFFDTSPYY-----GGTLS--EKVLGKALKALGiP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVagpGRMDHIRDgnprLDRKNITAALEASLKRLNTDYLDLYQLHwpDRKtnfFGVLgythdpdDQAVeiEE 158
Cdd:PLN02587 74 REKYVVSTKC---GRYGEGFD----FSAERVTKSVDESLARLQLDYVDILHCH--DIE---FGSL-------DQIV--NE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHFGLSNeTPWGTQRFLhlaetLDL--PRAVSIQNPY--NLLNRTFEVGLAEIAIREQIGLLAYSP 234
Cdd:PLN02587 133 TIPALQKLKESGKVRFIGITG-LPLAIFTYV-----LDRvpPGTVDVILSYchYSLNDSSLEDLLPYLKSKGVGVISASP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 235 LAFGVLAGKYLDGARPAdgrltlferfqrynNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQL 314
Cdd:PLN02587 207 LAMGLLTENGPPEWHPA--------------PPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQV 272
|
330 340
....*....|....*....|....*...
gi 966352627 315 K------INLESIDVtlSDEVIAGIEAI 336
Cdd:PLN02587 273 EenvaaaTELETSGI--DEELLSEVEAI 298
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-340 |
4.92e-18 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 83.23 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 8 KTDLSVSAICLGTmtWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD-----RNDW 82
Cdd:cd19154 7 SNGVKMPLIGLGT--W--QSKGAEGITAVRTALKAGYRLIDTAFLY----------QNEEAIGEALAELLEegvvkREDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 83 VLASKVagpgrmdhirdGNPRLDRKNITAALEASLKRLNTDYLDLYQLH--WPDRKTNFFGVLGYTHDPDDQAVEIEETL 160
Cdd:cd19154 73 FITTKL-----------WTHEHAPEDVEEALRESLKKLQLEYVDLYLIHapAAFKDDEGESGTMENGMSIHDAVDVEDVW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 161 SVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETldlpRAVSIQNPYNLLNRTFEvgLAEIAIREQIGLLAYSPLafgvl 240
Cdd:cd19154 142 RGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARV----KPHNNQVECHLYFPQKE--LVEFCKKHNISVTSYATL----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 241 agkyldgARPadGRlTLFERFQRYNNPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLES 320
Cdd:cd19154 211 -------GSP--GR-ANFTKSTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAV--IPKSATPSRIKENFNI 278
|
330 340
....*....|....*....|
gi 966352627 321 IDVTLSDEVIAGIEAIHTAQ 340
Cdd:cd19154 279 FDFSLSEEDMATLEEIEKSL 298
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-322 |
8.00e-18 |
|
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: 82.76 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTMTWGEQN---TQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYaDRNDWVLASKVA- 89
Cdd:cd19161 1 SELGLGTAGLGNLYtavSNADADATLDAAWDSGIRYFDTAPMY-------GHGLAEHRLGDFLREK-PRDEFVLSTKVGr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 90 --GPGRMDHIRDGNPRLD-----------RKNITAALEASLKRLNTDYLDLYQLHWPDRktnffgvlgYTHDPDDQAVEI 156
Cdd:cd19161 73 llKPAREGSVPDPNGFVDplpfeivydysYDGIMRSFEDSLQRLGLNRIDILYVHDIGV---------YTHGDRKERHHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 157 EETLS----VLGDLVKAGKIRHFGLS-NETpwgtQRFLHLAETLDLPRAVsIQNPYNLLNRTFEVGLAEIAIREQIGLLA 231
Cdd:cd19161 144 AQLMSggfkALEELKKAGVIKAFGLGvNEV----QICLEALDEADLDCFL-LAGRYSLLDQSAEEEFLPRCEQRGTSLVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 232 YSPLAFGVLA------GKYLDGARPADgrltLFERfqrynnpqaVSATAKyvaLAREHGLDPSQMALAYVTSRPFVTSNI 305
Cdd:cd19161 219 GGVFNSGILAtgtksgAKFNYGDAPAE----IISR---------VMEIEK---ICDAYNVPLAAAALQFPLRHPAVASVL 282
|
330
....*....|....*..
gi 966352627 306 IGATKLDQLKINLESID 322
Cdd:cd19161 283 TGARNPAQLRQNVEAFQ 299
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-328 |
6.71e-17 |
|
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: 79.96 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 14 SAICLGTMTWG---EQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprGetYTKTESIIGEYFKKYaDRNDWVLASKV-- 88
Cdd:cd19152 1 PKLGFGTAPLGnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWY-----G--AGLSEERLGAALREL-GREDYVISTKVgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 89 ------AGPGRMDHIRDGNPRLDRKN-ITAA-----LEASLKRLNTDYLDLYQLHWPDRktnffgvlgYTHDPDDQAVE- 155
Cdd:cd19152 73 llvplqEVEPTFEPGFWNPLPFDAVFdYSYDgilrsIEDSLQRLGLSRIDLLSIHDPDE---------DLAGAESDEHFa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 156 --IEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAeTLDLpraVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYS 233
Cdd:cd19152 144 qaIKGAFRALEELREEGVIKAIGLGVNDWEVILRILEEA-DLDW---VMLAGRYTLLDHSAARELLPECEKRGVKVVNAG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 234 PLAFGVLAG-----KYLDGARPADgrltLFERFQRYNnpqavsatakyvALAREHGLDPSQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19152 220 PFNSGFLAGgdnfdYYEYGPAPPE----LIARRDRIE------------ALCEQHGVSLAAAALQFALAPPAVASVAPGA 283
|
330 340
....*....|....*....|
gi 966352627 309 TKLDQLKINLESIDVTLSDE 328
Cdd:cd19152 284 SSPERVEENVALLATEIPAA 303
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-322 |
2.87e-16 |
|
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: 77.96 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 4 RKLGKTDLSVSAICLGTMTWGEQNT----QDEAFEQIRMAKDAKVNFLDTAEMYpvpprgeTYTKTESIIGEYFKKYA-D 78
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYGdgleQDEAVAIVAEAFAAGINHFDTSPYY-------GAESSEAVLGKALAALQvP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 79 RNDWVLASKVagpGRmdhIRDGNPRLDRKNITAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTHDPD--DQAVEI 156
Cdd:cd19153 76 RSSYTVATKV---GR---YRDSEFDYSAERVRASVATSLERLHTTYLDVV----------------YLHDIEfvDYDTLV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 157 EETLSVLGDLVKAGKIRHFGLS----NETPWGTQRFlhLAETLDlprAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAY 232
Cdd:cd19153 134 DEALPALRTLKDEGVIKRIGIAgyplDTLTRATRRC--SPGSLD---AVLSYCHLTLQDARLESDAPGLVRGAGPHVINA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 233 SPLAFGVLAGKYLDGARPADGRLTlferfqrynnpqavSATAKYVALAREHGLDPSQMALAY-VTSRPFVTSNIIGATKL 311
Cdd:cd19153 209 SPLSMGLLTSQGPPPWHPASGELR--------------HYAAAADAVCASVEASLPDLALQYsLAAHAGVGTVLLGPSSL 274
|
330
....*....|.
gi 966352627 312 DQLKINLESID 322
Cdd:cd19153 275 AQLRSMLAAVD 285
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
15-341 |
4.73e-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: 77.32 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 15 AICLGTmtWgeQNTQDEAFEQ-IRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYF-KKYAD----RNDWVLASKV 88
Cdd:cd19116 13 AIALGT--W--KLKDDEGVRQaVKHAIEAGYRHIDTAYLY----------GNEAEVGEAIrEKIAEgvvkREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 89 agpgrmdhirdGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPdrkTNFFGVLGYTHDPDDQAVEIE--ETLSVLGDL 166
Cdd:cd19116 79 -----------WNSYHEREQVEPALRESLKRLGLDYVDLYLIHWP---VAFKENNDSESNGDGSLSDIDylETWRGMEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 167 VKAGKIRHFGLSNETPWGTQRFLHLAETldLPRAVSIQNPYNLLNRTfevgLAEIAIREQIGLLAYSPLAFGVLAGKYLD 246
Cdd:cd19116 145 VKLGLTRSIGVSNFNSEQINRLLSNCNI--KPAVNQIEVHPTLTQEK----LVAYCQSNGIVVMAYSPFGRLVPRGQTNP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 247 GARPADGRLtlferfqrynnpqavsatakyVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLS 326
Cdd:cd19116 219 PPRLDDPTL---------------------VAIAKKYGKTTAQIVLRYLIDRGVVP--IPKSSNKKRIKENIDIFDFQLT 275
|
330
....*....|....*
gi 966352627 327 DEVIAGIEAIHTAQP 341
Cdd:cd19116 276 PEEVAALNSFNTNQR 290
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
33-336 |
9.26e-16 |
|
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: 76.13 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 33 FEQIRMAKDAKVN----FLDTAEMYpvpprgetytKTESIIGEYFK----KY-ADRNDWVLASKVAgpgRMDHIRDGnpr 103
Cdd:cd19136 14 EEEVRQAVDAALKagyrLIDTASVY----------RNEADIGKALRdllpKYgLSREDIFITSKLA---PKDQGYEK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 104 ldrknITAALEASLKRLNTDYLDLYQLHWPdrktnffGVLGYTHDPDDQAVEIEETLSVLGDLVKAGKIRHFGLSNETPw 183
Cdd:cd19136 78 -----ARAACLGSLERLGTDYLDLYLIHWP-------GVQGLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVSNYTV- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 184 gtqrfLHLAETL---DLPRAVSiQNPYN--LLNRTfevgLAEIAIREQIGLLAYSPLafGVLAGKYLDGARPadgrltlf 258
Cdd:cd19136 145 -----RHLEELLkycEVPPAVN-QVEFHphLVQKE----LLKFCKDHGIHLQAYSSL--GSGDLRLLEDPTV-------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966352627 259 erfqrynnpqavsatakyVALAREHGLDPSQMALAYVTSRPfvTSNIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19136 205 ------------------LAIAKKYGRTPAQVLLRWALQQG--IGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
107-337 |
3.79e-15 |
|
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: 74.28 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 107 KNITAALEASLKRLNTDYLDLYQLHWPDrktnffgvlgyTHDPDDQAVEI-EETLSVLGDLVKAGKIRHFGLSNetpWGT 185
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPD-----------CPSSGKNVKETrAETWRALEELYDEGLCRAIGVSN---FLI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 186 QRFLHLAETLDLPRAVSiQNPYNLLNRtfEVGLAEIAIREQIGLLAYSPLAfgvlAGKYLdgarpadgrltlferfqryN 265
Cdd:cd19135 149 EHLEQLLEDCSVVPHVN-QVEFHPFQN--PVELIEYCRDNNIVFEGYCPLA----KGKAL-------------------E 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966352627 266 NPqavsataKYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAIH 337
Cdd:cd19135 203 EP-------TVTELAKKYQKTPAQILIRWSIQNGVVT--IPKSTKEERIKENCQVFDFSLSEEDMATLDSLH 265
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-334 |
7.04e-15 |
|
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: 73.69 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 15 AICLGTmtWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD-----RNDWVLASKVA 89
Cdd:cd19111 6 VIGLGT--Y--QSPPEEVRAAVDYALFVGYRHIDTALSY----------QNEKAIGEALKWWLKngklkREEVFITTKLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 90 GPGrmdhirdgnprLDRKNITAALEASLKRLNTDYLDLYQLHWPdrktnffgvLGYTHDPDDQAVE-----IEETLSVLG 164
Cdd:cd19111 72 PVY-----------LEFKDTEKSLEKSLENLKLPYVDLYLIHHP---------CGFVNKKDKGERElassdVTSVWRAME 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 165 DLVKAGKIRHFGLSNETPWGTQRFLHLAETldlpravsiqNPYNL---LNRTFEV-GLAEIAIREQIGLLAYSPLAFGVL 240
Cdd:cd19111 132 ALVSEGKVKSIGLSNFNPRQINKILAYAKV----------KPSNLqleCHAYLQQrELRKFCNKKNIVVTAYAPLGSPGR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 241 AGKYLDGARPADgrltlferfqrYNNPqavsataKYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLES 320
Cdd:cd19111 202 ANQSLWPDQPDL-----------LEDP-------TVLAIAKELDKTPAQVLLRFVLQRGTGV--LPKSTNKERIEENFEV 261
|
330
....*....|....
gi 966352627 321 IDVTLSDEVIAGIE 334
Cdd:cd19111 262 FDFELTEEHFKKLK 275
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
15-336 |
1.48e-14 |
|
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: 73.21 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 15 AICLGTMTWGEQntqdEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGE-----YFKKYADRNDWVLASKVa 89
Cdd:cd19123 14 ALGLGTWKSKPG----EVGQAVKQALEAGYRHIDCAAIY----------GNEAEIGAalaevFKEGKVKREDLWITSKL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 90 gpgrmdhirdGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPdrkTNFFGVLGYTHDPDD----QAVEIEETLSVLGD 165
Cdd:cd19123 79 ----------WNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWP---VALKKGVGFPESGEDllslSPIPLEDTWRAMEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 166 LVKAGKIRHFGLSNETpwgTQRFLHLAETLDLPRAVSiQ---NPYnLLNRTfevgLAEIAIREQIGLLAYSPLAfgvlag 242
Cdd:cd19123 146 LVDKGLCRHIGVSNFS---VKKLEDLLATARIKPAVN-QvelHPY-LQQPE----LLAFCRDNGIHLTAYSPLG------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 243 kyldgarpadgrltlfeRFQRynnPQAVSATAKYVAL--------AREHGLDPSQMALAYVTSRPfvTSNIIGATKLDQL 314
Cdd:cd19123 211 -----------------SGDR---PAAMKAEGEPVLLedpvinkiAEKHGASPAQVLIAWAIQRG--TVVIPKSVNPERI 268
|
330 340
....*....|....*....|..
gi 966352627 315 KINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19123 269 QQNLEAAEVELDASDMATIAAL 290
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
30-336 |
1.72e-14 |
|
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: 72.22 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 30 DEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASKVagpgrmdHIRDGnprlDRKN 108
Cdd:cd19133 23 EECERAVLEAIKAGYRLIDTAAAY----------GNEEAVGRAIKKSGiPREELFITTKL-------WIQDA----GYEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 109 ITAALEASLKRLNTDYLDLYQLHWPdrktnfFGvlgythdpddqavEIEETLSVLGDLVKAGKIRHFGLSNETPwgtQRF 188
Cdd:cd19133 82 AKKAFERSLKRLGLDYLDLYLIHQP------FG-------------DVYGAWRAMEELYKEGKIRAIGVSNFYP---DRL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 189 LHLAETLDLPRAVsIQ---NPYNLlnrtfEVGLAEIAIREQIGLLAYSPLafgvlagkyldgarpADGRLTLFerfqryN 265
Cdd:cd19133 140 VDLILHNEVKPAV-NQietHPFNQ-----QIEAVEFLKKYGVQIEAWGPF---------------AEGRNNLF------E 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966352627 266 NPQAVSatakyvaLAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19133 193 NPVLTE-------IAEKYGKSVAQVILRWLIQRGIVV--IPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-336 |
4.15e-14 |
|
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: 71.67 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 12 SVSAICLGTmtWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD------RNDWVLA 85
Cdd:cd19118 6 KIPAIGLGT--W--QAEPGEVGAAVKIALKAGYRHLDLAKVY----------QNQHEVGQALKELLKeepgvkREDLFIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 86 SKVagpgrmdhirdGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPdrkTNF------FGVLGYTHDPD----DQAVE 155
Cdd:cd19118 72 SKL-----------WNNSHRPEYVEPALDDTLKELGLDYLDLYLIHWP---VAFkptgdlNPLTAVPTNGGevdlDLSVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 156 IEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFlhLAETLDLPRAVSIQNPYNLLNRTfevgLAEIAIREQIGLLAYSPL 235
Cdd:cd19118 138 LVDTWKAMVELKKTGKVKSIGVSNFSIDHLQAI--IEETGVVPAVNQIEAHPLLLQDE----LVDYCKSKNIHITAYSPL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 236 AfGVLAGKYLDGARPAdgrltlferfqrynnpqavsatakYVALAREHGLDPSQMALAYVTSRPFvtSNIIGATKLDQLK 315
Cdd:cd19118 212 G-NNLAGLPLLVQHPE------------------------VKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRIR 264
|
330 340
....*....|....*....|.
gi 966352627 316 INLEsiDVTLSDEVIAGIEAI 336
Cdd:cd19118 265 SNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
30-343 |
5.61e-14 |
|
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: 70.88 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 30 DEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKY-ADRNDWVLASKVagpgrmdhirdGNPRLDRKN 108
Cdd:cd19157 24 SEVVNAVKTALKNGYRSIDTAAIY----------GNEEGVGKGIKESgIPREELFITSKV-----------WNADQGYDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 109 ITAALEASLKRLNTDYLDLYQLHWPDRKTNffgvlgythdpddqaveiEETLSVLGDLVKAGKIRHFGLSNetpwgtqrF 188
Cdd:cd19157 83 TLKAFEASLERLGLDYLDLYLIHWPVKGKY------------------KETWKALEKLYKDGRVRAIGVSN--------F 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 189 L--HLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLafgvLAGKYLDgarpadgrltlferfqrynN 266
Cdd:cd19157 137 QvhHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL----MQGQLLD-------------------N 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 267 PQavsatakYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAIHTAQ---PNP 343
Cdd:cd19157 194 PV-------LKEIAEKYNKSVAQVILRWDLQNGVVT--IPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLrvgPDP 264
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
28-336 |
2.29e-13 |
|
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: 69.78 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 28 TQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD-----RNDWVLASKVagpgrmdhirdGNP 102
Cdd:cd19113 22 DNATAADQIYQAIKAGYRLFDGAEDY----------GNEKEVGEGVNRAIDeglvkREELFLTSKL-----------WNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 103 RLDRKNITAALEASLKRLNTDYLDLYQLHWP--------DRK--TNFfgvlgYTHDPDD---QAVEIEETLSVLGDLVKA 169
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpiEEKypPGF-----YCGDGDNfvyEDVPILDTWKALEKLVDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 170 GKIRHFGLSNETPwgtqrflhlAETLDLPRAVSIQ--------NPYNLLNRtfevgLAEIAIREQIGLLAYSplAFGVLA 241
Cdd:cd19113 156 GKIKSIGVSNFPG---------ALILDLLRGATIKpavlqiehHPYLQQPK-----LIEYAQKAGITITAYS--SFGPQS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 GKYLDGARPADGRlTLFErfqrynnpqavSATAKyvALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESI 321
Cdd:cd19113 220 FVELNQGRALNTP-TLFE-----------HDTIK--SIAAKHNKTPAQVLLRWATQRGIAV--IPKSNLPERLLQNLSVN 283
|
330
....*....|....*
gi 966352627 322 DVTLSDEVIAGIEAI 336
Cdd:cd19113 284 DFDLTKEDFEEIAKL 298
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-335 |
6.05e-13 |
|
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: 67.68 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 12 SVSAICLGT-MTWGeqntqDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASKVa 89
Cdd:cd19132 6 QIPAIGFGTyPLKG-----DEGVEAVVAALQAGYRLLDTAFNY----------ENEGAVGEAVRRSGvPREELFVTTKL- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 90 gPGRmDHirdgnprlDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNFfgvlgYThdpddqaveieETLSVLGDLVKA 169
Cdd:cd19132 70 -PGR-HH--------GYEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDL-----YV-----------EAWQALIEAREE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 170 GKIRHFGLSNetpwgtqrFL--HL----AETLDLPRAVSIQ-NPYnlLNRTfevglAEIAIREQIGLL--AYSPLafgvl 240
Cdd:cd19132 124 GLVRSIGVSN--------FLpeHLdrliDETGVTPAVNQIElHPY--FPQA-----EQRAYHREHGIVtqSWSPL----- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 241 agkyldgarpadGRltlferfqrynnPQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLES 320
Cdd:cd19132 184 ------------GR------------GSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVP--IPKSANPERQRENLAI 237
|
330
....*....|....*
gi 966352627 321 IDVTLSDEVIAGIEA 335
Cdd:cd19132 238 FDFELSDEDMAAIAA 252
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-336 |
3.49e-12 |
|
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: 66.01 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 17 CLGTMTWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKK-----YADRNDWVLASKVagp 91
Cdd:cd19128 3 RLGFGTY--KITESESKEAVKNAIKAGYRHIDCAYYY----------GNEAFIGIAFSEifkdgGVKREDLFITSKL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 92 grmdhirdGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWP---DRKTnffgVLGYTHDPDDQAVE---IEETLSVLGD 165
Cdd:cd19128 68 --------WPTMHQPENVKEQLLITLQDLQLEYLDLFLIHWPlafDMDT----DGDPRDDNQIQSLSkkpLEDTWRAMEQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 166 LVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQnPYNLLNRtfevgLAEIAIREQIGLLAYSPlafgvLAGKYL 245
Cdd:cd19128 136 CVDEKLTKNIGVSNYSTKLLTDLLNYCKIKPFMNQIECH-PYFQNDK-----LIKFCIENNIHVTAYRP-----LGGSYG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 246 DGARPADGRLTLferfqrynnpqavsatakyVALAREHGLDPSQMALAY-VTSRPFVTSNIIGATKLDQLKINLESIDVT 324
Cdd:cd19128 205 DGNLTFLNDSEL-------------------KALATKYNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDINDLA 265
|
330
....*....|..
gi 966352627 325 LSDEVIAGIEAI 336
Cdd:cd19128 266 LTKEDMDAINTL 277
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
9-320 |
4.07e-12 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 65.76 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 9 TDLSVSAICLGTMTWGEQNTQD----EAFEQIRMAKDAKVNFLDTAEMYpvpprGETytktESIIGEYFKKYAD---RND 81
Cdd:cd19164 9 SLAGLPPLIFGAATFSYQYTTDpesiPPVDIVRRALELGIRAFDTSPYY-----GPS----EIILGRALKALRDefpRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 82 WVLASKVA--GPGRMDHIRDgnprldrkNITAALEASLKRLNTDYLDLYqlhwpdrktnffgvlgYTHD----PDDqavE 155
Cdd:cd19164 80 YFIITKVGryGPDDFDYSPE--------WIRASVERSLRRLHTDYLDLV----------------YLHDvefvADE---E 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 156 IEETLSVLGDLVKAGKIRHFGLSNETpwgTQRFLHLAETLDLPRAVSIQ-----NPYNLLNRTFevgLAEIAIREQIGLL 230
Cdd:cd19164 133 VLEALKELFKLKDEGKIRNVGISGYP---LPVLLRLAELARTTAGRPLDavlsyCHYTLQNTTL---LAYIPKFLAAAGV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 231 AY----SPLAFGVLAGKyldGAR---PADGRLTlferfqrynnpQAVSATAKYvalAREHGLDPSQMALAYV-TSRPFVT 302
Cdd:cd19164 207 KVvlnaSPLSMGLLRSQ---GPPewhPASPELR-----------AAAAKAAEY---CQAKGTDLADVALRYAlREWGGEG 269
|
330
....*....|....*...
gi 966352627 303 SNIIGATKLDQLKINLES 320
Cdd:cd19164 270 PTVVGCSNVDELEEAVEA 287
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
111-336 |
4.19e-12 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 65.43 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 111 AALEASLKRLNTDYLDLYQLHWPdrktnffgvlgythDPDDQaVEIEETLSVLGDLVKAGKIRHFGLSNETpwgtqrFLH 190
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWP--------------SPNDE-VSVEEFMQALLEAKKQGLTREIGISNFT------IAL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 191 LAETLDLPRAVSIQ------NPYnLLNRTfevgLAEIAIREQIGLLAYSPLAFG-VLAGKYLdgarpadgrltlferfqr 263
Cdd:PRK11172 136 MKQAIAAVGAENIAtnqielSPY-LQNRK----VVAFAKEHGIHVTSYMTLAYGkVLKDPVI------------------ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966352627 264 ynnpqavsatakyVALAREHGLDPSQMALAYVTSRPFvtSNIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:PRK11172 193 -------------ARIAAKHNATPAQVILAWAMQLGY--SVIPSSTKRENLASNLLAQDLQLDAEDMAAIAAL 250
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-336 |
1.48e-11 |
|
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: 64.29 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 8 KTDLSVSAICLGTmtWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKK-----YADRNDW 82
Cdd:cd19125 6 NTGAKIPAVGLGT--W--QADPGVVGNAVKTAIKEGYRHIDCAAIY----------GNEKEIGKALKKlfedgVVKREDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 83 VLASKVAgpgRMDHirdgnprlDRKNITAALEASLKRLNTDYLDLYQLHWPDR-KTNffgvlgyTHDPDDQAVE---IEE 158
Cdd:cd19125 72 FITSKLW---CTDH--------APEDVPPALEKTLKDLQLDYLDLYLIHWPVRlKKG-------AHMPEPEEVLppdIPS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 159 TLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAETldlPRAVSiQ---NPYNLLNRtfevgLAEIAIREQIGLLAYSPL 235
Cdd:cd19125 134 TWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARV---PPAVN-QvecHPGWQQDK-----LHEFCKSKGIHLSAYSPL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 236 AFGvlagkyldGARPADGRLTlferfqryNNPQAVSatakyvaLAREHGLDPSQMALAYVTSRPfvTSNIIGATKLDQLK 315
Cdd:cd19125 205 GSP--------GTTWVKKNVL--------KDPIVTK-------VAEKLGKTPAQVALRWGLQRG--TSVLPKSTNEERIK 259
|
330 340
....*....|....*....|.
gi 966352627 316 INLESIDVTLSDEVIAGIEAI 336
Cdd:cd19125 260 ENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-337 |
2.18e-10 |
|
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: 60.59 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 9 TDLSVSAICLGTmtWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASK 87
Cdd:cd19117 10 TGAEIPAVGLGT--W--QSKPNEVAKAVEAALKAGYRHIDTAAIY----------GNEEEVGQGIKDSGvPREEIFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 88 VAGPgrmdhirdgnprlDRKNITAALEASLKRLNTDYLDLYQLHWP-----DRKTNFFGVLGYTHDpDDQAVEIEETLSV 162
Cdd:cd19117 76 LWCT-------------WHRRVEEALDQSLKKLGLDYVDLYLMHWPvpldpDGNDFLFKKDDGTKD-HEPDWDFIKTWEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 163 LGDLVKAGKIRHFGLSNETPWGTQRFLHLAETLDLPRAVSIQ-NPYNLLNRtfevgLAEIAIREQIGLLAYSPLAfgvla 241
Cdd:cd19117 142 MQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIVPAVNQIElHPLLPQPK-----LVDFCKSKGIHATAYSPLG----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 242 gkyldgarPADGRLtlferfqrYNNPQAVSatakyvaLAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESI 321
Cdd:cd19117 212 --------STNAPL--------LKEPVIIK-------IAKKHGKTPAQVIISWGLQRGYSV--LPKSVTPSRIESNFKLF 266
|
330
....*....|....*.
gi 966352627 322 dvTLSDEVIAGIEAIH 337
Cdd:cd19117 267 --TLSDEEFKEIDELH 280
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
30-336 |
2.48e-10 |
|
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: 60.14 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 30 DEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASKVAGpgrmDHIRDgnprldrKN 108
Cdd:cd19126 23 DETERAVQTALENGYRSIDTAAIY----------KNEEGVGEAIRESGvPREELFVTTKLWN----DDQRA-------RR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 109 ITAALEASLKRLNTDYLDLYQLHWPDRKtnffgvlgythdpddqavEIEETLSVLGDLVKAGKIRHFGLSNetpwgtqrF 188
Cdd:cd19126 82 TEDAFQESLDRLGLDYVDLYLIHWPGKD------------------KFIDTWKALEKLYASGKVKAIGVSN--------F 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 189 L--HLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAgkyldgarpadgrltlferfqrynn 266
Cdd:cd19126 136 QehHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLL------------------------- 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 267 pqavsATAKYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19126 191 -----SNPVLAAIGEKYGKSAAQVVLRWDIQHGVVT--IPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
123-331 |
3.72e-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: 60.05 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 123 DYLDLYQLHwpdRKTNFFGVLgythdpDDQAVeieetLSVLGDLVKAGkiRHFGLSNEtpwGTQRflhlAETLDLPRAV- 201
Cdd:cd19098 123 KHLDLYQIH---SATLESGVL------EDADV-----LAALAELKAEG--VKIGLSLS---GPQQ----AETLRRALEIe 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 202 --------SIQNPYNLlnrtFEVGLAEIaireqigLLAYSPLAFGVLAGKYLdgarpADGRLTlferfqrYNNPQAVSAT 273
Cdd:cd19098 180 idgarlfdSVQATWNL----LEQSAGEA-------LEEAHEAGMGVIVKEAL-----ANGRLT-------DRNPSPELAP 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 274 AKYV--ALAREHGLDPSQMALAYVTSRPFVTSNIIGATKLDQLKINLESIDVTLSDEVIA 331
Cdd:cd19098 237 LMAVlkAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLA 296
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-327 |
3.99e-10 |
|
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: 59.85 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 9 TDLSVSAICLGTmtWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD----RNDWVL 84
Cdd:cd19121 8 TGASIPAVGLGT--W--QAKAGEVKAAVAHALKIGYRHIDGALCY----------QNEDEVGEGIKEAIAggvkREDLFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 85 ASKVAGpgrmdhirdgnprLDRKNITAALEASLKRLNTDYLDLYQLHWPDRkTNFFGvlgyTHD-----PD-----DQAV 154
Cdd:cd19121 74 TTKLWS-------------TYHRRVELCLDRSLKSLGLDYVDLYLVHWPVL-LNPNG----NHDlfptlPDgsrdlDWDW 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 155 EIEETLSVLGDLVKAGKIRHFGLSNET-PWGTQRflhLAETLDLPRAVSIQN-PYnlLNRTfevGLAEIAIREQIGLLAY 232
Cdd:cd19121 136 NHVDTWKQMEKVLKTGKTKAIGVSNYSiPYLEEL---LKHATVVPAVNQVENhPY--LPQQ---ELVDFCKEKGILIEAY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 233 SPLAfgvLAGKYLDGARPAdgrltlferfqrynnpqavsatakyVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLD 312
Cdd:cd19121 208 SPLG---STGSPLISDEPV-------------------------VEIAKKHNVGPGTVLISYQVARGAVV--LPKSVTPD 257
|
330
....*....|....*
gi 966352627 313 QLKINLESIDVTLSD 327
Cdd:cd19121 258 RIKSNLEIIDLDDED 272
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
100-336 |
4.67e-09 |
|
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: 56.46 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 100 GNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNFFgvlgythdpddqaveiEETLSVLGDLVKAGKIRHFGLSN 179
Cdd:cd19130 73 WNDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGNY----------------VHTWEAMIELRAAGRTRSIGVSN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 180 ETPWGTQRFlhLAETLDLPRAVSIQ-NPYnLLNRTfevgLAEIAIREQIGLLAYSPLAFGVLAGKyldgarPADGRltlf 258
Cdd:cd19130 137 FLPPHLERI--VAATGVVPAVNQIElHPA-YQQRT----IRDWAQAHDVKIEAWSPLGQGKLLGD------PPVGA---- 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966352627 259 erfqrynnpqavsatakyvaLAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19130 200 --------------------IAAAHGKTPAQIVLRWHLQKGHVV--FPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
34-239 |
1.05e-08 |
|
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: 55.54 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 34 EQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD-----RNDWVLASKvagpgrmdhIRDGNPRLDRkn 108
Cdd:cd19129 23 NAVKAALEAGFRHFDCAERY----------RNEAEVGEAMQEVFKagkirREDLFVTTK---------LWNTNHRPER-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 109 ITAALEASLKRLNTDYLDLYQLHWPdrktnFFGVLGYTHDPDDQ--------AVEIEETLSVLGDLVKAGKIRHFGLSNE 180
Cdd:cd19129 82 VKPAFEASLKRLQLDYLDLYLIHTP-----FAFQPGDEQDPRDAngnviyddGVTLLDTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 181 TPWGTQRFLHLAETldLPRAVSIQ-NPYnllnrTFEVGLAEIAIREQIGLLAYSPLAFGV 239
Cdd:cd19129 157 SLEKLREIFEAARI--KPAVVQVEsHPY-----LPEWELLDFCKNHGIVLQAFAPLGHGM 209
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
123-336 |
3.55e-08 |
|
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: 54.35 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 123 DYLDLYQLHWP------DRKTNFfgVLGYTHDPDD---QAVEIEETLSVLGDLVKAGKIRHFGLSNETPWGTQRFLHLAE 193
Cdd:cd19115 103 DYFDLFLIHFPialkyvDPAVRY--PPGWFYDGKKvefSNAPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYAR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 194 TLdlPRAVSIQ-NPYnlLNRTfevGLAEIAIREQIGLLAYSplAFGVLAgkyldgarpadgrltlferFQRYNNPQAVSA 272
Cdd:cd19115 181 IR--PATLQIEhHPY--LTQP---RLVKYAQKEGIAVTAYS--SFGPQS-------------------FLELDLPGAKDT 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966352627 273 TAKY-----VALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19115 233 PPLFehdviKSIAEKHGKTPAQVLLRWATQRGIAV--IPKSNNPKRLAQNLDVTGFDLEAEEIKAISAL 299
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
106-328 |
3.74e-08 |
|
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: 54.10 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 106 RKNITAALEASLKRLNTDYLDLYQLHWP------DRKTNF-FGvlgyTHDPDDQAVEIE-----ETLSVLGDLVKAGKIR 173
Cdd:cd19114 77 KDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvDPAENYpFL----WKDKELKKFPLEqspmqECWREMEKLVDAGLVR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 174 HFGLSNetpwgtqrfLHLAETLDL-------PRAVSIQ-NPYNLLNRtfevgLAEIAIREQIGLLAYSplAFGVLAgkyl 245
Cdd:cd19114 153 NIGIAN---------FNVQLILDLltyakikPAVLQIEhHPYLQQKR-----LIDWAKKQGIQITAYS--SFGNAV---- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 246 dgarpadgrLTLFERFQRYNNPQAVSATAKyvALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTL 325
Cdd:cd19114 213 ---------YTKVTKHLKHFTNLLEHPVVK--KLADKHKRDTGQVLLRWAVQRNITV--IPKSVNVERMKTNLDITSYKL 279
|
...
gi 966352627 326 SDE 328
Cdd:cd19114 280 DEE 282
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
18-251 |
4.70e-08 |
|
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: 53.53 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 18 LGTMTWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASKVAgpgrmdh 96
Cdd:cd19131 13 LGLGVW--QVSNDEAASAVREALEVGYRSIDTAAIY----------GNEEGVGKAIRASGvPREELFITTKLW------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 97 irdgNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKTNFFgvlgythdpddqaveiEETLSVLGDLVKAGKIRHFG 176
Cdd:cd19131 74 ----NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDKY----------------VETWKALIELKKEGRVKSIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 177 LSNETPWGTQRFLHlaETLDLPRAVSIQ-NPYnLLNRTFEVGLAEIAIREQigllAYSPLAFGVL---------AGKYld 246
Cdd:cd19131 134 VSNFTIEHLQRLID--ETGVVPVVNQIElHPR-FQQRELRAFHAKHGIQTE----SWSPLGQGGLlsdpvigeiAEKH-- 204
|
....*
gi 966352627 247 GARPA 251
Cdd:cd19131 205 GKTPA 209
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
112-336 |
5.81e-08 |
|
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: 53.18 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 112 ALEASLKRLNTDYLDLYQLHWPdRKTNFfgvlgythDPDDQAVEIEETLsvLGDlvkaGKIRHFGLSNETPwgtqrfLHL 191
Cdd:cd19127 84 GFDASLRRLGLDYVDLYLLHWP-VPNDF--------DRTIQAYKALEKL--LAE----GRVRAIGVSNFTP------EHL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 192 AETLDLPRAVSIQN-----PYnLLNRTFEVGLAEIAIREQigllAYSPLAfGVLagKYLDGARPAdgrltlferfqrynn 266
Cdd:cd19127 143 ERLIDATTVVPAVNqvelhPY-FSQKDLRAFHRRLGIVTQ----AWSPIG-GVM--RYGASGPTG--------------- 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 267 PQAVSATAKYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19127 200 PGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSA--IPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
18-338 |
1.26e-07 |
|
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: 52.39 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 18 LGTMTWGEQNTQDEafEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFK------KYADRNDWVLASKVagp 91
Cdd:cd19106 10 IGLGTWKSKPGQVK--AAVKYALDAGYRHIDCAAVY----------GNEQEVGEALKekvgpgKAVPREDLFVTSKL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 92 grmdhirdGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWP---DRKTNFFgvlgyTHDPDDQ----AVEIEETLSVLG 164
Cdd:cd19106 75 --------WNTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPyafERGDNPF-----PKNPDGTirydSTHYKETWKAME 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 165 DLVKAGKIRHFGLSNetpwgtqrF--LHLAETLDLPR---AVsIQ---NPY----NLLNRTFEVGLAeiaireqigLLAY 232
Cdd:cd19106 142 KLVDKGLVKAIGLSN--------FnsRQIDDILSVARikpAV-LQvecHPYlaqnELIAHCKARGLV---------VTAY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 233 SPLafgvlagkyldGA--RPadgrltlferFQRYNNPQAVSaTAKYVALAREHGLDPSQMALAYVTSRPFVTsnIIGATK 310
Cdd:cd19106 204 SPL-----------GSpdRP----------WAKPDEPVLLE-EPKVKALAKKYNKSPAQILLRWQVQRGVVV--IPKSVT 259
|
330 340
....*....|....*....|....*...
gi 966352627 311 LDQLKINLESIDVTLSDEVIAGIEAIHT 338
Cdd:cd19106 260 PSRIKQNIQVFDFTLSPEEMKQLDALNR 287
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
105-336 |
1.43e-07 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 52.49 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 105 DRKNITAALEASLKRLNTDYLDLYQLHWP-DRKTNFFGVLGYTHDPD-----DQAVEIEETLSVLGDLVKAGKIRHFGLS 178
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPvATKHTGVGTTGSALGEDgvldiDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 179 NETPWGTQRFlhLAETLDLPRAVSIQ-NPYnlLNRTfevGLAEIAIREQIGLLAYSPLAfGVLAGKyldgarpadgrltl 257
Cdd:cd19112 161 NYDIFLTRDC--LAYSKIKPAVNQIEtHPY--FQRD---SLVKFCQKHGISVTAHTPLG-GAAANA-------------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 258 fERFqrynnpQAVSATAK--YVALAREHGLDPSQMALAYVTSRPfvTSNIIGATKLDQLKINLESIDVTLSDEVIAGIEA 335
Cdd:cd19112 219 -EWF------GSVSPLDDpvLKDLAKKYGKSAAQIVLRWGIQRN--TAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKS 289
|
.
gi 966352627 336 I 336
Cdd:cd19112 290 L 290
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
18-331 |
6.40e-07 |
|
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: 50.22 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 18 LGTMTWgeQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD-----RNDWVLASKVAgpg 92
Cdd:cd19155 15 VGLGTW--QSSPEEIETAVDTALEAGYRHIDTAYVY----------RNEAAIGNVLKKWIDsgkvkREELFIVTKLP--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 93 rmdhiRDGNprlDRKNITAALEASLKRLNTDYLDLYQLHWPdrktnfFGVLGYTHD----PDDQAVEIEETLSVLG---- 164
Cdd:cd19155 80 -----PGGN---RREKVEKFLLKSLEKLQLDYVDLYLIHFP------VGSLSKEDDsgklDPTGEHKQDYTTDLLDiwka 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 165 --DLVKAGKIRHFGLSNETPWGTQRFLHLAETldlpRAVSIQNPYNLLNRTFEvgLAEIAIREQIGLLAYSPLAFGVLAg 242
Cdd:cd19155 146 meAQVDQGLTRSIGLSNFNREQMARILKNARI----KPANLQVELHVYLQQKD--LVDFCSTHSITVTAYAPLGSPGAA- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 243 KYLDGARPADGRLTlferfqrynNPQAVSATAKyvaLAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESID 322
Cdd:cd19155 219 HFSPGTGSPSGSSP---------DLLQDPVVKA---IAERHGKSPAQVLLRWLMQRGVVV--IPKSTNAARIKENFQVFD 284
|
....*....
gi 966352627 323 VTLSDEVIA 331
Cdd:cd19155 285 FELTEADMA 293
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-337 |
1.42e-06 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 49.41 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 12 SVSAICLGTMTWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFK-KYAD----RNDWVLAS 86
Cdd:cd19109 3 SIPIIGLGTYSEPKTTPKGACAEAVKVAIDTGYRHIDGAYIY----------QNEHEVGQAIReKIAEgkvkREDIFYCG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 87 KVAGpgrMDHirdgNPRLDRknitAALEASLKRLNTDYLDLYQLHWP----------DRKTNffGVLGYtHDPDDQAVei 156
Cdd:cd19109 73 KLWN---TCH----PPELVR----PTLERTLKVLQLDYVDLYIIEMPmafkpgdeiyPRDEN--GKWLY-HKTNLCAT-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 157 EETLSVLGDlvkAGKIRHFGLSNetpwGTQRFLHLaeTLDLP----RAVSIQ---NPYnlLNRTfevGLAEIAIREQIGL 229
Cdd:cd19109 137 WEALEACKD---AGLVKSIGVSN----FNRRQLEL--ILNKPglkhKPVSNQvecHPY--FTQP---KLLEFCQQHDIVI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 230 LAYSPLAfGVLAGKYLDGARPAdgrltLFErfqrynNPQAVSATAKYvalarehGLDPSQMALAYVTSRPFVTsnIIGAT 309
Cdd:cd19109 203 VAYSPLG-TCRDPIWVNVSSPP-----LLE------DPLLNSIGKKY-------NKTAAQVVLRFNIQRGVVV--IPKSF 261
|
330 340
....*....|....*....|....*...
gi 966352627 310 KLDQLKINLESIDVTLSDEVIAGIEAIH 337
Cdd:cd19109 262 NPERIKENFQIFDFSLTEEEMKDIEALN 289
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
26-336 |
2.17e-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: 48.31 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 26 QNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASKVAGPgrmDHIRDGNprl 104
Cdd:cd19134 20 ELSDDEAERSVSAALEAGYRLIDTAAAY----------GNEAAVGRAIAASGiPRGELFVTTKLATP---DQGFTAS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 105 drkniTAALEASLKRLNTDYLDLYQLHWPdrktnffgvlgythdpddqAVEIEETLSVLGDLVKA---GKIRHFGLSNET 181
Cdd:cd19134 84 -----QAACRASLERLGLDYVDLYLIHWP-------------------AGREGKYVDSWGGLMKLreeGLARSIGVSNFT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 182 PwgtqrfLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVLAgkyldgarpadgrltlferf 261
Cdd:cd19134 140 A------EHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLL-------------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966352627 262 qryNNPQAVSatakyvaLAREHGLDPSQMALAYvtSRPFVTSNIIGATKLDQLKINLESIDVTLSDEVIAGIEAI 336
Cdd:cd19134 194 ---DNPAVTA-------IAAAHGRTPAQVLLRW--SLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGL 256
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
105-189 |
2.88e-06 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 48.15 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 105 DRKNITAALEASLKRLNTDYLDLYQLHWPDrktnffgvlgythDPDDQAVEIEETLSvlgDLVKAGKIRHFGLSNETPWG 184
Cdd:PRK11565 81 DHKRPREALEESLKKLQLDYVDLYLMHWPV-------------PAIDHYVEAWKGMI---ELQKEGLIKSIGVCNFQIHH 144
|
....*
gi 966352627 185 TQRFL 189
Cdd:PRK11565 145 LQRLI 149
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
18-240 |
7.92e-06 |
|
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: 46.74 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 18 LGTMTWGEQNTqDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYA-DRNDWVLASKVagpgrmdh 96
Cdd:cd19156 12 LGLGVWRVQDG-AEAENAVKWAIEAGYRHIDTAAIY----------KNEEGVGQGIRESGvPREEVFVTTKL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 97 irdGNPRLDRKNITAALEASLKRLNTDYLDLYQLHWPDRKtnffgvlgythdpddqavEIEETLSVLGDLVKAGKIRHFG 176
Cdd:cd19156 73 ---WNSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKG------------------KFKDTWKAFEKLYKEKKVRAIG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966352627 177 LSNETPWgtqrflHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPLAFGVL 240
Cdd:cd19156 132 VSNFHEH------HLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKL 189
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-235 |
3.67e-05 |
|
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: 44.80 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 9 TDLSVSAICLGTmtWGEQNTQDEAFEQIRMAKDAKVNFLDTAEMYpvpprgetytKTESIIGEYFKKYAD-----RNDWV 83
Cdd:cd19119 8 TGASIPALGLGT--ASPHEDRAEVKEAVEAAIKEGYRHIDTAYAY----------ETEDFVGEAIKRAIDdgsikREELF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 84 LASKVaGPGRMDHIRDGnprldrknitaaLEASLKRLNTDYLDLYQLHWP---DRKTNFFGVLGYTHDPD-----DQAVE 155
Cdd:cd19119 76 ITTKV-WPTFYDEVERS------------LDESLKALGLDYVDLLLVHWPvcfEKDSDDSGKPFTPVNDDgktryAASGD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 156 IEETLSVLGDLVKAGKIRHFGLSNETpwgtqrFLHLAETLDLPRAVSIQNPYNLLNRTFEVGLAEIAIREQIGLLAYSPL 235
Cdd:cd19119 143 HITTYKQLEKIYLDGRAKAIGVSNYS------IVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPL 216
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
112-235 |
9.45e-05 |
|
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: 43.38 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 112 ALEASLKRLNTDYLDLYQLHWP------DRKTNFFGVLGYTHDPDDQAVEIEETLSVLGDLVKAGKIRHFGLSNETPWGT 185
Cdd:cd19122 91 SIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKLGPDGKYVILKDLTENPEPTWRAMEEIYESGKAKAIGVSNWTIPGL 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 966352627 186 QRFLHLAETldLPRAVSIQ-NPYnLLNRTfevgLAEIAIREQIGLLAYSPL 235
Cdd:cd19122 171 KKLLSFAKV--KPHVNQIEiHPF-LPNEE----LVDYCFSNDILPEAYSPL 214
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
48-133 |
1.42e-04 |
|
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: 43.03 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 48 DTAEMYpvpprgetytKTESIIGEYFKK------YADRNDWVLASKVAgpgrmdhIRDGNPRLdrknITAALEASLKRLN 121
Cdd:cd19124 38 DTAAAY----------GTEEALGEALAEalrlglVKSRDELFVTSKLW-------CSDAHPDL----VLPALKKSLRNLQ 96
|
90
....*....|..
gi 966352627 122 TDYLDLYQLHWP 133
Cdd:cd19124 97 LEYVDLYLIHWP 108
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
109-328 |
3.36e-04 |
|
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: 41.87 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 109 ITAALEASLKRLNTDYLDLYQLHWPdrktnffgvLGYTHDPDDQAVE-----------IEETLSVLGDLVKAGKIRHFGL 177
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHWP---------MGFKPGEPDLPLDrsgmvipsdtdFLDTWEAMEDLVIEGLVKNIGV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352627 178 SNETPWGTQRFLHLAETLDLPRAVSIQ-NPYnlLNRTfevGLAEIAIREQIGLLAYSPLAfGVLAGkyldgarpadgrlt 256
Cdd:cd19110 151 SNFNHEQLERLLNKPGLRVKPVTNQIEcHPY--LTQK---KLISFCQSRNVSVTAYRPLG-GSCEG-------------- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966352627 257 lferFQRYNNPQAVSatakyvaLAREHGLDPSQMALAYVTSRPFVTsnIIGATKLDQLKINLESIDVTLSDE 328
Cdd:cd19110 211 ----VDLIDDPVIQR-------IAKKHGKSPAQILIRFQIQRNVIV--IPKSVTPSRIKENIQVFDFELTEH 269
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
112-133 |
9.26e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 40.68 E-value: 9.26e-04
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| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
105-189 |
2.74e-03 |
|
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: 38.94 E-value: 2.74e-03
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gi 966352627 105 DRKNITAALEASLKRLNTDYLDLYQLHWPdrktnffgvLGYTHDP-----DDQAVEIE------ETLSVLGDLVKAGKIR 173
Cdd:cd19107 76 EKGLVKGACQKTLSDLKLDYLDLYLIHWP---------TGFKPGKelfplDESGNVIPsdttflDTWEAMEELVDEGLVK 146
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90
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gi 966352627 174 HFGLSNETPWGTQRFL 189
Cdd:cd19107 147 AIGVSNFNHLQIERIL 162
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