|
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: 551.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 13 VSALCLGTMTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVPPRAETYASTERIIGNWFRRSGDRADWILASKIAGPG 92
Cdd:cd19094 1 VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQGRTEEIIGSWLKKKGNRDKVVLATKVAGPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 93 NGISHVRDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTNFFGQLGY--QHQEESFTPLEETLEVLDEQVRAG 170
Cdd:cd19094 81 EGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLFGGGYYtePSEEEDSVSFEEQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 171 KIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYADGA-R 249
Cdd:cd19094 161 KIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAaR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 250 PANARISLYSRF-TRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDLRLDEE 328
Cdd:cd19094 241 PEGGRLNLFPGYmARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVPLSDE 320
|
....*...
gi 15599630 329 VLAGIDAI 336
Cdd:cd19094 321 LLAEIDAV 328
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-345 |
2.78e-172 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 482.43 E-value: 2.78e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTMTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVPPRAETYASTERIIGNWFRRSGDRA 80
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQGLTETYIGNWLAKRGSRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 81 DWILASKIAGPGNGISHVRDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTNFFGQLGYQHQEESFT-PLEET 159
Cdd:PRK10625 81 KLIIASKVSGPSRNNDKGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYSWTDSAPAvSLLET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 160 LEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGM 239
Cdd:PRK10625 161 LDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 240 LSGKYADGARPANARISLYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLG 319
Cdd:PRK10625 241 LTGKYLNGAKPAGARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIE 320
|
330 340
....*....|....*....|....*.
gi 15599630 320 SVDLRLDEEVLAGIDAIHREQPNPAP 345
Cdd:PRK10625 321 SLHLTLSEEVLAEIEAVHQVYTYPAP 346
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-343 |
2.04e-130 |
|
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: 374.90 E-value: 2.04e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTMTWGE---QNSEQDAFAQIARAKAAGINFMDTAEMYPVppraetyASTERIIGNWFRRSg 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGP-------GRSEELLGEALKGR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 DRADWILASKIAGPGNGISHVRDGNlkfnRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLE 157
Cdd:COG0667 73 PRDDVVIATKVGRRMGPGPNGRGLS----REHIRRAVEASLRRLGTDYIDLYQLHRPDPDT----------------PIE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 158 ETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEerGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAF 237
Cdd:COG0667 133 ETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 238 GMLSGKYADGAR-PANARISlYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLET 316
Cdd:COG0667 211 GLLTGKYRRGATfPEGDRAA-TNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEE 289
|
330 340
....*....|....*....|....*..
gi 15599630 317 NLGSVDLRLDEEVLAGIDAIHREQPNP 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 |
4.59e-115 |
|
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: 335.70 E-value: 4.59e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTMTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVPpraetyaSTERIIGNWFRrsGDRA 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGG-------RSEEIIGRWIA--GRRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 81 DWILASKIAGP-GNGIShvrDGNLkfNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEET 159
Cdd:cd19087 72 DIVLATKVFGPmGDDPN---DRGL--SRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDT----------------PLEET 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 160 LEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGM 239
Cdd:cd19087 131 LRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 240 LSGKYADGARPANARISLYSRFT-RYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNL 318
Cdd:cd19087 211 LTGKYGKGKRPESGRLVERARYQaRYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSL 290
|
330
....*....|....*...
gi 15599630 319 GSVDLRLDEEVLAGIDAI 336
Cdd:cd19087 291 AALEITLTPELLAEIDEL 308
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-334 |
2.33e-96 |
|
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: 288.34 E-value: 2.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 5 PLGRTDLKVSALCLGTMTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVPPRAETYASTERIIGNWFRRSGDRADWIL 84
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGNAGGESETIIGRWLKSRGKRDRVVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 85 ASKIAGPgngishVRDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEETLEVLD 164
Cdd:cd19081 81 ATKVGFP------MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPAT----------------PLEETLGALN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 165 EQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNR-SFEVGLAEIAIREQCGLLAYSPMAFGMLSGK 243
Cdd:cd19081 139 DLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 244 YADGARPANARISlYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDL 323
Cdd:cd19081 219 YRSEADLPGSTRR-GEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL 297
|
330
....*....|.
gi 15599630 324 RLDEEVLAGID 334
Cdd:cd19081 298 RLTDEEVARLD 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-336 |
1.94e-94 |
|
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: 283.74 E-value: 1.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTMTWGEQN---------SEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGN 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGgffgawggvDQEEADRLVDIALDAGINFFDTADVY-------SEGESEEILGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 72 WFRrsGDRADWILASKIAGP-GNGISHVrdGNlkfNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqe 150
Cdd:cd19091 74 ALK--GRRDDVLIATKVRGRmGEGPNDV--GL---SRHHIIRAVEASLKRLGTDYIDLYQLHGFDALT------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 151 esftPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLL 230
Cdd:cd19091 135 ----PLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 231 AYSPMAFGMLSGKY-ADGARPANARISLYSR-FTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19091 211 VWSPLAGGLLSGKYrRGQPAPEGSRLRRTGFdFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGA 290
|
330 340
....*....|....*....|....*...
gi 15599630 309 TSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19091 291 RNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-328 |
3.25e-92 |
|
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: 277.93 E-value: 3.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 2 EYRPLGRTDLKVSALCLGTMTWGEQNS------EQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRR 75
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVY-------SGGASEEILGRALKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 76 SGDRADWILASKIAGPgngishVRDGNLK--FNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesf 153
Cdd:cd19079 74 FAPRDEVVIATKVYFP------MGDGPNGrgLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYET--------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 154 tPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYS 233
Cdd:cd19079 133 -PIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 234 PMAFGMLSGKYADGARPANARISLYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQ 313
Cdd:cd19079 212 PLARGRLARPWGDTTERRRSTTDTAKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEH 291
|
330
....*....|....*
gi 15599630 314 LETNLGSVDLRLDEE 328
Cdd:cd19079 292 LEDAVAALDIKLSEE 306
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-334 |
7.80e-80 |
|
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: 245.51 E-value: 7.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 10 DLKVSALCLGTM-----TWGEQNsEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRrsGDRADWIL 84
Cdd:cd19084 1 DLKVSRIGLGTWaiggtWWGEVD-DQESIEAIKAAIDLGINFFDTAPVY-------GFGHSEEILGKALK--GRRDDVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 85 ASKIAG-PGNGISHVRDGNlkfnRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEETLEVL 163
Cdd:cd19084 71 ATKCGLrWDGGKGVTKDLS----PESIRKEVEQSLRRLQTDYIDLYQIHWPDPNT----------------PIEETAEAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 164 DEQVRAGKIRHIGLSNETPwgtmTFLRLAEERGwpRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGK 243
Cdd:cd19084 131 EKLKKEGKIRYIGVSNFSV----EQLEEARKYG--PIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 244 YADGAR--PANARislySRFTRYTNPQAE---AACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNL 318
Cdd:cd19084 205 YKKEPTfpPDDRR----SRFPFFRGENFEknlEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENA 280
|
330
....*....|....*.
gi 15599630 319 GSVDLRLDEEVLAGID 334
Cdd:cd19084 281 GALDWELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-319 |
1.21e-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: 235.11 E-value: 1.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTMTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraETYAStERIIGNWFRRSGDRADWILASKIAGPGN 93
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVY------GDGRS-ERLLGRWLKGRGNRDDVVIATKGGHPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 94 GISHVRDgnlkFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEETLEVLDEQVRAGKIR 173
Cdd:cd06660 74 GDPSRSR----LSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPST----------------PVEETLEALNELVREGKIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 174 HIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSF-EVGLAEIAIREQCGLLAYSPMAFGmlsgkyadgarpan 252
Cdd:cd06660 134 YIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG-------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599630 253 arislysrftrytnpqaeaacaryvalarehglePAQMALAYVTSRPFVTSNIIGATSLEQLETNLG 319
Cdd:cd06660 200 ----------------------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-336 |
3.17e-75 |
|
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: 233.74 E-value: 3.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 16 LCLGTMTWG---EQNSEQDAFAQIARAKAAGINFMDTAEMYPvppraETYAstERIIGNWF-RRSGDRADWILASKIagp 91
Cdd:pfam00248 1 IGLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYG-----DGKS--EELLGEALkDYPVKRDKVVIATKV--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 92 GNGISHVRDGnlkFNRQHIVAALDASLERLQTDWLDLYQLHWPERrtnffgqlgyqhqeesFTPLEETLEVLDEQVRAGK 171
Cdd:pfam00248 71 PDGDGPWPSG---GSKENIRKSLEESLKRLGTDYIDLYYLHWPDP----------------DTPIEETWDALEELKKEGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 172 IRHIGLSNETPWgtmtFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYADGARPA 251
Cdd:pfam00248 132 IRAIGVSNFDAE----QIEKALTKGKIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 252 NARislYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDLRLDEEVLA 331
Cdd:pfam00248 208 PGE---RRRLLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVA 284
|
....*
gi 15599630 332 GIDAI 336
Cdd:pfam00248 285 RIDEL 289
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-339 |
1.54e-73 |
|
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: 229.40 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 13 VSALCLGTM-----TWGEQNSEQDAFAQIARAKAAGINFMDTAEMYpvpprAETYAstERIIGNwfRRSGDRADWILASK 87
Cdd:cd19085 1 VSRLGLGCWqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAY-----GDGHS--EEVLGK--ALKGRRDDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 88 IAGPgngishvrdgNLKFNRqhIVAALDASLERLQTDWLDLYQLHWPERrtnffgqlgyqhqeesFTPLEETLEVLDEQV 167
Cdd:cd19085 72 VSPD----------NLTPED--VRKSCERSLKRLGTDYIDLYQIHWPSS----------------DVPLEETMEALEKLK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 168 RAGKIRHIGLSNETPWGtmtfLRLAEERGwpRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYADG 247
Cdd:cd19085 124 EEGKIRAIGVSNFGPAQ----LEEALDAG--RIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 248 AR--PANARislySRFTRYTNPQAEAACARYVA----LAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSV 321
Cdd:cd19085 198 EDfpPGDAR----TRLFRHFEPGAEEETFEALEklkeIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAV 273
|
330
....*....|....*...
gi 15599630 322 DLRLDEEVLAGIDAIHRE 339
Cdd:cd19085 274 DLELSPSVLERLDEISDP 291
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-334 |
1.83e-73 |
|
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: 229.80 E-value: 1.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 4 RPLGRTDLKVSALCLGTMTWGEQ----NSEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRrsGDR 79
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNY-------TNGTSERLLGEFIA--GNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 80 ADWILASK--IAGPGNGISHVrdGNlkfNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLE 157
Cdd:cd19080 72 DRIVLATKytMNRRPGDPNAG--GN---HRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTT----------------PVE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 158 ETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAF 237
Cdd:cd19080 131 EVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 238 GMLSGKYADGARPANARISLYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETN 317
Cdd:cd19080 211 GLLTGKYQRGEEGRAGEAKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDN 290
|
330
....*....|....*..
gi 15599630 318 LGSVDLRLDEEVLAGID 334
Cdd:cd19080 291 LGALDLTLSPEQLARLD 307
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-329 |
3.75e-70 |
|
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: 220.93 E-value: 3.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 11 LKVSALCLGT-MTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYpvpprAETYAstERIIGNW---FRRSgdraDWILAS 86
Cdd:cd19074 2 LKVSELSLGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVY-----AAGQA--EEVLGKAlkgWPRE----SYVIST 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 87 KIAGPGNGisHVRDGNLkfNRQHIVAALDASLERLQTDWLDLYQLHWPErrtnffgqlgyqhqEEsfTPLEETLEVLDEQ 166
Cdd:cd19074 71 KVFWPTGP--GPNDRGL--SRKHIFESIHASLKRLQLDYVDIYYCHRYD--------------PE--TPLEETVRAMDDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 167 VRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYAD 246
Cdd:cd19074 131 IRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 247 G-ARPANARIS---LYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVD 322
Cdd:cd19074 211 GiPPPSRSRATdedNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASG 290
|
....*..
gi 15599630 323 LRLDEEV 329
Cdd:cd19074 291 VKLSPEV 297
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-336 |
5.03e-61 |
|
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: 198.20 E-value: 5.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGT-MTWGEQNSEQDAFAQIARAKAAGINFMDTAEmypvppraeTYAS--TERIIGNWFRRSG 77
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDVDEAKECMKAAYDAGVNFFDNAE---------VYANgqSEEIMGQAIKELG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 -DRADWILASKIAGPGNGISHVRDGNlkfNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPL 156
Cdd:cd19143 72 wPRSDYVVSTKIFWGGGGPPPNDRGL---SRKHIVEGTKASLKRLQLDYVDLVFCHRPDPAT----------------PI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 157 EETLEVLDEQVRAGKIRHiglsnetpWGT--------MTFLRLAEERGWPRAVSIQNPYNLLNRS-FEVGLAEIAIREQC 227
Cdd:cd19143 133 EETVRAMNDLIDQGKAFY--------WGTsewsaqqiEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 228 GLLAYSPMAFGMLSGKYADGArPANARISL--YSRFTRYTNPQAEAACARYVAL---AREHGLEPAQMALAYVTSRPFVT 302
Cdd:cd19143 205 GTTTWSPLASGLLTGKYNNGI-PEGSRLALpgYEWLKDRKEELGQEKIEKVRKLkpiAEELGCSLAQLAIAWCLKNPNVS 283
|
330 340 350
....*....|....*....|....*....|....*.
gi 15599630 303 SNIIGATSLEQLETNLGSVDL--RLDEEVLAGIDAI 336
Cdd:cd19143 284 TVITGATKVEQLEENLKALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-320 |
1.42e-57 |
|
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: 186.53 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 11 LKVSALCLGTMT----WGEQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRrsGDRADWILAS 86
Cdd:cd19086 1 LEVSEIGFGTWGlggdWWGDVDDAEAIRALRAALDLGINFFDTADVY-------GDGHSERLLGKALK--GRRDKVVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 87 KIagpGNGISHVRDGNLKFNRQHIVAALDASLERLQTDWLDLYQLH-WPerrtnffgqlgyqhqeESFTPLEETLEVLDE 165
Cdd:cd19086 72 KF---GNRFDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPP----------------DEVLDNDELFEALEK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 166 QVRAGKIRHIGLSNETPWGtmtfLRLAEERGwpRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKya 245
Cdd:cd19086 133 LKQEGKIRAYGVSVGDPEE----ALAALRRG--GIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK-- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599630 246 dgarpanarislysrftrytnpqaeaacaryvalarehglePAQMALAYVTSRPFVTSNIIGATSLEQLETNLGS 320
Cdd:cd19086 205 -----------------------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-335 |
3.54e-55 |
|
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: 182.86 E-value: 3.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 3 YRPLGRTDLKVSALCLGT------MTWGEQNsEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRrs 76
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTwaigggPWWGGSD-DNESIRTIHAALDLGINLIDTAPAY-------GFGHSEEIVGKAIK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 77 GDRADWILASKIA----GPGNGISHVRDG-----NLKfnRQHIVAALDASLERLQTDWLDLYQLHWPErrtnffgqlgyq 147
Cdd:cd19149 71 GRRDKVVLATKCGlrwdREGGSFFFVRDGvtvykNLS--PESIREEVEQSLKRLGTDYIDLYQTHWQD------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 148 hqeeSFTPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEergwprAVSIQNPYNLLNRSFEVGLAEIAIREQC 227
Cdd:cd19149 137 ----VETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQ------LDIIQEKYSMLDRGIEKELLPYCKKNNI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 228 GLLAYSPMAFGMLSGKY-------ADGARpanARISLYSRFTRytnPQAEAACARYVALAREHGLEPAQMALAYVTSRPF 300
Cdd:cd19149 207 AFQAYSPLEQGLLTGKItpdrefdAGDAR---SGIPWFSPENR---EKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPG 280
|
330 340 350
....*....|....*....|....*....|....*
gi 15599630 301 VTSNIIGATSLEQLETNLGSVDLRLDEEVLAGIDA 335
Cdd:cd19149 281 ITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-331 |
3.82e-55 |
|
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: 182.46 E-value: 3.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 3 YRPLGRTDLKVSALCLGTmtW---GEQNSEQDAFAQIARAKAAGINFMDTAEMY-PVPPRAEtyasteRIIGNWFRRS-- 76
Cdd:cd19089 1 YRRCGRSGLHLPAISLGL--WhnfGDYTSPEEARELLRTAFDLGITHFDLANNYgPPPGSAE------ENFGRILKRDlr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 77 GDRADWILASKIA-----GP-GNGIShvrdgnlkfnRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQE 150
Cdd:cd19089 73 PYRDELVISTKAGygmwpGPyGDGGS----------RKYLLASLDQSLKRMGLDYVDIF----------------YHHRY 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 151 ESFTPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPrAVSIQNPYNLLNRSFEVGLAEIAIREQCGLL 230
Cdd:cd19089 127 DPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELGVP-LIIHQPRYSLLDRWAEDGLLEVLEEAGIGFI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 231 AYSPMAFGMLSGKYADGARPANARISLYSRFT-RYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGAT 309
Cdd:cd19089 206 AFSPLAQGLLTDKYLNGIPPDSRRAAESKFLTeEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGAS 285
|
330 340
....*....|....*....|...
gi 15599630 310 SLEQLETNLGSVD-LRLDEEVLA 331
Cdd:cd19089 286 SPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-334 |
1.07e-54 |
|
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: 180.89 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 12 KVSALCLGTMTWGEQ-------NSEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSGDRADWIL 84
Cdd:cd19093 1 EVSPLGLGTWQWGDRlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVY-------GTGRSERLLGRFLKELGDRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 85 ASKIAGPgngishvrdgNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPerrtNFFGQlgyqhqeesftPLEETLEVLD 164
Cdd:cd19093 74 ATKFAPL----------PWRLTRRSVVKALKASLERLGLDSIDLYQLHWP----GPWYS-----------QIEALMDGLA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 165 EQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPrAVSIQNPYNLLNRSFEV-GLAEIAIREQCGLLAYSPMAFGMLSGK 243
Cdd:cd19093 129 DAVEEGLVRAVGVSNYSADQLRRAHKALKERGVP-LASNQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQGLLTGK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 244 YADGARPANARISLysrFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDL 323
Cdd:cd19093 208 YSPENPPPGGRRRL---FGRKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGVVP--IPGAKNAEQAEENAGALGW 282
|
330
....*....|.
gi 15599630 324 RLDEEVLAGID 334
Cdd:cd19093 283 RLSEEEVAELD 293
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-334 |
2.67e-52 |
|
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: 173.57 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 12 KVSALCLGTMTWGEQNS-----EQDAFAQIARAKAAGINFMDTAEMYpvpprAETYAstERIIGNWFRrSGDRADWILAS 86
Cdd:cd19072 3 EVPVLGLGTWGIGGGMSkdysdDKKAIEALRYAIELGINLIDTAEMY-----GGGHA--EELVGKAIK-GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 87 KIAgpgngISHvrdgnLKFNRqhIVAALDASLERLQTDWLDLYQLHWPerrtnffgqlgyqhqeESFTPLEETLEVLDEQ 166
Cdd:cd19072 75 KVS-----PDH-----LKYDD--VIKAAKESLKRLGTDYIDLYLIHWP----------------NPSIPIEETLRAMEEL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 167 VRAGKIRHIGLSNetpwgtmtfLRLAE-ERGWPRA-----VSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGML 240
Cdd:cd19072 127 VEEGKIRYIGVSN---------FSLEElEEAQSYLkkgpiVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 241 SGKYADgarpanarislysrftrytnpqaeaacARYVALAREHGLEPAQMALAYVTSRPFVTSnIIGATSLEQLETNLGS 320
Cdd:cd19072 198 SNAKGS---------------------------PLLDEIAKKYGKTPAQIALNWLISKPNVIA-IPKASNIEHLEENAGA 249
|
330
....*....|....
gi 15599630 321 VDLRLDEEVLAGID 334
Cdd:cd19072 250 LGWELSEEDLQRLD 263
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-322 |
7.99e-52 |
|
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: 173.51 E-value: 7.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTMTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPvppRAETYASTERIIGNWFRRSGDRADWILASKIAGPGN 93
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYG---DWVERGASERVIGEWLKSRGNRDKVVIATKGGHPDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 94 GISHVRdgnlKFNRQHIVAALDASLERLQTDWLDLYQLHW--PERrtnffgqlgyqhqeesftPLEETLEVLDEQVRAGK 171
Cdd:cd19082 78 EDMSRS----RLSPEDIRADLEESLERLGTDYIDLYFLHRddPSV------------------PVGEIVDTLNELVRAGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 172 IRHIGLSNetpWgtmTFLRLAE------ERGWPRAVSIQNPYNL--LNRSFEVGLAEIAI---------REQCGLLAYSP 234
Cdd:cd19082 136 IRAFGASN---W---STERIAEanayakAHGLPGFAASSPQWSLarPNEPPWPGPTLVAMdeemrawheENQLPVFAYSS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 235 MAFGMLSGKYADGARPANARISlysrftRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQL 314
Cdd:cd19082 210 QARGFFSKRAAGGAEDDSELRR------VYYSEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQL 283
|
....*...
gi 15599630 315 ETNLGSVD 322
Cdd:cd19082 284 RDSLAAAD 291
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-336 |
5.81e-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: 171.59 E-value: 5.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 18 LGTMTWGEQNS--EQDAFAQIARA-KAAGINFMDTAEMYPvppraetYASTERIIGNwfRRSGDRaDWILASKiAGPGNG 94
Cdd:cd19075 5 LGTMTFGSQGRftTAEAAAELLDAfLERGHTEIDTARVYP-------DGTSEELLGE--LGLGER-GFKIDTK-ANPGVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 95 ISHVRDGnlkfnrqhIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEETLEVLDEQVRAGKIRH 174
Cdd:cd19075 74 GGLSPEN--------VRKQLETSLKRLKVDKVDVFYLHAPDRST----------------PLEETLAAIDELYKEGKFKE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 175 IGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIA----IReqcgLLAYSPMAFGMLSGKYADGARP 250
Cdd:cd19075 130 FGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITRQVETELFPCLrklgIR----FYAYSPLAGGFLTGKYKYSEDK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 251 ANArislySRF-----------TRYTNPQAEAACARYVALAREHGLEPAQMALAYVT--SRPFVTSN---IIGATSLEQL 314
Cdd:cd19075 206 AGG-----GRFdpnnalgklyrDRYWKPSYFEALEKVEEAAEKEGISLAEAALRWLYhhSALDGEKGdgvILGASSLEQL 280
|
330 340
....*....|....*....|...
gi 15599630 315 ETNLGSVDL-RLDEEVLAGIDAI 336
Cdd:cd19075 281 EENLAALEKgPLPEEVVKAIDEA 303
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-322 |
8.31e-51 |
|
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: 170.59 E-value: 8.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTMTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVPPRAETYASTERIIGNWFRRSGDRADWILASKI-AGPG 92
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGGESERLIGRWLKDRGNRDDVVIATKVgAGPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 93 --NGISHVRDGnlkFNRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFTPLEETLEVLDEQVRAG 170
Cdd:cd19752 81 dpDGGPESPEG---LSAETIEQEIDKSLRRLGTDYIDLY----------------YAHVDDRDTPLEETLEAFNELVKAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 171 KIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLL--NRSFEVGLAEIAIREQC---------GLLAYSPmafgM 239
Cdd:cd19752 142 KVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLrpRPGADFGVQRIVTDELLdyassrpdlTLLAYSP----L 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 240 LSGKYADGARPANArislysrftRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLG 319
Cdd:cd19752 218 LSGAYTRPDRPLPE---------QYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLA 288
|
...
gi 15599630 320 SVD 322
Cdd:cd19752 289 ALD 291
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-336 |
1.38e-49 |
|
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: 167.85 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 21 MTWGEQNsEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSGDRAdwILASKIA----GPGNGIS 96
Cdd:cd19102 18 GGWGPQD-DRDSIAAIRAALDLGINWIDTAAVY-------GLGHSEEVVGRALKGLRDRP--IVATKCGllwdEEGRIRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 97 HVRDGNLKfnrqhivAALDASLERLQTDWLDLYQLHWPERRtnffgqlgyqhqeesfTPLEETLEVLDEQVRAGKIRHIG 176
Cdd:cd19102 88 SLKPASIR-------AECEASLRRLGVDVIDLYQIHWPDPD----------------EPIEEAWGALAELKEEGKVRAIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 177 LSNETpwgtmtflrlAEERGWPRAV----SIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYaDGARPAN 252
Cdd:cd19102 145 VSNFS----------VDQMKRCQAIhpiaSLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKM-TPERVAS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 253 ARISLYSRFTRYTNPQAEAACARYV----ALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDLRLDEE 328
Cdd:cd19102 214 LPADDWRRRSPFFQEPNLARNLALVdalrPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPE 293
|
....*...
gi 15599630 329 VLAGIDAI 336
Cdd:cd19102 294 ELAEIEAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-333 |
1.04e-46 |
|
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: 160.46 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 2 EYRPLGRTDLKVSALCLGTM----TWGEQnSEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSG 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmsaFYGPA-DEEESIATLHRALELGVTFLDTADMY-------GPGTNEELLGKALKDRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 DRAdwILASKIA---GPGNGIShVRDGNlkfnRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFT 154
Cdd:cd19076 73 DEV--VIATKFGivrDPGSGFR-GVDGR----PEYVRAACEASLKRLGTDVIDLY----------------YQHRVDPNV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 155 PLEETLEVLDEQVRAGKIRHIGLSNETPwGTmtfLRLAEergwprAV----SIQNPYNLLNRSFEVG----LAEIAIreq 226
Cdd:cd19076 130 PIEETVGAMAELVEEGKVRYIGLSEASA-DT---IRRAH------AVhpitAVQSEYSLWTRDIEDEvlptCRELGI--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 227 cGLLAYSPMAFGMLSGKYADGARPANARislYSRFT-RYtnpQAEAACA------RYVALAREHGLEPAQMALAYVTSRp 299
Cdd:cd19076 197 -GFVAYSPLGRGFLTGAIKSPEDLPEDD---FRRNNpRF---QGENFDKnlklveKLEAIAAEKGCTPAQLALAWVLAQ- 268
|
330 340 350
....*....|....*....|....*....|....*..
gi 15599630 300 fvTSNII---GATSLEQLETNLGSVDLRLDEEVLAGI 333
Cdd:cd19076 269 --GDDIVpipGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-339 |
8.50e-44 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 154.59 E-value: 8.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTMtWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPvppraetyaSTERIIGNWFrrSGDRA 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM-RLPRKDEEEAEALIRRAIDNGINYIDTARGYG---------DSEEFLGKAL--KGPRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 81 DWILASKIAgpgngiSHVRDgnlkfnRQHIVAALDASLERLQTDWLDLYQLHWPERRTNFfgqlgyqhqEESFTPLeETL 160
Cdd:COG1453 69 KVILATKLP------PWVRD------PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDL---------EKVLKPG-GAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 161 EVLDEQVRAGKIRHIGLS--NETPwgtmTFLRLAEERGWpRAVSIQnpYNLLNRSFEVGLA--EIAIREQCGLLAYSPMA 236
Cdd:COG1453 127 EALEKAKAEGKIRHIGFSthGSLE----VIKEAIDTGDF-DFVQLQ--YNYLDQDNQAGEEalEAAAEKGIGVIIMKPLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 237 FGMLsgkyadgarpanarislysrftrYTNPQAeaacaryVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLET 316
Cdd:COG1453 200 GGRL-----------------------ANPPEK-------LVELLCPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDE 249
|
330 340
....*....|....*....|....*
gi 15599630 317 NLGSVDL--RLDEEVLAGIDAIHRE 339
Cdd:COG1453 250 NLKTADNlePLTEEELAILERLAEE 274
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-331 |
1.36e-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: 152.56 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 2 EYRPLGRTDLKVSALCLGTmtW---GEQNSEQDAFAQIARAKAAGINFMDTAEMY-PVPPRAETyaSTERIIGNWFRRSg 77
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGL--WhnfGDVDRYENSRAMLRRAFDLGITHFDLANNYgPPPGSAEE--NFGRILKEDLKPY- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 dRADWILASKIA-----GP-GNGIShvrdgnlkfnRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEE 151
Cdd:cd19151 76 -RDELIISTKAGytmwpGPyGDWGS----------KKYLIASLDQSLKRMGLDYVDIF----------------YHHRPD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 152 SFTPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPraVSIQNP-YNLLNRSFEVGLAEIAIREQCGLL 230
Cdd:cd19151 129 PETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLGTP--CLIHQPkYSMFNRWVEEGLLDVLEEEGIGCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 231 AYSPMAFGMLSGKYADGArPANARISLYSRFTRYTNPQAE--AACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19151 207 AFSPLAQGLLTDRYLNGI-PEDSRAAKGSSFLKPEQITEEklAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGA 285
|
330 340
....*....|....*....|....
gi 15599630 309 TSLEQLETNLGSVD-LRLDEEVLA 331
Cdd:cd19151 286 SKPSQIEDAVGALDnREFSEEELA 309
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-318 |
4.32e-42 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 146.47 E-value: 4.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 3 YRPLGRTDLKVSALCLGTMTWGEqNSEQDAFAQIARAKAAGINFMDTAEMYPvppraetyaSTERIIGNWFRrsGDRADW 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR-LSQEEAAAIIRRALDLGINYFDTAPSYG---------DSEEKIGKALK--GRRDKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 83 ILASKIagpgngisHVRDgnlkfnRQHIVAALDASLERLQTDWLDLYQLHwperrtnffgQLGYQHQEESFTPLEETLEV 162
Cdd:cd19100 69 FLATKT--------GARD------YEGAKRDLERSLKRLGTDYIDLYQLH----------AVDTEEDLDQVFGPGGALEA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 163 LDEQVRAGKIRHIGLSNETPwgtmTFLRLAEERGWPRAVsiQNPYNLL---NRSFEVGLAEIAIREQCGLLAYSPMAFGM 239
Cdd:cd19100 125 LLEAKEEGKIRFIGISGHSP----EVLLRALETGEFDVV--LFPINPAgdhIDSFREELLPLAREKGVGVIAMKVLAGGR 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599630 240 LSGKyadgarpanarislysrftrytnpqaeaacaryvalarehGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNL 318
Cdd:cd19100 199 LLSG----------------------------------------DPLDPEQALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-336 |
4.64e-42 |
|
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: 148.34 E-value: 4.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 4 RPLGRTDLKVSALCLGTMTWGEQN-----SEQDAFAQIARAKAAGINFMDTAEMYPvPPRaetyasTERIIGNWFRrSGD 78
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNlypnlDEEEGKDLVREALDNGVNLLDTAFIYG-LGR------SEELVGEVLK-EYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASKIAGPGNGISHVRDGNLKFNRQhivaALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEE 158
Cdd:cd19083 74 RNEVVIATKGAHKFGGDGSVLNNSPEFLRS----AVEKSLKRLNTDYIDLYYIHFPDGET----------------PKAE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 TLEVLDEQVRAGKIRHIGLSNetpwGTMTFLRLAEERGWPRAVsiQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFG 238
Cdd:cd19083 134 AVGALQELKDEGKIRAIGVSN----FSLEQLKEANKDGYVDVL--QGEYNLLQREAEEDILPYCVENNISFIPYFPLASG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 239 MLSGKYadgarpaNARISLYSRFTRYTNP--QAEA------ACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATS 310
Cdd:cd19083 208 LLAGKY-------TKDTKFPDNDLRNDKPlfKGERfsenldKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKR 280
|
330 340
....*....|....*....|....*.
gi 15599630 311 LEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19083 281 AEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-334 |
5.63e-42 |
|
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: 147.76 E-value: 5.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 10 DLKVSALCLGTM----TWGEQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFrrSGDRADWILA 85
Cdd:cd19078 1 GLEVSAIGLGCMgmshGYGPPPDKEEMIELIRKAVELGITFFDTAEVY-------GPYTNEELVGEAL--KPFRDQVVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 86 SKIagpgnGISHVRDGN----LKFNRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFTPLEETLE 161
Cdd:cd19078 72 TKF-----GFKIDGGKPgplgLDSRPEHIRKAVEGSLKRLQTDYIDLY----------------YQHRVDPNVPIEEVAG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 162 VLDEQVRAGKIRHIGLSnETpwgTMTFLRLAEergwprAV----SIQNPYNLLNRSFEVG----LAEIAIreqcGLLAYS 233
Cdd:cd19078 131 TMKELIKEGKIRHWGLS-EA---GVETIRRAH------AVcpvtAVQSEYSMMWREPEKEvlptLEELGI----GFVPFS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 234 PMAFGMLSGKYADGAR--PANARISLySRFTrytnPQAEAACARYVAL----AREHGLEPAQMALAYV-TSRPFVTSnII 306
Cdd:cd19078 197 PLGKGFLTGKIDENTKfdEGDDRASL-PRFT----PEALEANQALVDLlkefAEEKGATPAQIALAWLlAKKPWIVP-IP 270
|
330 340
....*....|....*....|....*...
gi 15599630 307 GATSLEQLETNLGSVDLRLDEEVLAGID 334
Cdd:cd19078 271 GTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-321 |
7.66e-42 |
|
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: 146.19 E-value: 7.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTMTWGEQNSEQdafaqIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRsGDRA 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESPEL-----LRRALDLGINYFDTAEGY-------GNGNSEEIIGEALKG-LRRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 81 DWILASKIAGPGNGIShvrdgnlkfnRQHIVAALDASLERLQTDWLDLYQLH---WPERRTNFfgqlgyqhqeesftplE 157
Cdd:cd19105 68 KVFLATKASPRLDKKD----------KAELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLN----------------E 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 158 ETLEVLDEQVRAGKIRHIGLSNETPWGTMtFLRLAEERGWPravSIQNPYNLLNRSFEVG--LAEiAIREQCGLLAYSPM 235
Cdd:cd19105 122 ELLEALEKLKKEGKVRFIGFSTHDNMAEV-LQAAIESGWFD---VIMVAYNFLNQPAELEeaLAA-AAEKGIGVVAMKTL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 236 AFGMLsgkyadgarpanarislySRFTRYTNPQAeaacaryvalarehGLEPAQMALAYVTSRPFVTSNIIGATSLEQLE 315
Cdd:cd19105 197 AGGYL------------------QPALLSVLKAK--------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELE 244
|
....*.
gi 15599630 316 TNLGSV 321
Cdd:cd19105 245 ENLAAA 250
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-336 |
3.16e-41 |
|
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: 145.91 E-value: 3.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 10 DLKVSALCLGTMT-----WGEQNsEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSGDRADWIL 84
Cdd:cd19148 1 DLPVSRIALGTWAiggwmWGGTD-EKEAIETIHKALDLGINLIDTAPVY-------GFGLSEEIVGKALKEYGKRDRVVI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 85 ASKIAGP-GNGISHVRDGNlkfnRQHIVAALDASLERLQTDWLDLYQLHWPerrtnffgqlgyqhqeESFTPLEETLEVL 163
Cdd:cd19148 73 ATKVGLEwDEGGEVVRNSS----PARIRKEVEDSLRRLQTDYIDLYQVHWP----------------DPLVPIEETAEAL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 164 DEQVRAGKIRHIGLSNETPWGTMTFLRLAeergwPRAVsIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGK 243
Cdd:cd19148 133 KELLDEGKIRAIGVSNFSPEQMETFRKVA-----PLHT-VQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 244 Y-------ADGARPANARISlYSRFTRYTnpqaeAACARYVALAREHGLEP-AQMALAYVTSRPFVTSNIIGATSLEQLE 315
Cdd:cd19148 207 MtkdtkfeGDDLRRTDPKFQ-EPRFSQYL-----AAVEELDKLAQERYGKSvIHLAVRWLLDQPGVSIALWGARKPEQLD 280
|
330 340
....*....|....*....|.
gi 15599630 316 TNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19148 281 AVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-330 |
1.06e-40 |
|
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: 143.85 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTMTWG---EQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyASTERIIGnWFRRSGDRADWILASKIaG 90
Cdd:cd19090 1 SALGLGTAGLGgvfGGVDDDEAVATIRAALDLGINYIDTAPAY---------GDSEERLG-LALAELPREPLVLSTKV-G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 91 PgngishVRDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhQEESFTPlEETLEVLDEQVRAG 170
Cdd:cd19090 70 R------LPEDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVP----------WVDILAP-GGALEALLELKEEG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 171 KIRHIGLSNETPwgtmTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYADGARP 250
Cdd:cd19090 133 LIKHIGLGGGPP----DLLRRAIETGDFDVVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 251 ANARISlysrftrytnPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDLRLDEEVL 330
Cdd:cd19090 209 TYRWLS----------PELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-336 |
1.22e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 145.10 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 2 EYRPLGRTDLKVSALCLG----TMTWGEQnSEQDAFAQIARAKAAGINFMDTAEMYPVppraetyASTERIIGNWFRrsG 77
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggiGGLMGRT-TREEQIAAVRRALDLGINFFDTAPSYGD-------GKSEENLGRALK--G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 DRADWILASKIagpgnGISHVRDGNLKfnrQHIVAALDASLERLQTDWLDLYQLH---WPERRTNFFGQLGYQHqeesFT 154
Cdd:cd19104 71 LPAGPYITTKV-----RLDPDDLGDIG---GQIERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVGGTLSTTD----VL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 155 PLEETLEVLDEQVRAGKIRHIGLsneTPWGTMTFLRLAEERGwpRAVSIQNPYNLLN--------RSFEV----GLAEIA 222
Cdd:cd19104 139 GLGGVADAFERLRSEGKIRFIGI---TGLGNPPAIRELLDSG--KFDAVQVYYNLLNpsaaearpRGWSAqdygGIIDAA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 223 IREQCGLLAYSPMAFGMLSGKYADGARPANARISLYSRFTRytnpQAeaacARYVALAREHGLEPAQMALAYVTSRPFVT 302
Cdd:cd19104 214 AEHGVGVMGIRVLAAGALTTSLDRGREAPPTSDSDVAIDFR----RA----AAFRALAREWGETLAQLAHRFALSNPGVS 285
|
330 340 350
....*....|....*....|....*....|....*
gi 15599630 303 SNIIGATSLEQLETNLGSVDL-RLDEEVLAGIDAI 336
Cdd:cd19104 286 TVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-331 |
3.81e-40 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 143.08 E-value: 3.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTMTWGE---QNSEQDAFAQIARAKAAGINFMDTAEMYpvpprAETYAstERIIGnWFRRSG 77
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGvfgPVDEEEAIRTVHEALDSGINYIDTAPWY-----GQGRS--ETVLG-KALKGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 DRADWILASKIAGPGNGISHVRDgnlkFNRQHIVAALDASLERLQTDWLDLYQLHWPErrtnfFGQLGYQHqeesftpLE 157
Cdd:cd19163 73 PRDSYYLATKVGRYGLDPDKMFD----FSAERITKSVEESLKRLGLDYIDIIQVHDIE-----FAPSLDQI-------LN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 158 ETLEVLDEQVRAGKIRHIGLSnetpwG-TMTFLRLAEERGwprAVSIQ-----NPYNLLNRSFEvGLAEIAIREQCGLLA 231
Cdd:cd19163 137 ETLPALQKLKEEGKVRFIGIT-----GyPLDVLKEVLERS---PVKIDtvlsyCHYTLNDTSLL-ELLPFFKEKGVGVIN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 232 YSPMAFGMLSGKYADGARPANARIslysrftrytnpqaEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSL 311
Cdd:cd19163 208 ASPLSMGLLTERGPPDWHPASPEI--------------KEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASP 273
|
330 340
....*....|....*....|
gi 15599630 312 EQLETNLGSVDLRLDEEVLA 331
Cdd:cd19163 274 ENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-345 |
1.71e-39 |
|
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: 142.20 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTM----TWGEQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyASTERIIGNWFRRS 76
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsaFYGPPKPDEERFAVLDAAFELGCTFWDTADIY---------GDSEELIGRWFKQN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 77 -GDRADWILASKIAGPGNGISHVR--DGNLKFnrqhIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESF 153
Cdd:cd19144 72 pGKREKIFLATKFGIEKNVETGEYsvDGSPEY----VKKACETSLKRLGVDYIDLY----------------YQHRVDGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 154 TPLEETLEVLDEQVRAGKIRHIGLSNETPWGtmtfLRLAEERGWPRAVSIQ----------NPYNLLNRSFEVGLAeiai 223
Cdd:cd19144 132 TPIEKTVAAMAELVQEGKIKHIGLSECSAET----LRRAHAVHPIAAVQIEyspfsldierPEIGVLDTCRELGVA---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 224 reqcgLLAYSPMAFGMLSGKYA--DGARPANARISLySRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFV 301
Cdd:cd19144 204 -----IVAYSPLGRGFLTGAIRspDDFEEGDFRRMA-PRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDD 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15599630 302 TSNIIGATSLEQLETNLGSVDLRLDEEVLAGIDAIHREQPNPAP 345
Cdd:cd19144 278 IIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEVVGE 321
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-331 |
1.32e-38 |
|
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: 139.51 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 3 YRPLGRTDLKVSALCLGT-MTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVPPraetyASTERIIGNWFRR--SGDR 79
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLwHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPP-----GSAEENFGRILREdfAGYR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 80 ADWILASKI-----AGP-GNGIShvrdgnlkfnRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESF 153
Cdd:cd19150 77 DELIISTKAgydmwPGPyGEWGS----------RKYLLASLDQSLKRMGLDYVDIF----------------YSHRFDPD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 154 TPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSiQNPYNLLNRSFE-VGLAEIAIREQCGLLAY 232
Cdd:cd19150 131 TPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELGTPLLIH-QPSYNMLNRWVEeSGLLDTLQELGVGCIAF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 233 SPMAFGMLSGKYADGArPANARISLYSRFTRYTNPQAEAACARYV-ALAREHGLEPAQMALAYVTSRPFVTSNIIGATSL 311
Cdd:cd19150 210 TPLAQGLLTDKYLNGI-PEGSRASKERSLSPKMLTEANLNSIRALnEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRP 288
|
330 340
....*....|....*....|.
gi 15599630 312 EQLETNLGSVD-LRLDEEVLA 331
Cdd:cd19150 289 EQLEENVGALDnLTFSADELA 309
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-320 |
1.76e-38 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 137.37 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTM-TWGEQN--SEQDAFAQIARAKAAGINFMDTAEMYpvppraetyASTERIIGNWFRRSgDRADWILASKIAG 90
Cdd:cd19095 1 SVLGLGTSgIGRVWGvpSEAEAARLLNTALDLGINLIDTAPAY---------GRSEERLGRALAGL-RRDDLFIATKVGT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 91 PGNGISHVRDgnlkFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTNffgqlgyqhqeesftpLEETLEVLDEQVRAG 170
Cdd:cd19095 71 HGEGGRDRKD----FSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDEL----------------TGEVLETLEDLKAAG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 171 KIRHIGLSNETPwgtmtflRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIReQCGLLAYSPMAfgmlSGKYadgaRP 250
Cdd:cd19095 131 KVRYIGVSGDGE-------ELEAAIASGVFDVVQLPYNVLDREEEELLPLAAEA-GLGVIVNRPLA----NGRL----RR 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 251 ANARISLYSRFTRYTNPQAEAACARyvalarehglePAQMALAYVTSRPFVTSNIIGATSLEQLETNLGS 320
Cdd:cd19095 195 RVRRRPLYADYARRPEFAAEIGGAT-----------WAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-326 |
2.55e-38 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 136.96 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 13 VSALCLGTMT------WGEQNSEQDAFAQIARAKAAGINFMDTAEMY-PvppraetyASTERIIGNWFRRSGDRAdwILA 85
Cdd:cd19088 1 VSRLGYGAMRltgpgiWGPPADREEAIAVLRRALELGVNFIDTADSYgP--------DVNERLIAEALHPYPDDV--VIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 86 SKIagpgngiSHVRDGNLKFNR----QHIVAALDASLERLQTDWLDLYQLHWPErrtnffgqlgyqhqeeSFTPLEETLE 161
Cdd:cd19088 71 TKG-------GLVRTGPGWWGPdgspEYLRQAVEASLRRLGLDRIDLYQLHRID----------------PKVPFEEQLG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 162 VLDEQVRAGKIRHIGLSNETPwgtmtfLRLAEERGWPRAVSIQNPYNLLNRSFEvGLAEIAIREQCGLLAYSPMAfgmls 241
Cdd:cd19088 128 ALAELQDEGLIRHIGLSNVTV------AQIEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLG----- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 242 gkyadGARPAnarislysrftrytnpQAEAACAryvALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSV 321
Cdd:cd19088 196 -----GGDLA----------------QPGGLLA---EVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAA 251
|
....*
gi 15599630 322 DLRLD 326
Cdd:cd19088 252 GLRLS 256
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-334 |
3.94e-37 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 136.27 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTM-TWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVPPraetyASTERIIGNWFRR--SG 77
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPP-----GSAEENFGRLLREdfAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 DRADWILASKIA-----GP-GNGIShvrdgnlkfnRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEE 151
Cdd:PRK09912 88 YRDELIISTKAGydmwpGPyGSGGS----------RKYLLASLDQSLKRMGLEYVDIF----------------YSHRVD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 152 SFTPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEErgWPRAVSIQNP-YNLLNRSFE-VGLAEIAIREQCGL 229
Cdd:PRK09912 142 ENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLRE--WKIPLLIHQPsYNLLNRWVDkSGLLDTLQNNGVGC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 230 LAYSPMAFGMLSGKYADGArPANARISLYSRFTRYTNP----QAEAACARYV-ALAREHGLEPAQMALAYVTSRPFVTSN 304
Cdd:PRK09912 220 IAFTPLAQGLLTGKYLNGI-PQDSRMHREGNKVRGLTPkmltEANLNSLRLLnEMAQQRGQSMAQMALSWLLKDERVTSV 298
|
330 340 350
....*....|....*....|....*....|.
gi 15599630 305 IIGATSLEQLETNLGSV-DLRLDEEVLAGID 334
Cdd:PRK09912 299 LIGASRAEQLEENVQALnNLTFSTEELAQID 329
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-334 |
9.02e-36 |
|
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: 130.45 E-value: 9.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 9 TDLKVSALCLGTmtWGEQNSEQDAFAQIARAKA---AGINFMDTAEMYpvppraetyAS--TERIIGNWFRrsGDRADWI 83
Cdd:cd19138 7 DGTKVPALGQGT--WYMGEDPAKRAQEIEALRAgidLGMTLIDTAEMY---------GDggSEELVGEAIR--GRRDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 84 LASKIAgPGNGishvrdgnlkfNRQHIVAALDASLERLQTDWLDLYQLHWPERrtnffgqlgyqhqeesfTPLEETLEVL 163
Cdd:cd19138 74 LVSKVL-PSNA-----------SRQGTVRACERSLRRLGTDYLDLYLLHWRGG-----------------VPLAETVAAM 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 164 DEQVRAGKIRHIGLSNetpWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGK 243
Cdd:cd19138 125 EELKKEGKIRAWGVSN---FDTDDMEELWAVPGGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 244 yadgarpanarislysrfTRYTNPqaeaacaRYVALAREHGLEPAQMALAYVTSRPFVTSnIIGATSLEQLETNLGSVDL 323
Cdd:cd19138 202 ------------------GLLENP-------TLKEIAARHGATPAQVALAWVLRDGNVIA-IPKSGSPEHARENAAAADL 255
|
330
....*....|.
gi 15599630 324 RLDEEVLAGID 334
Cdd:cd19138 256 ELTEEDLAELD 266
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-341 |
1.13e-33 |
|
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: 126.69 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGT-MTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVppraetyASTERIIGNWFRRSG-D 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASKIAGPGNGishvrDGNLKFNRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFTPLEE 158
Cdd:cd19159 74 RSSLVITTKLYWGGKA-----ETERGLSRKHIIEGLKGSLQRLQLEYVDVV----------------FANRPDSNTPMEE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 TLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRS-FEVGLAEIAIREQCGLLAYSPMAF 237
Cdd:cd19159 133 IVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLAC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 238 GMLSGKYADGArPANARISLYS------RFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSL 311
Cdd:cd19159 213 GIISGKYGNGV-PESSRASLKCyqwlkeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTP 291
|
330 340 350
....*....|....*....|....*....|..
gi 15599630 312 EQLETNLGSVDL--RLDEEVLAGIDAIHREQP 341
Cdd:cd19159 292 EQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 323
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-333 |
3.67e-33 |
|
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: 124.85 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 4 RPLGRTDLKVSALCLGTM----TWGEQNSEQDAFAQIARAKAAGINFMDTAEMY-PvppraetyASTERIIGNWFRrSGD 78
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsgDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgP--------NTNEVLLGKALK-DGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASK--IAGPGNGISHVRdGNLKFNRqhivAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFTPL 156
Cdd:cd19145 74 REKVQLATKfgIHEIGGSGVEVR-GDPAYVR----AACEASLKRLDVDYIDLY----------------YQHRIDTTVPI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 157 EETLEVLDEQVRAGKIRHIGLSNETPwgtmTFLRLAEergwprAV----SIQNPYNLLNRSFEvglAEI--AIRE-QCGL 229
Cdd:cd19145 133 EITMGELKKLVEEGKIKYIGLSEASA----DTIRRAH------AVhpitAVQLEWSLWTRDIE---EEIipTCRElGIGI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 230 LAYSPMAFGMLSGKYADGARPANA-RISLYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19145 200 VPYSPLGRGFFAGKAKLEELLENSdVRKSHPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGT 279
|
330 340
....*....|....*....|....*
gi 15599630 309 TSLEQLETNLGSVDLRLDEEVLAGI 333
Cdd:cd19145 280 TKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-344 |
6.44e-33 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 122.86 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 12 KVSALCLGTmtWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAg 90
Cdd:COG0656 4 EIPALGLGT--W--QLPGEEAAAAVRTALEAGYRHIDTAAMY----------GNEEGVGEAIAASGvPREELFVTTKVW- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 91 pgngishvrdgNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPerrtnffgqlgyqhqeeSFTPLEETLEVLDEQVRAG 170
Cdd:COG0656 69 -----------NDNHGYDDTLAAFEESLERLGLDYLDLYLIHWP-----------------GPGPYVETWRALEELYEEG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 171 KIRHIGLSNetpwgtmtFL-----RLAEERGWPRAVsIQNPYNLLNRSFEVglaeiaiREQC---GLL--AYSPMAFGML 240
Cdd:COG0656 121 LIRAIGVSN--------FDpehleELLAETGVKPAV-NQVELHPYLQQREL-------LAFCrehGIVveAYSPLGRGKL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 241 sgkyadgarPANARIslysrftrytnpqaeaacaryVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGS 320
Cdd:COG0656 185 ---------LDDPVL---------------------AEIAEKHGKTPAQVVLRWHLQRGVVV--IPKSVTPERIRENLDA 232
|
330 340
....*....|....*....|....*..
gi 15599630 321 VDLRLDEEVLAGIDAIHREQ---PNPA 344
Cdd:COG0656 233 FDFELSDEDMAAIDALDRGErlgPDPD 259
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-341 |
2.34e-32 |
|
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: 123.17 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGT-MTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVppraetyASTERIIGNWFRRSG-D 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA-------GKAERTLGNILKSKGwR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASKIAGPGNGishvrDGNLKFNRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFTPLEE 158
Cdd:cd19160 76 RSSYVVTTKIYWGGQA-----ETERGLSRKHIIEGLRGSLDRLQLEYVDIV----------------FANRSDPNSPMEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 TLEVLDEQVRAGKIRHIGLSNetpWGTMTFLR---LAEERGWPRAVSIQNPYNLLNRS-FEVGLAEIAIREQCGLLAYSP 234
Cdd:cd19160 135 IVRAMTYVINQGMAMYWGTSR---WSAMEIMEaysVARQFNLIPPVCEQAEYHLFQREkVEMQLPELYHKIGVGSVTWSP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 235 MAFGMLSGKYaDGARPANARIS------LYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGA 308
Cdd:cd19160 212 LACGLITGKY-DGRVPDTCRAAvkgyqwLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGV 290
|
330 340 350
....*....|....*....|....*....|....*
gi 15599630 309 TSLEQLETNLGSVDL--RLDEEVLAGIDAIHREQP 341
Cdd:cd19160 291 SSAEQLIENLGSIQVlsQLTPQTVMEIDALLGNKP 325
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-324 |
2.50e-32 |
|
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: 122.56 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 3 YRPLGRTDLKVSALCLGT-MTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVppraetyASTERIIGNWFRRSG-DRA 80
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTwVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAA-------GKAEIVLGKILKKKGwRRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 81 DWILASKIAGPGNGishvrDGNLKFNRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFTPLEETL 160
Cdd:cd19141 75 SYVITTKIFWGGKA-----ETERGLSRKHIIEGLKASLERLQLEYVDIV----------------FANRPDPNTPMEEIV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 161 EVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNR-SFEVGLAEIAIREQCGLLAYSPMAFGM 239
Cdd:cd19141 134 RAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 240 LSGKYADGArPANARISL--YS----RFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQ 313
Cdd:cd19141 214 LSGKYDDGV-PEYSRASLkgYQwlkeKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQ 292
|
330
....*....|.
gi 15599630 314 LETNLGSVDLR 324
Cdd:cd19141 293 LYENLQAIQVL 303
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-336 |
3.04e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 122.32 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 23 WGEQNSEQDAFAQIARAKAAGINFMDTAEmypvppraeTYASTERIIG---NWFRRSGDRADWILA-SKIAgpgngishV 98
Cdd:cd19101 16 HGGIRDEDAAVRAMAAYVDAGLTTFDCAD---------IYGPAEELIGefrKRLRRERDAADDVQIhTKWV--------P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 99 RDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPErrtnfFGQLGYqhqeesftplEETLEVLDEQVRAGKIRHIGLS 178
Cdd:cd19101 79 DPGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWD-----YSDPGY----------LDAAKHLAELQEEGKIRHLGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 179 N-ETPwgtmtflRLAE--ERGwPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYADGARPA---- 251
Cdd:cd19101 144 NfDTE-------RLREilDAG-VPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYLGVPEPTgpal 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 252 -NARISLYSRFTRYTNP----QAEAACARyvALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDLRLD 326
Cdd:cd19101 216 eTRSLQKYKLMIDEWGGwdlfQELLRTLK--AIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLD 293
|
330
....*....|
gi 15599630 327 EEVLAGIDAI 336
Cdd:cd19101 294 DEDRAAIDAV 303
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-334 |
4.80e-31 |
|
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: 118.88 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 11 LKVSALCLGTM--TWGEQNSEQD-AFAQIARAKAAGINFMDTAEMYPVPPRAetyaSTERIIGNWFRRSGDRADWILASk 87
Cdd:cd19077 3 KLVGPIGLGLMglTWRPNPTPDEeAFETMKAALDAGSNLWNGGEFYGPPDPH----ANLKLLARFFRKYPEYADKVVLS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 88 IAGPGNGISHVRDGNLKFNRQHIvaalDASLERL-QTDWLDLYQlhwPERRtnffgqlgyqhqeESFTPLEETLEVLDEQ 166
Cdd:cd19077 78 VKGGLDPDTLRPDGSPEAVRKSI----ENILRALgGTKKIDIFE---PARV-------------DPNVPIEETIKALKEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 167 VRAGKIRHIGLSN---ETpwgtmtfLRLAEERGWPRAVSIQnpYNLLNRS-FEVGLAEIAIREQCGLLAYSPMAFGMLSG 242
Cdd:cd19077 138 VKEGKIRGIGLSEvsaET-------IRRAHAVHPIAAVEVE--YSLFSREiEENGVLETCAELGIPIIAYSPLGRGLLTG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 243 KYADGAR-PANARISLYSRFTRyTNPQAEAACARYV-ALAREHGLEPAQMALAYVTSRPFVTsnII---GATSLEQLETN 317
Cdd:cd19077 209 RIKSLADiPEGDFRRHLDRFNG-ENFEKNLKLVDALqELAEKKGCTPAQLALAWILAQSGPK--IIpipGSTTLERVEEN 285
|
330
....*....|....*..
gi 15599630 318 LGSVDLRLDEEVLAGID 334
Cdd:cd19077 286 LKAANVELTDEELKEIN 302
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-328 |
2.36e-30 |
|
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: 116.89 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 9 TDLKVSALCLGTMTWGEQNSE-QDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSGDRADWI-LAS 86
Cdd:cd19092 2 EGLEVSRLVLGCMRLADWGESaEELLSLIEAALELGITTFDHADIY-------GGGKCEELFGEALALNPGLREKIeIQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 87 K-----IAGPGNGISHVRDgnlkFNRQHIVAALDASLERLQTDWLDLYQLHWPErrtnffgqlgyqhqeesftPL---EE 158
Cdd:cd19092 75 KcgirlGDDPRPGRIKHYD----TSKEHILASVEGSLKRLGTDYLDLLLLHRPD-------------------PLmdpEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 TLEVLDEQVRAGKIRHIGLSNETPWGtmtfLRLAEERGWPRAVSIQNPYNLLNRS-FEVGLAEIAIREQCGLLAYSPMAF 237
Cdd:cd19092 132 VAEAFDELVKSGKVRYFGVSNFTPSQ----IELLQSYLDQPLVTNQIELSLLHTEaIDDGTLDYCQLLDITPMAWSPLGG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 238 GMLSGKYADGARPANARISlysrftrytnpqaeaacaryvALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETN 317
Cdd:cd19092 208 GRLFGGFDERFQRLRAALE---------------------ELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSA 266
|
330
....*....|.
gi 15599630 318 LGSVDLRLDEE 328
Cdd:cd19092 267 VKALDIELTRE 277
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
11-336 |
5.11e-30 |
|
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: 116.75 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 11 LKVSALCLGTMTWGEQN-------SEQDAFAQIARAKAAGINFMDTAEMYpvppRAETyasTERIIGNWFRRSGDRADWI 83
Cdd:cd19146 9 VRVSPLCLGAMSFGEAWksmmgecDKETAFKLLDAFYEQGGNFIDTANNY----QGEE---SERWVGEWMASRGNRDEMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 84 LASKIAgpgngISHVRDGNLKF-------NRQHIVAALDASLERLQTDWLDLYQLHWPErrtnffgqlgYQhqeesfTPL 156
Cdd:cd19146 82 LATKYT-----TGYRRGGPIKIksnyqgnHAKSLRLSVEASLKKLQTSYIDILYVHWWD----------YT------TSI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 157 EETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMA 236
Cdd:cd19146 141 PELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 237 FGMLsgKYADGARPANarislysRFTRYTNPQAE---AACARYVALAREHGLEPAQMALAYVTSR-PFVTSnIIGATSLE 312
Cdd:cd19146 221 QGQF--RTEEEFKRRG-------RSGRKGGPQTEkerKVSEKLEKVAEEKGTAITSVALAYVMHKaPYVFP-IVGGRKVE 290
|
330 340
....*....|....*....|....
gi 15599630 313 QLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19146 291 HLKGNIEALGISLSDEEIQEIEDA 314
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-322 |
7.99e-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: 114.58 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTM----TWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPvppraeTYAStERIIGNWFRRsGDRADWILASKIa 89
Cdd:cd19096 1 SVLGFGTMrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYG------GGKS-EEILGEALKE-GPREKFYLATKL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 90 gPGNGISHVRDgnlkFNRQhivaaLDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhQEESFTPLEeTLEVLDEQVRA 169
Cdd:cd19096 72 -PPWSVKSAED----FRRI-----LEESLKRLGVDYIDFYLLHGLNSPE----------WLEKARKGG-LLEFLEKAKKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 170 GKIRHIGLS----NETpwgtmtFLRLAEERGWpRAVSIQnpYNLLNRSFE--VGLAEIAIREQCGLLAYSPMAFGMLSgk 243
Cdd:cd19096 131 GLIRHIGFSfhdsPEL------LKEILDSYDF-DFVQLQ--YNYLDQENQagRPGIEYAAKKGMGVIIMEPLKGGGLA-- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599630 244 yadgarpanarislysrftrYTNPQAEAACARYvalarehGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVD 322
Cdd:cd19096 200 --------------------NNPPEALAILCGA-------PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-341 |
8.83e-30 |
|
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: 116.34 E-value: 8.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGT-MTWGEQNSEQDAFAQIARAKAAGINFMDTAEMYPVppraetyASTERIIGNWFRRSG-D 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASKIAGPGNGishvrDGNLKFNRQHIVAALDASLERLQTDWLDLYqlhwperrtnffgqlgYQHQEESFTPLEE 158
Cdd:cd19158 74 RSSLVITTKIFWGGKA-----ETERGLSRKHIIEGLKASLERLQLEYVDVV----------------FANRPDPNTPMEE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 TLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRS-FEVGLAEIAIREQCGLLAYSPMAF 237
Cdd:cd19158 133 TVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLAC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 238 GMLSGKYADGArPANARIS------LYSRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSL 311
Cdd:cd19158 213 GIVSGKYDSGI-PPYSRASlkgyqwLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNA 291
|
330 340 350
....*....|....*....|....*....|..
gi 15599630 312 EQLETNLGSVDL--RLDEEVLAGIDAIHREQP 341
Cdd:cd19158 292 EQLMENIGAIQVlpKLSSSIVHEIDSILGNKP 323
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-341 |
6.82e-28 |
|
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: 111.02 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRTDLKVSALCLGTM-TWGEQNSEQDAFAQIARAKAAGINFMDTAEMYpVPPRAETyaSTERII--GNWFRRSg 77
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWsTFSTAISEEQAEEIVTLAYENGINYFDTSDAF-TSGQAET--ELGRILkkKGWKRSS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 78 dradWILASKI---AGP-GNGIShvrdgnlkfnRQHIVAALDASLERLQTDWLDLYQLhwperrtnffgqlgyqHQEESF 153
Cdd:cd19142 77 ----YIVSTKIywsYGSeERGLS----------RKHIIESVRASLRRLQLDYIDIVII----------------HKADPM 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 154 TPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRS-FEVGLAEIAIREQCGLLAY 232
Cdd:cd19142 127 CPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREkMELYMPELYNKVGVGLITW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 233 SPMAFGMLSGKyADGARPANARISLysRFTRYTNPQ-----------AEAACARYVALAREHGLEPAQMALAYVTSRPFV 301
Cdd:cd19142 207 SPLSLGLDPGI-SEETRRLVTKLSF--KSSKYKVGSdgngiheetrrASHKLRELSLIAERLGCDLTQLLIAWSLKNENV 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15599630 302 TSNIIGATSLEQLETNLGSVDL--RLDEEVLAGIDAIHREQP 341
Cdd:cd19142 284 QCVLIGASSLEQLYSQLNSLQLlpKLNSAVMEELERILDNKP 325
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-318 |
6.28e-27 |
|
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: 106.84 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGT----MTWGEQN-----SEQDAFAQIARAKAAGINFMDTAEMYPvppraetyaSTERIIGNWFRRSGDradWIL 84
Cdd:cd19097 1 SKLALGTaqfgLDYGIANksgkpSEKEAKKILEYALKAGINTLDTAPAYG---------DSEKVLGKFLKRLDK---FKI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 85 ASKIAGPgngishvrDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTNFFGQLgyqhqeesftpleetLEVLD 164
Cdd:cd19097 69 ITKLPPL--------KEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKL---------------VEALL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 165 EQVRAGKIRHIGLS----NEtpwgtmtfLRLAEERGWPRAvsIQNPYNLLNRSFevglaeiairEQCGLLayspmafgml 240
Cdd:cd19097 126 ELKKEGLIRKIGVSvyspEE--------LEKALESFKIDI--IQLPFNILDQRF----------LKSGLL---------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 241 sgkyadgARPANARISLYSR--------FTRYTNPQAEAACA-----RYVALAREHGLEPAQMALAYVTSRPFVTSNIIG 307
Cdd:cd19097 176 -------AKLKKKGIEIHARsvflqgllLMEPDKLPAKFAPAkpllkKLHELAKKLGLSPLELALGFVLSLPEIDKIVVG 248
|
330
....*....|.
gi 15599630 308 ATSLEQLETNL 318
Cdd:cd19097 249 VDSLEQLKEII 259
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
11-334 |
1.18e-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: 107.60 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 11 LKVSALCLGTMTWGEQNS-------EQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSGDRADWI 83
Cdd:cd19147 8 IRVSPLILGAMSIGDAWSgfmgsmdKEQAFELLDAFYEAGGNFIDTANNY-------QDEQSETWIGEWMKSRKNRDQIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 84 LASKIA------GPGNGISHVRDGNLKfnrQHIVAALDASLERLQTDWLDLYQLHWPERRTNffgqlgyqhqeesftpLE 157
Cdd:cd19147 81 IATKFTtdykayEVGKGKAVNYCGNHK---RSLHVSVRDSLRKLQTDWIDILYVHWWDYTTS----------------IE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 158 ETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAF 237
Cdd:cd19147 142 EVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 238 GMLSGKYADGARPANARISLYSRFTRYTNPQAEAACARYVALAREHGLEP-AQMALAYVTSRPFVTSNIIGATSLEQLET 316
Cdd:cd19147 222 GKFQSKKAVEERKKNGEGLRSFVGGTEQTPEEVKISEALEKVAEEHGTESvTAIALAYVRSKAPNVFPLVGGRKIEHLKD 301
|
330
....*....|....*...
gi 15599630 317 NLGSVDLRLDEEVLAGID 334
Cdd:cd19147 302 NIEALSIKLTPEEIEYLE 319
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-334 |
1.80e-26 |
|
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: 105.05 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 18 LGTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAgpgngIS 96
Cdd:cd19073 4 LGLGTW--QLRGDDCANAVKEALELGYRHIDTAEIY----------NNEAEVGEAIAESGvPREDLFITTKVW-----RD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 97 HVRDGNLKfnrqhivAALDASLERLQTDWLDLYQLHWPERRtnffgqlgyqhqeesfTPLEETLEVLDEQVRAGKIRHIG 176
Cdd:cd19073 67 HLRPEDLK-------KSVDRSLEKLGTDYVDLLLIHWPNPT----------------VPLEETLGALKELKEAGKVKSIG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 177 LSNETPwgtmtflrlaeergwpravsiqnpyNLLNRSFEVGLAEIAIRE--------QCGLLAYspmafgmlsgkyadgA 248
Cdd:cd19073 124 VSNFTI-------------------------ELLEEALDISPLPIAVNQvefhpflyQAELLEY---------------C 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 249 RPANARISLYSRFTRYTNPQAEaacaRYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEE 328
Cdd:cd19073 164 RENDIVITAYSPLARGEVLRDP----VIQEIAEKYDKTPAQVALRWLVQKGIVV--IPKASSEDHLKENLAIFDWELTSE 237
|
....*.
gi 15599630 329 VLAGID 334
Cdd:cd19073 238 DVAKID 243
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-336 |
2.85e-26 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 106.40 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 3 YRPLGRTDLKVSALCLGTMTWGE---QNSEQDAFAQIARAKAAGINFMDTAEMYpvpprAETYAstERIIGNWFRRSG-D 78
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSvfgPVSEEDAIASVREAFRLGINFFDTSPYY-----GGTLS--EKVLGKALKALGiP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASKIAGPGNGishvrdgnLKFNRQHIVAALDASLERLQTDWLDLYQLHWPErrtnfFGQLGyqhqeesfTPLEE 158
Cdd:PLN02587 74 REKYVVSTKCGRYGEG--------FDFSAERVTKSVDESLARLQLDYVDILHCHDIE-----FGSLD--------QIVNE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 TLEVLDEQVRAGKIRHIGLSNeTPWGTMTFLRlaeERGWPRAVSIQNPY--NLLNRSFEVGLAEIAIREQCGLLAYSPMA 236
Cdd:PLN02587 133 TIPALQKLKESGKVRFIGITG-LPLAIFTYVL---DRVPPGTVDVILSYchYSLNDSSLEDLLPYLKSKGVGVISASPLA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 237 FGMLSGKYADGARPAnarislysrftrytNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLET 316
Cdd:PLN02587 209 MGLLTENGPPEWHPA--------------PPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEE 274
|
330 340
....*....|....*....|....
gi 15599630 317 NLGSVD----LRLDEEVLAGIDAI 336
Cdd:PLN02587 275 NVAAATeletSGIDEELLSEVEAI 298
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-334 |
3.26e-26 |
|
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: 104.96 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 12 KVSALCLGTmtWGEQNSEQDAFAQ-------IARAKAAGINFMDTAEMYpvppraeTYASTERIIGN---WFRRSgdraD 81
Cdd:cd19137 3 KIPALGLGT--WGIGGFLTPDYSRdeemvelLKTAIELGYTHIDTAEMY-------GGGHTEELVGKaikDFPRE----D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 82 WILASKIAgPGNgishvrdgnlkFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEETLE 161
Cdd:cd19137 70 LFIVTKVW-PTN-----------LRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNI----------------PLEETLS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 162 VLDEQVRAGKIRHIGLSNetpwGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEV-GLAEIAIREQCGLLAYSPMAFGML 240
Cdd:cd19137 122 AMAEGVRQGLIRYIGVSN----FNRRLLEEAISKSQTPIVCNQVKYNLEDRDPERdGLLEYCQKNGITVVAYSPLRRGLE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 241 sgkyadgarPANARISlysrftrytnpqaeaacaryvALAREHGLEPAQMALAYVTSRPFVTSnIIGATSLEQLETNLGS 320
Cdd:cd19137 198 ---------KTNRTLE---------------------EIAKNYGKTIAQIALAWLIQKPNVVA-IPKAGRVEHLKENLKA 246
|
330
....*....|....
gi 15599630 321 VDLRLDEEVLAGID 334
Cdd:cd19137 247 TEIKLSEEEMKLLD 260
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-333 |
9.26e-25 |
|
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: 101.67 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTMTWGEQN--SEQDAFAQIARAKAAGINFMDTAEMYPVppraetyASTERIIGNwFRRSGDRADWILASK---- 87
Cdd:cd19162 1 PRLGLGAASLGNLAraGEDEAAATLDAAWDAGIRYFDTAPLYGL-------GLSERRLGA-ALARHPRAEYVVSTKvgrl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 88 IAGPGNGISHVRDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTNffgqlgyqhqeesfTPLEETLEVLDEQV 167
Cdd:cd19162 73 LEPGAAGRPAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLL--------------QALTDAFPALEELR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 168 RAGKIRHIGLSNetpwGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYADG 247
Cdd:cd19162 139 AEGVVGAIGVGV----TDWAALLRAARRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 248 ARpanarislysRFTRYTNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDLRLDE 327
Cdd:cd19162 215 DR----------YDYRPATPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPA 284
|
....*.
gi 15599630 328 EVLAGI 333
Cdd:cd19162 285 EFWAEL 290
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
17-336 |
7.66e-24 |
|
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: 98.48 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 17 CLGTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIagpgngi 95
Cdd:cd19140 10 ALGLGTY--PLTGEECTRAVEHALELGYRHIDTAQMY----------GNEAQVGEAIAASGvPRDELFLTTKV------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 96 shvrdGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftPLEETLEVLDEQVRAGKIRHI 175
Cdd:cd19140 71 -----WPDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDV----------------PLAETLGALNEAQEAGLARHI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 176 GLSNETPwgtmTFLRLAEERGWPRAVSIQNPYN-LLNRSfevGLAEIAIREQCGLLAYSPMAfgmlsgkyaDGARPANAR 254
Cdd:cd19140 130 GVSNFTV----ALLREAVELSEAPLFTNQVEYHpYLDQR---KLLDAAREHGIALTAYSPLA---------RGEVLKDPV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 255 IslysrftrytnpqaeaacaryVALAREHGLEPAQMALAYVTSRPFVTSnIIGATSLEQLETNLGSVDLRLDEEVLAGID 334
Cdd:cd19140 194 L---------------------QEIGRKHGKTPAQVALRWLLQQEGVAA-IPKATNPERLEENLDIFDFTLSDEEMARIA 251
|
..
gi 15599630 335 AI 336
Cdd:cd19140 252 AL 253
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-318 |
3.35e-23 |
|
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: 97.77 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 11 LKVSALCLGTMTwGEQNSEQDAFAQ--IARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRR-----SGDRADWI 83
Cdd:cd19099 1 LTLSSLGLGTYR-GDSDDETDEEYReaLKAALDSGINVIDTAINY-------RGGRSERLIGKALREliekgGIKRDEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 84 LASK--------------------IAGPGNGISHVRDGNLK-FNRQHIVAALDASLERLQTDWLDLYQLHWPERrtnffg 142
Cdd:cd19099 73 IVTKagyipgdgdeplrplkyleeKLGRGLIDVADSAGLRHcISPAYLEDQIERSLKRLGLDTIDLYLLHNPEE------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 143 QLGYQHQEESFTPLEETLEVLDEQVRAGKIRHIGLSNET----PWGTMTFLRLAEERGWPRAVS--------IQNPYNLL 210
Cdd:cd19099 147 QLLELGEEEFYDRLEEAFEALEEAVAEGKIRYYGISTWDgfraPPALPGHLSLEKLVAAAEEVGgdnhhfkvIQLPLNLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 211 NRSFEVG----------LAEIAIREQCGLLAYSPMAFGMLSGKYADGARPANArislysrftrytnpqaeaacaryvala 280
Cdd:cd19099 227 EPEALTEkntvkgealsLLEAAKELGLGVIASRPLNQGQLLGELRLADLLALP--------------------------- 279
|
330 340 350
....*....|....*....|....*....|....*...
gi 15599630 281 reHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNL 318
Cdd:cd19099 280 --GGATLAQRALQFARSTPGVDSALVGMRRPEHVDENL 315
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-334 |
7.08e-23 |
|
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: 95.63 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 15 ALCLGTmtWGEQNSEqdAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAGPGN 93
Cdd:cd19071 3 LIGLGT--YKLKPEE--TAEAVLAALEAGYRHIDTAAAY----------GNEAEVGEAIRESGvPREELFITTKLWPTDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 94 GISHVRdgnlkfnrqhivAALDASLERLQTDWLDLYQLHWPerrtnffgqlGYQHQEESFTPLEETLEVLDEQVRAGKIR 173
Cdd:cd19071 69 GYERVR------------EALEESLKDLGLDYLDLYLIHWP----------VPGKEGGSKEARLETWRALEELVDEGLVR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 174 HIGLSNETPWGTMTFLRLAEERgwPRAVSIQ-NPYNllnrsfevglAEIAIREQC---GLL--AYSPMAFGMLSGKyadg 247
Cdd:cd19071 127 SIGVSNFNVEHLEELLAAARIK--PAVNQIElHPYL----------QQKELVEFCkehGIVvqAYSPLGRGRRPLL---- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 248 arpANARIslysrftrytnpqaeaacaryVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDE 327
Cdd:cd19071 191 ---DDPVL---------------------KEIAKKYGKTPAQVLLRWALQRGVVV--IPKSSNPERIKENLDVFDFELSE 244
|
....*..
gi 15599630 328 EVLAGID 334
Cdd:cd19071 245 EDMAAID 251
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-322 |
8.00e-23 |
|
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: 96.45 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 4 RPLGRTDLKVSALCLGTMTWGEQ----NSEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSG-D 78
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVygdgLEQDEAVAIVAEAFAAGINHFDTSPYY-------GAESSEAVLGKALAALQvP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASKIAgpgngisHVRDGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPErrtnfFGQLgyqhqeesFTPLEE 158
Cdd:cd19153 76 RSSYTVATKVG-------RYRDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIE-----FVDY--------DTLVDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 TLEVLDEQVRAGKIRHIGLSNeTPWGTMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFG 238
Cdd:cd19153 136 ALPALRTLKDEGVIKRIGIAG-YPLDTLTRATRRCSPGSLDAVLSYCHLTLQDARLESDAPGLVRGAGPHVINASPLSMG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 239 MLSGKYADGARPAnarislysrftrytNPQAEAACARYVALAREHGLEPAQMALAY-VTSRPFVTSNIIGATSLEQLETN 317
Cdd:cd19153 215 LLTSQGPPPWHPA--------------SGELRHYAAAADAVCASVEASLPDLALQYsLAAHAGVGTVLLGPSSLAQLRSM 280
|
....*
gi 15599630 318 LGSVD 322
Cdd:cd19153 281 LAAVD 285
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-327 |
1.01e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 93.55 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 10 DLKVSALCLGTMTWGE----------QNSEQDAFAQIA-RAKAAGINFMDTAEMYPVppraetyASTERIIGNwFRRSGD 78
Cdd:cd19103 1 DKKLPKIALGTWSWGSggaggdqvfgNHLDEDTLKAVFdKAMAAGLNLWDTAAVYGM-------GASEKILGE-FLKRYP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 79 RADWILASK----IAGPGNGisHVRDgnlkfnrqhivaALDASLERLQTDWLDLYQLHWP---ERRTnffgqlgyqhqeE 151
Cdd:cd19103 73 REDYIISTKftpqIAGQSAD--PVAD------------MLEGSLARLGTDYIDIYWIHNPadvERWT------------P 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 152 SFTPLeetlevldeqVRAGKIRHIGLSNEtpwgTMTFLRLAEE---RGWPRAVSIQNPYNLLNRSfevglaeiaiREQCG 228
Cdd:cd19103 127 ELIPL----------LKSGKVKHVGVSNH----NLAEIKRANEilaKAGVSLSAVQNHYSLLYRS----------SEEAG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 229 LLAY---------SPMAF--GMLSGKYaDGARP---ANARISLYSRFTrytnPQAEAACARYVALAREHGLEPAQMALAY 294
Cdd:cd19103 183 ILDYckengitffAYMVLeqGALSGKY-DTKHPlpeGSGRAETYNPLL----PQLEELTAVMAEIGAKHGASIAQVAIAW 257
|
330 340 350
....*....|....*....|....*....|....*
gi 15599630 295 VTSRPfvTSNIIGATSLEQLE--TNLGSVDLRLDE 327
Cdd:cd19103 258 AIAKG--TTPIIGVTKPHHVEdaARAASITLTDDE 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
30-336 |
2.03e-20 |
|
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: 88.95 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 30 QDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIagpgngisHVRDgnlkFNRQ 108
Cdd:cd19139 14 DVVIDSVRTALELGYRHIDTAQIY----------DNEAAVGQAIAESGvPRDELFITTKI--------WIDN----LSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 109 HIVAALDASLERLQTDWLDLYQLHWPERRTNffgqlgyqhqeesfTPLEETLEVLDEQVRAGKIRHIGLSNetpwGTMTF 188
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWPSPNDE--------------VPVEEYIGALAEAKEQGLTRHIGVSN----FTIAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 189 LRLAEERGWPRAVSIQ----NPYnLLNRsfevGLAEIAIREQCGLLAYSPMAFGMLsgkyadGARPANARIslysrftry 264
Cdd:cd19139 134 LDEAIAVVGAGAIATNqielSPY-LQNR----KLVAHCKQHGIHVTSYMTLAYGKV------LDDPVLAAI--------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599630 265 tnpqaeaacaryvalAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19139 194 ---------------AERHGATPAQIALAWAMARGYAV--IPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-336 |
1.29e-16 |
|
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: 78.43 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 12 KVSALCLGTMTW----GEQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILAS 86
Cdd:cd19120 3 KIPAIAFGTGTAwyksGDDDIQRDLVDSVKLALKAGFRHIDTAEMY----------GNEKEVGEALKESGvPREDLFITT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 87 KIagpGNGISHVRdgnlkfnrqhivAALDASLERLQTDWLDLYQLHWPerrtnFFGQlgyqhqeESFTPLEETLEVLDEQ 166
Cdd:cd19120 73 KV---SPGIKDPR------------EALRKSLAKLGVDYVDLYLIHSP-----FFAK-------EGGPTLAEAWAELEAL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 167 VRAGKIRHIGLSNETPWGTMTFLRLAEERgwPRAVSIQ-NPYNLlnrsfevglaeiaiREQCGLLAYSP------MAFGM 239
Cdd:cd19120 126 KDAGLVRSIGVSNFRIEDLEELLDTAKIK--PAVNQIEfHPYLY--------------PQQPALLEYCRehgivvSAYSP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 240 LS--GKYADGarPANARISlysrftrytnpqaeaacaryvALAREHGLEPAQMALAYVTSR---PFVTSniigaTSLEQL 314
Cdd:cd19120 190 LSplTRDAGG--PLDPVLE---------------------KIAEKYGVTPAQVLLRWALQKgivVVTTS-----SKEERM 241
|
330 340
....*....|....*....|..
gi 15599630 315 ETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19120 242 KEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-338 |
2.68e-15 |
|
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: 75.14 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLgRTDLKVSALCLGTmtWGeqNSEQDAFAQIARAKAAGINFMDTAEMYPvpPRAETYASteriIGNWFRRSG-DR 79
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGT--WK--SKPGEVGQAVKQALEAGYRHIDCAAIYG--NEAEIGAA----LAEVFKEGKvKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 80 ADWILASKIagpgngishvrdgnlkFNRQH----IVAALDASLERLQTDWLDLYQLHWPerrTNFFGQLGYQHQEESFT- 154
Cdd:cd19123 70 EDLWITSKL----------------WNNSHapedVLPALEKTLADLQLDYLDLYLMHWP---VALKKGVGFPESGEDLLs 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 155 ----PLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIqNPYnllnrsfevgLAEIAIREQCG-- 228
Cdd:cd19123 131 lspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATARIKPAVNQVEL-HPY----------LQQPELLAFCRdn 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 229 ---LLAYSPMAfgmlSGKYADGARPANARISLysrftryTNPQAEaacaryvALAREHGLEPAQMALAYVTSRPfvTSNI 305
Cdd:cd19123 200 gihLTAYSPLG----SGDRPAAMKAEGEPVLL-------EDPVIN-------KIAEKHGASPAQVLIAWAIQRG--TVVI 259
|
330 340 350
....*....|....*....|....*....|...
gi 15599630 306 IGATSLEQLETNLGSVDLRLDEEVLAGIDAIHR 338
Cdd:cd19123 260 PKSVNPERIQQNLEAAEVELDASDMATIAALDR 292
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-339 |
7.79e-15 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 73.85 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 1 MEYRPLGRT----DLKVSALCLGTM------TWGEQNSEQDAFAQIARAKAAGINFMDTAEMY-P-----------VPPR 58
Cdd:PRK10376 1 MSTIMSSGTftlgGRSVNRLGYGAMqlagpgVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYgPhvtnqlirealHPYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 59 AETYASTEriIGnwFRRsGDRADWILAskiagpgngishvrdgnlkFNRQHIVAALDASLERLQTDWLDLYQLhwperRT 138
Cdd:PRK10376 81 DDLTIVTK--VG--ARR-GEDGSWLPA-------------------FSPAELRRAVHDNLRNLGLDVLDVVNL-----RL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 139 NFFGQlgyQHQEESftpLEETLEVLDEQVRAGKIRHIGLSNETPwgtmtfLRLAEERGWPRAVSIQNPYNLLNRS---FE 215
Cdd:PRK10376 132 MGDGH---GPAEGS---IEEPLTVLAELQRQGLVRHIGLSNVTP------TQVAEARKIAEIVCVQNHYNLAHRAddaLI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 216 VGLAEIAIreqcgllAYSPmaFGMLSGkyadgarpanarislysrftrYTNPQAEAacarYVALAREHGLEPAQMALAYV 295
Cdd:PRK10376 200 DALARDGI-------AYVP--FFPLGG---------------------FTPLQSST----LSDVAASLGATPMQVALAWL 245
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15599630 296 TSRpfvTSNII---GATSLEQLETNLGSVDLRLDEEVLAGIDAIHRE 339
Cdd:PRK10376 246 LQR---SPNILlipGTSSVAHLRENLAAAELVLSEEVLAELDGIARE 289
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
102-341 |
9.97e-14 |
|
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: 70.39 E-value: 9.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 102 NLKFNRQHIVAALDASLERLQTDWLDLYQLHWPerrtnffgqLGYQHQEESFTPLE---------ETLEVLDEQVRAGKI 172
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWP---------VAFKENNDSESNGDgslsdidylETWRGMEDLVKLGLT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 173 RHIGLSNETPWGTMTFLRLAEERgwPRAVSIQNPYNLLNRSfevgLAEIAIREQCGLLAYSPmaFGMLSGKYADGARPan 252
Cdd:cd19116 151 RSIGVSNFNSEQINRLLSNCNIK--PAVNQIEVHPTLTQEK----LVAYCQSNGIVVMAYSP--FGRLVPRGQTNPPP-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 253 arislysrftRYTNPqaeaacaRYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAG 332
Cdd:cd19116 221 ----------RLDDP-------TLVAIAKKYGKTTAQIVLRYLIDRGVVP--IPKSSNKKRIKENIDIFDFQLTPEEVAA 281
|
....*....
gi 15599630 333 IDAIHREQP 341
Cdd:cd19116 282 LNSFNTNQR 290
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
104-338 |
3.43e-13 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 68.51 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 104 KFNRQHIVAALDASLERLQTDWLDLYQLHWPerrtnffgqlgyqhQEESFTPLEETLEVLDEQVRAGKIRHIGLSNetpw 183
Cdd:PRK11172 69 NLAKDKLIPSLKESLQKLRTDYVDLTLIHWP--------------SPNDEVSVEEFMQALLEAKKQGLTREIGISN---- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 184 GTMTFLRLAEERGWPRAVSIQ----NPYnLLNRSfevgLAEIAIREQCGLLAYSPMAFGMLSGKyadgarPANARIslys 259
Cdd:PRK11172 131 FTIALMKQAIAAVGAENIATNqielSPY-LQNRK----VVAFAKEHGIHVTSYMTLAYGKVLKD------PVIARI---- 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599630 260 rftrytnpqaeaacaryvalAREHGLEPAQMALAYVTSRPFvtSNIIGATSLEQLETNLGSVDLRLDEEVLAGIDAIHR 338
Cdd:PRK11172 196 --------------------AAKHNATPAQVILAWAMQLGY--SVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDR 252
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-322 |
3.56e-13 |
|
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: 69.28 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTMTWGEQN---SEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNWFRRSgDRADWILASK--- 87
Cdd:cd19161 1 SELGLGTAGLGNLYtavSNADADATLDAAWDSGIRYFDTAPMY-------GHGLAEHRLGDFLREK-PRDEFVLSTKvgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 88 IAGPGNGiSHVRDGN-----LKFNR------QHIVAALDASLERLQTDWLDLYQLHWPERRTNffgqlGYQHQEESF-TP 155
Cdd:cd19161 73 LLKPARE-GSVPDPNgfvdpLPFEIvydysyDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTH-----GDRKERHHFaQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 156 LEETLEVLDEQVRAGKIRHIGLS-NETPwgtmTFLRLAEERGWPRAVsIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSP 234
Cdd:cd19161 147 MSGGFKALEELKKAGVIKAFGLGvNEVQ----ICLEALDEADLDCFL-LAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 235 MAFGMLsgkyADGARPanarislySRFTRYTNPQAE--AACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLE 312
Cdd:cd19161 222 FNSGIL----ATGTKS--------GAKFNYGDAPAEiiSRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPA 289
|
330
....*....|
gi 15599630 313 QLETNLGSVD 322
Cdd:cd19161 290 QLRQNVEAFQ 299
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-338 |
7.51e-13 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 67.93 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 17 CLGTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIG----NWFRRSG-DRADWILASKIAGP 91
Cdd:cd19128 3 RLGFGTY--KITESESKEAVKNAIKAGYRHIDCAYYY----------GNEAFIGiafsEIFKDGGvKREDLFITSKLWPT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 92 GNGISHVRDgnlkfnrqhivaALDASLERLQTDWLDLYQLHWP---ERRTNFFGQLGYQHQEESFTPLEETLEVLDEQVR 168
Cdd:cd19128 71 MHQPENVKE------------QLLITLQDLQLEYLDLFLIHWPlafDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 169 AGKIRHIGLSNETPWGTMTFLRLAEERGWPRAVSIQnPYNLLNRsfevgLAEIAIREQCGLLAYSPMAfgmlsGKYADGA 248
Cdd:cd19128 139 EKLTKNIGVSNYSTKLLTDLLNYCKIKPFMNQIECH-PYFQNDK-----LIKFCIENNIHVTAYRPLG-----GSYGDGN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 249 RpanarislysrfTRYTNPQAEaacaryvALAREHGLEPAQMALAY-VTSRPFVTSNIIGATSLEQLETNLGSVDLRLDE 327
Cdd:cd19128 208 L------------TFLNDSELK-------ALATKYNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDINDLALTK 268
|
330
....*....|.
gi 15599630 328 EvlaGIDAIHR 338
Cdd:cd19128 269 E---DMDAINT 276
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
13-318 |
9.44e-13 |
|
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: 67.69 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 13 VSALCLGTMTWGEQ----NSEQDAFAQIARAKAAGINFMDTAEmYpvppraetYASTERIIGNWFRRSGD---RADWILA 85
Cdd:cd19164 13 LPPLIFGAATFSYQyttdPESIPPVDIVRRALELGIRAFDTSP-Y--------YGPSEIILGRALKALRDefpRDTYFII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 86 SKiAGpgngishvRDGNLKFN--RQHIVAALDASLERLQTDWLDLYQLHWPErrtnffgqlgyqhqeesFTPLEETLEVL 163
Cdd:cd19164 84 TK-VG--------RYGPDDFDysPEWIRASVERSLRRLHTDYLDLVYLHDVE-----------------FVADEEVLEAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 164 DEQVR---AGKIRHIGLSNET-PwgtmTFLRLAE----ERGWP-RAVSIQNPYNLLNRSFevgLAEIAIREQCGLLAY-- 232
Cdd:cd19164 138 KELFKlkdEGKIRNVGISGYPlP----VLLRLAElartTAGRPlDAVLSYCHYTLQNTTL---LAYIPKFLAAAGVKVvl 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 233 --SPMAFGMLSgkyADGAR---PAnarislysrftrytNPQAEAACARYVALAREHGLEPAQMALAYV-TSRPFVTSNII 306
Cdd:cd19164 211 naSPLSMGLLR---SQGPPewhPA--------------SPELRAAAAKAAEYCQAKGTDLADVALRYAlREWGGEGPTVV 273
|
330
....*....|..
gi 15599630 307 GATSLEQLETNL 318
Cdd:cd19164 274 GCSNVDELEEAV 285
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
42-336 |
3.17e-12 |
|
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: 65.67 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 42 AGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAgpgngISHVRDGNLKfnrqhivAALDASLER 120
Cdd:cd19133 35 AGYRLIDTAAAY----------GNEEAVGRAIKKSGiPREELFITTKLW-----IQDAGYEKAK-------KAFERSLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 121 LQTDWLDLYQLHWPerrtnffgqlgyqhqeesFTPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEERgwPRA 200
Cdd:cd19133 93 LGLDYLDLYLIHQP------------------FGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVK--PAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 201 VSIQ-NPYNLlnrsfEVGLAEIAIREQCGLLAYSPMAFGmlsgkyadgarpanarislysRFTRYTNPQAEaacaryvAL 279
Cdd:cd19133 153 NQIEtHPFNQ-----QIEAVEFLKKYGVQIEAWGPFAEG---------------------RNNLFENPVLT-------EI 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599630 280 AREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19133 200 AEKYGKSVAQVILRWLIQRGIVV--IPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
29-182 |
8.72e-12 |
|
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: 64.58 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 29 EQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSGD-----RADWILASKIAGPGNGISHVRdgnl 103
Cdd:cd19136 14 EEEVRQAVDAALKAGYRLIDTASVY----------RNEADIGKALRDLLPkyglsREDIFITSKLAPKDQGYEKAR---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 104 kfnrqhivAALDASLERLQTDWLDLYQLHWPerrtnffGQLGYQHQEESFTPLE-ETLEVLDEQVRAGKIRHIGLSNETP 182
Cdd:cd19136 80 --------AACLGSLERLGTDYLDLYLIHWP-------GVQGLKPSDPRNAELRrESWRALEDLYKEGKLRAIGVSNYTV 144
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-328 |
9.98e-12 |
|
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: 64.94 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 14 SALCLGTMTWG---EQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraeTYASTERIIGNwFRRSGDRADWILASKI-- 88
Cdd:cd19152 1 PKLGFGTAPLGnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWY-------GAGLSEERLGA-ALRELGREDYVISTKVgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 89 -----AGPGNGISHVRDGNLKFN------RQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqLGYQHQEESFTPLE 157
Cdd:cd19152 73 llvplQEVEPTFEPGFWNPLPFDavfdysYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDL-----AGAESDEHFAQAIK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 158 ETLEVLDEQVRAGKIRHIGL-SNEtpwgtMTFLRLAEERGWPRAVSIQNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMA 236
Cdd:cd19152 148 GAFRALEELREEGVIKAIGLgVND-----WEVILRILEEADLDWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 237 FGMLSGKyadgarpanarislySRFTRY----TNPQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLE 312
Cdd:cd19152 223 SGFLAGG---------------DNFDYYeygpAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPE 287
|
330
....*....|....*.
gi 15599630 313 QLETNLGSVDLRLDEE 328
Cdd:cd19152 288 RVEENVALLATEIPAA 303
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
30-338 |
1.37e-11 |
|
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: 63.83 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 30 QDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAGPGNGishvrdgnlkfnRQ 108
Cdd:cd19132 20 DEGVEAVVAALQAGYRLLDTAFNY----------ENEGAVGEAVRRSGvPREELFVTTKLPGRHHG------------YE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 109 HIVAALDASLERLQTDWLDLYQLHWPERRTNFFgqlgyqhqeesftplEETLEVLDEQVRAGKIRHIGLSNetpwgtmtF 188
Cdd:cd19132 78 EALRTIEESLYRLGLDYVDLYLIHWPNPSRDLY---------------VEAWQALIEAREEGLVRSIGVSN--------F 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 189 L-----RLAEERGWPRAVS-IQ-NPYnLLNRSFEVGLAEIAIREQcgllAYSPMAFGmlsgkyadgarpanarislysrf 261
Cdd:cd19132 135 LpehldRLIDETGVTPAVNqIElHPY-FPQAEQRAYHREHGIVTQ----SWSPLGRG----------------------- 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599630 262 trytnpQAEAACARYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDAIHR 338
Cdd:cd19132 187 ------SGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVP--IPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
26-336 |
2.45e-11 |
|
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: 63.19 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 26 QNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAGPGNGishvRDGNLK 104
Cdd:cd19127 18 QTPPEETADAVATALADGYRLIDTAAAY----------GNEREVGEGIRRSGvDRSDIFVTTKLWISDYG----YDKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 105 fnrqhivaALDASLERLQTDWLDLYQLHWPERrtNFFgqlgyQHQEESFTPLEETLEvldeqvrAGKIRHIGLSNETPwg 184
Cdd:cd19127 84 --------GFDASLRRLGLDYVDLYLLHWPVP--NDF-----DRTIQAYKALEKLLA-------EGRVRAIGVSNFTP-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 185 tMTFLRLAEERGWPRAVSiQ---NPYnLLNRSFEVGLAEIAIREQcgllAYSPmafgmLSGKYADGARPANARISLYSRF 261
Cdd:cd19127 140 -EHLERLIDATTVVPAVN-QvelHPY-FSQKDLRAFHRRLGIVTQ----AWSP-----IGGVMRYGASGPTGPGDVLQDP 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599630 262 TrytnpqaeaacarYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19127 208 T-------------ITGLAEKYGKTPAQIVLRWHLQNGVSA--IPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
18-340 |
4.31e-11 |
|
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: 62.90 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 18 LGTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIG---NWFRRSG--DRADWILASKIAGPG 92
Cdd:cd19111 7 IGLGTY--QSPPEEVRAAVDYALFVGYRHIDTALSY----------QNEKAIGealKWWLKNGklKREEVFITTKLPPVY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 93 NGISHVRDGnlkfnrqhivaaLDASLERLQTDWLDLYQLHWPERRTNffgQLGYQHQEESFTPLEETLEVLDEQVRAGKI 172
Cdd:cd19111 75 LEFKDTEKS------------LEKSLENLKLPYVDLYLIHHPCGFVN---KKDKGERELASSDVTSVWRAMEALVSEGKV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 173 RHIGLSNETPWGTMTFLRLAEERgwpravsiqnPYNlLNRSFEVGLAEIAIREQC-----GLLAYSPMAFGMLSGKYADG 247
Cdd:cd19111 140 KSIGLSNFNPRQINKILAYAKVK----------PSN-LQLECHAYLQQRELRKFCnkkniVVTAYAPLGSPGRANQSLWP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 248 ARPANarislysrftrYTNPQAeaacaryVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDE 327
Cdd:cd19111 209 DQPDL-----------LEDPTV-------LAIAKELDKTPAQVLLRFVLQRGTGV--LPKSTNKERIEENFEVFDFELTE 268
|
330
....*....|...
gi 15599630 328 EVLAGIDAIHREQ 340
Cdd:cd19111 269 EHFKKLKTLDRNM 281
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-341 |
6.24e-11 |
|
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: 62.36 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 39 AKAAGINFMDTAEMYPvppRAETYasteriIGNWFRRSG-DRADWILASKIagpgnGISHVRDGNLKfNRQHIVAalDAS 117
Cdd:cd19098 44 AWAAGVRYFDAARSYG---RAEEF------LGSWLRSRNiAPDAVFVGSKW-----GYTYTADWQVD-AAVHEVK--DHS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 118 LERLQTDW----------LDLYQLHwperrtnffgqlgyQHQEESftPLEETLEVLDE--QVRAGKIRhIGLSNETPWGT 185
Cdd:cd19098 107 LARLLKQWeetrsllgkhLDLYQIH--------------SATLES--GVLEDADVLAAlaELKAEGVK-IGLSLSGPQQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 186 MTFLRLAEER--GWPRAVSIQNPYNLLNRSFEVGLAEiAIREQCGLLAYSPMAFGMLSGKyadgarpanarislysrftr 263
Cdd:cd19098 170 ETLRRALEIEidGARLFDSVQATWNLLEQSAGEALEE-AHEAGMGVIVKEALANGRLTDR-------------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 264 ytNPQAEAACARYV--ALAREHGLEPAQMALAYVTSRPFVTSNIIGATSLEQLETNLGSVDLRLDEEVLAgIDAIHREQP 341
Cdd:cd19098 229 --NPSPELAPLMAVlkAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLA-ALADLAEPP 305
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
11-337 |
1.13e-10 |
|
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: 61.19 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 11 LKVSALCLGTMTWGEQNSEQDAFAqiarAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIA 89
Cdd:cd19135 11 VEMPILGLGTSHSGGYSHEAVVYA----LKECGYRHIDTAKRY----------GCEELLGKAIKESGvPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 90 GPGNGISHVRdgnlkfnrqhivAALDASLERLQTDWLDLYQLHWPErrtnffGQLGYQHQEESftpLEETLEVLDEQVRA 169
Cdd:cd19135 77 PSDYGYESTK------------QAFEASLKRLGVDYLDLYLLHWPD------CPSSGKNVKET---RAETWRALEELYDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 170 GKIRHIGLSNETPwgtmTFLRLAEERGWPRAVSIQNPYNLLNRsfEVGLAEIAIREQCGLLAYSPMAFGMLsgkyadgar 249
Cdd:cd19135 136 GLCRAIGVSNFLI----EHLEQLLEDCSVVPHVNQVEFHPFQN--PVELIEYCRDNNIVFEGYCPLAKGKA--------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 250 panarislysrftrYTNPqaeaacaRYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEV 329
Cdd:cd19135 201 --------------LEEP-------TVTELAKKYQKTPAQILIRWSIQNGVVT--IPKSTKEERIKENCQVFDFSLSEED 257
|
....*...
gi 15599630 330 LAGIDAIH 337
Cdd:cd19135 258 MATLDSLH 265
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-339 |
1.52e-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: 60.97 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 9 TDLKVSALCLGTmtWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASK 87
Cdd:cd19117 10 TGAEIPAVGLGT--W--QSKPNEVAKAVEAALKAGYRHIDTAAIY----------GNEEEVGQGIKDSGvPREEIFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 88 IAGpgngishvrdgnlKFNRqHIVAALDASLERLQTDWLDLYQLHWP-----ERRTNFFGQLGYQHQEESFTPLEETLEV 162
Cdd:cd19117 76 LWC-------------TWHR-RVEEALDQSLKKLGLDYVDLYLMHWPvpldpDGNDFLFKKDDGTKDHEPDWDFIKTWEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 163 LDEQVRAGKIRHIGLSNetpwgtmtflrlaeergwpraVSIQNPYNLLNRSfevGLAEIAIREQCGLLAYSPmafgmlSG 242
Cdd:cd19117 142 MQKLPATGKVKAIGVSN---------------------FSIKNLEKLLASP---SAKIVPAVNQIELHPLLP------QP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 243 KYADGARPANARISLYSRFTRYTNP--QAEAAcaryVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGS 320
Cdd:cd19117 192 KLVDFCKSKGIHATAYSPLGSTNAPllKEPVI----IKIAKKHGKTPAQVIISWGLQRGYSV--LPKSVTPSRIESNFKL 265
|
330
....*....|....*....
gi 15599630 321 VDLRLDEevLAGIDAIHRE 339
Cdd:cd19117 266 FTLSDEE--FKEIDELHKE 282
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
35-339 |
2.60e-10 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 60.54 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 35 QIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSGD-----RADWILASKIagpGNGISHvrdgnlkfnRQH 109
Cdd:cd19113 29 QIYQAIKAGYRLFDGAEDY----------GNEKEVGEGVNRAIDeglvkREELFLTSKL---WNNFHD---------PKN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 110 IVAALDASLERLQTDWLDLYQLHWP--------ERR--TNFFGQLGYQHQEESfTPLEETLEVLDEQVRAGKIRHIGLSN 179
Cdd:cd19113 87 VETALNKTLSDLKLDYVDLFLIHFPiafkfvpiEEKypPGFYCGDGDNFVYED-VPILDTWKALEKLVDAGKIKSIGVSN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 180 ETPWGTMTFLRLAEERgwPRAVSIQ-NPYNLLNRSFE-VGLAEIAIreqcglLAYSpmAFGMLSGKYADGARPANARisl 257
Cdd:cd19113 166 FPGALILDLLRGATIK--PAVLQIEhHPYLQQPKLIEyAQKAGITI------TAYS--SFGPQSFVELNQGRALNTP--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 258 ysrfTRYTNPQAEaacaryvALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDAIH 337
Cdd:cd19113 233 ----TLFEHDTIK-------SIAAKHNKTPAQVLLRWATQRGIAV--IPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLD 299
|
..
gi 15599630 338 RE 339
Cdd:cd19113 300 IG 301
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
113-193 |
4.05e-10 |
|
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: 59.67 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 113 ALDASLERLQTDWLDLYQLHWPERRTNffGQLGYQHQEESFTPLEETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLA 192
Cdd:cd19125 90 ALEKTLKDLQLDYLDLYLIHWPVRLKK--GAHMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVA 167
|
.
gi 15599630 193 E 193
Cdd:cd19125 168 R 168
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
107-340 |
6.03e-10 |
|
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: 59.49 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 107 RQHIVAALDASLERLQTDWLDLYQLHWP------ERRTNFfgQLGYQHQEESFTPLE-----ETLEVLDEQVRAGKIRHI 175
Cdd:cd19114 77 KDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvDPAENY--PFLWKDKELKKFPLEqspmqECWREMEKLVDAGLVRNI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 176 GLSNETPWGTMTFLRLAEERgwPRAVSIQ-NPYNLLNRsfevgLAEIAIREQCGLLAYSpmAFGmlsgkyadgarpaNAR 254
Cdd:cd19114 155 GIANFNVQLILDLLTYAKIK--PAVLQIEhHPYLQQKR-----LIDWAKKQGIQITAYS--SFG-------------NAV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 255 ISLYSRFTRYTNPQAEAACARyvALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGID 334
Cdd:cd19114 213 YTKVTKHLKHFTNLLEHPVVK--KLADKHKRDTGQVLLRWAVQRNITV--IPKSVNVERMKTNLDITSYKLDEEDMEALY 288
|
....*.
gi 15599630 335 AIHREQ 340
Cdd:cd19114 289 ELEANA 294
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
107-338 |
6.10e-10 |
|
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: 59.36 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 107 RQHIVAALDASLERLQTDWLDLYQLHWP------ERRTNFfgQLGYQHQEE----SFTPLEETLEVLDEQVRAGKIRHIG 176
Cdd:cd19115 86 GERVEPICRKQLADWGIDYFDLFLIHFPialkyvDPAVRY--PPGWFYDGKkvefSNAPIQETWTAMEKLVDKGLARSIG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 177 LSNETPWGTMTFLRLAEERgwPRAVSIQ-NPYnLLNRsfevGLAEIAIREQCGLLAYSpmAFGMLSgkyadgarpanari 255
Cdd:cd19115 164 VSNFSAQLLMDLLRYARIR--PATLQIEhHPY-LTQP----RLVKYAQKEGIAVTAYS--SFGPQS-------------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 256 slysrFTRYTNPQAEAACARY-----VALAREHGLEPAQMALAYVTSRPFVtsnIIGATSLEQ-LETNLGSVDLRLDEEV 329
Cdd:cd19115 221 -----FLELDLPGAKDTPPLFehdviKSIAEKHGKTPAQVLLRWATQRGIA---VIPKSNNPKrLAQNLDVTGFDLEAEE 292
|
....*....
gi 15599630 330 LAGIDAIHR 338
Cdd:cd19115 293 IKAISALDI 301
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
39-179 |
5.27e-09 |
|
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: 56.25 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 39 AKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAGPGNGIshvrDGNLKfnrqhivaALDAS 117
Cdd:cd19157 33 ALKNGYRSIDTAAIY----------GNEEGVGKGIKESGiPREELFITSKVWNADQGY----DSTLK--------AFEAS 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599630 118 LERLQTDWLDLYQLHWPERRTNffgqlgyqhqeesftplEETLEVLDEQVRAGKIRHIGLSN 179
Cdd:cd19157 91 LERLGLDYLDLYLIHWPVKGKY-----------------KETWKALEKLYKDGRVRAIGVSN 135
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
102-336 |
6.05e-09 |
|
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: 56.27 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 102 NLKFNRQHIVAALDASLERLQTDWLDLYQLHWPerrTNFFGQlGYQHQeESFTPLEETLEVLDEQV-------------R 168
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWP---VAFKPT-GDLNP-LTAVPTNGGEVDLDLSVslvdtwkamvelkK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 169 AGKIRHIGLSNETPWGTMTFLRLAEERgwPRAVSIQNPYNLLNRSfevgLAEIAIREQCGLLAYSPMAfGMLSGKYADGA 248
Cdd:cd19118 151 TGKVKSIGVSNFSIDHLQAIIEETGVV--PAVNQIEAHPLLLQDE----LVDYCKSKNIHITAYSPLG-NNLAGLPLLVQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 249 RPAnarislysrftrytnpqaeaacarYVALAREHGLEPAQMALAYVTSRPFvtSNIIGATSLEQLETNLGSVDlrLDEE 328
Cdd:cd19118 224 HPE------------------------VKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRIRSNFEQVE--LSDD 275
|
....*...
gi 15599630 329 VLAGIDAI 336
Cdd:cd19118 276 EFNAVTAL 283
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
18-336 |
7.53e-09 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 56.38 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 18 LGTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRR---SG--DRADWILASKIAGPG 92
Cdd:cd19155 15 VGLGTW--QSSPEEIETAVDTALEAGYRHIDTAYVY----------RNEAAIGNVLKKwidSGkvKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 93 NgishvrdgnlkfNRQHIVAALDASLERLQTDWLDLYQLHWP-----ERRTNFFGQLGYQHQEESFTPLEETLEVLDEQV 167
Cdd:cd19155 83 N------------RREKVEKFLLKSLEKLQLDYVDLYLIHFPvgslsKEDDSGKLDPTGEHKQDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 168 RAGKIRHIGLSNETPWGTMTFLRLAEERgwPRAVSIQNPYNLLNRSfevgLAEIAIREQCGLLAYSPmafgmLSGKYADG 247
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNARIK--PANLQVELHVYLQQKD----LVDFCSTHSITVTAYAP-----LGSPGAAH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 248 ARPANARISLySRFTRYTNPQAEaacaryvALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDE 327
Cdd:cd19155 220 FSPGTGSPSG-SSPDLLQDPVVK-------AIAERHGKSPAQVLLRWLMQRGVVV--IPKSTNAARIKENFQVFDFELTE 289
|
....*....
gi 15599630 328 EVLAGIDAI 336
Cdd:cd19155 290 ADMAKLSSL 298
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
26-336 |
8.25e-09 |
|
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: 55.63 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 26 QNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAGPGNGISHVRdgnlk 104
Cdd:cd19134 20 ELSDDEAERSVSAALEAGYRLIDTAAAY----------GNEAAVGRAIAASGiPRGELFVTTKLATPDQGFTASQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 105 fnrqhivAALDASLERLQTDWLDLYQLHWPERRTNFFgqlgyqhqEESFTPLeetlevldEQVRA-GKIRHIGLSNETPW 183
Cdd:cd19134 85 -------AACRASLERLGLDYVDLYLIHWPAGREGKY--------VDSWGGL--------MKLREeGLARSIGVSNFTAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 184 GTMTFLRLAeerGWPRAVSIQNPYNLLN-RSFEVGLAEIAIREQcgllAYSPMAFGMLsgkyadgarpanarislysrft 262
Cdd:cd19134 142 HLENLIDLT---FFTPAVNQIELHPLLNqAELRKVNAQHGIVTQ----AYSPLGVGRL---------------------- 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599630 263 rYTNPQAeaacaryVALAREHGLEPAQMALAYvtSRPFVTSNIIGATSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19134 193 -LDNPAV-------TAIAAAHGRTPAQVLLRW--SLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGL 256
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
19-340 |
1.04e-08 |
|
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: 55.88 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 19 GTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIG----NWFRR-SGDRADWILASKIagpgn 93
Cdd:cd19154 16 GLGTW--QSKGAEGITAVRTALKAGYRLIDTAFLY----------QNEEAIGealaELLEEgVVKREDLFITTKL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 94 gishvrdGNLKFNRQHIVAALDASLERLQTDWLDLYQLHWPerrtnffgqLGYQHQEESFTP------------LEETLE 161
Cdd:cd19154 79 -------WTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAP---------AAFKDDEGESGTmengmsihdavdVEDVWR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 162 VLDEQVRAGKIRHIGLSNetpWGTMTFLR-LAEERGWPRAVSIQ-NPYnllnrsfevgLAEIAIREQCGLLAYSPMAFGM 239
Cdd:cd19154 143 GMEKVYDEGLTKAIGVSN---FNNDQIQRiLDNARVKPHNNQVEcHLY----------FPQKELVEFCKKHNISVTSYAT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 240 LsgkyadgARPANARISLYSRFTRYTNPQAEAACAryvALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLG 319
Cdd:cd19154 210 L-------GSPGRANFTKSTGVSPAPNLLQDPIVK---AIAEKHGKTPAQVLLRYLLQRGIAV--IPKSATPSRIKENFN 277
|
330 340
....*....|....*....|.
gi 15599630 320 SVDLRLDEEVLAGIDAIHREQ 340
Cdd:cd19154 278 IFDFSLSEEDMATLEEIEKSL 298
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
106-179 |
6.13e-08 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 53.04 E-value: 6.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599630 106 NRQHIVAALDASLERLQTDWLDLYQLHWPERRTNffGQLGYQHQEESFTPL--EETLEVLDEQVRAGKIRHIGLSN 179
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKP--GKFSFPIEEEDFLPFdiKGVWEAMEECQRLGLTKAIGVSN 153
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
109-345 |
6.73e-08 |
|
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: 53.26 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 109 HIVAALDASLERLQTDWLDLYQLHWP-ERRTNFFGQLGYQHQEESF------TPLEETLEVLDEQVRAGKIRHIGLSNET 181
Cdd:cd19112 84 HVIEACKDSLKKLQLDYLDLYLVHFPvATKHTGVGTTGSALGEDGVldidvtISLETTWHAMEKLVSAGLVRSIGISNYD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 182 PWGTMTFLRLAEERgwPRAVSIQ-NPY----NLLNRSFEVGLAeiaireqcgLLAYSPMafgmlsgkyadGARPANAris 256
Cdd:cd19112 164 IFLTRDCLAYSKIK--PAVNQIEtHPYfqrdSLVKFCQKHGIS---------VTAHTPL-----------GGAAANA--- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 257 lySRFTrYTNPQAEAAcarYVALAREHGLEPAQMALAYVTSRPfvTSNIIGATSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19112 219 --EWFG-SVSPLDDPV---LKDLAKKYGKSAAQIVLRWGIQRN--TAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSL 290
|
....*....
gi 15599630 337 HREQPNPAP 345
Cdd:cd19112 291 DRKYRTNQP 299
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
18-182 |
9.84e-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: 52.37 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 18 LGTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAGPGNGis 96
Cdd:cd19131 13 LGLGVW--QVSNDEAASAVREALEVGYRSIDTAAIY----------GNEEGVGKAIRASGvPREELFITTKLWNSDQG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 97 hvRDGNLKfnrqhivaALDASLERLQTDWLDLYQLHWPERRTNFFgqlgyqhqeesftplEETLEVLDEQVRAGKIRHIG 176
Cdd:cd19131 79 --YDSTLR--------AFDESLRKLGLDYVDLYLIHWPVPAQDKY---------------VETWKALIELKKEGRVKSIG 133
|
....*.
gi 15599630 177 LSNETP 182
Cdd:cd19131 134 VSNFTI 139
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
36-336 |
1.28e-07 |
|
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: 52.05 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 36 IARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKiagpgngishVRDGNLKFNRQhiVAAL 114
Cdd:cd19126 29 VQTALENGYRSIDTAAIY----------KNEEGVGEAIRESGvPREELFVTTK----------LWNDDQRARRT--EDAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 115 DASLERLQTDWLDLYQLHWPerrtnffGQLGYQhqeesftpleETLEVLDEQVRAGKIRHIGLSNETPWGTMTFLRLAEE 194
Cdd:cd19126 87 QESLDRLGLDYVDLYLIHWP-------GKDKFI----------DTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 195 RgwPRAVSIQ-NPYnllnrsfevgLAEIAIREQCG-----LLAYSPMAFGMLsgkyadgarpanarislysrftrYTNPq 268
Cdd:cd19126 150 V--PAVNQVEfHPY----------LTQKELRGYCKskgivVEAWSPLGQGGL-----------------------LSNP- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599630 269 aeaacaRYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19126 194 ------VLAAIGEKYGKSAAQVVLRWDIQHGVVT--IPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
39-179 |
1.64e-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: 52.00 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 39 AKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG------DRADWILASKIagpgngishvrdGNLKFNRQHIVA 112
Cdd:cd19106 29 ALDAGYRHIDCAAVY----------GNEQEVGEALKEKVgpgkavPREDLFVTSKL------------WNTKHHPEDVEP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599630 113 ALDASLERLQTDWLDLYQLHWP---ERRTNFF-----GQLGYqhqeeSFTPLEETLEVLDEQVRAGKIRHIGLSN 179
Cdd:cd19106 87 ALRKTLKDLQLDYLDLYLIHWPyafERGDNPFpknpdGTIRY-----DSTHYKETWKAMEKLVDKGLVKAIGLSN 156
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
34-336 |
2.01e-07 |
|
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: 51.45 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 34 AQIARAKAA----GINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIagpgngishvrdGNLKFNRQ 108
Cdd:cd19130 23 ADTQRAVATalevGYRHIDTAAIY----------GNEEGVGAAIAASGiPRDELFVTTKL------------WNDRHDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 109 HIVAALDASLERLQTDWLDLYQLHWP-ERRTNFFgqlgyqhqeesftpleETLEVLDEQVRAGKIRHIGLSNETPwgtMT 187
Cdd:cd19130 81 EPAAAFAESLAKLGLDQVDLYLVHWPtPAAGNYV----------------HTWEAMIELRAAGRTRSIGVSNFLP---PH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 188 FLRLAEERGWPRAVsiqNPYNLLNRSFEVGLAEIAIREQCGLLAYSPMAFGMLSGKYADGarpanarislysrftrytnp 267
Cdd:cd19130 142 LERIVAATGVVPAV---NQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVG-------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599630 268 qaeaacaryvALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDAI 336
Cdd:cd19130 199 ----------AIAAAHGKTPAQIVLRWHLQKGHVV--FPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-336 |
6.76e-07 |
|
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: 50.22 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 9 TDLKVSALCLGTmtWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSGD----RADWIL 84
Cdd:cd19121 8 TGASIPAVGLGT--W--QAKAGEVKAAVAHALKIGYRHIDGALCY----------QNEDEVGEGIKEAIAggvkREDLFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 85 ASKIAGpgngISHVRdgnlkfnrqhIVAALDASLERLQTDWLDLYQLHWPERrtnffgqLGYQHQEESFTPLEE------ 158
Cdd:cd19121 74 TTKLWS----TYHRR----------VELCLDRSLKSLGLDYVDLYLVHWPVL-------LNPNGNHDLFPTLPDgsrdld 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 159 -------TLEVLDEQVRAGKIRHIGLSNET-PWgtMTFLrLAEERGWPRAVSIQN-PYnllnrsfevgLAEIAIREQC-- 227
Cdd:cd19121 133 wdwnhvdTWKQMEKVLKTGKTKAIGVSNYSiPY--LEEL-LKHATVVPAVNQVENhPY----------LPQQELVDFCke 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 228 -GLL--AYSPMAfgmlsgkyADGArpanarislysrftrytnPQAEAACAryVALAREHGLEPAQMALAYVTSRPFVTsn 304
Cdd:cd19121 200 kGILieAYSPLG--------STGS------------------PLISDEPV--VEIAKKHNVGPGTVLISYQVARGAVV-- 249
|
330 340 350
....*....|....*....|....*....|..
gi 15599630 305 IIGATSLEQLETNLGSVDlrLDEEVLAGIDAI 336
Cdd:cd19121 250 LPKSVTPDRIKSNLEIID--LDDEDMNKLNDI 279
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
18-343 |
2.44e-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: 48.28 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 18 LGTMTWGEQNSEQDAFAqIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKIAGPGNGIs 96
Cdd:cd19156 12 LGLGVWRVQDGAEAENA-VKWAIEAGYRHIDTAAIY----------KNEEGVGQGIRESGvPREEVFVTTKLWNSDQGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 97 hvrdgnlkfnrQHIVAALDASLERLQTDWLDLYQLHWPERRTnffgqlgyqhqeesftpLEETLEVLDEQVRAGKIRHIG 176
Cdd:cd19156 80 -----------ESTLAAFEESLEKLGLDYVDLYLIHWPVKGK-----------------FKDTWKAFEKLYKEKKVRAIG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 177 LSNETPWGTMTFLRLAEERgwPRAVSIQ-NPynLLNRSfevGLAEIAIREQCGLLAYSPMAFGMLsgkyadgarpanari 255
Cdd:cd19156 132 VSNFHEHHLEELLKSCKVA--PMVNQIElHP--LLTQE---PLRKFCKEKNIAVEAWSPLGQGKL--------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 256 slysrftrYTNPqaeaacaRYVALAREHGLEPAQMALAYVTSRPFVTsnIIGATSLEQLETNLGSVDLRLDEEVLAGIDA 335
Cdd:cd19156 190 --------LSNP-------VLKAIGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEERIQENFDVFDFELTAEEIRQIDG 252
|
330
....*....|.
gi 15599630 336 I---HREQPNP 343
Cdd:cd19156 253 LntdHRYGPDP 263
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
105-179 |
1.20e-05 |
|
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: 46.26 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 105 FNRQHIV-AALDASLERLQTDWLDLYQLHWPerrtnffgqLGYQHQEESF------------TPLEETLEVLDEQVRAGK 171
Cdd:cd19107 74 FHEKGLVkGACQKTLSDLKLDYLDLYLIHWP---------TGFKPGKELFpldesgnvipsdTTFLDTWEAMEELVDEGL 144
|
....*...
gi 15599630 172 IRHIGLSN 179
Cdd:cd19107 145 VKAIGVSN 152
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
18-134 |
7.26e-05 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 43.91 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 18 LGTMTWgeQNSEQDAFAQIARAKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRRSG-DRADWILASKiagpgngis 96
Cdd:PRK11565 18 LGLGVW--QASNEEVITAIHKALEVGYRSIDTAAIY----------KNEEGVGKALKEASvAREELFITTK--------- 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 15599630 97 hvrdgnLKFNRQHIV-AALDASLERLQTDWLDLYQLHWP 134
Cdd:PRK11565 77 ------LWNDDHKRPrEALEESLKKLQLDYVDLYLMHWP 109
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
113-193 |
1.28e-04 |
|
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: 42.99 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 113 ALDASLERLQTDWLDLYQLHWP---ERRTNFFGQLG----YQHQEESFTPLEETLEVLDEQVRAGKIRHIGLSNETPWGT 185
Cdd:cd19122 91 SIDNSLKNLKLDYIDLFLVHWPiaaEKNDQRSPKLGpdgkYVILKDLTENPEPTWRAMEEIYESGKAKAIGVSNWTIPGL 170
|
....*...
gi 15599630 186 MTFLRLAE 193
Cdd:cd19122 171 KKLLSFAK 178
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
39-179 |
2.05e-04 |
|
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: 42.44 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 39 AKAAGINFMDTAEMYpvppraetyaSTERIIGNWFRR---SGD--RADWILASKIagpgngishvrdgnlkFNRQH---- 109
Cdd:cd19129 28 ALEAGFRHFDCAERY----------RNEAEVGEAMQEvfkAGKirREDLFVTTKL----------------WNTNHrper 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 110 IVAALDASLERLQTDWLDLYQLHWPerrtnFFGQLGYQHQ----------EESFTpLEETLEVLDEQVRAGKIRHIGLSN 179
Cdd:cd19129 82 VKPAFEASLKRLQLDYLDLYLIHTP-----FAFQPGDEQDprdangnviyDDGVT-LLDTWRAMERLVDEGRCKAIGLSD 155
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
112-179 |
1.65e-03 |
|
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: 39.94 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 112 AALDASLERLQTDWLDLYQLHWPerrtnffgqLGYQHQEE------------SFTPLEETLEVLDEQVRAGKIRHIGLSN 179
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWP---------MGFKPGEPdlpldrsgmvipSDTDFLDTWEAMEDLVIEGLVKNIGVSN 152
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
105-179 |
3.09e-03 |
|
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: 38.75 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599630 105 FNRQHIV-AALDASLERLQTDWLDLYQLHWPerrtnffgqLGYQHQEESFtPLEE-------------TLEVLDEQVRAG 170
Cdd:cd19108 84 FHRPELVrPALEKSLKKLQLDYVDLYLIHFP---------VALKPGEELF-PKDEngklifdtvdlcaTWEAMEKCKDAG 153
|
....*....
gi 15599630 171 KIRHIGLSN 179
Cdd:cd19108 154 LAKSIGVSN 162
|
|
| |
