|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-322 |
3.38e-170 |
|
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: 475.28 E-value: 3.38e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 14 TEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKVGRLLRPVPTG 93
Cdd:cd19161 1 SELGLGTAGLGNLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKVGRLLKPAREG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 94 TVPDYS-YVDPLSFDADYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHGAAKNAVHQKQFLDSGVKALEELKSS 172
Cdd:cd19161 81 SVPDPNgFVDPLPFEIVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERHHFAQLMSGGFKALEELKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 173 GAISAFGLGVNEVPVCLDVMRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILATGPVPGSHFDYM 252
Cdd:cd19161 161 GVIKAFGLGVNEVQICLEALDEADLDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKSGAKFNYG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 253 PADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVEPRLADEIYAEF 322
Cdd:cd19161 241 DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIPEELWQAL 310
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-322 |
6.71e-119 |
|
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: 345.36 E-value: 6.71e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 14 TEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKVGRLLRPVPTG 93
Cdd:cd19152 1 PKLGFGTAPLGNLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVGRLLVPLQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 94 TVPDYSYVD-PLSFDADYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHGAAkNAVHQKQFLDSGVKALEELKSS 172
Cdd:cd19152 81 EPTFEPGFWnPLPFDAVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAE-SDEHFAQAIKGAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 173 GAISAFGLGVNEVPVCLDVMRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILATGPvPGSHFDYM 252
Cdd:cd19152 160 GVIKAIGLGVNDWEVILRILEEADLDWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGD-NFDYYEYG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 253 PADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIveprLADEIYAEF 322
Cdd:cd19152 239 PAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVAL----LATEIPAAF 304
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-321 |
8.12e-104 |
|
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: 306.21 E-value: 8.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 14 TEISFGAAALGGLYRAcPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKVGRLLRPVPTG 93
Cdd:cd19162 1 PRLGLGAASLGNLARA-GEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVGRLLEPGAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 94 TVPDysyvdplsFDADYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVythgaaknavHQKQFLDSGVKALEELKSSG 173
Cdd:cd19162 80 RPAG--------ADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDR----------HLLQALTDAFPALEELRAEG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 174 AISAFGLGVNEVPVCLDVMRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILATGPVPGSHFDYMP 253
Cdd:cd19162 142 VVGAIGVGVTDWAALLRAARRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGDRYDYRP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517055799 254 ADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVEPRLADEIYAE 321
Cdd:cd19162 222 ATPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAEFWAE 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-321 |
1.67e-80 |
|
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: 247.78 E-value: 1.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLS 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGRLLRPVPTGtvpdysyvdplsfdadYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHgaaknavhqkqfLD 160
Cdd:COG0667 81 TKVGRRMGPGPNG----------------RGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTP------------IE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SGVKALEELKSSGAISAFGLGVNEVPVCLDVMRHSDL--DCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGI 238
Cdd:COG0667 133 ETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGlpPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 239 LATGPVPGSHF--------DYMP--ADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNME 308
Cdd:COG0667 213 LTGKYRRGATFpegdraatNFVQgyLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLA 292
|
330
....*....|...
gi 517055799 309 IVEPRLADEIYAE 321
Cdd:COG0667 293 AADLELSAEDLAA 305
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-319 |
3.20e-78 |
|
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: 240.53 E-value: 3.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 14 TEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLglAERRVGDFLRDQPDGSYVLSTKVGRLLRPvptg 93
Cdd:cd19090 1 SALGLGTAGLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAELPREPLVLSTKVGRLPED---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 94 tvpdysyvdplsfdaDYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHGA--AKNAVhqkqfldsgVKALEELKS 171
Cdd:cd19090 75 ---------------TADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDilAPGGA---------LEALLELKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 172 SGAISAFGLGVNEVPVCLDVMRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILATGPVPGSHFDY 251
Cdd:cd19090 131 EGLIKHIGLGGGPPDLLRRAIETGDFDVVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTY 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517055799 252 MPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVEPRLADEIY 319
Cdd:cd19090 211 RWLSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-318 |
2.91e-74 |
|
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: 230.90 E-value: 2.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLS 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSYYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGRLLRPVPTgtvpdysyvdplsfdaDYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLgvythgaaKNAVHQKQFLD 160
Cdd:cd19163 81 TKVGRYGLDPDK----------------MFDFSAERITKSVEESLKRLGLDYIDIIQVHDI--------EFAPSLDQILN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SGVKALEELKSSGAISAFGLGVNEVPVCLDVMRHS--DLDCILLAGRYTLLDRSaVAELLPLCRQKGTSLVVGGVFNSGI 238
Cdd:cd19163 137 ETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSpvKIDTVLSYCHYTLNDTS-LLELLPFFKEKGVGVINASPLSMGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 239 LATGPVPGSHfdymPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIV-EPRLADE 317
Cdd:cd19163 216 LTERGPPDWH----PASPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAeEPLDAHL 291
|
.
gi 517055799 318 I 318
Cdd:cd19163 292 L 292
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-323 |
7.95e-45 |
|
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: 154.78 E-value: 7.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 16 ISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDG--SYVLSTKVGRLLRPVPtg 93
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKrdKVVIATKVPDGDGPWP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 94 tvpdysyvdplsfdadYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHgaaknavhqkqfLDSGVKALEELKSSG 173
Cdd:pfam00248 79 ----------------SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTP------------IEETWDALEELKKEG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 174 AISAFGLGVNEVPVCLDVMRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILATGPVPGSHFDYMP 253
Cdd:pfam00248 131 KIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGE 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517055799 254 ADDDV-------LAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVEPRLADEIYAEFE 323
Cdd:pfam00248 211 RRRLLkkgtplnLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARID 287
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
11-323 |
1.24e-42 |
|
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: 149.21 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAALGGL-YRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFL---RDQpdgsYVLSTKVGrl 86
Cdd:cd19084 2 LKVSRIGLGTWAIGGTwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALkgrRDD----VVIATKCG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 87 LRPVPTGTVPdysyvdplsfdadYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHgaaknavhqkqfLDSGVKAL 166
Cdd:cd19084 76 LRWDGGKGVT-------------KDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTP------------IEETAEAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 167 EELKSSGAISAFGL---GVNEVpvcLDVMRHSDLDCILlaGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILaTGP 243
Cdd:cd19084 131 EKLKKEGKIRYIGVsnfSVEQL---EEARKYGPIVSLQ--PPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLL-TGK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 244 V-PGSHFdymPADDD--------------VLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNME 308
Cdd:cd19084 205 YkKEPTF---PPDDRrsrfpffrgenfekNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAG 281
|
330
....*....|....*
gi 517055799 309 IVEPRLADEIYAEFE 323
Cdd:cd19084 282 ALDWELTEEELKEID 296
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-306 |
9.32e-41 |
|
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: 142.62 E-value: 9.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAALGG-LYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFL---RDQPdgsyVLSTKVGRL 86
Cdd:cd19086 1 LEVSEIGFGTWGLGGdWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALkgrRDKV----VIATKFGNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 87 LRPVPtgtvpdysyvdplsfDADYDYSYDGIMRSVEFSYARLGLNRIDILYVhdlgvytHGAAKNAVHQKQFLDsgvkAL 166
Cdd:cd19086 77 FDGGP---------------ERPQDFSPEYIREAVEASLKRLGTDYIDLYQL-------HNPPDEVLDNDELFE----AL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 167 EELKSSGAISAFGLGVNEVPVCLDVMRHSDLDCILLAgrYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILAtgpvpg 246
Cdd:cd19086 131 EKLKQEGKIRAYGVSVGDPEEALAALRRGGIDVVQVI--YNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLT------ 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 247 shfdympadddvlakvGAMeaiakshgvplAAPALQFPLREAIVASVLIGTAKPSSLTRN 306
Cdd:cd19086 203 ----------------GKL-----------AQAALRFILSHPAVSTVIPGARSPEQVEEN 235
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-308 |
1.64e-39 |
|
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: 140.06 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 14 TEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYglGLAERRVGDFLRDQPDGSYVLSTKVGrllrpvptg 93
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDDLFIATKVG--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 94 tvpdYSYVDPLSFdadYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVythgAAKNAVHqkqfldsgVKALEELKSSG 173
Cdd:cd19095 70 ----THGEGGRDR---KDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSD----DELTGEV--------LETLEDLKAAG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 174 AISAfgLGVN-EVPVCLDVMRHSDLDCILLAgrYTLLDRSAvAELLPLCRQKGTslvvggvfnsGILATGPVPGSHFDYM 252
Cdd:cd19095 131 KVRY--IGVSgDGEELEAAIASGVFDVVQLP--YNVLDREE-EELLPLAAEAGL----------GVIVNRPLANGRLRRR 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 517055799 253 PADDDVLAKVGAMEAIAKSHGVPLAAP-ALQFPLREAIVASVLIGTAKPSSLTRNME 308
Cdd:cd19095 196 VRRRPLYADYARRPEFAAEIGGATWAQaALRFVLSHPGVSSAIVGTTNPEHLEENLA 252
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-303 |
2.20e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 138.94 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 2 KKRRIGKTKLEVTEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVlST 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGGLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYI-TT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 82 KVGrlLRPVPTGTVpdysyvdplsfdadydysYDGIMRSVEFSYARLGLNRIDILYVHD-LGVYTHGAAKNAVHQKQFLD 160
Cdd:cd19104 80 KVR--LDPDDLGDI------------------GGQIERSVEKSLKRLKRDSVDLLQLHNrIGDERDKPVGGTLSTTDVLG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SG--VKALEELKSSGAISAFGL-GVNEVPVCLDVMRHSDLDCILLAgrYTLLDRSAVA------------ELLPLCRQKG 225
Cdd:cd19104 140 LGgvADAFERLRSEGKIRFIGItGLGNPPAIRELLDSGKFDAVQVY--YNLLNPSAAEarprgwsaqdygGIIDAAAEHG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 226 TSLVVGGVFNSGILATG---PVPGSHFDYMPADDDvLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSS 302
Cdd:cd19104 218 VGVMGIRVLAAGALTTSldrGREAPPTSDSDVAID-FRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREE 296
|
.
gi 517055799 303 L 303
Cdd:cd19104 297 L 297
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
4-324 |
1.02e-36 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 134.14 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 4 RRIGKTKLEVTEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQ--PDGSYVLST 81
Cdd:PLN02587 2 RELGSTGLKVSSVGFGASPLGSVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALgiPREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 82 KVGRllrpvptgtvpdysYVDplsfdaDYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLgvythgaakNAVHQKQFLDS 161
Cdd:PLN02587 82 KCGR--------------YGE------GFDFSAERVTKSVDESLARLQLDYVDILHCHDI---------EFGSLDQIVNE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 162 GVKALEELKSSGA---ISAFGLGVNEVPVCLDVMRHSDLDCILLAGRYTLLDrSAVAELLPLCRQKGTSLVVGGVFNSGI 238
Cdd:PLN02587 133 TIPALQKLKESGKvrfIGITGLPLAIFTYVLDRVPPGTVDVILSYCHYSLND-SSLEDLLPYLKSKGVGVISASPLAMGL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 239 LATGPVPGSHfdymPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEI--------V 310
Cdd:PLN02587 212 LTENGPPEWH----PAPPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAateletsgI 287
|
330
....*....|....
gi 517055799 311 EPRLADEIYAEFEP 324
Cdd:PLN02587 288 DEELLSEVEAILAP 301
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-318 |
1.93e-33 |
|
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: 125.01 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAA--LGGLyracPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKVGRllr 88
Cdd:cd19074 2 LKVSELSLGTWLtfGGQV----DDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKVFW--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 89 pvPTGTVPDysyvdplsfdaDYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHgaaknavhqkqfLDSGVKALEE 168
Cdd:cd19074 75 --PTGPGPN-----------DRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETP------------LEETVRAMDD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 169 LKSSGAIsaFGLGVNEVPVCLdVMRHSDL-DCILLAG------RYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILAT 241
Cdd:cd19074 130 LIRQGKI--LYWGTSEWSAEQ-IAEAHDLaRQFGLIPpvveqpQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 242 ----GPVPGSH-------FDYMPAD---DDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNM 307
Cdd:cd19074 207 kyrdGIPPPSRsratdedNRDKKRRlltDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENV 286
|
330
....*....|.
gi 517055799 308 EIVEPRLADEI 318
Cdd:cd19074 287 KASGVKLSPEV 297
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-317 |
2.84e-33 |
|
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: 125.08 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 3 KRRIGKTKLEVTEISFGAAALGG--LYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDgSYVLS 80
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGgpWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRD-KVVLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGrlLRPVPTGTvpdYSYVDPLSFDADYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHgaaknavhqkqfLD 160
Cdd:cd19149 80 TKCG--LRWDREGG---SFFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETP------------IE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SGVKALEELKSSGAISAFGLGVNEVPVCLDVMRHSDLDCIllAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILa 240
Cdd:cd19149 143 ETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLDII--QEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 241 TGPV-PGSHFDYMPADDD-----------VLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNME 308
Cdd:cd19149 220 TGKItPDREFDAGDARSGipwfspenrekVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAK 299
|
....*....
gi 517055799 309 IVEPRLADE 317
Cdd:cd19149 300 AGDIRLSAE 308
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-321 |
5.24e-32 |
|
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: 121.15 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 13 VTEISFGAAALGGLYRACP--REQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGsYVLSTKVGrllrpv 90
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGDqdDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDD-VVIATKVS------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 91 ptgtvPDYSYvdplsfdadydysYDGIMRSVEFSYARLGLNRIDILYVHdlgvythgAAKNAVHQKQFLdsgvKALEELK 170
Cdd:cd19085 74 -----PDNLT-------------PEDVRKSCERSLKRLGTDYIDLYQIH--------WPSSDVPLEETM----EALEKLK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 171 SSGAISAFGL---GVNEVPvclDVMRHSDLDCILLAgrYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILaTGPVpgS 247
Cdd:cd19085 124 EEGKIRAIGVsnfGPAQLE---EALDAGRIDSNQLP--YNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLL-TGKF--S 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 248 HFDYMPADDD---------------VLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVEP 312
Cdd:cd19085 196 SAEDFPPGDArtrlfrhfepgaeeeTFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL 275
|
....*....
gi 517055799 313 RLADEIYAE 321
Cdd:cd19085 276 ELSPSVLER 284
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-311 |
3.86e-30 |
|
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: 114.99 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGGlyracpreQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLS 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPR--------ESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGrlLRPVPTgtvpdysyvdplsfdadydySYDGIMRSVEFSYARLGLNRIDILYVHDLgvythgaakNAVHQKQFLD 160
Cdd:cd19105 73 TKAS--PRLDKK--------------------DKAELLKSVEESLKRLQTDYIDIYQLHGV---------DTPEERLLNE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SGVKALEELKSSGAISAFGLGV--NEVPVCLDVMRHSDLDCILLAgrYTLLDRSAVA-ELLPLCRQKGTSLVVGGVFNSG 237
Cdd:cd19105 122 ELLEALEKLKKEGKVRFIGFSThdNMAEVLQAAIESGWFDVIMVA--YNFLNQPAELeEALAAAAEKGIGVVAMKTLAGG 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517055799 238 ILAtgpvpgshfdympadddvlakvGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGtakpsslTRNMEIVE 311
Cdd:cd19105 200 YLQ----------------------PALLSVLKAKGFSLPQAALKWVLSNPRVDTVVPG-------MRNFAELE 244
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-308 |
3.34e-29 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 112.19 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 3 KRRIGKTKLEVTEISFGAAALGGLyracPREQAMDTLQAAWDSGIRYFDVAPWYglGLAERRVGDFLRDqPDGSYVLSTK 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRL----SQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG-RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 83 VGrllrpvptgtvpdysyvdplsfdadyDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGvythgaAKNAVHQKQFLDSG 162
Cdd:cd19100 74 TG--------------------------ARDYEGAKRDLERSLKRLGTDYIDLYQLHAVD------TEEDLDQVFGPGGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 163 VKALEELKSSGAISAFGLGVNEVPVCLDVMRHSDLDCIL----LAGRYTlldRSAVAELLPLCRQKGTslvvggvfnsGI 238
Cdd:cd19100 122 LEALLEAKEEGKIRFIGISGHSPEVLLRALETGEFDVVLfpinPAGDHI---DSFREELLPLAREKGV----------GV 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517055799 239 LatgpvpgshfdympadddvlakvgAMEAIAKSH----GVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNME 308
Cdd:cd19100 189 I------------------------AMKVLAGGRllsgDPLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
3-320 |
1.10e-28 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 112.51 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 3 KRRIGKTKLEVTEISFGAAALGG--LYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLS 80
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGGhnLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGrlLRPVPTGTVpdysyvdplsFDADYDYsydgIMRSVEFSYARLGLNRIDILYVHdlgvythgaaknAVHQKQFLD 160
Cdd:cd19083 81 TKGA--HKFGGDGSV----------LNNSPEF----LRSAVEKSLKRLNTDYIDLYYIH------------FPDGETPKA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SGVKALEELKSSGAISAFGLGvnevPVCLDVMRHSDLDCIL--LAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGI 238
Cdd:cd19083 133 EAVGALQELKDEGKIRAIGVS----NFSLEQLKEANKDGYVdvLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 239 LATGPVPGSHFDympaDDDV---------------LAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSL 303
Cdd:cd19083 209 LAGKYTKDTKFP----DNDLrndkplfkgerfsenLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQV 284
|
330
....*....|....*..
gi 517055799 304 TRNMEIVEPRLADEIYA 320
Cdd:cd19083 285 IDNLKALDVTLTEEEIA 301
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-311 |
6.68e-28 |
|
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: 110.32 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 4 RRIGKTKLEVTEISFGAAALGGLYRACPRE-QAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLR--DQPDGSYVLS 80
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYGDGLEQdEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAalQVPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGRLLrpvptgtvpdysyvdplsfDADYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLgvythgaakNAVHQKQFLD 160
Cdd:cd19153 83 TKVGRYR-------------------DSEFDYSAERVRASVATSLERLHTTYLDVVYLHDI---------EFVDYDTLVD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SGVKALEELKSSGAISAFGLGVNEVPVCLDVMRHSD---LDCILLAGRYTLLDrSAVAELLPLCRQKGTSlvvgGVFNSG 237
Cdd:cd19153 135 EALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSpgsLDAVLSYCHLTLQD-ARLESDAPGLVRGAGP----HVINAS 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517055799 238 ILATGPV-PGSHFDYMPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLRE-AIVASVLIGTAKPSSLTRNMEIVE 311
Cdd:cd19153 210 PLSMGLLtSQGPPPWHPASGELRHYAAAADAVCASVEASLPDLALQYSLAAhAGVGTVLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-324 |
1.67e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 109.30 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 13 VTEISFGAAALGGLYRACPR-----EQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVlSTKVGrll 87
Cdd:cd19102 1 LTTIGLGTWAIGGGGWGGGWgpqddRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIV-ATKCG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 88 rPVPTGTVPDYSYVDPlsfdadydysyDGIMRSVEFSYARLGLNRIDILYVH----DLGvythgaaknavhqkqfLDSGV 163
Cdd:cd19102 77 -LLWDEEGRIRRSLKP-----------ASIRAECEASLRRLGVDVIDLYQIHwpdpDEP----------------IEEAW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 164 KALEELKSSGAISAFGLG---VNEVPVCLDVmRHSDLdcilLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILa 240
Cdd:cd19102 129 GALAELKEEGKVRAIGVSnfsVDQMKRCQAI-HPIAS----LQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLL- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 241 TGPVPGSHFDYMPADDD--------------VLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRN 306
Cdd:cd19102 203 TGKMTPERVASLPADDWrrrspffqepnlarNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDET 282
|
330
....*....|....*...
gi 517055799 307 MEIVEPRLADEIYAEFEP 324
Cdd:cd19102 283 VGAADLRLTPEELAEIEA 300
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
9-308 |
1.14e-26 |
|
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: 106.98 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 9 TKLEVTEISFGAAALGGLYRACPREQA-MDTLQAAWDSGIRYFDVAPWYG-----LGLAERRVGD-FLRDqpdgSYVLST 81
Cdd:cd19164 9 SLAGLPPLIFGAATFSYQYTTDPESIPpVDIVRRALELGIRAFDTSPYYGpseiiLGRALKALRDeFPRD----TYFIIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 82 KVGRllrpvptgtvpdYSYvdplsfdADYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLgvythgaakNAVHQKQFLDs 161
Cdd:cd19164 85 KVGR------------YGP-------DDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDV---------EFVADEEVLE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 162 GVKALEELKSSGAISAFGLGVNEVPVCLDVMRHSD------LDCILLAGRYTlLDRSAVAELLPLCRQKGTSLVV--GGV 233
Cdd:cd19164 136 ALKELFKLKDEGKIRNVGISGYPLPVLLRLAELARttagrpLDAVLSYCHYT-LQNTTLLAYIPKFLAAAGVKVVlnASP 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517055799 234 FNSGILATGPVPGSHfdymPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAI-VASVLIGTAKPSSLTRNME 308
Cdd:cd19164 215 LSMGLLRSQGPPEWH----PASPELRAAAAKAAEYCQAKGTDLADVALRYALREWGgEGPTVVGCSNVDELEEAVE 286
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
5-317 |
4.56e-26 |
|
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: 105.74 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 5 RIGKTKLEVTEISFGAAALGGLYRAC---PREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRD-QPDGSYVLS 80
Cdd:cd19079 4 RLGNSGLKVSRLCLGCMSFGDPKWRPwvlDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEfAPRDEVVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGRLLRPVPTGTVpdysyvdpLSFDAdydysydgIMRSVEFSYARLGLNRIDILYVH--DLGV---YTHGAAKNAVhq 155
Cdd:cd19079 84 TKVYFPMGDGPNGRG--------LSRKH--------IMAEVDASLKRLGTDYIDLYQIHrwDYETpieETLEALHDVV-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 156 kqflDSG-VKALeelkssGAISAFGLGVNEVpvcLDVMRHSDLD-CILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGV 233
Cdd:cd19079 146 ----KSGkVRYI------GASSMYAWQFAKA---LHLAEKNGWTkFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 234 FNSGILATGPVPGS------------HFDYM-PADDDVLAKVgamEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKP 300
Cdd:cd19079 213 LARGRLARPWGDTTerrrsttdtaklKYDYFtEADKEIVDRV---EEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKL 289
|
330
....*....|....*..
gi 517055799 301 SSLTRNMEIVEPRLADE 317
Cdd:cd19079 290 EHLEDAVAALDIKLSEE 306
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-321 |
7.52e-26 |
|
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: 104.96 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGGLyraCPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDgSYVLS 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGR---TDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRD-DIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVGrllrpVPTGTVPDYSYVdplsfdadydySYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHgaaknavhqkqfLD 160
Cdd:cd19087 77 TKVF-----GPMGDDPNDRGL-----------SRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTP------------LE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 SGVKALEELKSSGAISAFG------------LGVNEvpvcldvmRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSL 228
Cdd:cd19087 129 ETLRALDDLVRQGKIRYIGvsnfaawqiakaQGIAA--------RRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 229 VV-----GGVFnSGILATGPVPGSHF-----DYM--PADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIG 296
Cdd:cd19087 201 IPysplaGGLL-TGKYGKGKRPESGRlveraRYQarYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIG 279
|
330 340
....*....|....*....|....*
gi 517055799 297 TAKPSSLTRNMEIVEPRLADEIYAE 321
Cdd:cd19087 280 PRTLEQLEDSLAALEITLTPELLAE 304
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
4-311 |
8.48e-26 |
|
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: 104.65 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 4 RRIGKTKLEVTEISFGAAALGGLYRacPREQAMDTLQAAWDSGIRYFDVAPWYGL--GLAERRVGDFLRdQPDGSY---- 77
Cdd:cd19089 2 RRCGRSGLHLPAISLGLWHNFGDYT--SPEEARELLRTAFDLGITHFDLANNYGPppGSAEENFGRILK-RDLRPYrdel 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 78 VLSTKVGRLLRPVPTGtvpDYSyvdplsfdadydySYDGIMRSVEFSYARLGLNRIDILYVH------DLGVyTHGAAKN 151
Cdd:cd19089 79 VISTKAGYGMWPGPYG---DGG-------------SRKYLLASLDQSLKRMGLDYVDIFYHHrydpdtPLEE-TMTALAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 152 AVHQKQFLDSGV-----KALEELkssgaisafglgvnevpvcLDVMRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGT 226
Cdd:cd19089 142 AVRSGKALYVGIsnypgAKARRA-------------------IALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 227 SLVVGGVFNSGILAT----GPVPGS-----HFDYMPA--DDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLI 295
Cdd:cd19089 203 GFIAFSPLAQGLLTDkylnGIPPDSrraaeSKFLTEEalTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLI 282
|
330
....*....|....*.
gi 517055799 296 GTAKPSSLTRNMEIVE 311
Cdd:cd19089 283 GASSPSQLEDNVAALK 298
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-317 |
1.14e-24 |
|
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: 101.92 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGG------LYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPD 74
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGgggffgAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 75 gSYVLSTKVGrllrpVPTGTVPDysyvdplsfdaDYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHgaaknavh 154
Cdd:cd19091 81 -DVLIATKVR-----GRMGEGPN-----------DVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTP-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 155 qkqfLDSGVKALEELKSSGAISAFG------------LGVNEvpvcldvmRHSDLDCILLAGRYTLLDRSAVAELLPLCR 222
Cdd:cd19091 136 ----LEETLRALDDLVRQGKVRYIGvsnfsawqimkaLGISE--------RRGLARFVALQAYYSLLGRDLEHELMPLAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 223 QKGTSLVV-----GGVFNSGILATGPVP------GSHFDYMPADDD-VLAKVGAMEAIAKSHGVPLAAPALQFPLREAIV 290
Cdd:cd19091 204 DQGVGLLVwsplaGGLLSGKYRRGQPAPegsrlrRTGFDFPPVDRErGYDVVDALREIAKETGATPAQVALAWLLSRPTV 283
|
330 340
....*....|....*....|....*..
gi 517055799 291 ASVLIGTAKPSSLTRNMEIVEPRLADE 317
Cdd:cd19091 284 SSVIIGARNEEQLEDNLGAAGLSLTPE 310
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-238 |
3.25e-24 |
|
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: 98.74 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 14 TEISFGAAALGGLYracPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPD-GSYVLSTKVGrllrpvpt 92
Cdd:cd06660 1 SRLGLGTMTFGGDG---DEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNrDDVVIATKGG-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 93 gtvpdysyVDPLSFDADYDYSYDGIMRSVEFSYARLGLNRIDILYVH--DLGVYthgaaknavhqkqfLDSGVKALEELK 170
Cdd:cd06660 70 --------HPPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHrdDPSTP--------------VEETLEALNELV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517055799 171 SSGAISAFGL---GVNEVPVCLDV-MRHSDLDCILLAGRYTLLDRSAV-AELLPLCRQKGTSLVVGGVFNSGI 238
Cdd:cd06660 128 REGKIRYIGVsnwSAERLAEALAYaKAHGLPGFAAVQPQYSLLDRSPMeEELLDWAEENGLPLLAYSPLARGP 200
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-323 |
1.59e-21 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 93.73 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGaaalGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYglGLAERRVGDFLRdQPDGSYVLS 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFG----GMRLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALK-GPRDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 81 TKVgrllrPVPTGTvpdysyvdplsfdadydysYDGIMRSVEFSYARLGLNRIDILYVHdlGVYTHGAAKNAVHQKQFLD 160
Cdd:COG1453 74 TKL-----PPWVRD-------------------PEDMRKDLEESLKRLQTDYIDLYLIH--GLNTEEDLEKVLKPGGALE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 sgvkALEELKSSGAISAFGLGV-NEVPVCLDVMRHSDLDCILLagRYTLLDR--SAVAELLPLCRQKGTslvvggvfnsG 237
Cdd:COG1453 128 ----ALEKAKAEGKIRHIGFSThGSLEVIKEAIDTGDFDFVQL--QYNYLDQdnQAGEEALEAAAEKGI----------G 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 238 ILATGPVPGSHFDYMPADDDVLAKVGAMeaiakshgvPLAApALQFPL-REAiVASVLIGTAKPSSLTRNMEIVEP--RL 314
Cdd:COG1453 192 VIIMKPLKGGRLANPPEKLVELLCPPLS---------PAEW-ALRFLLsHPE-VTTVLSGMSTPEQLDENLKTADNlePL 260
|
....*....
gi 517055799 315 ADEIYAEFE 323
Cdd:COG1453 261 TEEELAILE 269
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
7-317 |
3.66e-20 |
|
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: 89.20 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 7 GKTKLEVTEISFGAAALGGLY-RACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDgSYVLSTKVGR 85
Cdd:cd19080 4 GRSGLRVSPLALGTMTFGTEWgWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRD-RIVLATKYTM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 86 LLRPVptgtvpdysyvDPlsfdadydySYDG-----IMRSVEFSYARLGLNRIDILYVHDLGVYThgaaknAVHQKqfld 160
Cdd:cd19080 83 NRRPG-----------DP---------NAGGnhrknLRRSVEASLRRLQTDYIDLLYVHAWDFTT------PVEEV---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 161 sgVKALEELKSSGAIsaFGLGVNEVPV-----CLDVMRHSDLD-CILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVF 234
Cdd:cd19080 133 --MRALDDLVRAGKV--LYVGISDTPAwvvarANTLAELRGWSpFVALQIEYSLLERTPERELLPMARALGLGVTPWSPL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 235 NSGIL----------ATGPVPGSHFDYMPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLT 304
Cdd:cd19080 209 GGGLLtgkyqrgeegRAGEAKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLK 288
|
330
....*....|...
gi 517055799 305 RNMEIVEPRLADE 317
Cdd:cd19080 289 DNLGALDLTLSPE 301
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-281 |
4.42e-19 |
|
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: 85.74 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 12 EVTEISFGAAA----LGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGS-YVLSTKVGrl 86
Cdd:cd19093 1 EVSPLGLGTWQwgdrLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRDeVVIATKFA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 87 lrPVPtgtvpdysyvdplsfdadYDYSYDGIMRSVEFSYARLGLNRIDILYVHdlGVYTHGAAKNAVhqkqfldsgVKAL 166
Cdd:cd19093 79 --PLP------------------WRLTRRSVVKALKASLERLGLDSIDLYQLH--WPGPWYSQIEAL---------MDGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 167 EELKSSGAISAFGL---GVNEVPVCLDVMRHSDLDCILLAGRYTLLDRSAVA-ELLPLCRQKGTSLV---------VGGV 233
Cdd:cd19093 128 ADAVEEGLVRAVGVsnySADQLRRAHKALKERGVPLASNQVEYSLLYRDPEQnGLLPACDELGITLIaysplaqglLTGK 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 517055799 234 FNSGILATGPVPGSHFDYMPADDDVLakVGAMEAIAKSHGVPLAAPAL 281
Cdd:cd19093 208 YSPENPPPGGRRRLFGRKNLEKVQPL--LDALEEIAEKYGKTPAQVAL 253
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-311 |
1.59e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 83.73 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 15 EISFGAAALGGLY------RACPREQAMDTLQAAWDSGIRYFDVAPWYglGLAERRVGDFLRDQPDGSYVlsTKVGRLlr 88
Cdd:cd19097 2 KLALGTAQFGLDYgianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLDKFKII--TKLPPL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 89 pvptgtvpdysyvdplsfDADYDYSYDGIMRSVEFSYARLGLNRIDILYVHDlgvythgAAKNAVHQKQFLDsgvkALEE 168
Cdd:cd19097 76 ------------------KEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHN-------PDDLLKHGGKLVE----ALLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 169 LKSSGAISAFGLGVNEVPVCLDVMRHSDLDCILLAgrYTLLDRSAVAE-LLPLCRQKGTSLVVGGVFNSGILATGP--VP 245
Cdd:cd19097 127 LKKEGLIRKIGVSVYSPEELEKALESFKIDIIQLP--FNILDQRFLKSgLLAKLKKKGIEIHARSVFLQGLLLMEPdkLP 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517055799 246 GSHFDYMPadddvlaKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVE 311
Cdd:cd19097 205 AKFAPAKP-------LLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-323 |
3.55e-18 |
|
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: 83.80 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGGlyRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQ--PDGSYV 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFG--NQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELgwPRSDYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 79 LSTKV-GRLLRPVPTGTvpdysyvdPLSfdadYDYSYDGIMRSVEfsyaRLGLNRIDILYVH--DlgvyTHGAAKNAVHQ 155
Cdd:cd19143 79 VSTKIfWGGGGPPPNDR--------GLS----RKHIVEGTKASLK----RLQLDYVDLVFCHrpD----PATPIEETVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 156 KQFL-DSGvKAL---------EELKSSGAIsAFGLG----VNEVPvcldvmrhsdldcillagRYTLLDRSAV-AELLPL 220
Cdd:cd19143 139 MNDLiDQG-KAFywgtsewsaQQIEEAHEI-ADRLGlippVMEQP------------------QYNLFHRERVeVEYAPL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 221 CRQKGTSLVVGGVFNSGILaTG------PvPGSHF----------DYMPADDDVLAKVGAMEAIAKSHGVPLAAPALQFP 284
Cdd:cd19143 199 YEKYGLGTTTWSPLASGLL-TGkynngiP-EGSRLalpgyewlkdRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWC 276
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 517055799 285 LREAIVASVLIGTAKPSSLTRNMEIVE--PRLADEIYAEFE 323
Cdd:cd19143 277 LKNPNVSTVITGATKVEQLEENLKALEvlPKLTPEVMEKIE 317
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-308 |
5.38e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 83.14 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAaLGGLYRAcPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSY------VLSTKVG 84
Cdd:cd19099 1 LTLSSLGLGTY-RGDSDDE-TDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELIEKGGikrdevVIVTKAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 85 -------RLLRP--------VPTGTVPDYSYVDPLSFDADYdysydgIMRSVEFSYARLGLNRIDILYVHDLGVYTHGAA 149
Cdd:cd19099 79 yipgdgdEPLRPlkyleeklGRGLIDVADSAGLRHCISPAY------LEDQIERSLKRLGLDTIDLYLLHNPEEQLLELG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 150 KNAVHQKqfLDSGVKALEELKSSGAISAFGLGVNEVPVCL-DVMRHSDLDCILLAGR---------------YTLLDRSA 213
Cdd:cd19099 153 EEEFYDR--LEEAFEALEEAVAEGKIRYYGISTWDGFRAPpALPGHLSLEKLVAAAEevggdnhhfkviqlpLNLLEPEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 214 VAE----------LLPLCRQKGTSLVVGGVFNSGILAtGPVPGSHFDYMPadddvlakvgameaiaksHGVPLAAPALQF 283
Cdd:cd19099 231 LTEkntvkgealsLLEAAKELGLGVIASRPLNQGQLL-GELRLADLLALP------------------GGATLAQRALQF 291
|
330 340
....*....|....*....|....*
gi 517055799 284 PLREAIVASVLIGTAKPSSLTRNME 308
Cdd:cd19099 292 ARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-307 |
8.70e-17 |
|
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: 78.80 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 13 VTEISFGAAALGGLYRACP---REQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVlSTKVGrLLRP 89
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPpadREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVI-ATKGG-LVRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 90 VPTGTVPDYSyvdplsfdADYdysydgIMRSVEFSYARLGLNRIDILYVH--DLGVythgaaknavhqkQFLDSgVKALE 167
Cdd:cd19088 79 GPGWWGPDGS--------PEY------LRQAVEASLRRLGLDRIDLYQLHriDPKV-------------PFEEQ-LGALA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 168 ELKSSGAISAfgLGVNEVPVCL--DVMRHSDLDCIllAGRYTLLDRSAvAELLPLCRQKGTslvvggvfnsGILATGPVp 245
Cdd:cd19088 131 ELQDEGLIRH--IGLSNVTVAQieEARAIVRIVSV--QNRYNLANRDD-EGVLDYCEAAGI----------AFIPWFPL- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517055799 246 gshfdympADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNM 307
Cdd:cd19088 195 --------GGGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENL 248
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-300 |
1.13e-16 |
|
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: 78.75 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 8 KTKLEVTEISFGAAALGGLYRacPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPD--GSYVLSTKVGR 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGE--SAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGlrEKIEIQTKCGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 86 LLRPVPTGTVPDYsyvdplsfdadYDYSYDGIMRSVEFSYARLGLNRIDILYVH--DLgvythgaaknavhqkqFLDSG- 162
Cdd:cd19092 79 RLGDDPRPGRIKH-----------YDTSKEHILASVEGSLKRLGTDYLDLLLLHrpDP----------------LMDPEe 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 163 -VKALEELKSSGAISAFGLGvNEVPVCLDvmrhsdldciLLAGRytlLDRSAVA---ELLPLCrqkgTSLVVGGVF---- 234
Cdd:cd19092 132 vAEAFDELVKSGKVRYFGVS-NFTPSQIE----------LLQSY---LDQPLVTnqiELSLLH----TEAIDDGTLdycq 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517055799 235 --NSGILATGPVPGSHFdYMPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKP 300
Cdd:cd19092 194 llDITPMAWSPLGGGRL-FGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNP 260
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-317 |
1.15e-16 |
|
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: 79.18 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 5 RIGKTKLEVTEISFGAAALGglyRACPREQAMDTLQAAWDSGIRYFDVAPWYGL-------GLAERRVGDFLRDQPD-GS 76
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFG---WTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRGKrDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 77 YVLSTKVGRLLRPVPTGTVPDYsyvdplsfdadydysydgIMRSVEFSYARLGLNRIDILYVHdlgvythgAAKNAVHQK 156
Cdd:cd19081 78 VVIATKVGFPMGPNGPGLSRKH------------------IRRAVEASLRRLQTDYIDLYQAH--------WDDPATPLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 157 QFLdsgvKALEELKSSGAISAFGLG------VNEVpvcLDVMR-HSDLDCILLAGRYTLLDRSAV-AELLPLCRQKG--- 225
Cdd:cd19081 132 ETL----GALNDLIRQGKVRYIGASnysawrLQEA---LELSRqHGLPRYVSLQPEYNLVDRESFeGELLPLCREEGigv 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 226 ---TSLVVG---GVFNSGILATGPVPGSHFDYMPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAK 299
Cdd:cd19081 205 ipySPLAGGfltGKYRSEADLPGSTRRGEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGART 284
|
330
....*....|....*...
gi 517055799 300 PSSLTRNMEIVEPRLADE 317
Cdd:cd19081 285 VEQLEDLLAAAGLRLTDE 302
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-323 |
1.25e-16 |
|
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: 78.42 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 10 KLEVTEISFGAAALGGLYRACPR--EQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKVGrll 87
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSddKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTKVS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 88 rpvptgtvPDYsyvdplsfdadydYSYDGIMRSVEFSYARLGLNRIDILYVHdlgvythgAAKNAVHQKQFLdsgvKALE 167
Cdd:cd19072 78 --------PDH-------------LKYDDVIKAAKESLKRLGTDYIDLYLIH--------WPNPSIPIEETL----RAME 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 168 ELKSSGAISAFGLG---VNEVPVCLDVMRHSDLDCILLagRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILATGPV 244
Cdd:cd19072 125 ELVEEGKIRYIGVSnfsLEELEEAQSYLKKGPIVANQV--EYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517055799 245 PGShfdympadddvlakvgaMEAIAKSHGVPLAAPALQFPLREAIVAsVLIGTAKPSSLTRNMEIVEPRLADEIYAEFE 323
Cdd:cd19072 203 SPL-----------------LDEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-313 |
1.31e-16 |
|
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: 78.98 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 2 KKRRIGKTKLEVTEISFGA-AALGGLYRAcprEQAMDTLQAAWDSGIRYFDVAPWYG--LGLAERRVGDFLRDQPDG--- 75
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLwHNFGDVDRY---ENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEDLKPyrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 76 SYVLSTKVGRLLRPVPTGtvpDYSyvdplsfdadydySYDGIMRSVEFSYARLGLNRIDILYVH----DLGVY-THGAAK 150
Cdd:cd19151 78 ELIISTKAGYTMWPGPYG---DWG-------------SKKYLIASLDQSLKRMGLDYVDIFYHHrpdpETPLEeTMGALD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 151 NAVHQKQFLDSGVKALEELKSSGAIsafglgvnevpvclDVMRHSDLDCILLAGRYTLLDRSAVAELLPLCRQKGtslvV 230
Cdd:cd19151 142 QIVRQGKALYVGISNYPPEEAREAA--------------AILKDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEG----I 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 231 GGVFNSGiLATGPVPGSHFDYMPAD----------------DDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVL 294
Cdd:cd19151 204 GCIAFSP-LAQGLLTDRYLNGIPEDsraakgssflkpeqitEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVL 282
|
330
....*....|....*....
gi 517055799 295 IGTAKPSSLTRNMEIVEPR 313
Cdd:cd19151 283 IGASKPSQIEDAVGALDNR 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-321 |
1.47e-16 |
|
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: 79.15 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 13 VTEISFGAAALGGlyrACPREQAMDTLQAAWDSGIRYFDVAPWYGL-------GLAERRVGDFLRDQPD-GSYVLSTKV- 83
Cdd:cd19094 1 VSEICLGTMTWGE---QNTEAEAHEQLDYAFDEGVNFIDTAEMYPVppspetqGRTEEIIGSWLKKKGNrDKVVLATKVa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 84 -GRLLRPVPTGTVPDYSYvdplsfdadydysyDGIMRSVEFSYARLGLNRIDILYVH--DLGVYTHGAAKNAVHQKQ--- 157
Cdd:cd19094 78 gPGEGITWPRGGGTRLDR--------------ENIREAVEGSLKRLGTDYIDLYQLHwpDRYTPLFGGGYYTEPSEEeds 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 158 --FLDSgVKALEELKSSGAISAFGLGvNEVPVclDVMRHSDLDCILLAGR-------YTLLDRSAVAELLPLCRQKGTSL 228
Cdd:cd19094 144 vsFEEQ-LEALGELVKAGKIRHIGLS-NETPW--GVMKFLELAEQLGLPRivsiqnpYSLLNRNFEEGLAEACHRENVGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 229 VV-----GGVFnSGILATGPV--PGSHFD----YMP--ADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLI 295
Cdd:cd19094 220 LAysplaGGVL-TGKYLDGAArpEGGRLNlfpgYMAryRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTII 298
|
330 340
....*....|....*....|....*.
gi 517055799 296 GTAKPSSLTRNMEIVEPRLADEIYAE 321
Cdd:cd19094 299 GATTLEQLKENIDAFDVPLSDELLAE 324
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
11-317 |
6.78e-16 |
|
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: 76.96 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAALGG-LYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRD-QPDGSYVLSTKVGrlLR 88
Cdd:cd19148 2 LPVSRIALGTWAIGGwMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEyGKRDRVVIATKVG--LE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 89 PVPTGTVPDYSyvdplsfdadydySYDGIMRSVEFSYARLGLNRIDILYVH--DLGVYTHGAAKnavhqkqfldsgvkAL 166
Cdd:cd19148 80 WDEGGEVVRNS-------------SPARIRKEVEDSLRRLQTDYIDLYQVHwpDPLVPIEETAE--------------AL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 167 EELKSSGAISAFGLGvNEVPVCLDVMRH-SDLDCILLagRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILATGPVP 245
Cdd:cd19148 133 KELLDEGKIRAIGVS-NFSPEQMETFRKvAPLHTVQP--PYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 246 GSHFdymPADD--------------DVLAKVGAMEAIAKSH-GVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIV 310
Cdd:cd19148 210 DTKF---EGDDlrrtdpkfqeprfsQYLAAVEELDKLAQERyGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVF 286
|
....*..
gi 517055799 311 EPRLADE 317
Cdd:cd19148 287 GWSLNDE 293
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
11-323 |
7.84e-16 |
|
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: 76.89 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAALGGLYRACP-REQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFL---RDQpdgsYVLSTKVGrl 86
Cdd:cd19078 2 LEVSAIGLGCMGMSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALkpfRDQ----VVIATKFG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 87 LRPVPTGTVPDYSyvdplsfdadyDYSYDGIMRSVEFSYARLGLNRIDILYVH--DLGVYTHGAAknavhqkqfldsgvK 164
Cdd:cd19078 76 FKIDGGKPGPLGL-----------DSRPEHIRKAVEGSLKRLQTDYIDLYYQHrvDPNVPIEEVA--------------G 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 165 ALEELKSSGAISAFGLgvNEVPVclDVMRHSDLDCILLA--GRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILaTG 242
Cdd:cd19078 131 TMKELIKEGKIRHWGL--SEAGV--ETIRRAHAVCPVTAvqSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFL-TG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 243 PV-PGSHFDympADDDV--------------LAKVGAMEAIAKSHGVPLAAPALQFPLREA--IVAsvLIGTAKPSSLTR 305
Cdd:cd19078 206 KIdENTKFD---EGDDRaslprftpealeanQALVDLLKEFAEEKGATPAQIALAWLLAKKpwIVP--IPGTTKLSRLEE 280
|
330
....*....|....*...
gi 517055799 306 NMEIVEPRLADEIYAEFE 323
Cdd:cd19078 281 NIGAADIELTPEELREIE 298
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-281 |
2.06e-15 |
|
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: 75.72 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 2 KKRRIGKTKLEVTEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDgSYVLST 81
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRD-EVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 82 KVGRLLRPVPTGTVPDYSyvdplsfdADYdysydgIMRSVEFSYARLGLNRIDILYVHdlgvythgaaknAVHQKQFLDS 161
Cdd:cd19076 80 KFGIVRDPGSGFRGVDGR--------PEY------VRAACEASLKRLGTDVIDLYYQH------------RVDPNVPIEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 162 GVKALEELKSSGAISAFGLgvNEvpVCLDVMR--HSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGIL 239
Cdd:cd19076 134 TVGAMAELVEEGKVRYIGL--SE--ASADTIRraHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 517055799 240 aTGPVpgSHFDYMPADD----------DVLAK----VGAMEAIAKSHGVPLAAPAL 281
Cdd:cd19076 210 -TGAI--KSPEDLPEDDfrrnnprfqgENFDKnlklVEKLEAIAAEKGCTPAQLAL 262
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
4-307 |
3.50e-14 |
|
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: 72.10 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 4 RRIGKTKLEVTEISFGA-AALGGlyrACPREQAMDTLQAAWDSGIRYFDVAPWYG--LGLAERRVGDFLRDQPDG---SY 77
Cdd:cd19150 3 RRCGKSGLKLPALSLGLwHNFGD---DTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDFAGyrdEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 78 VLSTKVGRLLRPVPTGTVPDYSYVdplsfdadydysydgiMRSVEFSYARLGLNRIDILYVHDLGVYT-----HGAAKNA 152
Cdd:cd19150 80 IISTKAGYDMWPGPYGEWGSRKYL----------------LASLDQSLKRMGLDYVDIFYSHRFDPDTpleetMGALDHA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 153 VHQKQFLDSGVKALEELKSSGAIsafglgvnevpvclDVMRHSDLDCILLAGRYTLLDR-SAVAELLPLCRQKGTSLVVg 231
Cdd:cd19150 144 VRSGKALYVGISSYSPERTREAA--------------AILRELGTPLLIHQPSYNMLNRwVEESGLLDTLQELGVGCIA- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 232 gvFNSgiLATGPVPGSHFDYMPAD---------------DDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIG 296
Cdd:cd19150 209 --FTP--LAQGLLTDKYLNGIPEGsraskerslspkmltEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIG 284
|
330
....*....|.
gi 517055799 297 TAKPSSLTRNM 307
Cdd:cd19150 285 ASRPEQLEENV 295
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-323 |
5.95e-14 |
|
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: 71.43 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 15 EISFGAAALGGLYRACPREQA---MDTLQAAwdsGIRYFDVAPWYGLGLAERRVGDFLRDQPDgsYVLSTKVgrllRPVP 91
Cdd:cd19075 2 KIILGTMTFGSQGRFTTAEAAaelLDAFLER---GHTEIDTARVYPDGTSEELLGELGLGERG--FKIDTKA----NPGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 92 TGtvpdysyvdplsfdadyDYSYDGIMRSVEFSYARLGLNRIDILYVHdlgvythgAAKNAVHqkqfLDSGVKALEELKS 171
Cdd:cd19075 73 GG-----------------GLSPENVRKQLETSLKRLKVDKVDVFYLH--------APDRSTP----LEETLAAIDELYK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 172 SGAISAFGLGvN----EVPVCLDVMRHSDLdcILLA---GRYTLLDRSAVAELLPLCRQKGTSLVV-----GGVFnSGIL 239
Cdd:cd19075 124 EGKFKEFGLS-NysawEVAEIVEICKENGW--VLPTvyqGMYNAITRQVETELFPCLRKLGIRFYAysplaGGFL-TGKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 240 ATG--PVPGSHFD------------YM-PADDDVLAKVgamEAIAKSHGVPLAAPALQF-----PLREAIVASVLIGTAK 299
Cdd:cd19075 200 KYSedKAGGGRFDpnnalgklyrdrYWkPSYFEALEKV---EEAAEKEGISLAEAALRWlyhhsALDGEKGDGVILGASS 276
|
330 340
....*....|....*....|....*
gi 517055799 300 PSSLTRNMEIVE-PRLADEIYAEFE 323
Cdd:cd19075 277 LEQLEENLAALEkGPLPEEVVKAID 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-308 |
1.09e-13 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 71.17 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGaaalggLYRACPREQAMDT----LQAAWDSGIRYFDVAPWYG--LGLAERRVGDFLRDQ-- 72
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLG------LWHNFGHVNALESqraiLRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 73 -PDGSYVLSTKVGRLLRPVPTGTVPDYSYvdplsfdadydysydgIMRSVEFSYARLGLNRIDILYVHdlgvythgaakn 151
Cdd:PRK09912 87 aYRDELIISTKAGYDMWPGPYGSGGSRKY----------------LLASLDQSLKRMGLEYVDIFYSH------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 152 AVHQKQFLDSGVKALEELKSSG-----AISAFGLGVNEVPVclDVMRHSDLDCILLAGRYTLLDRSA-VAELLPLCRQKG 225
Cdd:PRK09912 139 RVDENTPMEETASALAHAVQSGkalyvGISSYSPERTQKMV--ELLREWKIPLLIHQPSYNLLNRWVdKSGLLDTLQNNG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 226 TSLVvggVFNSgiLATGPVPGSHFDYMPADDDV-------------------LAKVGAMEAIAKSHGVPLAAPALQFPLR 286
Cdd:PRK09912 217 VGCI---AFTP--LAQGLLTGKYLNGIPQDSRMhregnkvrgltpkmlteanLNSLRLLNEMAQQRGQSMAQMALSWLLK 291
|
330 340
....*....|....*....|..
gi 517055799 287 EAIVASVLIGTAKPSSLTRNME 308
Cdd:PRK09912 292 DERVTSVLIGASRAEQLEENVQ 313
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
31-311 |
1.49e-13 |
|
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: 69.51 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 31 PREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKvgrllrpVPTGTVPdysyvdplsfdady 110
Cdd:cd19096 19 DEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATK-------LPPWSVK-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 111 dySYDGIMRSVEFSYARLGLNRIDILYVHDLGvythgaakNAVHQKQFLDSG-VKALEELKSSGAISAFGLGVN-EVPVC 188
Cdd:cd19096 78 --SAEDFRRILEESLKRLGVDYIDFYLLHGLN--------SPEWLEKARKGGlLEFLEKAKKEGLIRHIGFSFHdSPELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 189 LDVMRHSDLDCILLAgrYTLLDRSAVA--ELLPLCRQKGTslvvggvfnsGILATGPVPGSHFDYMPadddvlakvGAME 266
Cdd:cd19096 148 KEILDSYDFDFVQLQ--YNYLDQENQAgrPGIEYAAKKGM----------GVIIMEPLKGGGLANNP---------PEAL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 517055799 267 AIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVE 311
Cdd:cd19096 207 AILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-321 |
6.22e-13 |
|
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: 68.23 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 3 KRRIGKTKLEVTEISFGAAALGGLYRAC-PREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLST 81
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGDYGAPkPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 82 KVGrllrpvptgtvpdYSYVDP--LSFDADYDYsydgIMRSVEFSYARLGLNRIDILYVHdlgvythgaaknAVHQKQFL 159
Cdd:cd19145 82 KFG-------------IHEIGGsgVEVRGDPAY----VRAACEASLKRLDVDYIDLYYQH------------RIDTTVPI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 160 DSGVKALEELKSSGAISAFGLGvnevPVCLDVMR--HSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSG 237
Cdd:cd19145 133 EITMGELKKLVEEGKIKYIGLS----EASADTIRraHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 238 ILATGPVpgshFDYMPADDDVLAKVG---------------AMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSS 302
Cdd:cd19145 209 FFAGKAK----LEELLENSDVRKSHPrfqgenleknkvlyeRVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKN 284
|
330
....*....|....*....
gi 517055799 303 LTRNMEIVEPRLADEIYAE 321
Cdd:cd19145 285 LNQNIGALSVKLTKEDLKE 303
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-317 |
1.52e-12 |
|
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: 67.23 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 32 REQAMDTLQAAWDSGIRYFDVAPWYGLglAERRVGDFLRDQPDGSYVLS-----TKVgrllrpvptgtVPDYSYVDPlsf 106
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRRERDAADdvqihTKW-----------VPDPGELTM--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 107 dadyDYSYdgIMRSVEFSYARLGLNRIDILYVH--DLGVythgaaknavhqKQFLDsGVKALEELKSSGAIsafglgvNE 184
Cdd:cd19101 86 ----TRAY--VEAAIDRSLKRLGVDRLDLVQFHwwDYSD------------PGYLD-AAKHLAELQEEGKI-------RH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 185 VPVC-LDVMRhsdLDCILLAG--------RYTLLDRSAVAELLPLCRQKGTSLVVGGVFNSGILA---------TGPVPG 246
Cdd:cd19101 140 LGLTnFDTER---LREILDAGvpivsnqvQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSekylgvpepTGPALE 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517055799 247 --SHFDYMPADDD------VLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVEPRLADE 317
Cdd:cd19101 217 trSLQKYKLMIDEwggwdlFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDE 295
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-330 |
3.08e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 66.80 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGglyracprEQ-----AMDTLQAAWDSGIRYFDVAPWYGL-------GLAERRVGDF 68
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFG--------EQnseadAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 69 LRDQPD-GSYVLSTKVGRLLRPVPTGTVPDYSYvdplsfdadydySYDGIMRSVEFSYARLGLNRIDILYVH-------- 139
Cdd:PRK10625 73 LAKRGSrEKLIIASKVSGPSRNNDKGIRPNQAL------------DRKNIREALHDSLKRLQTDYLDLYQVHwpqrptnc 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 140 --DLGvYTHGAAKNAVHQKQFLDsgvkALEELKSSGAISAFGLGvNEVPvcLDVMRH------SDLDCIL-LAGRYTLLD 210
Cdd:PRK10625 141 fgKLG-YSWTDSAPAVSLLETLD----ALAEQQRAGKIRYIGVS-NETA--FGVMRYlhlaekHDLPRIVtIQNPYSLLN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 211 RSAVAELLPLCRQKGTSLVVGGVFNSGILA----TGPVPG-------SHFDYMPADDDVLAkVGAMEAIAKSHGVPLAAP 279
Cdd:PRK10625 213 RSFEVGLAEVSQYEGVELLAYSCLAFGTLTgkylNGAKPAgarntlfSRFTRYSGEQTQKA-VAAYVDIAKRHGLDPAQM 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 517055799 280 ALQFPLREAIVASVLIGTAKPSSLTRNMEIVEPRLADEIYAEFEP----YTLVAP 330
Cdd:PRK10625 292 ALAFVRRQPFVASTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAvhqvYTYPAP 346
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
11-323 |
8.43e-12 |
|
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: 65.14 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAALG----GLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFL-----RDQpdgsYVLST 81
Cdd:cd19146 9 VRVSPLCLGAMSFGeawkSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMasrgnRDE----MVLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 82 KVGrllrpvpTGtvpdYSYVDPLSFDADYDYSYDGIMR-SVEFSYARLGLNRIDILYVH--DlgvYTHGaaknavhqkqf 158
Cdd:cd19146 85 KYT-------TG----YRRGGPIKIKSNYQGNHAKSLRlSVEASLKKLQTSYIDILYVHwwD---YTTS----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 159 LDSGVKALEELKSSGAIsaFGLGVNEVPV-----CLDVMR-HSDLDCILLAGRYTLLDRSAVAELLPLCRQKGTSLVVGG 232
Cdd:cd19146 140 IPELMQSLNHLVAAGKV--LYLGVSDTPAwvvskANAYARaHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 233 VFNSGILATGP----VPGSHFDYMPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNME 308
Cdd:cd19146 218 VLGQGQFRTEEefkrRGRSGRKGGPQTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIE 297
|
330
....*....|....*
gi 517055799 309 IVEPRLADEIYAEFE 323
Cdd:cd19146 298 ALGISLSDEEIQEIE 312
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-331 |
8.87e-12 |
|
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: 65.06 E-value: 8.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 32 REQAMDTLQAAWDSGIRYFDVAPWYglGLAERRVGDFL--RDQPDGSYVLSTKVGrllrpvptgtvpdYSYVDPLSFDAD 109
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLrsRNIAPDAVFVGSKWG-------------YTYTADWQVDAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 110 Y----DYSYDGIMRSVEFSYARLGlnridilyvHDLGVY-THGAAknavhqkqfLDSGV-------KALEELKSSGAisA 177
Cdd:cd19098 99 VhevkDHSLARLLKQWEETRSLLG---------KHLDLYqIHSAT---------LESGVledadvlAALAELKAEGV--K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 178 FGLGVNEvPVCLDVMR---------HSDLDCIllAGRYTLLDRSAvAELLPLCRQKGTSLVVGGVFNSGILATGpvpgsh 248
Cdd:cd19098 159 IGLSLSG-PQQAETLRraleieidgARLFDSV--QATWNLLEQSA-GEALEEAHEAGMGVIVKEALANGRLTDR------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 249 fdymPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIGTAKPSSLTRNMEIVEPRLADEIYAEFEpyTLV 328
Cdd:cd19098 229 ----NPSPELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALA--DLA 302
|
...
gi 517055799 329 APP 331
Cdd:cd19098 303 EPP 305
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
29-293 |
1.67e-11 |
|
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: 63.81 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 29 ACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLStKVgrllrpVPTGTvpdysyvdplsfda 108
Cdd:cd19138 25 PAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVS-KV------LPSNA-------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 109 dydySYDGIMRSVEFSYARLGLNRIDILYVHDLGvythgaaknAVHqkqfLDSGVKALEELKSSGAISAFGLGvNevpvc 188
Cdd:cd19138 84 ----SRQGTVRACERSLRRLGTDYLDLYLLHWRG---------GVP----LAETVAAMEELKKEGKIRAWGVS-N----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 189 LDVMRHSDLDCILLAG-------RYTLLDRSAVAELLPLCRQKGTSLVVggvfnSGILATGPVPGSHfdympadddvLAK 261
Cdd:cd19138 141 FDTDDMEELWAVPGGGncaanqvLYNLGSRGIEYDLLPWCREHGVPVMA-----YSPLAQGGLLRRG----------LLE 205
|
250 260 270
....*....|....*....|....*....|..
gi 517055799 262 VGAMEAIAKSHGVPLAAPALQFPLREAIVASV 293
Cdd:cd19138 206 NPTLKEIAARHGATPAQVALAWVLRDGNVIAI 237
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-334 |
2.72e-11 |
|
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: 63.62 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGGLY-RACPREQAMDTLQAAWDSGIRYFDVAPWYGLglAERRVGDFLRDQPD--GSY 77
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSAFYgPPKPDEERFAVLDAAFELGCTFWDTADIYGD--SEELIGRWFKQNPGkrEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 78 VLSTKVGrLLRPVPTGTvpdysyvdpLSFDADYDYsydgIMRSVEFSYARLGLNRIDILYVHdlgvythgaaknAVHQKQ 157
Cdd:cd19144 79 FLATKFG-IEKNVETGE---------YSVDGSPEY----VKKACETSLKRLGVDYIDLYYQH------------RVDGKT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 158 FLDSGVKALEELKSSGAISAFGLgvNEV------------PVCLDVMRHSDldcillagrYTLLDRSAVAELLPLCRQKG 225
Cdd:cd19144 133 PIEKTVAAMAELVQEGKIKHIGL--SECsaetlrrahavhPIAAVQIEYSP---------FSLDIERPEIGVLDTCRELG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 226 TSLVVGGVFNSGILaTGPVPgSHFDYMPAD-------------DDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVAS 292
Cdd:cd19144 202 VAIVAYSPLGRGFL-TGAIR-SPDDFEEGDfrrmaprfqaenfPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDII 279
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517055799 293 VLIGTAKPSSLTRNMEIVEPRLADEIYAEFEPYTLVAPPLGA 334
Cdd:cd19144 280 PIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEVVGE 321
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-317 |
3.42e-10 |
|
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: 59.89 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 12 EVTEISFGAAALGG-LYRACPR-EQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKVgrllrp 89
Cdd:cd19137 3 KIPALGLGTWGIGGfLTPDYSRdEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTKV------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 90 VPTgtvpdysyvdplsfdadyDYSYDGIMRSVEFSYARLGLNRIDILYVHdlgvythgaaknAVHQKQFLDSGVKALEEL 169
Cdd:cd19137 77 WPT------------------NLRYDDLLRSLQNSLRRLDTDYIDLYLIH------------WPNPNIPLEETLSAMAEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 170 KSSGAISAFGLGVNEVPVCLDVMRHSDLDCILLAGRYTLLDRSAVAE-LLPLCRQKGTSLVVggvfnsgilatgpvpgsh 248
Cdd:cd19137 127 VRQGLIRYIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEDRDPERDgLLEYCQKNGITVVA------------------ 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517055799 249 fdYMPADDDVLAKVGAMEAIAKSHGVPLAAPALQFPLREAIVASVLIgTAKPSSLTRNMEIVEPRLADE 317
Cdd:cd19137 189 --YSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEIKLSEE 254
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-141 |
6.76e-10 |
|
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: 59.40 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAaaLGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQ--PDGSYV 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGT--WSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKgwKRSSYI 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517055799 79 LSTKVGRLLRPVPTGtvpdysyvdplsfdadydYSYDGIMRSVEFSYARLGLNRIDILYVHDL 141
Cdd:cd19142 79 VSTKIYWSYGSEERG------------------LSRKHIIESVRASLRRLQLDYIDIVIIHKA 123
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-321 |
7.15e-10 |
|
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: 59.17 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 11 LEVTEISFGAAALGGLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAE---RRVGDFLRDQPD--GSYVLSTKVGr 85
Cdd:cd19077 3 KLVGPIGLGLMGLTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHanlKLLARFFRKYPEyaDKVVLSVKGG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 86 llrpvptgtvpdysyVDPLsfDADYDYSYDGIMRSVEFSYARLG-LNRIDILyvhdlgvythGAAKnaVHQKQFLDSGVK 164
Cdd:cd19077 82 ---------------LDPD--TLRPDGSPEAVRKSIENILRALGgTKKIDIF----------EPAR--VDPNVPIEETIK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 165 ALEELKSSGAISafGLGVNEV-------------PVCLDVMrhsdldcillagrYTLLDRSAV-AELLPLCRQKGTSLVV 230
Cdd:cd19077 133 ALKELVKEGKIR--GIGLSEVsaetirrahavhpIAAVEVE-------------YSLFSREIEeNGVLETCAELGIPIIA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 231 GGVFNSGILaTG------PVPGSHFDYMPA--DDDVLAK----VGAMEAIAKSHGVPLAAPALQFPLR---EAIVAsvLI 295
Cdd:cd19077 198 YSPLGRGLL-TGrikslaDIPEGDFRRHLDrfNGENFEKnlklVDALQELAEKKGCTPAQLALAWILAqsgPKIIP--IP 274
|
330 340
....*....|....*....|....*.
gi 517055799 296 GTAKPSSLTRNMEIVEPRLADEIYAE 321
Cdd:cd19077 275 GSTTLERVEENLKAANVELTDEELKE 300
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
16-179 |
3.20e-09 |
|
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: 57.18 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 16 ISFGAAALGGLYracPREQAMDTLQAAWDSGIRYFDVAP----WYGLGLAERRVGDFL-----RDQpdgsYVLSTKVGrl 86
Cdd:cd19082 3 IVLGTADFGTRI---DEEEAFALLDAFVELGGNFIDTARvygdWVERGASERVIGEWLksrgnRDK----VVIATKGG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 87 lrpVPTGTVPDYSYVDPLSFDADydysydgimrsVEFSYARLGLNRIDILYVH--DLGVythgaaknAVhqkqflDSGVK 164
Cdd:cd19082 74 ---HPDLEDMSRSRLSPEDIRAD-----------LEESLERLGTDYIDLYFLHrdDPSV--------PV------GEIVD 125
|
170
....*....|....*
gi 517055799 165 ALEELKSSGAISAFG 179
Cdd:cd19082 126 TLNELVRAGKIRAFG 140
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
22-317 |
4.84e-09 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 56.22 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 22 ALG-GLYRAcPREQAMDTLQAAWDSGIRYFDVAPWYGlglAERRVGDFLRDQ--PDGSYVLSTKVgrllrpvptgtvpdy 98
Cdd:COG0656 7 ALGlGTWQL-PGEEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAASgvPREELFVTTKV--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 99 sYVDplsfdadyDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGVYTHGAAknavhqkqfldsgVKALEELKSSGAISAF 178
Cdd:COG0656 68 -WND--------NHGYDDTLAAFEESLERLGLDYLDLYLIHWPGPGPYVET-------------WRALEELYEEGLIRAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 179 GlgvnevpVClDVMRHsDLDCILLAGRYTLldrsAV-----------AELLPLCRQKgtslvvggvfnsGILATGpvpgs 247
Cdd:COG0656 126 G-------VS-NFDPE-HLEELLAETGVKP----AVnqvelhpylqqRELLAFCREH------------GIVVEA----- 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517055799 248 hfdYMP------ADDDVLAkvgameAIAKSHGVPLAAPALQFPLREAIVasVLIGTAKPSSLTRNMEIVEPRLADE 317
Cdd:COG0656 176 ---YSPlgrgklLDDPVLA------EIAEKHGKTPAQVVLRWHLQRGVV--VIPKSVTPERIRENLDAFDFELSDE 240
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-301 |
2.73e-08 |
|
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: 54.26 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 40 QAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQPDGSYVLSTKVgrllrpVPTGTvpdYSYVDPLSfdadydysydgimR 119
Cdd:cd19103 39 DKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIISTKF------TPQIA---GQSADPVA-------------D 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 120 SVEFSYARLGLNRIDILYVHDlgvyTHGAAKNAVHQKQFLDSG-VK-------ALEELKSSGAI-SAFGLGVNEvpvcld 190
Cdd:cd19103 97 MLEGSLARLGTDYIDIYWIHN----PADVERWTPELIPLLKSGkVKhvgvsnhNLAEIKRANEIlAKAGVSLSA------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 191 VMRHsdldcillagrYTLLDRSAV-AELLPLCRQKGTSLVVGGVFNSGILA-----TGPVP-GSHF--DYMPADDDVLAK 261
Cdd:cd19103 167 VQNH-----------YSLLYRSSEeAGILDYCKENGITFFAYMVLEQGALSgkydtKHPLPeGSGRaeTYNPLLPQLEEL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 517055799 262 VGAMEAIAKSHGVPLAAPALQFplreAIVASVL--IGTAKPS 301
Cdd:cd19103 236 TAVMAEIGAKHGASIAQVAIAW----AIAKGTTpiIGVTKPH 273
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
33-317 |
5.89e-08 |
|
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: 53.03 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 33 EQAMDTLQAAWDSGIRYFDVAPWYGlglAERRVGDFLRDQ--PDGSYVLSTKVGrllrpvptgtvPDysyvdplsfdady 110
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASgvPRDELFLTTKVW-----------PD------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 111 DYSYDGIMRSVEFSYARLGLNRIDILYVHdlgvythgaaknAVHQKQFLDSGVKALEELKSSGAISAFGLGVNEVPVCLD 190
Cdd:cd19140 74 NYSPDDFLASVEESLRKLRTDYVDLLLLH------------WPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 191 VMRHSDLDciLLAGR---YTLLDRSAVaelLPLCRQKGTSLVVggvfnSGILATGPVPgshfdympaDDDVLAKvgamea 267
Cdd:cd19140 142 AVELSEAP--LFTNQveyHPYLDQRKL---LDAAREHGIALTA-----YSPLARGEVL---------KDPVLQE------ 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 517055799 268 IAKSHGVPLAAPALQFPLREAIVAsVLIGTAKPSSLTRNMEIVEPRLADE 317
Cdd:cd19140 197 IGRKHGKTPAQVALRWLLQQEGVA-AIPKATNPERLEENLDIFDFTLSDE 245
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-323 |
3.63e-07 |
|
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: 51.24 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGA-AALGGlyrACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQ--PDGSY 77
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGG---QITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 78 VLSTKV---GRLlrpvptgtvpdysyvdplsfDADYDYSYDGIMRSVEFSYARLGLNRIDILYVhdlgvythgaakNAVH 154
Cdd:cd19158 78 VITTKIfwgGKA--------------------ETERGLSRKHIIEGLKASLERLQLEYVDVVFA------------NRPD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 155 QKQFLDSGVKALEELKSSGAISAFGL---GVNEVPVCLDVMRHSDL-DCILLAGRYTLLDRSAVAELLP-LCRQKGTSL- 228
Cdd:cd19158 126 PNTPMEETVRAMTHVINQGMAMYWGTsrwSSMEIMEAYSVARQFNLiPPICEQAEYHMFQREKVEVQLPeLFHKIGVGAm 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 229 --------VVGGVFNSGILATGPVPGSHFDYMpaDDDVL--------AKVGAMEAIAKSHGVPLAAPALQFPLREAIVAS 292
Cdd:cd19158 206 twsplacgIVSGKYDSGIPPYSRASLKGYQWL--KDKILseegrrqqAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSS 283
|
330 340 350
....*....|....*....|....*....|...
gi 517055799 293 VLIGTAKPSSLTRNMEIVE--PRLADEIYAEFE 323
Cdd:cd19158 284 VLLGASNAEQLMENIGAIQvlPKLSSSIVHEID 316
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-318 |
6.29e-07 |
|
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: 50.37 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGAAALGGlyRACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQP--DGSYV 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFG--SQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwrRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 79 LSTKV---GRLlrpvptgtvpdysyvdplsfDADYDYSYDGIMRSVEFSYARLGLNRIDILYVhdlgvythgaakNAVHQ 155
Cdd:cd19160 81 VTTKIywgGQA--------------------ETERGLSRKHIIEGLRGSLDRLQLEYVDIVFA------------NRSDP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 156 KQFLDSGVKALEELKSSGAISAFGL---GVNEVPVCLDVMRHSDL-DCILLAGRYTLLDRSAVAELLPLCRQKgtsLVVG 231
Cdd:cd19160 129 NSPMEEIVRAMTYVINQGMAMYWGTsrwSAMEIMEAYSVARQFNLiPPVCEQAEYHLFQREKVEMQLPELYHK---IGVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 232 GVFNSGiLATGPVPGSHFDYMPAD------------DDVL--------AKVGAMEAIAKSHGVPLAAPALQFPLREAIVA 291
Cdd:cd19160 206 SVTWSP-LACGLITGKYDGRVPDTcraavkgyqwlkEKVQseegkkqqAKVKELHPIADRLGCTVAQLAIAWCLRSEGVS 284
|
330 340 350
....*....|....*....|....*....|...
gi 517055799 292 SVLIGTAKPSSLTRNMEIVE------PRLADEI 318
Cdd:cd19160 285 SVLLGVSSAEQLIENLGSIQvlsqltPQTVMEI 317
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-323 |
3.36e-06 |
|
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: 48.11 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 1 MKKRRIGKTKLEVTEISFGA-AALGGLYRACPREQAMDTlqaAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQP--DGSY 77
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTI---AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 78 VLSTKV---GRLlrpvptgtvpdysyvdplsfDADYDYSYDGIMRSVEFSYARLGLNRIDILYVhdlgvythgaakNAVH 154
Cdd:cd19159 78 VITTKLywgGKA--------------------ETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA------------NRPD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 155 QKQFLDSGVKALEELKSSGAISAFGLG---VNEVPVCLDVMRHSDL-DCILLAGRYTLLDRSAVAELLPLCRQKgtslvV 230
Cdd:cd19159 126 SNTPMEEIVRAMTHVINQGMAMYWGTSrwsAMEIMEAYSVARQFNMiPPVCEQAEYHLFQREKVEVQLPELYHK-----I 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 231 G-GVFNSGILATGPVPGSHFDYMPAD------------DDVL--------AKVGAMEAIAKSHGVPLAAPALQFPLREAI 289
Cdd:cd19159 201 GvGAMTWSPLACGIISGKYGNGVPESsraslkcyqwlkERIVseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEG 280
|
330 340 350
....*....|....*....|....*....|....*.
gi 517055799 290 VASVLIGTAKPSSLTRNMEIVE--PRLADEIYAEFE 323
Cdd:cd19159 281 VSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEID 316
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
4-83 |
1.08e-05 |
|
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: 46.67 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 4 RRIGKTKLEVTEISFGA-AALGGlyrACPREQAMDTLQAAWDSGIRYFDVAPWYGLGLAERRVGDFLRDQP--DGSYVLS 80
Cdd:cd19141 3 RNLGKSGLRVSCLGLGTwVTFGS---QISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGwrRSSYVIT 79
|
...
gi 517055799 81 TKV 83
Cdd:cd19141 80 TKI 82
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
25-179 |
2.50e-04 |
|
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: 42.23 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 25 GLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGlglAERRVGDFLRDQPDGsYVLS-------TKVGRllrpvptgtvpd 97
Cdd:cd19136 7 GTFRLRGEEEVRQAVDAALKAGYRLIDTASVYR---NEADIGKALRDLLPK-YGLSredifitSKLAP------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 98 ysyvdplsfdadYDYSYDGIMRSVEFSYARLGLNRIDILYVHDLGV--YTHGAAKNAVHQKQFLdsgvKALEELKSSGAI 175
Cdd:cd19136 71 ------------KDQGYEKARAACLGSLERLGTDYLDLYLIHWPGVqgLKPSDPRNAELRRESW----RALEDLYKEGKL 134
|
....
gi 517055799 176 SAFG 179
Cdd:cd19136 135 RAIG 138
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-139 |
7.95e-04 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 40.78 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 32 REQAMDTLQAAWDSGIRYFDVAPWYGL-------GLAERRVGDFLRDQPD-GSYVLSTKVGrllrpvptgtvpdYSYVDP 103
Cdd:cd19752 16 EETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDRGNrDDVVIATKVG-------------AGPRDP 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 517055799 104 LSFDADYD-YSYDGIMRSVEFSYARLGLNRIDILYVH 139
Cdd:cd19752 83 DGGPESPEgLSAETIEQEIDKSLRRLGTDYIDLYYAH 119
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
22-317 |
6.08e-03 |
|
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: 37.94 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 22 ALG-GLYRACPREQAMDTLQAAWDSGIRYFDVAPWYGlglAERRVGDFLRDQ--PDGSYVLSTKVGrllrpvptgtvpdy 98
Cdd:cd19133 11 ILGfGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKSgiPREELFITTKLW-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 99 syvdpLSfdadyDYSYDGIMRSVEFSYARLGLNRIDiLYVhdlgvythgaaknaVHQkQFLD--SGVKALEELKSSGAIS 176
Cdd:cd19133 74 -----IQ-----DAGYEKAKKAFERSLKRLGLDYLD-LYL--------------IHQ-PFGDvyGAWRAMEELYKEGKIR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055799 177 AFGLGvNEVPVCL-DVMRHSDLdcillagrytlldRSAV--AELLPLCRQKGTsLVVGGVFNSGILATGPVPGSHFDYMp 253
Cdd:cd19133 128 AIGVS-NFYPDRLvDLILHNEV-------------KPAVnqIETHPFNQQIEA-VEFLKKYGVQIEAWGPFAEGRNNLF- 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517055799 254 aDDDVLAKvgameaIAKSHGVPLAAPALQFPLREAIVasVLIGTAKPSSLTRNMEIVEPRLADE 317
Cdd:cd19133 192 -ENPVLTE------IAEKYGKSVAQVILRWLIQRGIV--VIPKSVRPERIAENFDIFDFELSDE 246
|
|
| |
