|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
3-309 |
0e+00 |
|
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: 556.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 3 KVTIGKTDLKVFPIGLGTNAVGGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIA 82
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGGHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 83 TKAAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQL 162
Cdd:cd19083 81 TKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 163 KEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQGEQFKENI 242
Cdd:cd19083 161 KEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRNDKPLFKGERFSENL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494649899 243 KKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKLF 309
Cdd:cd19083 241 DKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDALF 307
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-309 |
2.89e-136 |
|
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: 388.38 E-value: 2.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGTNAVGGhnLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVF 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGG--PWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 81 IATKAAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:COG0667 79 IATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 QLKEANK--DGL--VDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDlRNDQAHFQGE 236
Cdd:COG0667 159 QLRRALAiaEGLppIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGD-RAATNFVQGY 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494649899 237 QFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKLF 309
Cdd:COG0667 238 LTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAAL 310
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-306 |
1.17e-130 |
|
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: 373.40 E-value: 1.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 10 DLKVFPIGLGTNAVGGHNlYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATKAAHRK 89
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTW-WGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG-RRDDVVIATKCGLRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 90 EGDDFVF-DNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKD 168
Cdd:cd19084 79 DGGKGVTkDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 169 GLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQGEQFKENIKKVNQL 248
Cdd:cd19084 159 GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPFFRGENFEKNLEIVDKL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 249 KPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19084 239 KEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
6-307 |
1.34e-108 |
|
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: 318.06 E-value: 1.34e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTNAVGGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATK- 84
Cdd:cd19149 4 LGKSGIEASVIGLGTWAIGGGPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG-RRDKVVLATKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 --------AAHRKEGDDF-VFDN-SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGV 154
Cdd:cd19149 83 glrwdregGSFFFVRDGVtVYKNlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 155 SNFSLEQLKEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQ 234
Cdd:cd19149 163 SNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGDARSGIPWFS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494649899 235 geqfKENIKKVNQL----KPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDK 307
Cdd:cd19149 243 ----PENREKVLALlekwKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
15-307 |
1.45e-101 |
|
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: 299.50 E-value: 1.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECnREDVFIATKAAHRkegddf 94
Cdd:cd19085 3 RLGLGCWQFGGGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGR-RDDVVIATKVSPD------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 95 vfDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGLVDVI 174
Cdd:cd19085 76 --NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRIDSN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 175 QGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRND-QAHFQGEQFKENIKKVNQLKPIAE 253
Cdd:cd19085 154 QLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRlFRHFEPGAEEETFEALEKLKEIAD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 494649899 254 KHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDK 307
Cdd:cd19085 234 ELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
3-305 |
7.24e-95 |
|
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: 282.95 E-value: 7.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 3 KVTIGKTDLKVFPIGLGtnAVGGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIA 82
Cdd:cd19076 2 TRKLGTQGLEVSALGLG--CMGMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD-RRDEVVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 83 TK-AAHRKEGDDFV-FDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:cd19076 79 TKfGIVRDPGSGFRgVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 QLKEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQGEQFKE 240
Cdd:cd19076 159 TIRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNPRFQGENFDK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 241 NIKKVNQLKPIAEKHNADTAHIVLAWYLARPEiDIL-IPGAKRADQLKDNMKAASITLSAEEIAFI 305
Cdd:cd19076 239 NLKLVEKLEAIAAEKGCTPAQLALAWVLAQGD-DIVpIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-308 |
2.39e-93 |
|
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: 278.79 E-value: 2.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGG-HNLYPNLNEETGK--ELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECnREDVFIATKAAHRKEG 91
Cdd:cd19102 3 TIGLGTWAIGGgGWGGGWGPQDDRDsiAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL-RDRPIVATKCGLLWDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 92 DDFVFDN-SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGL 170
Cdd:cd19102 82 EGRIRRSlKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 171 VDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENT--TFPEGDLRNDQAHFQGEQFKENIKKVNQL 248
Cdd:cd19102 162 IASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERvaSLPADDWRRRSPFFQEPNLARNLALVDAL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 249 KPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19102 242 RPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-308 |
1.16e-91 |
|
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: 274.19 E-value: 1.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAVGGHNLYPNlnEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECN--REDVFIATKAAHRKegDD 93
Cdd:pfam00248 1 IGLGTWQLGGGWGPIS--KEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPvkRDKVVIATKVPDGD--GP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 94 FVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGLVD- 172
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPi 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 173 -VIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRndqaHFQGEQFKENIKKVNQLKPI 251
Cdd:pfam00248 157 vAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERR----RLLKKGTPLNLEALEALEEI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 494649899 252 AEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:pfam00248 233 AKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-308 |
3.54e-90 |
|
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: 270.72 E-value: 3.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 10 DLKVFPIGLGTNAVGGhNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKE-CNREDVFIATKAA-H 87
Cdd:cd19148 1 DLPVSRIALGTWAIGG-WMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEyGKRDRVVIATKVGlE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 88 RKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANK 167
Cdd:cd19148 80 WDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 168 DGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQGEQFKENIKKVNQ 247
Cdd:cd19148 160 VAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTDPKFQEPRFSQYLAAVEE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494649899 248 LKPIA-EKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19148 240 LDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-307 |
9.26e-88 |
|
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: 264.48 E-value: 9.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 10 DLKVFPIGLGTNAVGgHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATKAAHRK 89
Cdd:cd19078 1 GLEVSAIGLGCMGMS-HGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP-FRDQVVIATKFGFKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 90 EGDDFV---FDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEAN 166
Cdd:cd19078 79 DGGKPGplgLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 167 KDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQGEQFKENIKKVN 246
Cdd:cd19078 159 AVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPRFTPEALEANQALVD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494649899 247 QLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDK 307
Cdd:cd19078 239 LLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-306 |
3.52e-87 |
|
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: 263.31 E-value: 3.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTNAVGGhnlypNLNEETGKELVREAIKSGVTMLDTAYIYGV-------GRSEELIGEVLK-ECNRE 77
Cdd:cd19081 2 LGRTGLSVSPLCLGTMVFGW-----TADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKsRGKRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 78 DVFIATKAAhRKEGDDFVfDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNF 157
Cdd:cd19081 77 RVVIATKVG-FPMGPNGP-GLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 158 SLEQLKEAN----KDGL--VDVIQGEYNLLNRE-AEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQ 230
Cdd:cd19081 155 SAWRLQEALelsrQHGLprYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 231 AhfqgEQF--KENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19081 235 A----KRYlnERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-291 |
1.73e-83 |
|
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: 251.28 E-value: 1.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGGHNlypnlNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKE-CNREDVFIATKAAHRKEGDD 93
Cdd:cd06660 2 RLGLGTMTFGGDG-----DEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGrGNRDDVVIATKGGHPPGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 94 FVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEAN----KDG 169
Cdd:cd06660 77 SRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALayakAHG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 170 L--VDVIQGEYNLLNR-EAEKTFFPYTTEHGISFIPYFPLVSGLlagkydenttfpegdlrndqahfqgeqfkenikkvn 246
Cdd:cd06660 157 LpgFAAVQPQYSLLDRsPMEEELLDWAEENGLPLLAYSPLARGP------------------------------------ 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 494649899 247 qlkpiaekhnadtAHIVLAWYLARPEIDILIPGAKRADQLKDNMK 291
Cdd:cd06660 201 -------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
4-306 |
2.91e-82 |
|
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: 250.96 E-value: 2.91e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 4 VTIGKTDLKVFPIGLGTNAVGGHNLYP-NLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKE-CNREDVFI 81
Cdd:cd19079 3 VRLGNSGLKVSRLCLGCMSFGDPKWRPwVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEfAPRDEVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 82 ATKAAHRkeGDDFVFDN--SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSL 159
Cdd:cd19079 83 ATKVYFP--MGDGPNGRglSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 160 EQLKEAN----KDGLVDVI--QGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHF 233
Cdd:cd19079 161 WQFAKALhlaeKNGWTKFVsmQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAKLKY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494649899 234 QGEQfKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19079 241 DYFT-EADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-309 |
3.34e-80 |
|
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: 245.56 E-value: 3.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGTNAVGGhnlypNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECnREDVF 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGG-----RTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR-RDDIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 81 IATKAaHRKEGDDfVFDN--SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFS 158
Cdd:cd19087 75 LATKV-FGPMGDD-PNDRglSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 159 LEQLKEA-------NKDGLVdVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQA 231
Cdd:cd19087 153 AWQIAKAqgiaarrGLLRFV-SEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERAR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 232 HFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKLF 309
Cdd:cd19087 232 YQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDELF 309
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-308 |
2.76e-78 |
|
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: 240.98 E-value: 2.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGTNAVGGHNLYP----NLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNR 76
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFFgawgGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 77 EDVFIATKAAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSN 156
Cdd:cd19091 80 DDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 157 FSLEQ----LKEANKDGLVDVI--QGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDlRNDQ 230
Cdd:cd19091 160 FSAWQimkaLGISERRGLARFValQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEGS-RLRR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 231 AHFQGEQFKE----NIkkVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19091 239 TGFDFPPVDRergyDV--VDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLD 316
|
..
gi 494649899 307 KL 308
Cdd:cd19091 317 KV 318
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-292 |
3.18e-77 |
|
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: 235.45 E-value: 3.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 11 LKVFPIGLGTNAVGGhNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATKAAHRKE 90
Cdd:cd19086 1 LEVSEIGFGTWGLGG-DWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG-RRDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 91 GDDFVFDN-SPAFLKQSVEDSLKRLQTDYIDLFYIHFP-DEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKD 168
Cdd:cd19086 79 GGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 169 GLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKydenttfpegdlrndqahfqgeqfkenikkvnql 248
Cdd:cd19086 159 GGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK---------------------------------- 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 494649899 249 kpIAEkhnadTAhivLAWYLARPEIDILIPGAKRADQLKDNMKA 292
Cdd:cd19086 205 --LAQ-----AA---LRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-306 |
4.42e-77 |
|
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: 235.97 E-value: 4.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 12 KVFPIGLGTNAVGGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIATKAAHRKEG 91
Cdd:cd19072 3 EVPVLGLGTWGIGGGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTKVSPDHLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 92 DDFVfdnspaflKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEAN---KD 168
Cdd:cd19072 83 YDDV--------IKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQsylKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 169 GLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTtfpegdlrndqahfqgeqfkenikkvnqL 248
Cdd:cd19072 155 GPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL----------------------------L 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 249 KPIAEKHNADTAHIVLAWYLARPEIdILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19072 207 DEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-300 |
5.86e-77 |
|
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: 237.10 E-value: 5.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 11 LKVFPIGLGTNAVGGhnlyPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIATKAAHRke 90
Cdd:cd19074 2 LKVSELSLGTWLTFG----GQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKVFWP-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 91 GDDFVFDN--SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEA--- 165
Cdd:cd19074 76 TGPGPNDRglSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAhdl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 166 ----NKDGLVdVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQ---AHFQGEQF 238
Cdd:cd19074 156 arqfGLIPPV-VEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEdnrDKKRRLLT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494649899 239 KENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAE 300
Cdd:cd19074 235 DENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-298 |
4.22e-72 |
|
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: 223.25 E-value: 4.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 13 VFPIGLGTNAVGGHNLY-PNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATKAAH-RKE 90
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWgPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP-YPDDVVIATKGGLvRTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 91 GDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGL 170
Cdd:cd19088 80 PGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 171 VDVIQGEYNLLNREAEKTFfPYTTEHGISFIPYFPLVSGLLAgkydenttFPEGDLRNdqahfqgeqfkenikkvnqlkp 250
Cdd:cd19088 160 IVSVQNRYNLANRDDEGVL-DYCEAAGIAFIPWFPLGGGDLA--------QPGGLLAE---------------------- 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 494649899 251 IAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLS 298
Cdd:cd19088 209 VAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-306 |
8.78e-71 |
|
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: 220.95 E-value: 8.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 12 KVFPIGLGTNAVGGHNL--YPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECN-REDVFIATKAA-- 86
Cdd:cd19093 1 EVSPLGLGTWQWGDRLWwgYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGdRDEVVIATKFApl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 87 -HRKEGDDFVfdnspaflkQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAV-QALNELKKEGKIRSIGVSNFSLEQLKE 164
Cdd:cd19093 81 pWRLTRRSVV---------KALKASLERLGLDSIDLYQLHWPGPWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 165 A----NKDGL-VDVIQGEYNLLNREAEKT-FFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRndqahFQGEQF 238
Cdd:cd19093 152 AhkalKERGVpLASNQVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRR-----LFGRKN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494649899 239 KENIKKV-NQLKPIAEKHNADTAHIVLAWYLARPEIDilIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19093 227 LEKVQPLlDALEEIAEKYGKTPAQVALNWLIAKGVVP--IPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-308 |
1.64e-68 |
|
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: 216.15 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGtnAVGGHNLY-PNLNEETGKELVREAIKSGVTMLDTAYIYGvgRSEELIGEVLKEC--NRE 77
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFG--AMGLSAFYgPPKPDEERFAVLDAAFELGCTFWDTADIYG--DSEELIGRWFKQNpgKRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 78 DVFIATKAAHRK--EGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVS 155
Cdd:cd19144 77 KIFLATKFGIEKnvETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 156 NFSLEQLKEANKDGLVDVIQGEYNLLNREAEKT---FFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAH 232
Cdd:cd19144 157 ECSAETLRRAHAVHPIAAVQIEYSPFSLDIERPeigVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFRRMAPR 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 233 FQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19144 237 FQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREI 312
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-308 |
7.34e-67 |
|
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: 211.04 E-value: 7.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 10 DLKVFPIGLGTNA-----VGGHNLYPN-LNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIAT 83
Cdd:cd19103 1 DKKLPKIALGTWSwgsggAGGDQVFGNhLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 84 K----AAHRKEGDdfvfdnspafLKQSVEDSLKRLQTDYIDLFYIHFPDE---HTPKdeavqaLNELKKEGKIRSIGVSN 156
Cdd:cd19103 81 KftpqIAGQSADP----------VADMLEGSLARLGTDYIDIYWIHNPADverWTPE------LIPLLKSGKVKHVGVSN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 157 FSLEQLKEAN----KDGL-VDVIQGEYNLLNREAEKT-FFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRndQ 230
Cdd:cd19103 145 HNLAEIKRANeilaKAGVsLSAVQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSGR--A 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494649899 231 AHFQGeqFKENIKKVNQ-LKPIAEKHNADTAHIVLAWYLARPEIDILipGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19103 223 ETYNP--LLPQLEELTAvMAEIGAKHGASIAQVAIAWAIAKGTTPII--GVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
5-306 |
9.84e-67 |
|
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: 210.92 E-value: 9.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 5 TIGKTDLKVFPIGLGTNAVGgHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATK 84
Cdd:cd19080 2 LLGRSGLRVSPLALGTMTFG-TEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG-NRDRIVLATK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 -------------AAHRKEgddfvfdnspafLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRS 151
Cdd:cd19080 80 ytmnrrpgdpnagGNHRKN------------LRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 152 IGVSNFSLEQLKEAN-------KDGLVdVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTfPEG 224
Cdd:cd19080 148 VGISDTPAWVVARANtlaelrgWSPFV-ALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEE-GRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 225 DLRNDQAHFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAF 304
Cdd:cd19080 226 GEAKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLAR 305
|
..
gi 494649899 305 ID 306
Cdd:cd19080 306 LD 307
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
15-300 |
1.34e-65 |
|
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: 207.41 E-value: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGGhnLYPNLNEETGKELVREAIKSGVTMLDTAYIYGvgRSEELIGEVLKECNREDVFIATKAAHRKEGDdf 94
Cdd:cd19090 2 ALGLGTAGLGG--VFGGVDDDEAVATIRAALDLGINYIDTAPAYG--DSEERLGLALAELPREPLVLSTKVGRLPEDT-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 95 vFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDE-----AVQALNELKKEGKIRSIGVSNFSLEQLKEANKDG 169
Cdd:cd19090 76 -ADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPPDLLRRAIETG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 170 LVDVI--QGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLrndqahfqgeqFKENIKKVNQ 247
Cdd:cd19090 155 DFDVVltANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYRWL-----------SPELLDRAKR 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 494649899 248 LKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAE 300
Cdd:cd19090 224 LYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-308 |
1.72e-65 |
|
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: 208.57 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 13 VFPIGLGTNAVGGHNlypnlNEETGKELVREAIKSGVTMLDTAYIYGV-------GRSEELIGEVLK-ECNREDVFIATK 84
Cdd:cd19094 1 VSEICLGTMTWGEQN-----TEAEAHEQLDYAFDEGVNFIDTAEMYPVppspetqGRTEEIIGSWLKkKGNRDKVVLATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 AAHRKEGDDFVFDNSPAF----LKQSVEDSLKRLQTDYIDLFYIHFPDEHTPK------------------DEAVQALNE 142
Cdd:cd19094 76 VAGPGEGITWPRGGGTRLdrenIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 143 LKKEGKIRSIGVSN---FSLEQ-LKEANKDGL--VDVIQGEYNLLNReaekTFFPYTTE----HGISFIPYFPLVSGLLA 212
Cdd:cd19094 156 LVKAGKIRHIGLSNetpWGVMKfLELAEQLGLprIVSIQNPYSLLNR----NFEEGLAEachrENVGLLAYSPLAGGVLT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 213 GKYDENTTFPEG----DLRNDQAHFQGEQFKENIKKvnqLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKD 288
Cdd:cd19094 232 GKYLDGAARPEGgrlnLFPGYMARYRSPQALEAVAE---YVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKE 308
|
330 340
....*....|....*....|
gi 494649899 289 NMKAASITLSAEEIAFIDKL 308
Cdd:cd19094 309 NIDAFDVPLSDELLAEIDAV 328
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
16-308 |
5.88e-64 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 202.21 E-value: 5.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTnavgghnlYPnLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAAhrkeGDD 93
Cdd:COG0656 8 LGLGT--------WQ-LPGEEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAASGvpREELFVTTKVW----NDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 94 FVFDNspafLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKdEAVQALNELKKEGKIRSIGVSNFSLEQLKEA--NKDGLV 171
Cdd:COG0656 72 HGYDD----TLAAFEESLERLGLDYLDLYLIHWPGPGPYV-ETWRALEELYEEGLIRAIGVSNFDPEHLEELlaETGVKP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 172 DVIQGEYNLLNREAEktFFPYTTEHGISFIPYFPLVsgllagkydenttfpEGDLRNDQAhfqgeqfkenikkvnqLKPI 251
Cdd:COG0656 147 AVNQVELHPYLQQRE--LLAFCREHGIVVEAYSPLG---------------RGKLLDDPV----------------LAEI 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 252 AEKHNADTAHIVLAWYLARpeiDIL-IPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:COG0656 194 AEKHGKTPAQVVLRWHLQR---GVVvIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-308 |
5.92e-62 |
|
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: 198.55 E-value: 5.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 18 LGTNAVGGHNLYPNLneETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcnREDVFIATKAAHRKEGDdfvfd 97
Cdd:cd19075 5 LGTMTFGSQGRFTTA--EAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLG--ERGFKIDTKANPGVGGG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 98 NSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKE----ANKDGLV-- 171
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEiveiCKENGWVlp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 172 DVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKY-DENTTFPEGdlRNDQAHFQGEQF------KENIKK 244
Cdd:cd19075 156 TVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkYSEDKAGGG--RFDPNNALGKLYrdrywkPSYFEA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494649899 245 VNQLKPIAEKHNADTAHIVLAW-----YLARPEIDILIPGAKRADQLKDNMKAasIT---LSAEEIAFIDKL 308
Cdd:cd19075 234 LEKVEEAAEKEGISLAEAALRWlyhhsALDGEKGDGVILGASSLEQLEENLAA--LEkgpLPEEVVKAIDEA 303
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-292 |
1.17e-60 |
|
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: 193.61 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGGHNLYPNlnEETGKELVREAIKSGVTMLDTAYIYGvgRSEELIGEVLKECNREDVFIATKAAHRKEGDDF 94
Cdd:cd19095 2 VLGLGTSGIGRVWGVPS--EAEAARLLNTALDLGINLIDTAPAYG--RSEERLGRALAGLRRDDLFIATKVGTHGEGGRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 95 VFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEqLKEANKDGLVDVI 174
Cdd:cd19095 78 RKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEE-LEAAIASGVFDVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 175 QGEYNLLNREAEKTfFPYTTEHGIsfipyfplvsGLLAgkydeNTTFPEGDLRNDQAHFQGEQFKEnikkvNQLKPIAEK 254
Cdd:cd19095 157 QLPYNVLDREEEEL-LPLAAEAGL----------GVIV-----NRPLANGRLRRRVRRRPLYADYA-----RRPEFAAEI 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 494649899 255 HNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKA 292
Cdd:cd19095 216 GGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-293 |
6.43e-59 |
|
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: 189.33 E-value: 6.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGTNAVGGHNlypnlneetgKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVF 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRES----------PELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 81 IATKAAHRKEGDDfvfdnsPAFLKQSVEDSLKRLQTDYIDLFYIH---FPDEHTPKDEAVQALNELKKEGKIRSIGVS-- 155
Cdd:cd19105 71 LATKASPRLDKKD------KAELLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELLEALEKLKKEGKVRFIGFSth 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 156 NFSLEQLKEANKDGLVDVIQGEYNLLNREAE-KTFFPYTTEHGISFIPYFPLVSGLLAGKYDenttfpegdlrndqahfq 234
Cdd:cd19105 145 DNMAEVLQAAIESGWFDVIMVAYNFLNQPAElEEALAAAAEKGIGVVAMKTLAGGYLQPALL------------------ 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 494649899 235 geqfkenikKVNQLKPiaekhnADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAA 293
Cdd:cd19105 207 ---------SVLKAKG------FSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
3-306 |
2.76e-58 |
|
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: 188.23 E-value: 2.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 3 KVTIGkTDLKVFPIGLGTNAVGGHnlyPNLNEETgKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECnREDVFIA 82
Cdd:cd19138 2 TVTLP-DGTKVPALGQGTWYMGED---PAKRAQE-IEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGR-RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 83 TKAAHRKEGDDFVFdnspaflkQSVEDSLKRLQTDYIDLFYIHFPDEHtPKDEAVQALNELKKEGKIRSIGVSNFSLEQL 162
Cdd:cd19138 76 SKVLPSNASRQGTV--------RACERSLRRLGTDYLDLYLLHWRGGV-PLAETVAAMEELKKEGKIRAWGVSNFDTDDM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 163 KEAN---KDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPL-VSGLLAGKYDENTTfpegdlrndqahfqgeqf 238
Cdd:cd19138 147 EELWavpGGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLaQGGLLRRGLLENPT------------------ 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 239 kenikkvnqLKPIAEKHNADTAHIVLAWYLARPEIdILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19138 209 ---------LKEIAARHGATPAQVALAWVLRDGNV-IAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-305 |
3.09e-58 |
|
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: 189.18 E-value: 3.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 3 KVTIGKTDLKVFPIGLGTNAVGGHNLYPnLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIA 82
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGDYGAP-KPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 83 TK-AAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQ 161
Cdd:cd19145 81 TKfGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 162 LKEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQGEQFKEN 241
Cdd:cd19145 161 IRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKSHPRFQGENLEKN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494649899 242 IKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFI 305
Cdd:cd19145 241 KVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-303 |
6.24e-58 |
|
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: 188.14 E-value: 6.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGTNAVGGhnLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVF 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGG--VFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 81 IATKAAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPdEHTPK-----DEAVQALNELKKEGKIRSIGVS 155
Cdd:cd19163 79 LATKVGRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDI-EFAPSldqilNETLPALQKLKEEGKVRFIGIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 156 NFSLEQLKE--ANKDGLVDVIQG--EYNLLNREAeKTFFPYTTEHGISFIPYFPLVSGLL--AGKYDEnttfpegdlrnd 229
Cdd:cd19163 158 GYPLDVLKEvlERSPVKIDTVLSycHYTLNDTSL-LELLPFFKEKGVGVINASPLSMGLLteRGPPDW------------ 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494649899 230 qaHFQGEQFKENIKKVNQLkpiAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIA 303
Cdd:cd19163 225 --HPASPEIKEACAKAAAY---CKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-306 |
5.94e-57 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 184.22 E-value: 5.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNavgghnlypNLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC--NREDVFIATKAAHRkegdd 93
Cdd:cd19071 4 IGLGTY---------KLKPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESgvPREELFITTKLWPT----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 94 fvfDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFP--DEHTPKD----EAVQALNELKKEGKIRSIGVSNFSLEQLKEANK 167
Cdd:cd19071 67 ---DHGYERVREALEESLKDLGLDYLDLYLIHWPvpGKEGGSKearlETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 168 DGLV--DVIQGEYNLLNREAEktFFPYTTEHGISFIPYFPLVSGllagkydenttfPEGDLRNDqahfqgeqfkenikkv 245
Cdd:cd19071 144 AARIkpAVNQIELHPYLQQKE--LVEFCKEHGIVVQAYSPLGRG------------RRPLLDDP---------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494649899 246 nQLKPIAEKHNADTAHIVLAWYLARpeiDIL-IPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19071 194 -VLKEIAKKYGKTPAQVLLRWALQR---GVVvIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
15-294 |
4.13e-56 |
|
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: 183.14 E-value: 4.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNavgghNLYPNLNEETGKELVREAIKSGVTMLDTAYIYG----VGRSEELIGEVLKE-CNREDVFIATKAAHRK 89
Cdd:cd19082 2 RIVLGTA-----DFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLKSrGNRDKVVIATKGGHPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 90 EGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEAN--- 166
Cdd:cd19082 77 LEDMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANaya 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 167 ----KDGLVdVIQGEYNL---------------LNREAEKtffpYTTEHGISFIPYFPLVSGLLAGKYDenttfpeGDLR 227
Cdd:cd19082 157 kahgLPGFA-ASSPQWSLarpneppwpgptlvaMDEEMRA----WHEENQLPVFAYSSQARGFFSKRAA-------GGAE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494649899 228 NDQAHFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAAS 294
Cdd:cd19082 225 DDSELRRVYYSEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-306 |
1.37e-55 |
|
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: 182.44 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 11 LKVFPIGLGTNA-VGGHNLYPnlnEETGKELVREAIKSGVTMLDTAYIYGVGR---SEELIGEVLKEC--NREDVFIATK 84
Cdd:cd19077 3 KLVGPIGLGLMGlTWRPNPTP---DEEAFETMKAALDAGSNLWNGGEFYGPPDphaNLKLLARFFRKYpeYADKVVLSVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 AAhrKEGDDFVFDNSPAFLKQSVEDSLKRL-QTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLK 163
Cdd:cd19077 80 GG--LDPDTLRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 164 EANKDGLVDVIQGEYNLLNREAEKT-FFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRNDQAHFQGEQFKENI 242
Cdd:cd19077 158 RAHAVHPIAAVEVEYSLFSREIEENgVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRFNGENFEKNL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494649899 243 KKVNQLKPIAEKHNADTAHIVLAWYLARPEIDIL-IPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19077 238 KLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
7-307 |
6.52e-55 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 180.87 E-value: 6.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 7 GKTDLKVFPIGLGtNAVGGHNlypNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECN--REDVFIATK 84
Cdd:cd19143 7 GRSGLKVSALSFG-SWVTFGN---QVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGwpRSDYVVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 AAHrkeGDDFVFDN----SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:cd19143 83 IFW---GGGGPPPNdrglSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 QLKEA----NKDGLVDVI--QGEYNLLNRE-AEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENttFPEGDLRNDQ--- 230
Cdd:cd19143 160 QIEEAheiaDRLGLIPPVmeQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNG--IPEGSRLALPgye 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 231 --AHFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASI--TLSAEEIAFID 306
Cdd:cd19143 238 wlKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVlpKLTPEVMEKIE 317
|
.
gi 494649899 307 K 307
Cdd:cd19143 318 A 318
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-306 |
6.95e-55 |
|
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: 179.30 E-value: 6.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 12 KVFPIGLGTNAVGGHnLYPNLN-EETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIATKAAHrke 90
Cdd:cd19137 3 KIPALGLGTWGIGGF-LTPDYSrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTKVWP--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 91 gDDFVFDNspafLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGL 170
Cdd:cd19137 79 -TNLRYDD----LLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 171 VDVI--QGEYNLLNREAEKT-FFPYTTEHGISFIPYFPLVSGLLagkydenttfpegdlrndqahfqgeqfkeniKKVNQ 247
Cdd:cd19137 154 TPIVcnQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGLE-------------------------------KTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 494649899 248 LKPIAEKHNADTAHIVLAWYLARPEIdILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKPNV-VAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
6-303 |
7.78e-54 |
|
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: 177.83 E-value: 7.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTnavgGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYG--VGRSEELIGEVLKE---CNREDVF 80
Cdd:cd19089 4 CGRSGLHLPAISLGL----WHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGppPGSAEENFGRILKRdlrPYRDELV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 81 IATKAAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:cd19089 80 ISTKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 QLKEA----NKDGLVDVI-QGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYdenttfPEGDLRNDQAHFQG 235
Cdd:cd19089 160 KARRAiallRELGVPLIIhQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY------LNGIPPDSRRAAES 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494649899 236 EQFK------ENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAA-SITLSAEEIA 303
Cdd:cd19089 234 KFLTeealtpEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALkNLDFSEEELA 308
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-308 |
1.03e-52 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 176.55 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGtnavGGHnlYPNLNEETGKELVREAIKSGVTMLDTAYIYGvgRSEELIGEVLKECnREDVF 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFG----GMR--LPRKDEEEAEALIRRAIDNGINYIDTARGYG--DSEEFLGKALKGP-RDKVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 81 IATKAAHRKE-GDDFvfdnspaflKQSVEDSLKRLQTDYIDLFYIHFPD--EHTPK----DEAVQALNELKKEGKIRSIG 153
Cdd:COG1453 72 LATKLPPWVRdPEDM---------RKDLEESLKRLQTDYIDLYLIHGLNteEDLEKvlkpGGALEALEKAKAEGKIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 154 VSNF-SLEQLKEANKDGLVDVIQGEYNLLNRE--AEKTFFPYTTEHGISFI---PyfplvsglLAGkydenttfpeGDLR 227
Cdd:COG1453 143 FSTHgSLEVIKEAIDTGDFDFVQLQYNYLDQDnqAGEEALEAAAEKGIGVIimkP--------LKG----------GRLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 228 NDQahfqgEQFKENIKKvnqlkpiaekhNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAAS--ITLSAEEIAFI 305
Cdd:COG1453 205 NPP-----EKLVELLCP-----------PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAIL 268
|
...
gi 494649899 306 DKL 308
Cdd:COG1453 269 ERL 271
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-301 |
1.62e-52 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 174.18 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGTNAVGGhnlyPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKE--CNRED 78
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGE----WDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLspSLREK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 79 VFIATKAAHRKEGDDFV-----FDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPD---EHtpkDEAVQALNELKKEGKIR 150
Cdd:COG4989 77 IELQTKCGIRLPSEARDnrvkhYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDplmDP---EEVAEAFDELKASGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 151 SIGVSNFSLEQ---LKEANKDGLVdVIQGEYNLLNREAektFF----PYTTEHGISFIPYFPLVSGLLAGKydenttfpe 223
Cdd:COG4989 154 HFGVSNFTPSQfelLQSALDQPLV-TNQIELSLLHTDA---FDdgtlDYCQLNGITPMAWSPLAGGRLFGG--------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494649899 224 gdlrndqahfQGEQFKEnIKKVnqLKPIAEKHNADTAHIVLAWYLARPEiDIL-IPGAKRADQLKDNMKAASITLSAEE 301
Cdd:COG4989 221 ----------FDEQFPR-LRAA--LDELAEKYGVSPEAIALAWLLRHPA-GIQpVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-300 |
3.65e-52 |
|
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: 173.56 E-value: 3.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGghNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIATKA-------AH 87
Cdd:cd19152 2 KLGFGTAPLG--NLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVgrllvplQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 88 RKEGDDFVFDNSPAF----------LKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDE-----------AVQALNELKKE 146
Cdd:cd19152 80 VEPTFEPGFWNPLPFdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAEsdehfaqaikgAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 147 GKIRSIGV-SNFS---LEQLKEANKDGLvdVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGkyDENTTFP 222
Cdd:cd19152 160 GVIKAIGLgVNDWeviLRILEEADLDWV--MLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAG--GDNFDYY 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 223 EGDLRNDQAhfqgeqfkenIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAE 300
Cdd:cd19152 236 EYGPAPPEL----------IARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-306 |
2.23e-50 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 167.06 E-value: 2.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNavgghnlypNLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKE--CNREDVFIATKAAHrkegdd 93
Cdd:cd19073 4 LGLGTW---------QLRGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAEsgVPREDLFITTKVWR------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 94 fvfDN-SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDG--L 170
Cdd:cd19073 66 ---DHlRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISplP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 171 VDVIQGEYNLLNREAEktFFPYTTEHGISFIPYFPLVsgllagkydenttfpegdlrndqahfQGEQFKENIkkvnqLKP 250
Cdd:cd19073 143 IAVNQVEFHPFLYQAE--LLEYCRENDIVITAYSPLA--------------------------RGEVLRDPV-----IQE 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 251 IAEKHNADTAHIVLAWyLARPEIdILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19073 190 IAEKYDKTPAQVALRW-LVQKGI-VVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-301 |
2.92e-49 |
|
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: 165.42 E-value: 2.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 8 KTDLKVFPIGLGTNAVGGHNLYPnlneETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECN--REDVFIATKA 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESA----EELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPglREKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 86 AHRKEGDDFV-----FDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:cd19092 77 GIRLGDDPRPgrikhYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 Q---LKEANKDGLVdVIQGEYNLLNREAektFFP----YTTEHGISFIPYFPLVSGLLAGKYDENTtfpegdlrndqahf 233
Cdd:cd19092 157 QielLQSYLDQPLV-TNQIELSLLHTEA---IDDgtldYCQLLDITPMAWSPLGGGRLFGGFDERF-------------- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 234 qgeqfkENIKKVnqLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEE 301
Cdd:cd19092 219 ------QRLRAA--LEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-291 |
6.91e-49 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 163.04 E-value: 6.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 3 KVTIGKTDLKVFPIGLGTNAVGghnlypNLNEETGKELVREAIKSGVTMLDTAYIYGvgRSEELIGEVLKEcNREDVFIA 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLG------RLSQEEAAAIIRRALDLGINYFDTAPSYG--DSEEKIGKALKG-RRDKVFLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 83 TKAAHRkegddfvfdnSPAFLKQSVEDSLKRLQTDYIDLFYIHF------PDEHTPKDEAVQALNELKKEGKIRSIGVSN 156
Cdd:cd19100 72 TKTGAR----------DYEGAKRDLERSLKRLGTDYIDLYQLHAvdteedLDQVFGPGGALEALLEAKEEGKIRFIGISG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 157 FSLEQLKEANKDGLVDVIQGEYNLL---NREAEKTFFPYTTEHGIsfipyfplvsGLLAGKydentTFPEGDLRNDQahf 233
Cdd:cd19100 142 HSPEVLLRALETGEFDVVLFPINPAgdhIDSFREELLPLAREKGV----------GVIAMK-----VLAGGRLLSGD--- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 234 qgeqfkenikkvnqlkpiaekhnADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMK 291
Cdd:cd19100 204 -----------------------PLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-308 |
1.99e-48 |
|
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: 162.43 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 10 DLKVFPIGLGTnavgghnlYPnLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAAH 87
Cdd:cd19140 5 GVRIPALGLGT--------YP-LTGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASGvpRDELFLTTKVWP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 88 rkegDDFvfdnSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANK 167
Cdd:cd19140 73 ----DNY----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 168 DGLVDV--IQGEYN-LLNREAektFFPYTTEHGISFIPYFPLVSgllagkydenttfpeGDLRNDQAhfqgeqfkenikk 244
Cdd:cd19140 145 LSEAPLftNQVEYHpYLDQRK---LLDAAREHGIALTAYSPLAR---------------GEVLKDPV------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494649899 245 vnqLKPIAEKHNADTAHIVLAWYLARPEIdILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19140 194 ---LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
16-300 |
4.45e-44 |
|
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: 152.13 E-value: 4.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAVGGHnlyPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIATKA--------AH 87
Cdd:cd19162 3 LGLGAASLGNL---ARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVgrllepgaAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 88 RKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEH--TPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEA 165
Cdd:cd19162 80 RPAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHllQALTDAFPALEELRAEGVVGAIGVGVTDWAALLRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 166 NKDGLVDV--IQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAgkydenttfpeGDLRNDQAHFQGEQFKENIK 243
Cdd:cd19162 160 ARRADVDVvmVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILA-----------TDDPAGDRYDYRPATPEVLA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 494649899 244 KVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAE 300
Cdd:cd19162 229 RARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAE 285
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-306 |
1.23e-43 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 151.21 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 24 GGHNLYPNLNEetgkelVREAIK----SGVTMLDTAYIYGvgRSEELIGEVLKE-----CNREDVFIATKaahrkegddF 94
Cdd:cd19101 14 GGHGGIRDEDA------AVRAMAayvdAGLTTFDCADIYG--PAEELIGEFRKRlrrerDAADDVQIHTK---------W 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 95 VFDN-----SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPK-DEAVQALNELKKEGKIRSIGVSNFSLEQLKEAnKD 168
Cdd:cd19101 77 VPDPgeltmTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPGyLDAAKHLAELQEEGKIRHLGLTNFDTERLREI-LD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 169 GLVDVI--QGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKY---DENTTfPEGDLRNDQ------AHFQGEQ 237
Cdd:cd19101 156 AGVPIVsnQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgvPEPTG-PALETRSLQkyklmiDEWGGWD 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494649899 238 FKENIKKVnqLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19101 235 LFQELLRT--LKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-303 |
4.45e-43 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 149.86 E-value: 4.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 7 GKTDLKVFPIGLGT-NAVGGHNLYpnlneETGKELVREAIKSGVTMLDTAYIYG--VGRSEELIGEVLKE---CNREDVF 80
Cdd:cd19151 6 GRSGLKLPAISLGLwHNFGDVDRY-----ENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlkPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 81 IATKAAHRK-EG--DDFvfdNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNF 157
Cdd:cd19151 81 ISTKAGYTMwPGpyGDW---GSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 158 SLEQLKEA----NKDGLVDVI-QGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKY------DENTTFPEGDL 226
Cdd:cd19151 158 PPEEAREAaailKDLGTPCLIhQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYlngipeDSRAAKGSSFL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 227 RNDQAHfqgeqfKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASIT-LSAEEIA 303
Cdd:cd19151 238 KPEQIT------EEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNReFSEEELA 309
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-295 |
4.07e-42 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 146.13 E-value: 4.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 32 LNEETGKELVREAIKSGVTMLDTAYIYGvgRSEELIGEVLKecNREDVFIATKAAHRKEGDDfvfdNSPAFLKQSVEDSL 111
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYG--DSEKVLGKFLK--RLDKFKIITKLPPLKEDKK----EDEAAIEASVEASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 112 KRLQTDYIDLFYIHFPDEHTPKDEAV-QALNELKKEGKIRSIGVSNFSLEQLKEANKDGLVDVIQGEYNLLNREAEKT-F 189
Cdd:cd19097 95 KRLKVDSLDGLLLHNPDDLLKHGGKLvEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDIIQLPFNILDQRFLKSgL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 190 FPYTTEHGISFIpyfplV-S----GLLAGKYDENTTFpegdlrndqahfqgeqFKENIKKVNQLKPIAEKHNADTAHIVL 264
Cdd:cd19097 175 LAKLKKKGIEIH-----ArSvflqGLLLMEPDKLPAK----------------FAPAKPLLKKLHELAKKLGLSPLELAL 233
|
250 260 270
....*....|....*....|....*....|.
gi 494649899 265 AWYLARPEIDILIPGAKRADQLKDNMKAASI 295
Cdd:cd19097 234 GFVLSLPEIDKIVVGVDSLEQLKEIIAAFKK 264
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-294 |
5.73e-42 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 146.71 E-value: 5.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAVGGhnlypNLNEETGKELVREAIKSGVTMLDTAYIYGV-------GRSEELIGEVLKE-CNREDVFIATKAAH 87
Cdd:cd19752 3 LCLGTMYFGT-----RTDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDrGNRDDVVIATKVGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 88 RKEGDDFVFDN----SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLK 163
Cdd:cd19752 78 GPRDPDGGPESpeglSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 164 EAN----KDGLVD--VIQGEYNLLNREAEKTF----------FPYTTEHG-ISFIPYFPlvsgLLAGKYDenttfpegdl 226
Cdd:cd19752 158 RARqiarQQGWAEfsAIQQRHSYLRPRPGADFgvqrivtdelLDYASSRPdLTLLAYSP----LLSGAYT---------- 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 227 RNDQAHFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAAS 294
Cdd:cd19752 224 RPDRPLPEQYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-309 |
4.26e-41 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 145.10 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 5 TIGKTDLKVFPIGLGTNAVGGhnLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATK 84
Cdd:cd19104 4 RFGRTGLKVSELTFGGGGIGG--LMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKG-LPAGPYITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 AAHRKEGDDFVFDNspafLKQSVEDSLKRLQTDYIDLFYIH----------FPDEHTPKD-----EAVQALNELKKEGKI 149
Cdd:cd19104 81 VRLDPDDLGDIGGQ----IERSVEKSLKRLKRDSVDLLQLHnrigderdkpVGGTLSTTDvlglgGVADAFERLRSEGKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 150 RSIGVSNFSLEQ-LKEANKDGLVDVIQGEYNLLNREAEKTFFP------------YTTEHGISFIPYFPLVSGLLAGKYD 216
Cdd:cd19104 157 RFIGITGLGNPPaIRELLDSGKFDAVQVYYNLLNPSAAEARPRgwsaqdyggiidAAAEHGVGVMGIRVLAAGALTTSLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 217 entTFPEGDlrndqaHFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASI- 295
Cdd:cd19104 237 ---RGREAP------PTSDSDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAg 307
|
330
....*....|....
gi 494649899 296 TLSAEEIAFIDKLF 309
Cdd:cd19104 308 PLPAENLARLEALW 321
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
7-307 |
1.82e-40 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 144.36 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 7 GKTDLKVFPIGLGTnavgGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYG--VGRSEELIGEVLKE---CNREDVFI 81
Cdd:PRK09912 19 GKSGLRLPALSLGL----WHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdfaAYRDELII 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 82 ATKAAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQ 161
Cdd:PRK09912 95 STKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 162 LKEankdgLVDVI----------QGEYNLLNREAEKTFFPYT-TEHGISFIPYFPLVSGLLAGKYDENttFPEGdlrnDQ 230
Cdd:PRK09912 175 TQK-----MVELLrewkipllihQPSYNLLNRWVDKSGLLDTlQNNGVGCIAFTPLAQGLLTGKYLNG--IPQD----SR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 231 AHFQGEQFK---------ENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAAS-ITLSAE 300
Cdd:PRK09912 244 MHREGNKVRgltpkmlteANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNnLTFSTE 323
|
....*..
gi 494649899 301 EIAFIDK 307
Cdd:PRK09912 324 ELAQIDQ 330
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
15-308 |
2.33e-40 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 141.34 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNavgghnlypNLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKE--CNREDVFIATKAAhrkegd 92
Cdd:cd19139 3 AFGLGTF---------RLKDDVVIDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAEsgVPRDELFITTKIW------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 93 dfvFDN-SPAFLKQSVEDSLKRLQTDYIDLFYIHFP--DEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEANK-- 167
Cdd:cd19139 65 ---IDNlSKDKLLPSLEESLEKLRTDYVDLTLIHWPspNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAvv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 168 -DGLVDVIQGEYN--LLNReaekTFFPYTTEHGISFIPYFPLVSGLLAGkyDEnttfpegdlrndqahfqgeqfkenikk 244
Cdd:cd19139 142 gAGAIATNQIELSpyLQNR----KLVAHCKQHGIHVTSYMTLAYGKVLD--DP--------------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494649899 245 vnQLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19139 189 --VLAAIAERHGATPAQIALAWAMARGY--AVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-295 |
1.59e-39 |
|
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: 140.92 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGghNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIATKA--------- 85
Cdd:cd19161 2 ELGLGTAGLG--NLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKVgrllkpare 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 86 AHRKEGDDFV--------FDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEA------------VQALNELKK 145
Cdd:cd19161 80 GSVPDPNGFVdplpfeivYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKerhhfaqlmsggFKALEELKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 146 EGKIR--SIGVSNFS--LEQLKEANKDGLvdVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENttf 221
Cdd:cd19161 160 AGVIKafGLGVNEVQicLEALDEADLDCF--LLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKSG--- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494649899 222 pegdlrndqAHFQ-GEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASI 295
Cdd:cd19161 235 ---------AKFNyGDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQT 300
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
11-306 |
1.96e-39 |
|
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: 141.02 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 11 LKVFPIGLGTNAVGG--HNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGE-VLKECNREDVFIATK--A 85
Cdd:cd19146 9 VRVSPLCLGAMSFGEawKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEwMASRGNRDEMVLATKytT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 86 AHRKEGDD----FVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQ 161
Cdd:cd19146 89 GYRRGGPIkiksNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 162 LKEANK----DGLVD--VIQGEYNLLNREAEKTFFPYTTEHGISFIPYfplvsGLLA-GKYDEnttfPEGDLRNDQAHFQ 234
Cdd:cd19146 169 VSKANAyaraHGLTQfvVYQGHWSAAFRDFERDILPMCEAEGMALAPW-----GVLGqGQFRT----EEEFKRRGRSGRK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494649899 235 GEQFKENIKKVNQ-LKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19146 240 GGPQTEKERKVSEkLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIE 312
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
7-303 |
3.23e-39 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 139.90 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 7 GKTDLKVFPIGLGTnavgGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYG--VGRSEELIGEVLKE---CNREDVFI 81
Cdd:cd19150 6 GKSGLKLPALSLGL----WHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREdfaGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 82 ATKAAHRKEGDDFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQ 161
Cdd:cd19150 82 STKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 162 LKEA----NKDGLVDVI-QGEYNLLNREAEKTFFPYT-TEHGISFIPYFPLVSGLLAGKYDENttFPEGDlRNDQAHFQG 235
Cdd:cd19150 162 TREAaailRELGTPLLIhQPSYNMLNRWVEESGLLDTlQELGVGCIAFTPLAQGLLTDKYLNG--IPEGS-RASKERSLS 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494649899 236 EQF--KENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKA-ASITLSAEEIA 303
Cdd:cd19150 239 PKMltEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGAlDNLTFSADELA 309
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
33-294 |
7.11e-39 |
|
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: 137.31 E-value: 7.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 33 NEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECNREDVFIATKAAHRKegddfvfDNSPAFLKQSVEDSLK 112
Cdd:cd19096 19 DEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLPPWS-------VKSAEDFRRILEESLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 113 RLQTDYIDLFYIH-----FPDEHTPKDEAVQALNELKKEGKIRSIGVSnF--SLEQLKEANKDGLVDVIQGEYNLLNREA 185
Cdd:cd19096 92 RLGVDYIDFYLLHglnspEWLEKARKGGLLEFLEKAKKEGLIRHIGFS-FhdSPELLKEILDSYDFDFVQLQYNYLDQEN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 186 EKTF--FPYTTEHGISFIPYFPLVSGLLAgkydenttfpegdlrndqahfqgeqfkENIKKVNQLKPIAEKHNADTAhiv 263
Cdd:cd19096 171 QAGRpgIEYAAKKGMGVIIMEPLKGGGLA---------------------------NNPPEALAILCGAPLSPAEWA--- 220
|
250 260 270
....*....|....*....|....*....|.
gi 494649899 264 LAWYLARPEIDILIPGAKRADQLKDNMKAAS 294
Cdd:cd19096 221 LRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
6-306 |
7.72e-39 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 139.99 E-value: 7.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTNAVGGHNlypnlNEETGKELVREAIKSGVTMLDTAYIYGV-------GRSEELIGEVLKE-CNRE 77
Cdd:PRK10625 6 IPHSSLEVSTLGLGTMTFGEQN-----SEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKrGSRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 78 DVFIATKAAHRKEGDDFVFDNSPAF----LKQSVEDSLKRLQTDYIDLFYIHFPDEHTP---------KD--------EA 136
Cdd:PRK10625 81 KLIIASKVSGPSRNNDKGIRPNQALdrknIREALHDSLKRLQTDYLDLYQVHWPQRPTNcfgklgyswTDsapavsllET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 137 VQALNELKKEGKIRSIGVSNFS----LEQLKEANKDGLVDV--IQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGL 210
Cdd:PRK10625 161 LDALAEQQRAGKIRYIGVSNETafgvMRYLHLAEKHDLPRIvtIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 211 LAGKYdENTTFPEGdLRNDQ----AHFQGEQFKeniKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQL 286
Cdd:PRK10625 241 LTGKY-LNGAKPAG-ARNTLfsrfTRYSGEQTQ---KAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQL 315
|
330 340
....*....|....*....|
gi 494649899 287 KDNMKAASITLSAEEIAFID 306
Cdd:PRK10625 316 KTNIESLHLTLSEEVLAEIE 335
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-308 |
3.39e-38 |
|
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: 135.84 E-value: 3.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAVGGhnlypnlnEETGKELVREAIKSGVTMLDTAYIYgvgRSEELIGEVLKEC------NREDVFIATKAAHRK 89
Cdd:cd19136 4 LGLGTFRLRG--------EEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDLlpkyglSREDIFITSKLAPKD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 90 EGDDFVfdnspaflKQSVEDSLKRLQTDYIDLFYIHFP--DEHTPKDEAV--------QALNELKKEGKIRSIGVSNFSL 159
Cdd:cd19136 73 QGYEKA--------RAACLGSLERLGTDYLDLYLIHWPgvQGLKPSDPRNaelrreswRALEDLYKEGKLRAIGVSNYTV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 160 EQLKEANKDGLVD--VIQGEYN--LLNREAEKtffpYTTEHGISFIPYFPLVSGllAGKYDENTTFPEgdlrndqahfqg 235
Cdd:cd19136 145 RHLEELLKYCEVPpaVNQVEFHphLVQKELLK----FCKDHGIHLQAYSSLGSG--DLRLLEDPTVLA------------ 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494649899 236 eqfkenikkvnqlkpIAEKHNADTAHIVLAWYLARpeiDI-LIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19136 207 ---------------IAKKYGRTPAQVLLRWALQQ---GIgVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
11-306 |
4.32e-37 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 134.57 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 11 LKVFPIGLGTNAVGG--HNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKE-CNREDVFIATK--- 84
Cdd:cd19147 8 IRVSPLILGAMSIGDawSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSrKNRDQIVIATKftt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 ---AAHRKEGDDFVF-DNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:cd19147 88 dykAYEVGKGKAVNYcGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 QLKEANK------DGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGK--YDENTTFPEGDLRndqAH 232
Cdd:cd19147 168 VVSAANYyatahgKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKkaVEERKKNGEGLRS---FV 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494649899 233 FQGEQFKENIKKVNQLKPIAEKHNADT-AHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19147 245 GGTEQTPEEVKISEALEKVAEEHGTESvTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-291 |
4.55e-37 |
|
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: 134.37 E-value: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 11 LKVFPIGLGTNAVGghnlypnLNEETGK---ELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKE------CNREDVFI 81
Cdd:cd19099 1 LTLSSLGLGTYRGD-------SDDETDEeyrEALKAALDSGINVIDTAINYRGGRSERLIGKALREliekggIKRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 82 ATKA--------------------AHRKEGDDFVFDN-----SPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKD-- 134
Cdd:cd19099 74 VTKAgyipgdgdeplrplkyleekLGRGLIDVADSAGlrhciSPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLELge 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 135 --------EAVQALNELKKEGKIRSIGVS-------------NFSLEQLKEANKDGLVD-----VIQGEYNLLNREAE-- 186
Cdd:cd19099 154 eefydrleEAFEALEEAVAEGKIRYYGIStwdgfrappalpgHLSLEKLVAAAEEVGGDnhhfkVIQLPLNLLEPEALte 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 187 --------KTFFPYTTEHGISFIPYFPLVSGLLAGkydenttfpEGDLRNDQAHFQGEqfkenikkvnqlkpiaekhnaD 258
Cdd:cd19099 234 kntvkgeaLSLLEAAKELGLGVIASRPLNQGQLLG---------ELRLADLLALPGGA---------------------T 283
|
330 340 350
....*....|....*....|....*....|...
gi 494649899 259 TAHIVLAWYLARPEIDILIPGAKRADQLKDNMK 291
Cdd:cd19099 284 LAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
15-308 |
4.72e-37 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 132.78 E-value: 4.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTnavgghnlYPnLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAAhrkeGD 92
Cdd:cd19132 9 AIGFGT--------YP-LKGDEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRSGvpREELFVTTKLP----GR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 93 DFVFDNSpaflKQSVEDSLKRLQTDYIDLFYIHFPDehtPKD----EAVQALNELKKEGKIRSIGVSNFSLEQLKE-ANK 167
Cdd:cd19132 73 HHGYEEA----LRTIEESLYRLGLDYVDLYLIHWPN---PSRdlyvEAWQALIEAREEGLVRSIGVSNFLPEHLDRlIDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 168 DGLVDVI-QGE-YNLLNREAEKTffpYTTEHGISFIPYFPLVSGllagkydenttfpeGDLRNDQAhfqgeqfkenikkv 245
Cdd:cd19132 146 TGVTPAVnQIElHPYFPQAEQRA---YHREHGIVTQSWSPLGRG--------------SGLLDEPV-------------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494649899 246 nqLKPIAEKHNADTAHIVLAWYLARPEIDilIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19132 195 --IKAIAEKHGKTPAQVVLRWHVQLGVVP--IPKSANPERQRENLAIFDFELSDEDMAAIAAL 253
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
16-308 |
8.26e-36 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 129.75 E-value: 8.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAVGGHNlypnlneetgKELVREAIK-SGVTMLDTAYIYGVgrsEELIGEVLKECN--REDVFIATKAAHRKEGD 92
Cdd:cd19135 16 LGLGTSHSGGYS----------HEAVVYALKeCGYRHIDTAKRYGC---EELLGKAIKESGvpREDLFLTTKLWPSDYGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 93 DFVfdnspaflKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKD-------EAVQALNELKKEGKIRSIGVSNFSLEQLKEA 165
Cdd:cd19135 83 EST--------KQAFEASLKRLGVDYLDLYLLHWPDCPSSGKnvketraETWRALEELYDEGLCRAIGVSNFLIEHLEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 166 NKDGLV--DVIQGEYNLLNREAEktFFPYTTEHGISFIPYFPLVSGLLAGkydenttfpegdlrndqahfqgeqfKENIK 243
Cdd:cd19135 155 LEDCSVvpHVNQVEFHPFQNPVE--LIEYCRDNNIVFEGYCPLAKGKALE-------------------------EPTVT 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494649899 244 KvnqlkpIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19135 208 E------LAKKYQKTPAQILIRWSIQNGV--VTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-295 |
1.49e-35 |
|
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: 130.26 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTNAVGGHNLypnlNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVL--KECNREDVFIAT 83
Cdd:cd19141 5 LGKSGLRVSCLGLGTWVTFGSQI----SDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILkkKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 84 K-----AAHRKEGddfvfdNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFS 158
Cdd:cd19141 81 KifwggKAETERG------LSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 159 LEQLKE----ANKDGLVD--VIQGEYNLLNREAEKTFFPYTTEH-GISFIPYFPLVSGLLAGKYDENTTF-PEGDLRNDQ 230
Cdd:cd19141 155 AMEIMEaysvARQFNLIPpiVEQAEYHLFQREKVEMQLPELFHKiGVGAMTWSPLACGILSGKYDDGVPEySRASLKGYQ 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 231 AH---FQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASI 295
Cdd:cd19141 235 WLkekILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-307 |
2.30e-35 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 128.50 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 12 KVFPIGLGTnavgGHNLYPNLNEETGKEL---VREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAA 86
Cdd:cd19120 3 KIPAIAFGT----GTAWYKSGDDDIQRDLvdsVKLALKAGFRHIDTAEMYG---NEKEVGEALKESGvpREDLFITTKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 87 HRkeGDDfvfdnspafLKQSVEDSLKRLQTDYIDLFYIHFP----DEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQL 162
Cdd:cd19120 76 PG--IKD---------PREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 163 KEankdgLVD-------VIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSgllagkydeNTTFPEGDLrnDQAhfqg 235
Cdd:cd19120 145 EE-----LLDtakikpaVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLSP---------LTRDAGGPL--DPV---- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494649899 236 eqfkenikkvnqLKPIAEKHNADTAHIVLAWYLARpeiDIL-IPGAKRADQLKDNMKAASITLSAEEIAFIDK 307
Cdd:cd19120 205 ------------LEKIAEKYGVTPAQVLLRWALQK---GIVvVTTSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
33-308 |
2.65e-35 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 128.28 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 33 NEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAAHRKEGDDFVFdnspaflkQSVEDS 110
Cdd:cd19157 22 EGSEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKESGipREELFITSKVWNADQGYDSTL--------KAFEAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 111 LKRLQTDYIDLFYIHFPDEHTPKdEAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGLVD--VIQGEYNllNREAEKT 188
Cdd:cd19157 91 LERLGLDYLDLYLIHWPVKGKYK-ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVpmVNQVEFH--PRLTQKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 189 FFPYTTEHGISFIPYFPLVsgllagkydenttfpegdlrndqahfQGEQFKENIkkvnqLKPIAEKHNADTAHIVLAWYL 268
Cdd:cd19157 168 LRDYCKKQGIQLEAWSPLM--------------------------QGQLLDNPV-----LKEIAEKYNKSVAQVILRWDL 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 494649899 269 ARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19157 217 QNGV--VTIPKSIKEHRIIENADVFDFELSQEDMDKIDAL 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
16-308 |
9.93e-35 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 127.91 E-value: 9.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNavgghnlypNLNEETGKELVREAIKSGVTMLDTAYIYgvgRSEELIGEVLKE------CNREDVFIATKAA-HR 88
Cdd:cd19154 15 IGLGTW---------QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAElleegvVKREDLFITTKLWtHE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 89 kegddfvfdNSPAFLKQSVEDSLKRLQTDYIDLFYIHFP-----------------DEHTPKD--EAVQALNELKKEGKI 149
Cdd:cd19154 83 ---------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmSIHDAVDveDVWRGMEKVYDEGLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 150 RSIGVSNFSLEQLKEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKYDENTTFPEGDLRND 229
Cdd:cd19154 154 KAIGVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTGVSPAPNLLQD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494649899 230 QAhfqgeqfkenikkvnqLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19154 234 PI----------------VKAIAEKHGKTPAQVLLRYLLQRGI--AVIPKSATPSRIKENFNIFDFSLSEEDMATLEEI 294
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
41-308 |
4.02e-34 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 125.85 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 41 VREAIKSGVTMLDTAYIYGVGRSEELIGEVLKEcNREDVFIATKAAHRKeGDD--FVFDNSPAFLKQSVEDSLKRLQTDY 118
Cdd:PRK10376 46 LREAVALGVNHIDTSDFYGPHVTNQLIREALHP-YPDDLTIVTKVGARR-GEDgsWLPAFSPAELRRAVHDNLRNLGLDV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 119 IDL--FYIHFpDEHTPKD----EAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGLVDVIQGEYNLLNREAEKtFFPY 192
Cdd:PRK10376 124 LDVvnLRLMG-DGHGPAEgsieEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDA-LIDA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 193 TTEHGISFIPYFPLvsgllagkydenttfpeGDLRNDQAhfqgeqfkenikkvNQLKPIAEKHNADTAHIVLAWYLAR-P 271
Cdd:PRK10376 202 LARDGIAYVPFFPL-----------------GGFTPLQS--------------STLSDVAASLGATPMQVALAWLLQRsP 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 494649899 272 EIdILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:PRK10376 251 NI-LLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
35-308 |
1.06e-32 |
|
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: 121.14 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 35 ETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAAHRkegdDFVFDNSpaflKQSVEDSLK 112
Cdd:cd19133 23 EECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKSGipREELFITTKLWIQ----DAGYEKA----KKAFERSLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 113 RLQTDYIDLFYIHFP--DEHtpkdEAVQALNELKKEGKIRSIGVSNFSLEQLKE--ANKDGLVDVIQGEYNLLNREAEKT 188
Cdd:cd19133 92 RLGLDYLDLYLIHQPfgDVY----GAWRAMEELYKEGKIRAIGVSNFYPDRLVDliLHNEVKPAVNQIETHPFNQQIEAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 189 ffPYTTEHGISFIPYFPLvsgllagkydenttfpegdlrndqAHFQGEQFKENIkkvnqLKPIAEKHNADTAHIVLAWYL 268
Cdd:cd19133 168 --EFLKKYGVQIEAWGPF------------------------AEGRNNLFENPV-----LTEIAEKYGKSVAQVILRWLI 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 494649899 269 ARpEIdILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19133 217 QR-GI-VVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
5-211 |
1.47e-32 |
|
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: 121.87 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 5 TIGKTDLKVFPIGLGTNAVGGhnLYPNLNEET-GKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLK--ECNREDVFI 81
Cdd:cd19153 4 TLEIALGNVSPVGLGTAALGG--VYGDGLEQDeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAalQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 82 ATKAAHRKEGDdfvFDNSPAFLKQSVEDSLKRLQTDYIDLFYIH---FPDEHTPKDEAVQALNELKKEGKIRSIGVSNFS 158
Cdd:cd19153 82 ATKVGRYRDSE---FDYSAERVRASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIKRIGIAGYP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 159 LEQLKEANKD---GLVDVIQG--EYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGLL 211
Cdd:cd19153 159 LDTLTRATRRcspGSLDAVLSycHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLL 216
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
15-162 |
2.06e-32 |
|
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: 121.62 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTnAVGGHNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGvgRSEELIGEVLK----ECNREDVFIATKAAhRKE 90
Cdd:cd19164 15 PLIFGA-ATFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYG--PSEIILGRALKalrdEFPRDTYFIITKVG-RYG 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 91 GDDFvfDNSPAFLKQSVEDSLKRLQTDYIDLFYIH---F-PDEHTpkDEAVQALNELKKEGKIRSIGVSNFSLEQL 162
Cdd:cd19164 91 PDDF--DYSPEWIRASVERSLRRLHTDYLDLVYLHdveFvADEEV--LEALKELFKLKDEGKIRNVGISGYPLPVL 162
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-309 |
2.76e-32 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 122.02 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGTNAVGGhnlyPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVL--KECNRED 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFG----SQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 79 VFIATK-----AAHRKEGddfvfdNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIG 153
Cdd:cd19160 79 YVVTTKiywggQAETERG------LSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 154 VSNFSLEQLKE----ANKDGLVDVI--QGEYNLLNREAEKTFFPYTTEH-GISFIPYFPLVSGLLAGKYDEntTFPEgdl 226
Cdd:cd19160 153 TSRWSAMEIMEaysvARQFNLIPPVceQAEYHLFQREKVEMQLPELYHKiGVGSVTWSPLACGLITGKYDG--RVPD--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 227 rNDQAHFQGEQF-KENIK---------KVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASI- 295
Cdd:cd19160 228 -TCRAAVKGYQWlKEKVQseegkkqqaKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVl 306
|
330
....*....|....*
gi 494649899 296 -TLSAEEIAFIDKLF 309
Cdd:cd19160 307 sQLTPQTVMEIDALL 321
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
33-308 |
1.05e-31 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 118.63 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 33 NEETGKeLVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC--NREDVFIATKAAHRKEGDDfvfdnSPaflKQSVEDS 110
Cdd:cd19131 22 NDEAAS-AVREALEVGYRSIDTAAIYG---NEEGVGKAIRASgvPREELFITTKLWNSDQGYD-----ST---LRAFDES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 111 LKRLQTDYIDLFYIHFPdehTPKD----EAVQALNELKKEGKIRSIGVSNFSLEQLKE-ANKDGLVDVI-QGE-YNLLNR 183
Cdd:cd19131 90 LRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQRlIDETGVVPVVnQIElHPRFQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 184 EAEKTFfpyTTEHGISFIPYFPLVSGLLAgkydENTTfpegdlrndqahfqgeqfkenikkvnqLKPIAEKHNADTAHIV 263
Cdd:cd19131 167 RELRAF---HAKHGIQTESWSPLGQGGLL----SDPV---------------------------IGEIAEKHGKTPAQVV 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 494649899 264 LAWYLArpEIDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19131 213 IRWHLQ--NGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
41-308 |
8.83e-31 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 116.66 E-value: 8.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 41 VREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC--NREDVFIATKAahrkegddFVFDNSPAFLKQSVEDSLKRLQTDY 118
Cdd:PRK11172 22 VKTALELGYRAIDTAQIYD---NEAAVGQAIAESgvPRDELFITTKI--------WIDNLAKDKLIPSLKESLQKLRTDY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 119 IDLFYIHFP--DEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKEAnkdglVDVIqGEYNLLNREAEktFFPY---- 192
Cdd:PRK11172 91 VDLTLIHWPspNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQA-----IAAV-GAENIATNQIE--LSPYlqnr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 193 -----TTEHGISFIPYFPLVsgllagkYdenttfpegdlrndqahfqGEQFKENIkkvnqLKPIAEKHNADTAHIVLAWY 267
Cdd:PRK11172 163 kvvafAKEHGIHVTSYMTLA-------Y-------------------GKVLKDPV-----IARIAAKHNATPAQVILAWA 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 494649899 268 LARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:PRK11172 212 MQLGY--SVIPSSTKRENLASNLLAQDLQLDAEDMAAIAAL 250
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
15-308 |
9.79e-31 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 117.00 E-value: 9.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVGGhnlypnlnEETGKELVREAIKSGVTMLDTAYIYGVgrsEELIGEVLKE------CNREDVFIATKaahr 88
Cdd:cd19116 13 AIALGTWKLKD--------DEGVRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIREkiaegvVKREDLFITTK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 89 kegddfVFDN--SPAFLKQSVEDSLKRLQTDYIDLFYIHFP-------DEHTPKD---------EAVQALNELKKEGKIR 150
Cdd:cd19116 78 ------LWNSyhEREQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 151 SIGVSNFSLEQLKEANKDGLVD--VIQGEYNL-LNREAektFFPYTTEHGISFIPYFPLvsgllaGKYD-ENTTFPEGDL 226
Cdd:cd19116 152 SIGVSNFNSEQINRLLSNCNIKpaVNQIEVHPtLTQEK---LVAYCQSNGIVVMAYSPF------GRLVpRGQTNPPPRL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 227 RNdqahfqgeqfkenikkvNQLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19116 223 DD-----------------PTLVAIAKKYGKTTAQIVLRYLIDRGV--VPIPKSSNKKRIKENIDIFDFQLTPEEVAALN 283
|
..
gi 494649899 307 KL 308
Cdd:cd19116 284 SF 285
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
33-308 |
2.51e-30 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 114.84 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 33 NEETGKELVREAIKSGVTMLDTAYIYgvgRSEELIGEVLKECN--REDVFIATKAAHRKEGDDFVFDnspAFlkqsvEDS 110
Cdd:cd19126 21 DGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGvpREELFVTTKLWNDDQRARRTED---AF-----QES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 111 LKRLQTDYIDLFYIHFPDEHTPKDeAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGLVD--VIQGEYN-LLNREAek 187
Cdd:cd19126 90 LDRLGLDYVDLYLIHWPGKDKFID-TWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVpaVNQVEFHpYLTQKE-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 188 tFFPYTTEHGISFIPYFPLVSGLLAgkydENTTfpegdlrndqahfqgeqfkenikkvnqLKPIAEKHNADTAHIVLAWY 267
Cdd:cd19126 167 -LRGYCKSKGIVVEAWSPLGQGGLL----SNPV---------------------------LAAIGEKYGKSAAQVVLRWD 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 494649899 268 LARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19126 215 IQHGV--VTIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
6-293 |
2.24e-29 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 114.10 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTNAVGghNLYPNLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECN--REDVFIAT 83
Cdd:PLN02587 4 LGSTGLKVSSVGFGASPLG--SVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGipREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 84 KAAHRKEGddfvFDNSPAFLKQSVEDSLKRLQTDYIDLFYIH---FPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:PLN02587 82 KCGRYGEG----FDFSAERVTKSVDESLARLQLDYVDILHCHdieFGSLDQIVNETIPALQKLKESGKVRFIGITGLPLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 QLK---EANKDGLVDVIQG--EYNLlNREAEKTFFPYTTEHGISFIPYFPLVSGLLAGKydentTFPEGdlrndqaHFQG 235
Cdd:PLN02587 158 IFTyvlDRVPPGTVDVILSycHYSL-NDSSLEDLLPYLKSKGVGVISASPLAMGLLTEN-----GPPEW-------HPAP 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 236 EQFKENIKKVNQlkpIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAA 293
Cdd:PLN02587 225 PELKSACAAAAT---HCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAA 279
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
6-286 |
2.49e-29 |
|
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: 114.10 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTNAVGGHNLypnlNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECN--REDVFIAT 83
Cdd:cd19142 6 LGKSGLRVSNVGLGTWSTFSTAI----SEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGwkRSSYIVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 84 KA--AHRKEGDDFvfdnSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQ 161
Cdd:cd19142 82 KIywSYGSEERGL----SRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 162 LKEA----NKDGLVDVI--QGEYNLLNREAEKTFFP--YtTEHGISFIPYFPLVSGLLAGKYDE------NTTFPEGDLR 227
Cdd:cd19142 158 IMEAfsiaRQFNCPTPIceQSEYHMFCREKMELYMPelY-NKVGVGLITWSPLSLGLDPGISEEtrrlvtKLSFKSSKYK 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 228 NDQ-AHFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQL 286
Cdd:cd19142 237 VGSdGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQL 296
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-309 |
5.07e-29 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 113.21 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 1 MSKVTIGKTDLKVFPIGLGT-NAVGGHnlypnLNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKECN--RE 77
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQ-----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 78 DVFIATK-----AAHRKEGddfvfdNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSI 152
Cdd:cd19159 76 SLVITTKlywggKAETERG------LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 153 GVSNFSLEQLKE----ANKDGLVDVI--QGEYNLLNREAEKTFFPYTTEH-GISFIPYFPLVSGLLAGKYDENTtfPEGD 225
Cdd:cd19159 150 GTSRWSAMEIMEaysvARQFNMIPPVceQAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGKYGNGV--PESS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 226 lRNDQAHFQ-------GEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASI--T 296
Cdd:cd19159 228 -RASLKCYQwlkerivSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpK 306
|
330
....*....|...
gi 494649899 297 LSAEEIAFIDKLF 309
Cdd:cd19159 307 MTSHVVNEIDNIL 319
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
6-309 |
5.28e-29 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 113.26 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 6 IGKTDLKVFPIGLGTNAVGGHNLypnlNEETGKELVREAIKSGVTMLDTAYIYGVGRSEELIGEVLKE--CNREDVFIAT 83
Cdd:cd19158 6 LGKSGLRVSCLGLGTWVTFGGQI----TDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 84 K-----AAHRKEGddfvfdNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDEHTPKDEAVQALNELKKEGKIRSIGVSNFS 158
Cdd:cd19158 82 KifwggKAETERG------LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 159 LEQLKE----ANKDGLVDVI--QGEYNLLNREAEKTFFPYTTEH-GISFIPYFPLVSGLLAGKYDENT-TFPEGDLRNDQ 230
Cdd:cd19158 156 SMEIMEaysvARQFNLIPPIceQAEYHMFQREKVEVQLPELFHKiGVGAMTWSPLACGIVSGKYDSGIpPYSRASLKGYQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 231 ---AHFQGEQFKENIKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASI--TLSAEEIAFI 305
Cdd:cd19158 236 wlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEI 315
|
....
gi 494649899 306 DKLF 309
Cdd:cd19158 316 DSIL 319
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
16-308 |
2.56e-28 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 110.51 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAVGghnlyPNLneetGKELVREAIKSGVTMLDTAYIYGVgrsEELIGEVLKE------CNREDVFIATKAahrk 89
Cdd:cd19125 14 VGLGTWQAD-----PGV----VGNAVKTAIKEGYRHIDCAAIYGN---EKEIGKALKKlfedgvVKREDLFITSKL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 90 egddFVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFP-----DEHTPKDEAV---------QALNELKKEGKIRSIGVS 155
Cdd:cd19125 78 ----WCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkGAHMPEPEEVlppdipstwKAMEKLVDSGKVRAIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 156 NFSLEQLKEANKDGLV--DVIQGEYNLLNREAEktFFPYTTEHGISFIPYFPLVSGllagkydeNTTFPEGDLRNDQAhf 233
Cdd:cd19125 154 NFSVKKLEDLLAVARVppAVNQVECHPGWQQDK--LHEFCKSKGIHLSAYSPLGSP--------GTTWVKKNVLKDPI-- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494649899 234 qgeqfkenikkvnqLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19125 222 --------------VTKVAEKLGKTPAQVALRWGLQRGT--SVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
41-308 |
2.30e-27 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 107.60 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 41 VREAIKSGVTMLDTAYIYgvgRSEELIGEVLKECN--REDVFIATKAAHRKEGddfvFDNSPAflkqSVEDSLKRLQTDY 118
Cdd:cd19156 29 VKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGvpREEVFVTTKLWNSDQG----YESTLA----AFEESLEKLGLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 119 IDLFYIHFPDEHTPKDeAVQALNELKKEGKIRSIGVSNFSLEQLKEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGI 198
Cdd:cd19156 98 VDLYLIHWPVKGKFKD-TWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 199 SFIPYFPLVSGllagkydenttfpegdlrndqahfqgeqfkeNIKKVNQLKPIAEKHNADTAHIVLAWYLarpEIDIL-I 277
Cdd:cd19156 177 AVEAWSPLGQG-------------------------------KLLSNPVLKAIGKKYGKSAAQVIIRWDI---QHGIItI 222
|
250 260 270
....*....|....*....|....*....|.
gi 494649899 278 PGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19156 223 PKSVHEERIQENFDVFDFELTAEEIRQIDGL 253
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
16-308 |
4.47e-27 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 107.50 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTnavgghnlypnLNEETGK--ELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC------NREDVFIATK--- 84
Cdd:cd19123 15 LGLGT-----------WKSKPGEvgQAVKQALEAGYRHIDCAAIYG---NEAEIGAALAEVfkegkvKREDLWITSKlwn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 AAHRKEgddfvfDNSPAFLKqsvedSLKRLQTDYIDLFYIHFP------------------DEHTPKDEAVQALNELKKE 146
Cdd:cd19123 81 NSHAPE------DVLPALEK-----TLADLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 147 GKIRSIGVSNFSLEQLKEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSGllaGKYDENTTFPEGDL 226
Cdd:cd19123 150 GLCRHIGVSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSG---DRPAAMKAEGEPVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 227 RNDQAhfqgeqfkenikkvnqLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFID 306
Cdd:cd19123 227 LEDPV----------------INKIAEKHGASPAQVLIAWAIQRGT--VVIPKSVNPERIQQNLEAAEVELDASDMATIA 288
|
..
gi 494649899 307 KL 308
Cdd:cd19123 289 AL 290
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
34-308 |
3.75e-26 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 104.03 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 34 EETGKElVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC--NREDVFIATKAAHrkegDDFVFDNSpaflKQSVEDSL 111
Cdd:cd19127 22 EETADA-VATALADGYRLIDTAAAYG---NEREVGEGIRRSgvDRSDIFVTTKLWI----SDYGYDKA----LRGFDASL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 112 KRLQTDYIDLFYIHFPdehTPKD-----EAVQALNELKKEGKIRSIGVSNFSLEQLKE-ANKDGLVDVI-QGEynLLNRE 184
Cdd:cd19127 90 RRLGLDYVDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPEHLERlIDATTVVPAVnQVE--LHPYF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 185 AEKTFFPYTTEHGISFIPYFPLvsgllagkydenttfpEGDLRNDQAHFQGEQfkeNIKKVNQLKPIAEKHNADTAHIVL 264
Cdd:cd19127 165 SQKDLRAFHRRLGIVTQAWSPI----------------GGVMRYGASGPTGPG---DVLQDPTITGLAEKYGKTPAQIVL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 494649899 265 AWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19127 226 RWHLQNGV--SAIPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
27-308 |
8.93e-26 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 8.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 27 NLYPNL--------NEETgKELVREAIKSGVTMLDTAYIYgvgRSEELIGEVLKECN--REDVFIATKaahrkegddfVF 96
Cdd:PRK11565 13 NVMPQLglgvwqasNEEV-ITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASvaREELFITTK----------LW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 97 DNSPAFLKQSVEDSLKRLQTDYIDLFYIHFPDehTPKD---EAVQALNELKKEGKIRSIGVSNFSLEQLKE-ANKDGLVD 172
Cdd:PRK11565 79 NDDHKRPREALEESLKKLQLDYVDLYLMHWPV--PAIDhyvEAWKGMIELQKEGLIKSIGVCNFQIHHLQRlIDETGVTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 173 VI-QGEYNLLNReaEKTFFPYTTEHGISFIPYFPLVSGllagkydenttfpeGDLRNDQahfqgeqfkENIKKvnqlkpI 251
Cdd:PRK11565 157 VInQIELHPLMQ--QRQLHAWNATHKIQTESWSPLAQG--------------GKGVFDQ---------KVIRD------L 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 252 AEKHNADTAHIVLAWYLarpeiD---ILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:PRK11565 206 ADKYGKTPAQIVIRWHL-----DsglVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKL 260
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
16-308 |
1.02e-25 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 103.35 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTnavgghnlYPNLNEETgKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKE------CNREDVFIATKAAhrk 89
Cdd:cd19111 7 IGLGT--------YQSPPEEV-RAAVDYALFVGYRHIDTALSYQ---NEKAIGEALKWwlkngkLKREEVFITTKLP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 90 egddfVFDNSPAFLKQSVEDSLKRLQTDYIDLFYIHFP-------------DEHTPKDEAVQALNELKKEGKIRSIGVSN 156
Cdd:cd19111 72 -----PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 157 FSLEQLKEANKDGLVDV--IQGEYN--LLNREAEKtffpYTTEHGISFIPYFPLVSGLLAGKYDENttfPEGDLRNDQah 232
Cdd:cd19111 147 FNPRQINKILAYAKVKPsnLQLECHayLQQRELRK----FCNKKNIVVTAYAPLGSPGRANQSLWP---DQPDLLEDP-- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 233 fqgeqfkenikKVNQlkpIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19111 218 -----------TVLA---IAKELDKTPAQVLLRFVLQRGT--GVLPKSTNKERIEENFEVFDFELTEEHFKKLKTL 277
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
16-308 |
7.24e-25 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 101.42 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAvgghnlyPNLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC------NREDVFIATKAAhrk 89
Cdd:cd19119 15 LGLGTAS-------PHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAiddgsiKREELFITTKVW--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 90 egddfvfdnsPAFLKQ---SVEDSLKRLQTDYIDLFYIHFP-------DEH----TPKD--------------EAVQALN 141
Cdd:cd19119 82 ----------PTFYDEverSLDESLKALGLDYVDLLLVHWPvcfekdsDDSgkpfTPVNddgktryaasgdhiTTYKQLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 142 ELKKEGKIRSIGVSNFSLEQLKEANKDGLVDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLVSgllagkydenttf 221
Cdd:cd19119 152 KIYLDGRAKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGS------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 222 pegdlrndqaHFQGEQFKENIKKvnqlkpIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITlsAEE 301
Cdd:cd19119 219 ----------HGAPNLKNPLVKK------IAEKYNVSTGDILISYHVRQGV--IVLPKSLKPVRIVSNGKIVSLT--KED 278
|
....*..
gi 494649899 302 IAFIDKL 308
Cdd:cd19119 279 LQKLDDI 285
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-308 |
1.84e-24 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 99.90 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAVgghnlypnlNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC------NREDVFIATK---AA 86
Cdd:cd19128 4 LGFGTYKI---------TESESKEAVKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEIfkdggvKREDLFITSKlwpTM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 87 HRkegddfvfdnsPAFLKQSVEDSLKRLQTDYIDLFYIHFP-------------------DEHTPKDEAVQALNELKKEG 147
Cdd:cd19128 72 HQ-----------PENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 148 KIRSIGVSNFSLEQLKE----ANKDGLVDVIQGEYNLLNREAEKtffpYTTEHGISFIPYFPlvsglLAGKYDENTTFPE 223
Cdd:cd19128 141 LTKNIGVSNYSTKLLTDllnyCKIKPFMNQIECHPYFQNDKLIK----FCIENNIHVTAYRP-----LGGSYGDGNLTFL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 224 GDlrndqahfqgeqfkenikkvNQLKPIAEKHNADTAHIVLAWYLAR-PEIDILIPGAKRADQLKDNMKAASITLSAEEI 302
Cdd:cd19128 212 ND--------------------SELKALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLALTKEDM 271
|
....*.
gi 494649899 303 AFIDKL 308
Cdd:cd19128 272 DAINTL 277
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
16-308 |
2.41e-23 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 96.95 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAvgghnlyPNLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKE-------CNREDVFIATKA--- 85
Cdd:cd19124 8 IGMGTAS-------DPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlglvKSRDELFVTSKLwcs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 86 -AHRkegDDFVfdnsPAfLKQSvedsLKRLQTDYIDLFYIHFP--------------DEHTPKD-EAV-QALNELKKEGK 148
Cdd:cd19124 78 dAHP---DLVL----PA-LKKS----LRNLQLEYVDLYLIHWPvslkpgkfsfpieeEDFLPFDiKGVwEAMEECQRLGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 149 IRSIGVSNFSLEQLKEANKDGLVD--VIQGEYNLLNReaEKTFFPYTTEHGISFIPYFPLvsGLLAGKYDENTTfpegdL 226
Cdd:cd19124 146 TKAIGVSNFSCKKLQELLSFATIPpaVNQVEMNPAWQ--QKKLREFCKANGIHVTAYSPL--GAPGTKWGSNAV-----M 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 227 RNDqahfqgeqfkenikkvnQLKPIAEKHNADTAHIVLAWYLarpEI-DILIPGAKRADQLKDNMKAASITLSAEEIAFI 305
Cdd:cd19124 217 ESD-----------------VLKEIAAAKGKTVAQVSLRWVY---EQgVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
...
gi 494649899 306 DKL 308
Cdd:cd19124 277 SEI 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
41-308 |
5.42e-23 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 95.94 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 41 VREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC-------NREDVFIATKA---AHRkegddfvfdnsPAFLKQSVEDS 110
Cdd:cd19118 26 VKIALKAGYRHLDLAKVYQ---NQHEVGQALKELlkeepgvKREDLFITSKLwnnSHR-----------PEYVEPALDDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 111 LKRLQTDYIDLFYIHFP-------DEH----TPKDEAVQALN-------------ELKKEGKIRSIGVSNFSLEQLKEAN 166
Cdd:cd19118 92 LKELGLDYLDLYLIHWPvafkptgDLNpltaVPTNGGEVDLDlsvslvdtwkamvELKKTGKVKSIGVSNFSIDHLQAII 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 167 KDGLV--DVIQGEYN--LLNREaektFFPYTTEHGISFIPYFPLvsgllagkydENTTFPEGDLRNDQAhfqgeqfkeni 242
Cdd:cd19118 172 EETGVvpAVNQIEAHplLLQDE----LVDYCKSKNIHITAYSPL----------GNNLAGLPLLVQHPE----------- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 243 kkvnqLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKaaSITLSAEEIAFIDKL 308
Cdd:cd19118 227 -----VKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
41-308 |
6.97e-23 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 95.64 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 41 VREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAA---HRKegddfvfdnspafLKQSVEDSLKRLQ 115
Cdd:cd19117 33 VEAALKAGYRHIDTAAIYG---NEEEVGQGIKDSGvpREEIFITTKLWctwHRR-------------VEEALDQSLKKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 116 TDYIDLFYIHFP------------------DEHTPKDEAVQA---LNELKKEGKIRSIGVSNFSLEQLKEANKDGLVDVI 174
Cdd:cd19117 97 LDYVDLYLMHWPvpldpdgndflfkkddgtKDHEPDWDFIKTwelMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 175 ----QGEYNLLNREAEktFFPYTTEHGISFIPYFPLVSGllagkydenttfpEGDLRNDQAhfqgeqfkenikkvnqLKP 250
Cdd:cd19117 177 pavnQIELHPLLPQPK--LVDFCKSKGIHATAYSPLGST-------------NAPLLKEPV----------------IIK 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 251 IAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAasITLSAEEIAFIDKL 308
Cdd:cd19117 226 IAKKHGKTPAQVIISWGLQRGY--SVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-303 |
8.68e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 96.26 E-value: 8.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 15 PIGLGTNAVG-------GHNlyPNLNEETGKELVRE--------AIKSGVTMLDTAYIYGvgRSEELIGEVLKECN--RE 77
Cdd:cd19098 2 RLGLGLAALGrpgyinlGHA--ADLGSGRSVEAMRAhthavldaAWAAGVRYFDAARSYG--RAEEFLGSWLRSRNiaPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 78 DVFIATK------AAHRKEGDDF-VFDNSPAFLKQSVEDSLKRLQtDYIDLFYIHFPDEHTP--KDEAV-QALNELKKEG 147
Cdd:cd19098 78 AVFVGSKwgytytADWQVDAAVHeVKDHSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGvlEDADVlAALAELKAEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 148 kiRSIGVS------NFSLEQLKEANKDG--LVDVIQGEYNLLNREAEKTFfpyTTEH--GISFIPYFPLVSGLLAGkyde 217
Cdd:cd19098 157 --VKIGLSlsgpqqAETLRRALEIEIDGarLFDSVQATWNLLEQSAGEAL---EEAHeaGMGVIVKEALANGRLTD---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 218 nttfpegdlRNDQAHFQgeqfkeniKKVNQLKPIAEKHNADTAHIVLAWYLARPEIDILIPGAKRADQLKDNMKAASITL 297
Cdd:cd19098 228 ---------RNPSPELA--------PLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSL 290
|
....*.
gi 494649899 298 SAEEIA 303
Cdd:cd19098 291 DLELLA 296
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
41-308 |
1.87e-22 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 94.90 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 41 VREAIKSGVTMLDTAYIYgvgRSEELIGEVLKE------CNREDVFIATKAAhrkegddfVFDNSPAFLKQSVEDSLKRL 114
Cdd:cd19155 31 VDTALEAGYRHIDTAYVY---RNEAAIGNVLKKwidsgkVKREELFIVTKLP--------PGGNRREKVEKFLLKSLEKL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 115 QTDYIDLFYIHFP---------------------DEHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQL---------KE 164
Cdd:cd19155 100 QLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMarilknariKP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 165 ANkdglvdvIQGEYNL-LNreaEKTFFPYTTEHGISFIPYFPLVSGLLAgKYDENTTFPEGDLRNDQAHfqgeqfkenik 243
Cdd:cd19155 180 AN-------LQVELHVyLQ---QKDLVDFCSTHSITVTAYAPLGSPGAA-HFSPGTGSPSGSSPDLLQD----------- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 244 kvNQLKPIAEKHNADTAHIVLAWYLARpeiDI-LIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19155 238 --PVVKAIAERHGKSPAQVLLRWLMQR---GVvVIPKSTNAARIKENFQVFDFELTEADMAKLSSL 298
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
38-308 |
3.37e-22 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 94.37 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 38 KELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC-------NREDVFIATK---AAHRKEgddfvfDNSPAFLKqsv 107
Cdd:cd19106 23 KAAVKYALDAGYRHIDCAAVYG---NEQEVGEALKEKvgpgkavPREDLFVTSKlwnTKHHPE------DVEPALRK--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 108 edSLKRLQTDYIDLFYIHFP------DEHTPKD-------------EAVQALNELKKEGKIRSIGVSNFSLEQLKEANKD 168
Cdd:cd19106 91 --TLKDLQLDYLDLYLIHWPyafergDNPFPKNpdgtirydsthykETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 169 GLVD--VIQGEYNllnreaektffPYTT---------EHGISFIPYFPLvsgllaGKYDENTTFPEGDLRNDQAhfqgeq 237
Cdd:cd19106 169 ARIKpaVLQVECH-----------PYLAqneliahckARGLVVTAYSPL------GSPDRPWAKPDEPVLLEEP------ 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494649899 238 fkenikkvnQLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19106 226 ---------KVKALAKKYNKSPAQILLRWQVQRGV--VVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDAL 285
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
38-308 |
8.63e-22 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 92.28 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 38 KELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKECN--REDVFIATKAAHRKEGDDFVfdnspaflKQSVEDSLKRLQ 115
Cdd:cd19130 26 QRAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASGipRDELFVTTKLWNDRHDGDEP--------AAAFAESLAKLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 116 TDYIDLFYIHFPdehTPKD----EAVQALNELKKEGKIRSIGVSNFSLEQLKE-ANKDGLVDVIQgEYNLLNREAEKTFF 190
Cdd:cd19130 95 LDQVDLYLVHWP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNFLPPHLERiVAATGVVPAVN-QIELHPAYQQRTIR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 191 PYTTEHGISFIPYFPLVSGLLAGkydenttfpegdlrnDQAhfqgeqfkenikkvnqLKPIAEKHNADTAHIVLAWYLAR 270
Cdd:cd19130 171 DWAQAHDVKIEAWSPLGQGKLLG---------------DPP----------------VGAIAAAHGKTPAQIVLRWHLQK 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 494649899 271 PEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19130 220 GH--VVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-308 |
1.05e-21 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 92.23 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 5 TIGKTDLKVFP-IGLGtnaVGGhnlypnLNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLK--ECNREDVFI 81
Cdd:cd19134 2 TVTLNDDNTMPvIGLG---VGE------LSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAasGIPRGELFV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 82 ATKAAHrkegDDFVFDNSPAFLKQSvedsLKRLQTDYIDLFYIHFPDEHTPKD-EAVQALNELKKEGKIRSIGVSNFSLE 160
Cdd:cd19134 70 TTKLAT----PDQGFTASQAACRAS----LERLGLDYVDLYLIHWPAGREGKYvDSWGGLMKLREEGLARSIGVSNFTAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 161 QLKE-ANKDGLVDVI-QGE-YNLLNREAEKTFfpyTTEHGISFIPYFPLVSGLLAgkydENttfpegdlrndqahfqgeq 237
Cdd:cd19134 142 HLENlIDLTFFTPAVnQIElHPLLNQAELRKV---NAQHGIVTQAYSPLGVGRLL----DN------------------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494649899 238 fkenikkvNQLKPIAEKHNADTAHIVLAWYLARPeiDILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19134 196 --------PAVTAIAAAHGRTPAQVLLRWSLQLG--NVVISRSSNPERIASNLDVFDFELTADHMDALDGL 256
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
22-206 |
2.95e-21 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 91.36 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 22 AVGGHNLYPNLNeeTGKELVREAIKSGVTMLDTAYIYgvgRSEELIGEVLKE------CNREDVFIATK---AAHRKEgd 92
Cdd:cd19129 8 ALGFGTLIPDPS--ATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEvfkagkIRREDLFVTTKlwnTNHRPE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 93 dfvfDNSPAFlkqsvEDSLKRLQTDYIDLFYIHFP------DEHTPKD--------------EAVQALNELKKEGKIRSI 152
Cdd:cd19129 81 ----RVKPAF-----EASLKRLQLDYLDLYLIHTPfafqpgDEQDPRDangnviyddgvtllDTWRAMERLVDEGRCKAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 153 GVSNFSLEQLKEANKDGLVD--VIQGEYNLLNREAEktFFPYTTEHGISFIPYFPL 206
Cdd:cd19129 152 GLSDVSLEKLREIFEAARIKpaVVQVESHPYLPEWE--LLDFCKNHGIVLQAFAPL 205
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
38-305 |
1.39e-20 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 89.78 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 38 KELVREAIKSGVTMLDTAYIYgvgRSEELIGEVLKE------CNREDVFIATK---AAHRKegddfvfdnspAFLKQSVE 108
Cdd:cd19107 20 TEAVKVAIDAGYRHIDCAYVY---QNENEVGEAIQEkikeqvVKREDLFIVSKlwcTFHEK-----------GLVKGACQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 109 DSLKRLQTDYIDLFYIHFP------DEHTPKDE-------------AVQALNELKKEGKIRSIGVSNFSLEQLKEA-NKD 168
Cdd:cd19107 86 KTLSDLKLDYLDLYLIHWPtgfkpgKELFPLDEsgnvipsdttfldTWEAMEELVDEGLVKAIGVSNFNHLQIERIlNKP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 169 GLvdviqgEYNLLNREAEktFFPYTTEH---------GISFIPYFPLvsgllaGKYDENTTFPEgdlrnDQAHFQGEQFK 239
Cdd:cd19107 166 GL------KYKPAVNQIE--CHPYLTQEkliqycqskGIVVTAYSPL------GSPDRPWAKPE-----DPSLLEDPKIK 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 240 EnikkvnqlkpIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFI 305
Cdd:cd19107 227 E----------IAAKHNKTTAQVLIRFPIQRNL--VVIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
16-170 |
1.63e-20 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 89.60 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 16 IGLGTNAvgghnlypnlNEETGKELVREAIK----SGVTMLDTAYIYGVgrsEELIGEVLKE------CNREDVFIATK- 84
Cdd:cd19108 14 LGFGTYA----------PEEVPKSKALEATKlaidAGFRHIDSAYLYQN---EEEVGQAIRSkiadgtVKREDIFYTSKl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 85 --AAHRkegddfvfdnsPAFLKQSVEDSLKRLQTDYIDLFYIHFP------DEHTPKDE-------AV------QALNEL 143
Cdd:cd19108 81 wcTFHR-----------PELVRPALEKSLKKLQLDYVDLYLIHFPvalkpgEELFPKDEngklifdTVdlcatwEAMEKC 149
|
170 180
....*....|....*....|....*...
gi 494649899 144 KKEGKIRSIGVSNFSLEQL-KEANKDGL 170
Cdd:cd19108 150 KDAGLAKSIGVSNFNRRQLeMILNKPGL 177
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
32-308 |
4.20e-20 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 88.31 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 32 LNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC------NREDVFIATKaahrkegddfVFDNSPAFLKQ 105
Cdd:cd19112 21 MEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAEAfktglvKREDLFITTK----------LWNSDHGHVIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 106 SVEDSLKRLQTDYIDLFYIHFP-----------------------DEHTPKDEAVQALNELKKEGKIRSIGVSNFSL--- 159
Cdd:cd19112 88 ACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYDIflt 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 160 -EQLKEANKDGLVDVIQgEYNLLNREaekTFFPYTTEHGISFIPYFPLvSGLLAGKYDENTTFPEGDlrndqahfqgeqf 238
Cdd:cd19112 168 rDCLAYSKIKPAVNQIE-THPYFQRD---SLVKFCQKHGISVTAHTPL-GGAAANAEWFGSVSPLDD------------- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 239 kenikkvNQLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19112 230 -------PVLKDLAKKYGKSAAQIVLRWGIQRNT--AVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSL 290
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-308 |
1.14e-19 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 86.82 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 9 TDLKVFPIGLGTNAVGGHNLypnlneetgKELVREAIKSGVTMLDTAYIYGvgrSEELIGEVLKEC-----NREDVFIAT 83
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEV---------KAAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEAiaggvKREDLFVTT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 84 K---AAHRKegddfvfdnspafLKQSVEDSLKRLQTDYIDLFYIHFP--------DEHTPKDE--------------AVQ 138
Cdd:cd19121 76 KlwsTYHRR-------------VELCLDRSLKSLGLDYVDLYLVHWPvllnpngnHDLFPTLPdgsrdldwdwnhvdTWK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 139 ALNELKKEGKIRSIGVSNFS---LEQ-LKEANKDGLVDVIQGEYNLLNREAEKtffpYTTEHGISFIPYFPLVSgllagk 214
Cdd:cd19121 143 QMEKVLKTGKTKAIGVSNYSipyLEElLKHATVVPAVNQVENHPYLPQQELVD----FCKEKGILIEAYSPLGS------ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 215 ydenTTFPegdlrndqahfqgeqfkenIKKVNQLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKaaS 294
Cdd:cd19121 213 ----TGSP-------------------LISDEPVVEIAKKHNVGPGTVLISYQVARGA--VVLPKSVTPDRIKSNLE--I 265
|
330
....*....|....
gi 494649899 295 ITLSAEEIAFIDKL 308
Cdd:cd19121 266 IDLDDEDMNKLNDI 279
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
32-308 |
3.18e-19 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 85.96 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 32 LNEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGE----VLKE--CNREDVFIATKaahrkegddfVFDN--SPAFL 103
Cdd:cd19113 21 LDNATAADQIYQAIKAGYRLFDGAEDYG---NEKEVGEgvnrAIDEglVKREELFLTSK----------LWNNfhDPKNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 104 KQSVEDSLKRLQTDYIDLFYIHFP-------------------------DEHTPKDEAVQALNELKKEGKIRSIGVSNFS 158
Cdd:cd19113 88 ETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPILDTWKALEKLVDAGKIKSIGVSNFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 159 ----LEQLKEAN-KDGLVDVIQGEYNLLNREAEktffpYTTEHGISFIPY--FPLVSGLlagkydenttfpegDLRNDQA 231
Cdd:cd19113 168 galiLDLLRGATiKPAVLQIEHHPYLQQPKLIE-----YAQKAGITITAYssFGPQSFV--------------ELNQGRA 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494649899 232 HFQGEQFKENIkkvnqLKPIAEKHNADTAHIVLAWYLARpEIDIlIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19113 229 LNTPTLFEHDT-----IKSIAAKHNKTPAQVLLRWATQR-GIAV-IPKSNLPERLLQNLSVNDFDLTKEDFEEIAKL 298
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
37-308 |
5.06e-19 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 85.30 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 37 GKELVREAIKSGVTMLDTAYIYG----VGRS-EELIGEVLkeCNREDVFIATK---AAHRKEgddfvfDNSPAFLKQsve 108
Cdd:cd19114 19 TEEVIYNAIKVGYRLIDGALLYGneaeVGRGiRKAIQEGL--VKREDLFIVTKlwnNFHGKD------HVREAFDRQ--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 109 dsLKRLQTDYIDLFYIHFPD-------------------------EHTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLK 163
Cdd:cd19114 88 --LKDYGLDYIDLYLIHFPIpaayvdpaenypflwkdkelkkfplEQSPMQECWREMEKLVDAGLVRNIGIANFNVQLIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 164 EANKDGLV--DVIQGEYN-LLNREaekTFFPYTTEHGISFIPYfplvSGLLAGKYDenttfpegDLRNDQAHFQgeqfke 240
Cdd:cd19114 166 DLLTYAKIkpAVLQIEHHpYLQQK---RLIDWAKKQGIQITAY----SSFGNAVYT--------KVTKHLKHFT------ 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494649899 241 NIKKVNQLKPIAEKHNADTAHIVLAWYLARpEIdILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19114 225 NLLEHPVVKKLADKHKRDTGQVLLRWAVQR-NI-TVIPKSVNVERMKTNLDITSYKLDEEDMEALYEL 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
41-308 |
1.92e-18 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 83.44 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 41 VREAIKSGVTMLDTAYIY-GVGRSEELIGEVLKE---CNREDVFIATKA-AHRKEGDDfvfdnspafLKQSVEDSLKRLQ 115
Cdd:cd19122 30 VTKALDVGYRHLDCAWFYlNEDEVGDAVRDFLKEnpsVKREDLFICTKVwNHLHEPED---------VKWSIDNSLKNLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 116 TDYIDLFYIHFP------DEHTPK-----------------DEAVQALNELKKEGKIRSIGVSNFSLEQLKE----ANKD 168
Cdd:cd19122 101 LDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRAMEEIYESGKAKAIGVSNWTIPGLKKllsfAKVK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 169 GLVDVIQGEYNLLNREaektFFPYTTEHGISFIPYFPLVSgllagkydenttfpegdlrNDQAHFQGEQFKENikkvNQL 248
Cdd:cd19122 181 PHVNQIEIHPFLPNEE----LVDYCFSNDILPEAYSPLGS-------------------QNQVPSTGERVSEN----PTL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 249 KPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKaaSITLSAEEIAFIDKL 308
Cdd:cd19122 234 NEVAEKGGYSLAQVLIAWGLRRGY--VVLPKSSTPSRIESNFK--SIELSDEDFEAINQV 289
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
36-308 |
6.44e-18 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 82.54 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 36 TGKELVREAIKSGVTMLDTAYIYgvgRSEELIGEVLKE------CNREDVFIATKAahrkegddFVFDNSPAFLKQSVED 109
Cdd:cd19109 22 ACAEAVKVAIDTGYRHIDGAYIY---QNEHEVGQAIREkiaegkVKREDIFYCGKL--------WNTCHPPELVRPTLER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 110 SLKRLQTDYIDLFYIHFP------DEHTPKDE-------------AVQALNELKKEGKIRSIGVSNFSLEQLKEA-NKDG 169
Cdd:cd19109 91 TLKVLQLDYVDLYIIEMPmafkpgDEIYPRDEngkwlyhktnlcaTWEALEACKDAGLVKSIGVSNFNRRQLELIlNKPG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 170 LvdviqgEYNLLNREAE-------KTFFPYTTEHGISFIPYFPLvsGLLAGKYDENTTFPEgdLRNDQAhfqgeqfkeni 242
Cdd:cd19109 171 L------KHKPVSNQVEchpyftqPKLLEFCQQHDIVIVAYSPL--GTCRDPIWVNVSSPP--LLEDPL----------- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494649899 243 kkvnqLKPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19109 230 -----LNSIGKKYNKTAAQVVLRFNIQRGV--VVIPKSFNPERIKENFQIFDFSLTEEEMKDIEAL 288
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
39-302 |
2.95e-17 |
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AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 80.39 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 39 ELVREAIKSGVTMLDTAYIY------GVGRSEELIGEVLKecnREDVFIATK---AAHRKegddfvfdnspAFLKQSVED 109
Cdd:cd19110 21 EAVKVAIDAGYRHFDCAYLYhnesevGAGIREKIKEGVVR---REDLFIVSKlwcTCHKK-----------SLVKTACTR 86
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 110 SLKRLQTDYIDLFYIHFP------------DE-------HTPKDEAVQALNELKKEGKIRSIGVSNFSLEQLKE-ANKDG 169
Cdd:cd19110 87 SLKALKLNYLDLYLIHWPmgfkpgepdlplDRsgmvipsDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERlLNKPG 166
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 170 L-VDVIQGEYNLLNREAEKTFFPYTTEHGISFIPYFPLvsgllaGKYDENTtfpegDLRNDQAhfqgeqfkenikkvnqL 248
Cdd:cd19110 167 LrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPL------GGSCEGV-----DLIDDPV----------------I 219
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 494649899 249 KPIAEKHNADTAHIVLAWYLARPEidILIPGAKRADQLKDNMKAASITLSAEEI 302
Cdd:cd19110 220 QRIAKKHGKSPAQILIRFQIQRNV--IVIPKSVTPSRIKENIQVFDFELTEHDM 271
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| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
33-308 |
2.57e-14 |
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AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 72.07 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 33 NEETGKELVREAIKSGVTMLDTAYIYGvgrSEELIGE----VLKE--CNREDVFIATKAAHRKEGDDFVfdnSPAFLKQs 106
Cdd:cd19115 24 NNDTCADQVYNAIKAGYRLFDGACDYG---NEVEAGQgvarAIKEgiVKREDLFIVSKLWNTFHDGERV---EPICRKQ- 96
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 107 vedsLKRLQTDYIDLFYIHFP--------------------DEHTPKDEAVQ----ALNELKKEGKIRSIGVSNFSLEQL 162
Cdd:cd19115 97 ----LADWGIDYFDLFLIHFPialkyvdpavryppgwfydgKKVEFSNAPIQetwtAMEKLVDKGLARSIGVSNFSAQLL 172
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494649899 163 KEANKDGLV--DVIQGEYNllnreaektffPYTTEHGIsfIPYFPLvSGLLAGKYdenTTF-PEG--DLRNDQAHFQGEQ 237
Cdd:cd19115 173 MDLLRYARIrpATLQIEHH-----------PYLTQPRL--VKYAQK-EGIAVTAY---SSFgPQSflELDLPGAKDTPPL 235
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250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494649899 238 FKENIkkvnqLKPIAEKHNADTAHIVLAWYLARpEIDIlIPGAKRADQLKDNMKAASITLSAEEIAFIDKL 308
Cdd:cd19115 236 FEHDV-----IKSIAEKHGKTPAQVLLRWATQR-GIAV-IPKSNNPKRLAQNLDVTGFDLEAEEIKAISAL 299
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