|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
73-531 |
7.22e-137 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 404.28 E-value: 7.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 73 VTQEDLSFFRALLPGRTITDPDLLKSSNVDWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVP 152
Cdd:COG0277 2 LTAALLAALRAILAGRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 153 VFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRG 232
Cdd:COG0277 82 LDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 233 TVLGLEVVLADGRVLNCLATLRKDNTGYDLKQLFIGSEGTLGVITAVSI-LCPrKPKAVNVAFLGCSSFQQLLETFQCCR 311
Cdd:COG0277 162 NVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLrLHP-LPEAVATALVAFPDLEAAAAAVRALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 312 GMlGEILSAFEFLDASCMNLLEKHLKLTNPiTECPFYIVIETAGSNATHDEEKLHQfLEEVMTSSLVTDGTVATEATKIK 391
Cdd:COG0277 241 AA-GIAPAALELMDRAALALVEAAPPLGLP-EDGGALLLVEFDGDDAEEVEAQLAR-LRAILEAGGATDVRVAADGAERE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 392 ALWSLRERVTEALTHE--GYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNITSPSKDFALLAAIE 469
Cdd:COG0277 318 RLWKARKAALPALGRLdgGAKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERAR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528471683 470 PY---VYEWTSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDN 531
Cdd:COG0277 398 AAaeeIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
286-526 |
6.03e-64 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 208.71 E-value: 6.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 286 KPKAVNVAFLGCSSFQQLLETFQCCRGMlGEILSAFEFLDASCMNLLEKHLKLTN-PITECPFYIVIETAGSNATHDEEK 364
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARA-GIIPAALELMDNDALDLVEATLGFPKgLPRDAAALLLVEFEGDDEETAEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 365 LhQFLEEVMTSSLVTDGTVATEATKIKALWSLRERVTE----ALTHEGYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNV 440
Cdd:pfam02913 80 L-EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPlrdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 441 VGYGHVGDGNLHLNITSPSKDFALLAAIEPYVYEW---TSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLD 517
Cdd:pfam02913 159 CLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEImdlALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFD 238
|
....*....
gi 528471683 518 PKGILNPYK 526
Cdd:pfam02913 239 PKGILNPGK 247
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
112-532 |
3.75e-46 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 169.80 E-value: 3.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 112 DVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHY 191
Cdd:PLN02805 135 DVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEY 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 192 LEERDFIMPLDLGAKGSchIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGRVLNCLATLRKDNTGYDLKQLFIGSEG 271
Cdd:PLN02805 215 LEPYGLFFPLDPGPGAT--IGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 272 TLGVITAVSILCPRKPKAVNVAFLGCSSFQQLLETfqCCRGMLGEI-LSAFEFLDascmnllEKHLKLTN-----PITEC 345
Cdd:PLN02805 293 TLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADV--AIATMLSGIqVSRVELLD-------EVQIRAINmangkNLPEA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 346 PfYIVIETAGSNATHDEEKLhqFLEEVMTSSLVTDGTVATEATKIKALWSLRErvtEAL--------THEGYTykYDISL 417
Cdd:PLN02805 364 P-TLMFEFIGTEAYAREQTL--IVQKIASKHNGSDFVFAEEPEAKKELWKIRK---EALwacfamepKYEAMI--TDVCV 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 418 PVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNIT-SPSKDFALLAA--IEPYVYEWTSQWKGSISAEHGLGLKKR 494
Cdd:PLN02805 436 PLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILfDPSQEDQRREAerLNHFMVHTALSMEGTCTGEHGVGTGKM 515
|
410 420 430
....*....|....*....|....*....|....*...
gi 528471683 495 NYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDNI 532
Cdd:PLN02805 516 KYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPPHV 553
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
112-249 |
6.50e-40 |
|
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 426326 [Multi-domain] Cd Length: 139 Bit Score: 141.18 E-value: 6.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 112 DVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPvFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHY 191
Cdd:pfam01565 2 AAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQ-TGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528471683 192 LEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGRVLNC 249
Cdd:pfam01565 81 LAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRL 138
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
78-529 |
3.94e-35 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 137.99 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 78 LSFFRALLPGRTIT-DPDLLKSSNVDWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDE 156
Cdd:PRK11230 22 LMALREHLPGLEILhTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 157 IILSTSLMNQVFAFDNISGILTCQAGcvLENL--SHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRGTV 234
Cdd:PRK11230 102 VLLVMARFNRILDINPVGRRARVQPG--VRNLaiSQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 235 LGLEVVLADGRVLNcLATLRKDNTGYDLKQLFIGSEGTLGVITAVSILCPRKPKAVNVaflgcssfqqLLETFQCCR--- 311
Cdd:PRK11230 180 LKVEILTLDGEALT-LGSDALDSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARV----------LLASFDSVEkag 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 312 GMLGEILSA------FEFLDASCMNLLEKHLKLTNPItECPFYIVIETAGSNATHDEEKLHqfLEEVMTSSLVTDGTVAT 385
Cdd:PRK11230 249 LAVGDIIAAgiipggLEMMDNLSIRAAEDFIHAGYPV-DAEAILLCELDGVESDVQEDCER--VNDILLKAGATDVRLAQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 386 EATKIKALWSLRERVTEAL--THEGYtYKYDISLP---VEKIYDLVQDMRRHLGGMAKNVVgygHVGDGNLH----LNIT 456
Cdd:PRK11230 326 DEAERVRFWAGRKNAFPAVgrISPDY-YCMDGTIPrreLPGVLEGIARLSQQYGLRVANVF---HAGDGNMHplilFDAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528471683 457 SPSkDFALLAAIEPYVYEWTSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLP 529
Cdd:PRK11230 402 EPG-ELERAEALGGKILELCVEVGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGKNIP 473
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
102-283 |
3.47e-13 |
|
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 71.47 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 102 DWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGntGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQA 181
Cdd:TIGR01678 6 NWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGG--GHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQITVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 182 GCVLENLSHYLEERDFIMPlDLGAKGSCHIGGNVSTNAGGLRlLRYGSLRGTVLGLEVVLADGRVLNCLATLRKdntgyD 261
Cdd:TIGR01678 84 GIRLYQLHEQLDEHGYSMS-NLGSISEVSVAGIISTGTHGSS-IKHGILATQVVALTIMTADGEVLECSEERNA-----D 156
|
170 180
....*....|....*....|..
gi 528471683 262 LKQLFIGSEGTLGVITAVSILC 283
Cdd:TIGR01678 157 VFQAARVSLGCLGIIVTVTIQV 178
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
176-281 |
2.59e-05 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 46.37 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 176 ILTCQAGCVLENLSHYLEERDFIMPL---DLGAKGSchIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGRVLNCLAT 252
Cdd:PRK11282 58 VITARAGTPLAELEAALAEAGQMLPFeppHFGGGAT--LGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRFGGQ 135
|
90 100
....*....|....*....|....*....
gi 528471683 253 LRKDNTGYDLKQLFIGSEGTLGVITAVSI 281
Cdd:PRK11282 136 VMKNVAGYDVSRLMAGSLGTLGVLLEVSL 164
|
|
| PRK11183 |
PRK11183 |
D-lactate dehydrogenase; Provisional |
109-221 |
6.28e-05 |
|
D-lactate dehydrogenase; Provisional
Pssm-ID: 236872 [Multi-domain] Cd Length: 564 Bit Score: 45.60 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 109 GSSDVL--LRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDE-----IILSTSLMNQVFAFDNISGILtCQA 181
Cdd:PRK11183 35 GQGDALavVFPGTLLELWRVLQACVAADKIIIMQAANTGLTGGSTPNGNDydrdiVIISTLRLDKIQLLNNGKQVL-ALP 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 528471683 182 GCVLENLSHYLeerdfimpLDLGAK-----GSCHIG----GNVSTNAGG 221
Cdd:PRK11183 114 GTTLYQLEKAL--------KPLGREphsviGSSCIGasviGGICNNSGG 154
|
|
|