|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
1-449 |
7.23e-121 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 360.36 E-value: 7.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 1 MLTSLVSAVGsHHVTTDPDVLAGRSVDHTGRYRGRASALVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAGTVPEHD 80
Cdd:COG0277 6 LLAALRAILA-GRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 81 DVLLSTERLCVVSDVDTVERRIEIGAGVTLAAVQHAASTAGLVFGVDLSARDTATVGGMASTNAGGLRTVRYGNMGEQVV 160
Cdd:COG0277 85 GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 161 GLDVALPDGTVLRRHSRVRRDNTGYDLPALFVGAEGTLGVITALDLRLHPTPSHRVTAVCGFAELAALVDA-GRMFRDVE 239
Cdd:COG0277 165 GLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAvRALLAAGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 240 GIAALELIDGRAAALTREHLGVRPPVEADWLLLVELAADHDQT--DRLADLLGGARMCGEPAVGV--DAAAQQRLWRTRE 315
Cdd:COG0277 245 APAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDDAEEveAQLARLRAILEAGGATDVRVaaDGAERERLWKARK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 316 SLAEVLGVYGPPLKF--DVSLPLSAISGFARDAVALVHRHvpdspEALPLLFGHIGEGNLHLNVLRCPPDREP-----AL 388
Cdd:COG0277 325 AALPALGRLDGGAKLleDVAVPPSRLPELLRELGALAAKY-----GLRATAFGHAGDGNLHVRILFDPADPEEverarAA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607303 389 YAKMMGLIAECGGNVSSEHGVGSRKRAYLGMSRQANDVAAMRRVKAALDPTGYLNAAVLFD 449
Cdd:COG0277 400 AEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
211-443 |
3.90e-58 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 191.37 E-value: 3.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 211 TPSHRVTAVCGFAELAALVDAGRMFRDV-EGIAALELIDGRAAALTREHLGV--RPPVEADWLLLVELAADHDQTDR--- 284
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAgIIPAALELMDNDALDLVEATLGFpkGLPRDAAALLLVEFEGDDEETAEeel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 285 --LADLLGGArMCGEPAVGVDAAAQQRLWRTRESLAE----VLGVYGPPLKFDVSLPLSAISGFARDAVALVHRHvpdsp 358
Cdd:pfam02913 81 eaVEAILEAG-GAGDVVVATDEAEAERLWAARKYALPlrdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKY----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 359 EALPLLFGHIGEGNLHLNVL-----RCPPDREPALYAKMMGLIAECGGNVSSEHGVGSRKRAYLGMSRQANDVAAMRRVK 433
Cdd:pfam02913 155 GLVVCLFGHAGDGNLHLYILfdfrdPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIK 234
|
250
....*....|
gi 15607303 434 AALDPTGYLN 443
Cdd:pfam02913 235 AAFDPKGILN 244
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
39-447 |
1.16e-44 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 163.64 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 39 LVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAGTVPEH-----DDVLLSTERLCVVSDVDTVerrieIGAGVTLAAV 113
Cdd:PLN02805 137 VVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHggvciDMSLMKSVKALHVEDMDVV-----VEPGIGWLEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 114 QHAASTAGLVFGVDLSArdTATVGGMASTNAGGLRTVRYGNMGEQVVGLDVALPDGTVLRRHSRVRRDNTGYDLPALFVG 193
Cdd:PLN02805 212 NEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 194 AEGTLGVITALDLRLHPTPSHRVTAVCGFAEL--AALVDAGRMFRDVEgIAALELID---------------GRAAALTR 256
Cdd:PLN02805 290 SEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIkdAADVAIATMLSGIQ-VSRVELLDevqirainmangknlPEAPTLMF 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 257 EHLGVRPPVEADWLLLVELAADHDQTDRLadllggarmcgepaVGVDAAAQQRLWRTRESLAEVLGVYGPPLKF---DVS 333
Cdd:PLN02805 369 EFIGTEAYAREQTLIVQKIASKHNGSDFV--------------FAEEPEAKKELWKIRKEALWACFAMEPKYEAmitDVC 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 334 LPLSAISgfarDAVALVHRHVPDSPEALPLLfGHIGEGNLHLNVLRCPPDREPALYAK-----MMGLIAECGGNVSSEHG 408
Cdd:PLN02805 435 VPLSHLA----ELISRSKKELDASPLVCTVI-AHAGDGNFHTIILFDPSQEDQRREAErlnhfMVHTALSMEGTCTGEHG 509
|
410 420 430
....*....|....*....|....*....|....*....
gi 15607303 409 VGSRKRAYLGMSRQANDVAAMRRVKAALDPTGYLNAAVL 447
Cdd:PLN02805 510 VGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKL 548
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
35-217 |
1.10e-06 |
|
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
Pssm-ID: 273750 [Multi-domain] Cd Length: 557 Bit Score: 51.02 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 35 RASALVRPGSAEEVAEVLRVCRDAGAYVTVqggrTSLVAGTVPE-------HDDVLLSTERLCVVSDVDTVERRIEIGAG 107
Cdd:TIGR01677 31 RAANVAYPKTEAELVSVVAAATAAGRKMKV----VTRYSHSIPKlacpdgsDGALLISTKRLNHVVAVDATAMTVTVESG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 108 VTLAAVQHAASTAGLVFGVDlSARDTATVGGMASTNA-GGLRTVRYGNMGEQVVGLDVALPdGTVLRRHSRVRRDNTGyD 186
Cdd:TIGR01677 107 MSLRELIVEAEKAGLALPYA-PYWWGLTVGGMMGTGAhGSSLWGKGSAVHDYVVGIRLVVP-ASAAEGFAKVRILSEG-D 183
|
170 180 190
....*....|....*....|....*....|....
gi 15607303 187 LPALFVGAE---GTLGVITALDLRLHPTPSHRVT 217
Cdd:TIGR01677 184 TPNEFNAAKvslGVLGVISQVTLALQPMFKRSVT 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
1-449 |
7.23e-121 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 360.36 E-value: 7.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 1 MLTSLVSAVGsHHVTTDPDVLAGRSVDHTGRYRGRASALVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAGTVPEHD 80
Cdd:COG0277 6 LLAALRAILA-GRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 81 DVLLSTERLCVVSDVDTVERRIEIGAGVTLAAVQHAASTAGLVFGVDLSARDTATVGGMASTNAGGLRTVRYGNMGEQVV 160
Cdd:COG0277 85 GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 161 GLDVALPDGTVLRRHSRVRRDNTGYDLPALFVGAEGTLGVITALDLRLHPTPSHRVTAVCGFAELAALVDA-GRMFRDVE 239
Cdd:COG0277 165 GLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAvRALLAAGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 240 GIAALELIDGRAAALTREHLGVRPPVEADWLLLVELAADHDQT--DRLADLLGGARMCGEPAVGV--DAAAQQRLWRTRE 315
Cdd:COG0277 245 APAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDDAEEveAQLARLRAILEAGGATDVRVaaDGAERERLWKARK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 316 SLAEVLGVYGPPLKF--DVSLPLSAISGFARDAVALVHRHvpdspEALPLLFGHIGEGNLHLNVLRCPPDREP-----AL 388
Cdd:COG0277 325 AALPALGRLDGGAKLleDVAVPPSRLPELLRELGALAAKY-----GLRATAFGHAGDGNLHVRILFDPADPEEverarAA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607303 389 YAKMMGLIAECGGNVSSEHGVGSRKRAYLGMSRQANDVAAMRRVKAALDPTGYLNAAVLFD 449
Cdd:COG0277 400 AEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
211-443 |
3.90e-58 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 191.37 E-value: 3.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 211 TPSHRVTAVCGFAELAALVDAGRMFRDV-EGIAALELIDGRAAALTREHLGV--RPPVEADWLLLVELAADHDQTDR--- 284
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAgIIPAALELMDNDALDLVEATLGFpkGLPRDAAALLLVEFEGDDEETAEeel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 285 --LADLLGGArMCGEPAVGVDAAAQQRLWRTRESLAE----VLGVYGPPLKFDVSLPLSAISGFARDAVALVHRHvpdsp 358
Cdd:pfam02913 81 eaVEAILEAG-GAGDVVVATDEAEAERLWAARKYALPlrdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKY----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 359 EALPLLFGHIGEGNLHLNVL-----RCPPDREPALYAKMMGLIAECGGNVSSEHGVGSRKRAYLGMSRQANDVAAMRRVK 433
Cdd:pfam02913 155 GLVVCLFGHAGDGNLHLYILfdfrdPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIK 234
|
250
....*....|
gi 15607303 434 AALDPTGYLN 443
Cdd:pfam02913 235 AAFDPKGILN 244
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
39-447 |
1.16e-44 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 163.64 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 39 LVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAGTVPEH-----DDVLLSTERLCVVSDVDTVerrieIGAGVTLAAV 113
Cdd:PLN02805 137 VVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHggvciDMSLMKSVKALHVEDMDVV-----VEPGIGWLEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 114 QHAASTAGLVFGVDLSArdTATVGGMASTNAGGLRTVRYGNMGEQVVGLDVALPDGTVLRRHSRVRRDNTGYDLPALFVG 193
Cdd:PLN02805 212 NEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 194 AEGTLGVITALDLRLHPTPSHRVTAVCGFAEL--AALVDAGRMFRDVEgIAALELID---------------GRAAALTR 256
Cdd:PLN02805 290 SEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIkdAADVAIATMLSGIQ-VSRVELLDevqirainmangknlPEAPTLMF 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 257 EHLGVRPPVEADWLLLVELAADHDQTDRLadllggarmcgepaVGVDAAAQQRLWRTRESLAEVLGVYGPPLKF---DVS 333
Cdd:PLN02805 369 EFIGTEAYAREQTLIVQKIASKHNGSDFV--------------FAEEPEAKKELWKIRKEALWACFAMEPKYEAmitDVC 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 334 LPLSAISgfarDAVALVHRHVPDSPEALPLLfGHIGEGNLHLNVLRCPPDREPALYAK-----MMGLIAECGGNVSSEHG 408
Cdd:PLN02805 435 VPLSHLA----ELISRSKKELDASPLVCTVI-AHAGDGNFHTIILFDPSQEDQRREAErlnhfMVHTALSMEGTCTGEHG 509
|
410 420 430
....*....|....*....|....*....|....*....
gi 15607303 409 VGSRKRAYLGMSRQANDVAAMRRVKAALDPTGYLNAAVL 447
Cdd:PLN02805 510 VGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKL 548
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
36-173 |
3.33e-37 |
|
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: 132.71 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 36 ASALVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAGTVPEhDDVLLSTERLCVVSDVDTVERRIEIGAGVTLAAVQH 115
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQT-GGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607303 116 AASTAGLVFGVDLSARDTATVGGMASTNAGGLRTVRYGNMGEQVVGLDVALPDGTVLR 173
Cdd:pfam01565 80 ALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVR 137
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
32-443 |
3.44e-36 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 139.14 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 32 YRGRASALVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAGTVPEHDDVLLSTERLCVVSDVDTVERRIEIGAGVTLA 111
Cdd:PRK11230 52 YRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVLLVMARFNRILDINPVGRRARVQPGVRNL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 112 AVQHAASTAGLVFGVDLSARDTATVGGMASTNAGGLRTVRYGNMGEQVVGLDVALPDGTVLRRHSRVrRDNTGYDLPALF 191
Cdd:PRK11230 132 AISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSDA-LDSPGFDLLALF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 192 VGAEGTLGVITALDLRLHPTPShrvTAVCGFAELAALVDAGRMFRDVegIAA------LELIDGRAAALTREHLGVRPPV 265
Cdd:PRK11230 211 TGSEGMLGVVTEVTVKLLPKPP---VARVLLASFDSVEKAGLAVGDI--IAAgiipggLEMMDNLSIRAAEDFIHAGYPV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 266 EADWLLLVEL---AAD-HDQTDRLADLL--GGARmcgEPAVGVDAAAQQRLWRTRESLAEVLGVYGPPLK-FDVSLPLSA 338
Cdd:PRK11230 286 DAEAILLCELdgvESDvQEDCERVNDILlkAGAT---DVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYcMDGTIPRRE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 339 ISGFARDAVALVHRHvpdspeALPL--LFgHIGEGNLHLNVL---RCPP--DREPALYAKMMGLIAECGGNVSSEHGVGS 411
Cdd:PRK11230 363 LPGVLEGIARLSQQY------GLRVanVF-HAGDGNMHPLILfdaNEPGelERAEALGGKILELCVEVGGSITGEHGVGR 435
|
410 420 430
....*....|....*....|....*....|..
gi 15607303 412 RKRAYLGMSRQANDVAAMRRVKAALDPTGYLN 443
Cdd:PRK11230 436 EKINQMCAQFNSDEITLFHAVKAAFDPDGLLN 467
|
|
| PRK11183 |
PRK11183 |
D-lactate dehydrogenase; Provisional |
2-89 |
1.01e-09 |
|
D-lactate dehydrogenase; Provisional
Pssm-ID: 236872 [Multi-domain] Cd Length: 564 Bit Score: 60.63 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 2 LTSLVSAVGSHHVTTDPDvlagrsvdHTGRYR-------GRASALVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAG 74
Cdd:PRK11183 6 INELTRIVGSSHVLTDPA--------KTERYRkgfrsgqGDALAVVFPGTLLELWRVLQACVAADKIIIMQAANTGLTGG 77
|
90 100
....*....|....*....|
gi 15607303 75 TVPEHDD-----VLLSTERL 89
Cdd:PRK11183 78 STPNGNDydrdiVIISTLRL 97
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
35-217 |
1.10e-06 |
|
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
Pssm-ID: 273750 [Multi-domain] Cd Length: 557 Bit Score: 51.02 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 35 RASALVRPGSAEEVAEVLRVCRDAGAYVTVqggrTSLVAGTVPE-------HDDVLLSTERLCVVSDVDTVERRIEIGAG 107
Cdd:TIGR01677 31 RAANVAYPKTEAELVSVVAAATAAGRKMKV----VTRYSHSIPKlacpdgsDGALLISTKRLNHVVAVDATAMTVTVESG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 108 VTLAAVQHAASTAGLVFGVDlSARDTATVGGMASTNA-GGLRTVRYGNMGEQVVGLDVALPdGTVLRRHSRVRRDNTGyD 186
Cdd:TIGR01677 107 MSLRELIVEAEKAGLALPYA-PYWWGLTVGGMMGTGAhGSSLWGKGSAVHDYVVGIRLVVP-ASAAEGFAKVRILSEG-D 183
|
170 180 190
....*....|....*....|....*....|....
gi 15607303 187 LPALFVGAE---GTLGVITALDLRLHPTPSHRVT 217
Cdd:TIGR01677 184 TPNEFNAAKvslGVLGVISQVTLALQPMFKRSVT 217
|
|
| PRK14652 |
PRK14652 |
UDP-N-acetylmuramate dehydrogenase; |
31-210 |
6.19e-06 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237777 [Multi-domain] Cd Length: 302 Bit Score: 47.94 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 31 RYRGRASALVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSLVAGTVPEHDDVL-LSTERLCVVSDvdtvERRIEIGAGVT 109
Cdd:PRK14652 31 RVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLrLPQDFPGESTD----GGRLVLGAGAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 110 LAAVQHAASTAGLVfGVDLSARDTATVGGMASTNAGglrtVRYGNMGEQVVGLDVALPDGTVLRRHSRVRRDNTGYDLPA 189
Cdd:PRK14652 107 ISRLPARAHAHGLV-GMEFLAGIPGTLGGAVAMNAG----TKLGEMKDVVTAVELATADGAGFVPAAALGYAYRTCRLPP 181
|
170 180
....*....|....*....|.
gi 15607303 190 lfvgaegtLGVITALDLRLHP 210
Cdd:PRK14652 182 --------GAVITRVEVRLRP 194
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
30-210 |
9.09e-06 |
|
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: 47.97 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 30 GRYRGRASALVRPGSAEEVAEVLRVCRDAGAYVTVQGG--RTSLVAGTvpehDDVLLSTERLCVVSDVDTVERRIEIGAG 107
Cdd:TIGR01678 9 KTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGghSPSDIACT----DGFLIHLDKMNKVLQFDKEKKQITVEAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 108 VTLAAVQHAASTAGLVFGVDLSARDTaTVGGMASTNAGGlRTVRYGNMGEQVVGLDVALPDGTVLrrhsRVRRDNTgydl 187
Cdd:TIGR01678 85 IRLYQLHEQLDEHGYSMSNLGSISEV-SVAGIISTGTHG-SSIKHGILATQVVALTIMTADGEVL----ECSEERN---- 154
|
170 180
....*....|....*....|....*.
gi 15607303 188 PALFVGAE---GTLGVITALDLRLHP 210
Cdd:TIGR01678 155 ADVFQAARvslGCLGIIVTVTIQVVP 180
|
|
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
34-248 |
2.84e-05 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 45.87 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 34 GRASALVRPGSAEEVAEVLRVCRDAGAYVTVQGGRTSL------VAGTVpehddvlLSTERLCvvSDVDTVERRIEIGAG 107
Cdd:PRK13905 29 GPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLlvrdggIRGVV-------IRLGKGL--NEIEVEGNRITAGAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 108 VTLAAVQHAASTAGLV---F-----GvdlsardtaTVGGMASTNAGGlrtvrYG-NMGEQVVGLDVALPDGTVLR----- 173
Cdd:PRK13905 100 APLIKLARFAAEAGLSgleFaagipG---------TVGGAVFMNAGA-----YGgETADVLESVEVLDRDGEIKTlsnee 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 174 -----RHSRVRRDNtGYDLPALFVGAEGTLGVITA-----LDLRL--HPT--PShrvtavcgfaelaalvdAGRMFRDVE 239
Cdd:PRK13905 166 lgfgyRHSALQEEG-LIVLSATFQLEPGDKEEIKArmdelLARREatQPLeyPS-----------------AGSVFKNPP 227
|
....*....
gi 15607303 240 GIAALELID 248
Cdd:PRK13905 228 GHFAGKLIE 236
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
132-228 |
2.40e-04 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 42.90 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607303 132 DTATVGGMASTNAGGLRTVRYGNMGEQVVGLDVALPDGTVLRRHSRVRRDNTGYDLPALFVGAEGTLGVITALDLRLHPT 211
Cdd:PRK11282 90 GGATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRFGGQVMKNVAGYDVSRLMAGSLGTLGVLLEVSLKVLPR 169
|
90
....*....|....*..
gi 15607303 212 PSHRVTAVCGFAELAAL 228
Cdd:PRK11282 170 PRAELTLRLEMDAAEAL 186
|
|
| |
