|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
200-652 |
2.05e-101 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 317.22 E-value: 2.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 200 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVE 279
Cdd:COG0277 34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 280 AGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRG-IIEKSCQGPRMSTGP 358
Cdd:COG0277 110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGeVVRTGGRVPKNVTGY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 359 DIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPqvss 438
Cdd:COG0277 190 DLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 439 iftsfldglkkfyitkfKGFDPNQLSVATLLFEGDREKVLQHE-KQVYDIAAKFGGLAAG--EDNGQRGYL---LTYVIA 512
Cdd:COG0277 266 -----------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGATDVRvaADGAERERLwkaRKAALP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 513 YIRDLALEYYVLgesFETSAPWDRVVDLCRnvkeRITRECKEKGVQFAPFStcrvtqtyDAG-ACIYFYFAFNyRGISDP 591
Cdd:COG0277 329 ALGRLDGGAKLL---EDVAVPPSRLPELLR----ELGALAAKYGLRATAFG--------HAGdGNLHVRILFD-PADPEE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4501993 592 LTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIF 652
Cdd:COG0277 393 VERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGIL 453
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
385-657 |
6.43e-56 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 190.22 E-value: 6.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 385 PEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVssiftsfldglkkfyitkfKGFDPNQLS 464
Cdd:pfam02913 2 PEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 465 VATLLFEGDREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYLLTYVIAyIRDLALEYYVLGESFETSAPWDR 536
Cdd:pfam02913 63 LLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 537 VVDLCRNVKERITRECkekgvqfapFSTCRVTQTYDAGACIYFYFAFNYRGISDPL-TVFEQTeaaaREEILANGGSLSH 615
Cdd:pfam02913 140 LADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEERAeKLFDEI----MDLALELGGSISG 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 4501993 616 HHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNL 657
Cdd:pfam02913 207 EHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
205-651 |
3.43e-29 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 122.42 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 205 IPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVEAGITG 284
Cdd:PLN02805 133 IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGG----VCIDMSLMKSVKALHVEDMDVVVEPGIGW 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 285 QELERQLKESGYCTGHEPDSleFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMST-GPDIHHF 363
Cdd:PLN02805 209 LELNEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAaGYDLTRL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 364 IMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGvaclreiakqrcAPASIRLMDNkqfqfghalKPQVSSIftSF 443
Cdd:PLN02805 287 VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDA------------ADVAIATMLS---------GIQVSRV--EL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 444 LDGLKKFYITKFKGfdPNQLSVATLLFE--GDREKVLQHEKQVYDIAAKFGG--LAAGEDNGQRGYLLTyviayIRDLAL 519
Cdd:PLN02805 344 LDEVQIRAINMANG--KNLPEAPTLMFEfiGTEAYAREQTLIVQKIASKHNGsdFVFAEEPEAKKELWK-----IRKEAL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 520 -EYYVLGESFETsapwdRVVDLC---RNVKERITRECKEkgVQFAPFsTCRVTQTYDAG---ACIYFyfafnyrgisDPL 592
Cdd:PLN02805 417 wACFAMEPKYEA-----MITDVCvplSHLAELISRSKKE--LDASPL-VCTVIAHAGDGnfhTIILF----------DPS 478
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501993 593 TVFEQTEAAAREEILANG-----GSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNI 651
Cdd:PLN02805 479 QEDQRREAERLNHFMVHTalsmeGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNI 542
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
209-383 |
2.63e-11 |
|
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: 66.42 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 209 VLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPAD-ETRTIISldTSQMNRILWVDENNLTAHVEAGITGQEL 287
Cdd:TIGR01677 35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGsDGALLIS--TKRLNHVVAVDATAMTVTVESGMSLREL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 288 ERQLKESGYCTGHEPdSLEFSTVGGWVSTRASGmkKNIYGN---IEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHF- 363
Cdd:TIGR01677 113 IVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHG--SSLWGKgsaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFn 189
|
170 180
....*....|....*....|.
gi 4501993 364 -IMGSEGTLGVITEATIKIRP 383
Cdd:TIGR01677 190 aAKVSLGVLGVISQVTLALQP 210
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
200-652 |
2.05e-101 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 317.22 E-value: 2.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 200 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVE 279
Cdd:COG0277 34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 280 AGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRG-IIEKSCQGPRMSTGP 358
Cdd:COG0277 110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGeVVRTGGRVPKNVTGY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 359 DIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPqvss 438
Cdd:COG0277 190 DLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 439 iftsfldglkkfyitkfKGFDPNQLSVATLLFEGDREKVLQHE-KQVYDIAAKFGGLAAG--EDNGQRGYL---LTYVIA 512
Cdd:COG0277 266 -----------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGATDVRvaADGAERERLwkaRKAALP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 513 YIRDLALEYYVLgesFETSAPWDRVVDLCRnvkeRITRECKEKGVQFAPFStcrvtqtyDAG-ACIYFYFAFNyRGISDP 591
Cdd:COG0277 329 ALGRLDGGAKLL---EDVAVPPSRLPELLR----ELGALAAKYGLRATAFG--------HAGdGNLHVRILFD-PADPEE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4501993 592 LTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIF 652
Cdd:COG0277 393 VERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGIL 453
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
385-657 |
6.43e-56 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 190.22 E-value: 6.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 385 PEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVssiftsfldglkkfyitkfKGFDPNQLS 464
Cdd:pfam02913 2 PEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 465 VATLLFEGDREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYLLTYVIAyIRDLALEYYVLGESFETSAPWDR 536
Cdd:pfam02913 63 LLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 537 VVDLCRNVKERITRECkekgvqfapFSTCRVTQTYDAGACIYFYFAFNYRGISDPL-TVFEQTeaaaREEILANGGSLSH 615
Cdd:pfam02913 140 LADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEERAeKLFDEI----MDLALELGGSISG 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 4501993 616 HHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNL 657
Cdd:pfam02913 207 EHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
206-347 |
9.31e-43 |
|
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: 150.81 E-value: 9.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 206 PDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSyglmcPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQ 285
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLL-----GGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501993 286 ELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEK 347
Cdd:pfam01565 76 DLVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVR 137
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
205-651 |
3.43e-29 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 122.42 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 205 IPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVEAGITG 284
Cdd:PLN02805 133 IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGG----VCIDMSLMKSVKALHVEDMDVVVEPGIGW 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 285 QELERQLKESGYCTGHEPDSleFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMST-GPDIHHF 363
Cdd:PLN02805 209 LELNEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAaGYDLTRL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 364 IMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGvaclreiakqrcAPASIRLMDNkqfqfghalKPQVSSIftSF 443
Cdd:PLN02805 287 VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDA------------ADVAIATMLS---------GIQVSRV--EL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 444 LDGLKKFYITKFKGfdPNQLSVATLLFE--GDREKVLQHEKQVYDIAAKFGG--LAAGEDNGQRGYLLTyviayIRDLAL 519
Cdd:PLN02805 344 LDEVQIRAINMANG--KNLPEAPTLMFEfiGTEAYAREQTLIVQKIASKHNGsdFVFAEEPEAKKELWK-----IRKEAL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 520 -EYYVLGESFETsapwdRVVDLC---RNVKERITRECKEkgVQFAPFsTCRVTQTYDAG---ACIYFyfafnyrgisDPL 592
Cdd:PLN02805 417 wACFAMEPKYEA-----MITDVCvplSHLAELISRSKKE--LDASPL-VCTVIAHAGDGnfhTIILF----------DPS 478
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501993 593 TVFEQTEAAAREEILANG-----GSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNI 651
Cdd:PLN02805 479 QEDQRREAERLNHFMVHTalsmeGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNI 542
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
205-448 |
1.35e-11 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 67.11 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 205 IPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMcPADETrtiISLDTSQMNRILWVDENNLTAHVEAGITG 284
Cdd:PRK11230 55 RPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGAL-PLEKG---VLLVMARFNRILDINPVGRRARVQPGVRN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 285 QELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGniedLVVH----IKMVTPRGiiEKSCQGPRM--STGP 358
Cdd:PRK11230 131 LAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYG----LTVHnllkVEILTLDG--EALTLGSDAldSPGF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 359 DIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQ----FGHALKP 434
Cdd:PRK11230 205 DLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRaaedFIHAGYP 284
|
250
....*....|....*
gi 4501993 435 -QVSSIFTSFLDGLK 448
Cdd:PRK11230 285 vDAEAILLCELDGVE 299
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
209-383 |
2.63e-11 |
|
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: 66.42 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 209 VLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPAD-ETRTIISldTSQMNRILWVDENNLTAHVEAGITGQEL 287
Cdd:TIGR01677 35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGsDGALLIS--TKRLNHVVAVDATAMTVTVESGMSLREL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 288 ERQLKESGYCTGHEPdSLEFSTVGGWVSTRASGmkKNIYGN---IEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHF- 363
Cdd:TIGR01677 113 IVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHG--SSLWGKgsaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFn 189
|
170 180
....*....|....*....|.
gi 4501993 364 -IMGSEGTLGVITEATIKIRP 383
Cdd:TIGR01677 190 aAKVSLGVLGVISQVTLALQP 210
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
212-383 |
1.24e-09 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 61.02 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 212 PTCHDDVVKIVNLACKYNLCIIPIGGGTSVSyGLmcpADETRTIISLdtSQMNRILWVDENNLTAHVEAGITGQELERQL 291
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRIRPVGSGLSPN-GL---AFSREGMVNL--ALMDKVLEVDKEKKRVTVQAGARVQQVVEAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 292 KESGYcTGHEPDSLEFSTVGGWVSTRASGMKKNIyGNIEDLVVHIKMVTP-RGIIEKSCQgprmsTGPDIHHFIMGSEGT 370
Cdd:PLN02465 177 RPHGL-TLQNYASIREQQIGGFIQVGAHGTGARI-PPIDEQVVSMKLVTPaKGTIELSKE-----DDPELFRLARCGLGG 249
|
170
....*....|...
gi 4501993 371 LGVITEATIKIRP 383
Cdd:PLN02465 250 LGVVAEVTLQCVP 262
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
200-383 |
2.52e-09 |
|
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: 59.91 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 200 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYglMCPADETrtIISLDtsQMNRILWVDENNLTAHVE 279
Cdd:TIGR01678 9 KTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSD--IACTDGF--LIHLD--KMNKVLQFDKEKKQITVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 280 AGITGQELERQLKESGYCTGHePDSLEFSTVGGWVS--TRASGMKkniYGNIEDLVVHIKMVTPRGIIeKSCQGPRmstG 357
Cdd:TIGR01678 83 AGIRLYQLHEQLDEHGYSMSN-LGSISEVSVAGIIStgTHGSSIK---HGILATQVVALTIMTADGEV-LECSEER---N 154
|
170 180
....*....|....*....|....*.
gi 4501993 358 PDIHHFIMGSEGTLGVITEATIKIRP 383
Cdd:TIGR01678 155 ADVFQAARVSLGCLGIIVTVTIQVVP 180
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
200-380 |
4.16e-07 |
|
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD.
Pssm-ID: 130737 [Multi-domain] Cd Length: 541 Bit Score: 53.14 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 200 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVS-YGLmcpadeTRTIIsLDTSQMNRILWVDENNLTAHV 278
Cdd:TIGR01676 56 GTHEVLTRTFHQPEAIEELEGIVKQANEKKARIRPVGSGLSPNgIGL------SRAGM-VNLALMDKVLEVDEEKKRVRV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 279 EAGITGQELERQLKESGYcTGHEPDSLEFSTVGGWVSTRASGMKKNIyGNIEDLVVHIKMVTP-RGIIEKSCQgprmsTG 357
Cdd:TIGR01676 129 QAGIRVQQLVDAIKEYGI-TLQNFASIREQQIGGIIQVGAHGTGAKL-PPIDEQVIAMKLVTPaKGTIEISKD-----KD 201
|
170 180
....*....|....*....|...
gi 4501993 358 PDIHHFIMGSEGTLGVITEATIK 380
Cdd:TIGR01676 202 PELFFLARCGLGGLGVVAEVTLQ 224
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
230-411 |
1.14e-05 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 47.91 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 230 LCIIpiGGGTSVSYGlMCPADETrtiisLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDslEF-- 307
Cdd:PRK11282 21 LRIR--GGGSKDFYG-RALAGEV-----LDTRAHRGIVSYDPTELVITARAGTPLAELEAALAEAGQMLPFEPP--HFgg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501993 308 -STVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIeKSCQGPRMST--GPDIHHFIMGSEGTLGVITEATIKIRPV 384
Cdd:PRK11282 91 gATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEH-LRFGGQVMKNvaGYDVSRLMAGSLGTLGVLLEVSLKVLPR 169
|
170 180
....*....|....*....|....*...
gi 4501993 385 PEYQkyGSVAFP-NFEQGVACLREIAKQ 411
Cdd:PRK11282 170 PRAE--LTLRLEmDAAEALRKLNEWGGQ 195
|
|
| |
