|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
213-665 |
3.31e-99 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 311.83 E-value: 3.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 213 GMFERIPDIVVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVE 292
Cdd:COG0277 34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 293 AGITGQDLERQLKESGYCTGHEPDSLEFSTVGGWISTRASGMKKNIYGNIEDLVVHMKMVTPRG-VIEKSSQGPRMSTGP 371
Cdd:COG0277 110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGeVVRTGGRVPKNVTGY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 372 DIHHFIMGSEGTLGVITEATIKIRPTPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNQQFQFghalkpqvss 451
Cdd:COG0277 190 DLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALAL---------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 452 iftsfldglkkfyITKFKGFDPNQISVATLL--FEGDREKVLQHE-KQVYDIAAKFGGLAAG--EDNGQRGYL---LTYV 523
Cdd:COG0277 260 -------------VEAAPPLGLPEDGGALLLveFDGDDAEEVEAQlARLRAILEAGGATDVRvaADGAERERLwkaRKAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 524 IAYIRDLGLEYYVIgesFETSAPWDRVIDLCRnvkeRIRRECKERGVQFAPLStcrvtqtyDAG-ACIYFYFAFNyRGIS 602
Cdd:COG0277 327 LPALGRLDGGAKLL---EDVAVPPSRLPELLR----ELGALAAKYGLRATAFG--------HAGdGNLHVRILFD-PADP 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295444834 603 DPLTVFEHTEAAAREEILANGGSLSHHHGVGKIRKQWLKESISDVGFGMLKSVKEYVDPSNIF 665
Cdd:COG0277 391 EEVERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGIL 453
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
397-670 |
1.25e-55 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 189.83 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 397 TPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNQQFQFGHALKPQVssiftsfldglkkfyitkfKGFDPNQI 476
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 477 SVATLLFEGDREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYLLTYVIAyIRDLGLEYYVIGESFETSAPWD 548
Cdd:pfam02913 62 ALLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 549 RVIDLCRNVKERIRRECkergvqfapLSTCRVTQTYDAGACIYFYFAFNYRGISDPL-TVFEhteaAAREEILANGGSLS 627
Cdd:pfam02913 139 RLADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEERAeKLFD----EIMDLALELGGSIS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 295444834 628 HHHGVGKIRKQWLKESISDVGFGMLKSVKEYVDPSNIFGNRNL 670
Cdd:pfam02913 206 GEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
173-664 |
9.23e-29 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 121.27 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 173 VNEDFLQELKE-ARISYSQEADDRVFraHG---HCLHEIFllregmfeRIPDIVVWPTCHDDVVKIVNLACKYNLCIIPI 248
Cdd:PLN02805 94 VPQELIDELKAiLQDNMTLDYDERYF--HGkpqNSFHKAV--------NIPDVVVFPRSEEEVSKIVKSCNKYKVPIVPY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 249 GGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVEAGITGQDLERQLKESGYCTGHEPDSleFSTVGGWIS 328
Cdd:PLN02805 164 GGATSIEGHTLAPHGG----VCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGP--GATIGGMCA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 329 TRASGMKKNIYGNIEDLVVHMKMVTPRG-VIEKSSQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPTPEYQKYGSVA 407
Cdd:PLN02805 238 TRCSGSLAVRYGTMRDNVISLKVVLPNGdVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 408 FPNFEQGvaclreiakqrcAPASIRLMDNqqfqfghalKPQVSSIftSFLDGLKKFYITKFKGfdPNQISVATLLFE--G 485
Cdd:PLN02805 318 FPTIKDA------------ADVAIATMLS---------GIQVSRV--ELLDEVQIRAINMANG--KNLPEAPTLMFEfiG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 486 DREKVLQHEKQVYDIAAKFGG--LAAGEDNGQRGYLLTyviayIRDLGL-EYYVIGESFETsapwdRVIDLC---RNVKE 559
Cdd:PLN02805 373 TEAYAREQTLIVQKIASKHNGsdFVFAEEPEAKKELWK-----IRKEALwACFAMEPKYEA-----MITDVCvplSHLAE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 560 RIRRECKErgVQFAPLsTCRVTQTYDAG---ACIYFyfafnyrgisDPLTVfEHTEAAAR------EEILANGGSLSHHH 630
Cdd:PLN02805 443 LISRSKKE--LDASPL-VCTVIAHAGDGnfhTIILF----------DPSQE-DQRREAERlnhfmvHTALSMEGTCTGEH 508
|
490 500 510
....*....|....*....|....*....|....
gi 295444834 631 GVGKIRKQWLKESISDVGFGMLKSVKEYVDPSNI 664
Cdd:PLN02805 509 GVGTGKMKYLEKELGIEALQTMKRIKKALDPNNI 542
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
222-396 |
9.08e-12 |
|
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: 67.96 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 222 VVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPAD-ETRTIISldTSQMNRILWVDENNLTAHVEAGITGQDL 300
Cdd:TIGR01677 35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGsDGALLIS--TKRLNHVVAVDATAMTVTVESGMSLREL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 301 ERQLKESGYCTGHEPdSLEFSTVGGWISTRASGmkKNIYGN---IEDLVVHMKMVTPRGVIEKSSQGPRMSTGPDIHHF- 376
Cdd:TIGR01677 113 IVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHG--SSLWGKgsaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFn 189
|
170 180
....*....|....*....|.
gi 295444834 377 -IMGSEGTLGVITEATIKIRP 396
Cdd:TIGR01677 190 aAKVSLGVLGVISQVTLALQP 210
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
213-665 |
3.31e-99 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 311.83 E-value: 3.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 213 GMFERIPDIVVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVE 292
Cdd:COG0277 34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 293 AGITGQDLERQLKESGYCTGHEPDSLEFSTVGGWISTRASGMKKNIYGNIEDLVVHMKMVTPRG-VIEKSSQGPRMSTGP 371
Cdd:COG0277 110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGeVVRTGGRVPKNVTGY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 372 DIHHFIMGSEGTLGVITEATIKIRPTPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNQQFQFghalkpqvss 451
Cdd:COG0277 190 DLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALAL---------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 452 iftsfldglkkfyITKFKGFDPNQISVATLL--FEGDREKVLQHE-KQVYDIAAKFGGLAAG--EDNGQRGYL---LTYV 523
Cdd:COG0277 260 -------------VEAAPPLGLPEDGGALLLveFDGDDAEEVEAQlARLRAILEAGGATDVRvaADGAERERLwkaRKAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 524 IAYIRDLGLEYYVIgesFETSAPWDRVIDLCRnvkeRIRRECKERGVQFAPLStcrvtqtyDAG-ACIYFYFAFNyRGIS 602
Cdd:COG0277 327 LPALGRLDGGAKLL---EDVAVPPSRLPELLR----ELGALAAKYGLRATAFG--------HAGdGNLHVRILFD-PADP 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295444834 603 DPLTVFEHTEAAAREEILANGGSLSHHHGVGKIRKQWLKESISDVGFGMLKSVKEYVDPSNIF 665
Cdd:COG0277 391 EEVERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGIL 453
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
397-670 |
1.25e-55 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 189.83 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 397 TPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNQQFQFGHALKPQVssiftsfldglkkfyitkfKGFDPNQI 476
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 477 SVATLLFEGDREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYLLTYVIAyIRDLGLEYYVIGESFETSAPWD 548
Cdd:pfam02913 62 ALLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 549 RVIDLCRNVKERIRRECkergvqfapLSTCRVTQTYDAGACIYFYFAFNYRGISDPL-TVFEhteaAAREEILANGGSLS 627
Cdd:pfam02913 139 RLADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEERAeKLFD----EIMDLALELGGSIS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 295444834 628 HHHGVGKIRKQWLKESISDVGFGMLKSVKEYVDPSNIFGNRNL 670
Cdd:pfam02913 206 GEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
219-362 |
1.35e-44 |
|
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: 155.82 E-value: 1.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 219 PDIVVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSyglmcPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQ 298
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLL-----GGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295444834 299 DLERQLKESGYCTGHEPDSLEFSTVGGWISTRASGMKKNIYGNIEDLVVHMKMVTPRGVIEKSS 362
Cdd:pfam01565 76 DLVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRLG 139
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
173-664 |
9.23e-29 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 121.27 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 173 VNEDFLQELKE-ARISYSQEADDRVFraHG---HCLHEIFllregmfeRIPDIVVWPTCHDDVVKIVNLACKYNLCIIPI 248
Cdd:PLN02805 94 VPQELIDELKAiLQDNMTLDYDERYF--HGkpqNSFHKAV--------NIPDVVVFPRSEEEVSKIVKSCNKYKVPIVPY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 249 GGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVEAGITGQDLERQLKESGYCTGHEPDSleFSTVGGWIS 328
Cdd:PLN02805 164 GGATSIEGHTLAPHGG----VCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGP--GATIGGMCA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 329 TRASGMKKNIYGNIEDLVVHMKMVTPRG-VIEKSSQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPTPEYQKYGSVA 407
Cdd:PLN02805 238 TRCSGSLAVRYGTMRDNVISLKVVLPNGdVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 408 FPNFEQGvaclreiakqrcAPASIRLMDNqqfqfghalKPQVSSIftSFLDGLKKFYITKFKGfdPNQISVATLLFE--G 485
Cdd:PLN02805 318 FPTIKDA------------ADVAIATMLS---------GIQVSRV--ELLDEVQIRAINMANG--KNLPEAPTLMFEfiG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 486 DREKVLQHEKQVYDIAAKFGG--LAAGEDNGQRGYLLTyviayIRDLGL-EYYVIGESFETsapwdRVIDLC---RNVKE 559
Cdd:PLN02805 373 TEAYAREQTLIVQKIASKHNGsdFVFAEEPEAKKELWK-----IRKEALwACFAMEPKYEA-----MITDVCvplSHLAE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 560 RIRRECKErgVQFAPLsTCRVTQTYDAG---ACIYFyfafnyrgisDPLTVfEHTEAAAR------EEILANGGSLSHHH 630
Cdd:PLN02805 443 LISRSKKE--LDASPL-VCTVIAHAGDGnfhTIILF----------DPSQE-DQRREAERlnhfmvHTALSMEGTCTGEH 508
|
490 500 510
....*....|....*....|....*....|....
gi 295444834 631 GVGKIRKQWLKESISDVGFGMLKSVKEYVDPSNI 664
Cdd:PLN02805 509 GVGTGKMKYLEKELGIEALQTMKRIKKALDPNNI 542
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
218-461 |
5.68e-12 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 68.65 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 218 IPDIVVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMcPADETrtiISLDTSQMNRILWVDENNLTAHVEAGITG 297
Cdd:PRK11230 55 RPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGAL-PLEKG---VLLVMARFNRILDINPVGRRARVQPGVRN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 298 QDLERQLKESGYCTGHEPDSLEFSTVGGWISTRASGMKKNIYGniedLVVH----MKMVTPRGviEKSSQGPRM--STGP 371
Cdd:PRK11230 131 LAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYG----LTVHnllkVEILTLDG--EALTLGSDAldSPGF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 372 DIHHFIMGSEGTLGVITEATIKIRPTPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNQQFQ----FGHALKP 447
Cdd:PRK11230 205 DLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRaaedFIHAGYP 284
|
250
....*....|....*
gi 295444834 448 -QVSSIFTSFLDGLK 461
Cdd:PRK11230 285 vDAEAILLCELDGVE 299
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
222-396 |
9.08e-12 |
|
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: 67.96 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 222 VVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPAD-ETRTIISldTSQMNRILWVDENNLTAHVEAGITGQDL 300
Cdd:TIGR01677 35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGsDGALLIS--TKRLNHVVAVDATAMTVTVESGMSLREL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 301 ERQLKESGYCTGHEPdSLEFSTVGGWISTRASGmkKNIYGN---IEDLVVHMKMVTPRGVIEKSSQGPRMSTGPDIHHF- 376
Cdd:TIGR01677 113 IVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHG--SSLWGKgsaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFn 189
|
170 180
....*....|....*....|.
gi 295444834 377 -IMGSEGTLGVITEATIKIRP 396
Cdd:TIGR01677 190 aAKVSLGVLGVISQVTLALQP 210
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
213-396 |
7.07e-11 |
|
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: 64.92 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 213 GMFERIPDIVVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYglMCPADETrtIISLDtsQMNRILWVDENNLTAHVE 292
Cdd:TIGR01678 9 KTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSD--IACTDGF--LIHLD--KMNKVLQFDKEKKQITVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 293 AGITGQDLERQLKESGYCTGHePDSLEFSTVGGWIS--TRASGMKkniYGNIEDLVVHMKMVTPRGVIEKSSQgprmSTG 370
Cdd:TIGR01678 83 AGIRLYQLHEQLDEHGYSMSN-LGSISEVSVAGIIStgTHGSSIK---HGILATQVVALTIMTADGEVLECSE----ERN 154
|
170 180
....*....|....*....|....*.
gi 295444834 371 PDIHHFIMGSEGTLGVITEATIKIRP 396
Cdd:TIGR01678 155 ADVFQAARVSLGCLGIIVTVTIQVVP 180
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
225-396 |
8.43e-11 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 64.87 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 225 PTCHDDVVKIVNLACKYNLCIIPIGGGTSVSyGLmcpADETRTIISLdtSQMNRILWVDENNLTAHVEAGITGQDLERQL 304
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRIRPVGSGLSPN-GL---AFSREGMVNL--ALMDKVLEVDKEKKRVTVQAGARVQQVVEAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 305 KESGYcTGHEPDSLEFSTVGGWISTRASGMKKNIyGNIEDLVVHMKMVTP-RGVIEKSSQgprmsTGPDIHHFIMGSEGT 383
Cdd:PLN02465 177 RPHGL-TLQNYASIREQQIGGFIQVGAHGTGARI-PPIDEQVVSMKLVTPaKGTIELSKE-----DDPELFRLARCGLGG 249
|
170
....*....|...
gi 295444834 384 LGVITEATIKIRP 396
Cdd:PLN02465 250 LGVVAEVTLQCVP 262
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
213-393 |
1.36e-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: 54.68 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 213 GMFERIPDIVVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVS-YGLmcpadeTRTIIsLDTSQMNRILWVDENNLTAHV 291
Cdd:TIGR01676 56 GTHEVLTRTFHQPEAIEELEGIVKQANEKKARIRPVGSGLSPNgIGL------SRAGM-VNLALMDKVLEVDEEKKRVRV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 292 EAGITGQDLERQLKESGYcTGHEPDSLEFSTVGGWISTRASGMKKNIyGNIEDLVVHMKMVTP-RGVIEKSSQgprmsTG 370
Cdd:TIGR01676 129 QAGIRVQQLVDAIKEYGI-TLQNFASIREQQIGGIIQVGAHGTGAKL-PPIDEQVIAMKLVTPaKGTIEISKD-----KD 201
|
170 180
....*....|....*....|...
gi 295444834 371 PDIHHFIMGSEGTLGVITEATIK 393
Cdd:TIGR01676 202 PELFFLARCGLGGLGVVAEVTLQ 224
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
243-424 |
2.89e-04 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 43.67 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 243 LCIIpiGGGTSVSYGlMCPADETrtiisLDTSQMNRILWVDENNLTAHVEAGITGQDLERQLKESGYCTGHEPDslEF-- 320
Cdd:PRK11282 21 LRIR--GGGSKDFYG-RALAGEV-----LDTRAHRGIVSYDPTELVITARAGTPLAELEAALAEAGQMLPFEPP--HFgg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295444834 321 -STVGGWISTRASGMKKNIYGNIEDLVVHMKMVTprgvieksSQGPRMS---------TGPDIHHFIMGSEGTLGVITEA 390
Cdd:PRK11282 91 gATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLIN--------GRGEHLRfggqvmknvAGYDVSRLMAGSLGTLGVLLEV 162
|
170 180 190
....*....|....*....|....*....|....*
gi 295444834 391 TIKIRPTPEYQkyGSVAFP-NFEQGVACLREIAKQ 424
Cdd:PRK11282 163 SLKVLPRPRAE--LTLRLEmDAAEALRKLNEWGGQ 195
|
|
| |
