|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
155-610 |
8.67e-98 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 306.82 E-value: 8.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 155 FRRIPDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGAITCPQNEsrmiCALDTSQMNRLLWLNRENLTVCFESG 234
Cdd:COG0277 36 YRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVEAG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 235 IVGQDLERVLRSEGLTVGHEPDSYEFSTLGGWVATRASGMKKNVYGNIEDLVVRVRMVTPSGTLER-ECSAPRVSCGPDF 313
Cdd:COG0277 112 VTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRtGGRVPKNVTGYDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 314 NHVILGSEGTLGVITEVVLKVRPLPSLRRYGSLAFPNFEQGVLFMREVARRRCQPASVRLMDNEQFMFgqalkpekswwa 393
Cdd:COG0277 192 FWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALAL------------ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 394 svvdamkqryVTSWKGIDLNQICAATLLFE---GDLKDVQRQEALIYEIAEKFQGFPAG-GQNG-ERGYILTFVIAYIRD 468
Cdd:COG0277 260 ----------VEAAPPLGLPEDGGALLLVEfdgDDAEEVEAQLARLRAILEAGGATDVRvAADGaERERLWKARKAALPA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 469 FGLHQGIVAESFETSVPWDRCSLLCRSVkQRVVSECSKRSINYytiscrvtqtYDAG-ACIYFYFGFRSTDvADPVELFE 547
Cdd:COG0277 330 LGRLDGGAKLLEDVAVPPSRLPELLREL-GALAAKYGLRATAF----------GHAGdGNLHVRILFDPAD-PEEVERAR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653753 548 AIEHSARDEILSCGGSLSHHHGVGKIRSHWYRNAVTETGSSLYSAAKRHLDPKNIFALGNLLP 610
Cdd:COG0277 398 AAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
337-608 |
4.82e-55 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 187.52 E-value: 4.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 337 LPSLRRYGSLAFPNFEQGVLFMREVARRRCQPASVRLMDNEQFMFGQALKPEKswwasvvdamkqryvtswKGIDLNQIC 416
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP------------------KGLPRDAAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 417 AATLLFEGDLKDVQRQEALiyEIAEKFQGFPAGGQNG--------ERGYILTFVIAyIRDFGLHQGIVAESFETSVPWDR 488
Cdd:pfam02913 63 LLLVEFEGDDEETAEEELE--AVEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 489 CSLLCRSVKQRVVSecskrsinYYTISCRVTQTYDAGACIYFYFGFRStdvADPVELFEAIEHSARDEILSCGGSLSHHH 568
Cdd:pfam02913 140 LADLVRDIKELLDK--------YGLVVCLFGHAGDGNLHLYILFDFRD---PEQEERAEKLFDEIMDLALELGGSISGEH 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 24653753 569 GVGKIRSHWYRNAVTETGSSLYSAAKRHLDPKNIFALGNL 608
Cdd:pfam02913 209 GVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
116-610 |
1.04e-36 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 144.77 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 116 FLHELKGTTQVDYSAEGIDRLVrcHGQTLNDIyslwhHKFRRIPDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVS 195
Cdd:PLN02805 98 LIDELKAILQDNMTLDYDERYF--HGKPQNSF-----HKAVNIPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 196 GAITCPQNEsrmICaLDTSQMNRLLWLNRENLTVCFESGIVGQDLERVLRSEGLTVGHEPDSYefSTLGGWVATRASGMK 275
Cdd:PLN02805 171 GHTLAPHGG---VC-IDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGPG--ATIGGMCATRCSGSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 276 KNVYGNIEDLVVRVRMVTPSGTLERECSAPRVS-CGPDFNHVILGSEGTLGVITEVVLKVRPLPSLRRYGSLAFPNFEQG 354
Cdd:PLN02805 245 AVRYGTMRDNVISLKVVLPNGDVVKTASRARKSaAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 355 VLFMREVARRRCQPASVRLMDNEQFmfgqalkpekswwasvvdamkqRYVTSWKGIDLNQicAATLLFE--GDLKDVQRQ 432
Cdd:PLN02805 325 ADVAIATMLSGIQVSRVELLDEVQI----------------------RAINMANGKNLPE--APTLMFEfiGTEAYAREQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 433 EALIYEIAEKFQGFpaggqngergyilTFVIA----------YIRDFGLHQGIVAE-SFETSVPwDRCSLLCRsvkqrvV 501
Cdd:PLN02805 381 TLIVQKIASKHNGS-------------DFVFAeepeakkelwKIRKEALWACFAMEpKYEAMIT-DVCVPLSH------L 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 502 SEC---SKRSINYYTISCRVTQTYDAGaciyfyfGFRSTDVADPVE-----LFEAIEHSARDEILSCGGSLSHHHGVGKI 573
Cdd:PLN02805 441 AELisrSKKELDASPLVCTVIAHAGDG-------NFHTIILFDPSQedqrrEAERLNHFMVHTALSMEGTCTGEHGVGTG 513
|
490 500 510
....*....|....*....|....*....|....*..
gi 24653753 574 RSHWYRNAVTETGSSLYSAAKRHLDPKNIFALGNLLP 610
Cdd:PLN02805 514 KMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIP 550
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
137-337 |
2.66e-09 |
|
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: 59.87 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 137 VRCHGQ----TLNDIYSLWHHKFRRIPDLVVWPRCHDEVVQLVRLANKHNVmlvPFGGGTSVSGAIT---CPqNESRMIC 209
Cdd:TIGR01677 6 VRCVSGgancTVSNAYGAFPDRSTCRAANVAYPKTEAELVSVVAAATAAGR---KMKVVTRYSHSIPklaCP-DGSDGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 210 ALDTSQMNRLLWLNRENLTVCFESGIVGQDLERVLRSEGLTVGHEPdSYEFSTLGGWVATRASGMKKNVYGN-IEDLVVR 288
Cdd:TIGR01677 82 LISTKRLNHVVAVDATAMTVTVESGMSLRELIVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHGSSLWGKGSaVHDYVVG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24653753 289 VRMVTPSGTLERECSAPRVSCGPD---FNHVILgSEGTLGVITEVVLKVRPL 337
Cdd:TIGR01677 161 IRLVVPASAAEGFAKVRILSEGDTpneFNAAKV-SLGVLGVISQVTLALQPM 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
155-610 |
8.67e-98 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 306.82 E-value: 8.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 155 FRRIPDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGAITCPQNEsrmiCALDTSQMNRLLWLNRENLTVCFESG 234
Cdd:COG0277 36 YRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVEAG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 235 IVGQDLERVLRSEGLTVGHEPDSYEFSTLGGWVATRASGMKKNVYGNIEDLVVRVRMVTPSGTLER-ECSAPRVSCGPDF 313
Cdd:COG0277 112 VTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRtGGRVPKNVTGYDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 314 NHVILGSEGTLGVITEVVLKVRPLPSLRRYGSLAFPNFEQGVLFMREVARRRCQPASVRLMDNEQFMFgqalkpekswwa 393
Cdd:COG0277 192 FWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALAL------------ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 394 svvdamkqryVTSWKGIDLNQICAATLLFE---GDLKDVQRQEALIYEIAEKFQGFPAG-GQNG-ERGYILTFVIAYIRD 468
Cdd:COG0277 260 ----------VEAAPPLGLPEDGGALLLVEfdgDDAEEVEAQLARLRAILEAGGATDVRvAADGaERERLWKARKAALPA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 469 FGLHQGIVAESFETSVPWDRCSLLCRSVkQRVVSECSKRSINYytiscrvtqtYDAG-ACIYFYFGFRSTDvADPVELFE 547
Cdd:COG0277 330 LGRLDGGAKLLEDVAVPPSRLPELLREL-GALAAKYGLRATAF----------GHAGdGNLHVRILFDPAD-PEEVERAR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653753 548 AIEHSARDEILSCGGSLSHHHGVGKIRSHWYRNAVTETGSSLYSAAKRHLDPKNIFALGNLLP 610
Cdd:COG0277 398 AAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
337-608 |
4.82e-55 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 187.52 E-value: 4.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 337 LPSLRRYGSLAFPNFEQGVLFMREVARRRCQPASVRLMDNEQFMFGQALKPEKswwasvvdamkqryvtswKGIDLNQIC 416
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP------------------KGLPRDAAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 417 AATLLFEGDLKDVQRQEALiyEIAEKFQGFPAGGQNG--------ERGYILTFVIAyIRDFGLHQGIVAESFETSVPWDR 488
Cdd:pfam02913 63 LLLVEFEGDDEETAEEELE--AVEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 489 CSLLCRSVKQRVVSecskrsinYYTISCRVTQTYDAGACIYFYFGFRStdvADPVELFEAIEHSARDEILSCGGSLSHHH 568
Cdd:pfam02913 140 LADLVRDIKELLDK--------YGLVVCLFGHAGDGNLHLYILFDFRD---PEQEERAEKLFDEIMDLALELGGSISGEH 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 24653753 569 GVGKIRSHWYRNAVTETGSSLYSAAKRHLDPKNIFALGNL 608
Cdd:pfam02913 209 GVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
159-300 |
2.66e-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: 143.50 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 159 PDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGAitcPQNESRMIcaLDTSQMNRLLWLNRENLTVCFESGIVGQ 238
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGG---AVQTGGIV--LDLSRLNGILEIDPEDGTATVEAGVTLG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653753 239 DLERVLRSEGLTVGHEPDSYEFSTLGGWVATRASGMKKNVYGNIEDLVVRVRMVTPSGTLER 300
Cdd:pfam01565 76 DLVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVR 137
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
116-610 |
1.04e-36 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 144.77 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 116 FLHELKGTTQVDYSAEGIDRLVrcHGQTLNDIyslwhHKFRRIPDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVS 195
Cdd:PLN02805 98 LIDELKAILQDNMTLDYDERYF--HGKPQNSF-----HKAVNIPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 196 GAITCPQNEsrmICaLDTSQMNRLLWLNRENLTVCFESGIVGQDLERVLRSEGLTVGHEPDSYefSTLGGWVATRASGMK 275
Cdd:PLN02805 171 GHTLAPHGG---VC-IDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGPG--ATIGGMCATRCSGSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 276 KNVYGNIEDLVVRVRMVTPSGTLERECSAPRVS-CGPDFNHVILGSEGTLGVITEVVLKVRPLPSLRRYGSLAFPNFEQG 354
Cdd:PLN02805 245 AVRYGTMRDNVISLKVVLPNGDVVKTASRARKSaAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 355 VLFMREVARRRCQPASVRLMDNEQFmfgqalkpekswwasvvdamkqRYVTSWKGIDLNQicAATLLFE--GDLKDVQRQ 432
Cdd:PLN02805 325 ADVAIATMLSGIQVSRVELLDEVQI----------------------RAINMANGKNLPE--APTLMFEfiGTEAYAREQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 433 EALIYEIAEKFQGFpaggqngergyilTFVIA----------YIRDFGLHQGIVAE-SFETSVPwDRCSLLCRsvkqrvV 501
Cdd:PLN02805 381 TLIVQKIASKHNGS-------------DFVFAeepeakkelwKIRKEALWACFAMEpKYEAMIT-DVCVPLSH------L 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 502 SEC---SKRSINYYTISCRVTQTYDAGaciyfyfGFRSTDVADPVE-----LFEAIEHSARDEILSCGGSLSHHHGVGKI 573
Cdd:PLN02805 441 AELisrSKKELDASPLVCTVIAHAGDG-------NFHTIILFDPSQedqrrEAERLNHFMVHTALSMEGTCTGEHGVGTG 513
|
490 500 510
....*....|....*....|....*....|....*..
gi 24653753 574 RSHWYRNAVTETGSSLYSAAKRHLDPKNIFALGNLLP 610
Cdd:PLN02805 514 KMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIP 550
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
155-376 |
2.63e-13 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 72.50 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 155 FRRIPDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGAiTCPQNESRMicaLDTSQMNRLLWLNRENLTVCFESG 234
Cdd:PRK11230 52 YRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGG-ALPLEKGVL---LVMARFNRILDINPVGRRARVQPG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 235 IVGQDLERVLRSEGLTVGHEPDSYEFSTLGGWVATRASGMKKNVYGNIEDLVVRVRMVTPSGTLERECSAPRVSCGPDFN 314
Cdd:PRK11230 128 VRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSDALDSPGFDLL 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653753 315 HVILGSEGTLGVITEVVLKVRPLPSLRRYGSLAFPNFEQGVLFMREVARRRCQPASVRLMDN 376
Cdd:PRK11230 208 ALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDN 269
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
137-337 |
2.66e-09 |
|
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: 59.87 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 137 VRCHGQ----TLNDIYSLWHHKFRRIPDLVVWPRCHDEVVQLVRLANKHNVmlvPFGGGTSVSGAIT---CPqNESRMIC 209
Cdd:TIGR01677 6 VRCVSGgancTVSNAYGAFPDRSTCRAANVAYPKTEAELVSVVAAATAAGR---KMKVVTRYSHSIPklaCP-DGSDGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 210 ALDTSQMNRLLWLNRENLTVCFESGIVGQDLERVLRSEGLTVGHEPdSYEFSTLGGWVATRASGMKKNVYGN-IEDLVVR 288
Cdd:TIGR01677 82 LISTKRLNHVVAVDATAMTVTVESGMSLRELIVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHGSSLWGKGSaVHDYVVG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24653753 289 VRMVTPSGTLERECSAPRVSCGPD---FNHVILgSEGTLGVITEVVLKVRPL 337
Cdd:TIGR01677 161 IRLVVPASAAEGFAKVRILSEGDTpneFNAAKV-SLGVLGVISQVTLALQPM 211
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
148-336 |
4.93e-07 |
|
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: 52.59 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 148 YSLWHHKFRRIPDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGaITCpqnESRMICALDtsQMNRLLWLNRENL 227
Cdd:TIGR01678 4 FQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSD-IAC---TDGFLIHLD--KMNKVLQFDKEKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 228 TVCFESGIVGQDLERVLRSEGLTVGHEPDSYEFSTLGGW-VATRASGMKknvYGNIEDLVVRVRMVTPSGTLeRECSAPR 306
Cdd:TIGR01678 78 QITVEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIIsTGTHGSSIK---HGILATQVVALTIMTADGEV-LECSEER 153
|
170 180 190
....*....|....*....|....*....|
gi 24653753 307 vscGPDFNHVILGSEGTLGVITEVVLKVRP 336
Cdd:TIGR01678 154 ---NADVFQAARVSLGCLGIIVTVTIQVVP 180
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
165-336 |
1.23e-06 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 51.39 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 165 PRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGAITcpqNESRMicaLDTSQMNRLLWLNRENLTVCFESGIVGQDLERVL 244
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAF---SREGM---VNLALMDKVLEVDKEKKRVTVQAGARVQQVVEAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 245 RSEGLTVGHEPDSYEfSTLGGWVATRASGMKKNVyGNIEDLVVRVRMVTPS-GTLERecSAPRvscGPDFNHVILGSEGT 323
Cdd:PLN02465 177 RPHGLTLQNYASIRE-QQIGGFIQVGAHGTGARI-PPIDEQVVSMKLVTPAkGTIEL--SKED---DPELFRLARCGLGG 249
|
170
....*....|...
gi 24653753 324 LGVITEVVLKVRP 336
Cdd:PLN02465 250 LGVVAEVTLQCVP 262
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
238-368 |
1.98e-05 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 47.14 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 238 QDLERVLRSEGLTVGHEPDSY-EFSTLGGWVATRASGMKKNVYGNIEDLVVRVRMVTPSGTLER------ECSAprvscG 310
Cdd:PRK11282 68 AELEAALAEAGQMLPFEPPHFgGGATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRfggqvmKNVA-----G 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24653753 311 PDFNHVILGSEGTLGVITEVVLKVRPLPSLRRygSLAFP-NFEQGVlfmREVARRRCQP 368
Cdd:PRK11282 143 YDVSRLMAGSLGTLGVLLEVSLKVLPRPRAEL--TLRLEmDAAEAL---RKLNEWGGQP 196
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
165-333 |
2.05e-05 |
|
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: 47.36 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 165 PRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGAitcpqNESRMiCALDTSQMNRLLWLNRENLTVCFESGIVGQDLERVL 244
Cdd:TIGR01676 68 PEAIEELEGIVKQANEKKARIRPVGSGLSPNGI-----GLSRA-GMVNLALMDKVLEVDEEKKRVRVQAGIRVQQLVDAI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653753 245 RSEGLTVGHEPDSYEfSTLGGWVATRASGMKKNVyGNIEDLVVRVRMVTPS-GTLERECSAprvscGPDFNHVILGSEGT 323
Cdd:TIGR01676 142 KEYGITLQNFASIRE-QQIGGIIQVGAHGTGAKL-PPIDEQVIAMKLVTPAkGTIEISKDK-----DPELFFLARCGLGG 214
|
170
....*....|
gi 24653753 324 LGVITEVVLK 333
Cdd:TIGR01676 215 LGVVAEVTLQ 224
|
|
| |
