|
Name |
Accession |
Description |
Interval |
E-value |
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
5-480 |
0e+00 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 834.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 5 IRFILNGEDIELTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVGRLVDGKLAYESVNACIRFTGSLHATHVVT 84
Cdd:COG4630 1 IRFLLNGELVELSDVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVGELDDGGLRYRAVNACILFLPQLDGKALVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 85 VEHLAGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAEQVSLMR 164
Cdd:COG4630 81 VEGLAGPDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARAMAEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 165 PSalfDPLERTRSEIIARLWAMQASGTIRIAKGEDRLIVPASVQALAEVLSQEPDATVVAGSTDVGLWVTKQMRRLSPVV 244
Cdd:COG4630 161 AP---DPFAADRAAVAAALRALADGETVELGAGGSRFLAPATLDELAALLAAHPDARLVAGATDVGLWVTKQLRDLPPVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 245 FINHLSELQTVTESEDGVTIGAGVSYTRAFEAIARKIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGA 324
Cdd:COG4630 238 FLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAHFPELAELLRRFASRQIRNAGTLGGNIANGSPIGDSPPALIALGA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 325 TLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVESVFVPYP-ANSRFAAYKITKRRDEDITAVLGAFLLTLDDaEIVTDI 403
Cdd:COG4630 318 ELVLRSGDGRRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPaAGQRLRAYKVSKRFDDDISAVCAAFALTLDD-GTVTEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2083981135 404 RIAYGGMAATPKRARTVETELIGKSWTEATIEAARPAFDVDFQPLTDWRATAEYRQLTAKNLLTRFYLETVGAPAEL 480
Cdd:COG4630 397 RIAFGGMAATPKRARAAEAALLGQPWTEATVAAAAAALAQDFTPLSDMRASAEYRLAVAANLLRRFFLETQGEAPAT 473
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
5-473 |
0e+00 |
|
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274365 [Multi-domain] Cd Length: 467 Bit Score: 807.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 5 IRFILNGEDIELTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVGRLVDG-KLAYESVNACIRFTGSLHATHVV 83
Cdd:TIGR02963 1 IRFFLNGETVTLSDVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVGELVDGgKLRYRSVNACIQFLPSLDGKAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 84 TVEHLAGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAEQVSLM 163
Cdd:TIGR02963 81 TVEDLRQPDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDAAEAAFDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 164 RPSalfDPLERTRSEIIARLWAMQASGTIRIAKGEDRLIVPASVQALAEVLSQEPDATVVAGSTDVGLWVTKQMRRLSPV 243
Cdd:TIGR02963 161 PCS---DPLDADRAPIIERLRALRAGETVELNFGGERFIAPTTLDDLAALKAAHPDARIVAGSTDVGLWVTKQMRDLPDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 244 VFINHLSELQTVTESEDGVTIGAGVSYTRAFEAIARKIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALG 323
Cdd:TIGR02963 238 IYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGELLRRFASLQIRNAGTLGGNIANGSPIGDSPPALIALG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 324 ATLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVESVFVPYPAN-SRFAAYKITKRRDEDITAVLGAFLLTLDDaEIVTD 402
Cdd:TIGR02963 318 ARLTLRKGEGRRTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPgERFRAYKISKRFDDDISAVCAAFNLELDG-GVVAE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2083981135 403 IRIAYGGMAATPKRARTVETELIGKSWTEATIEAARPAFDVDFQPLTDWRATAEYRQLTAKNLLTRFYLET 473
Cdd:TIGR02963 397 IRIAFGGMAATPKRAAATEAALLGKPWNEATVEAAMAALAGDFTPLSDMRASAEYRLLTAKNLLRRFFLET 467
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
24-475 |
5.41e-101 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 329.74 E-value: 5.41e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 24 TLLDFLRlKRRLTGTKEGCAEGDCGACTVLVGRL--VDGKLAYESVNACIRFTGSLHATHVVTVEHLAGRDGALHPVQQA 101
Cdd:PLN02906 3 TLLEYLR-DLGLTGTKLGCGEGGCGACTVMVSHYdrKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGNRRDGLHPVQEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 102 LVDCHGSQCGFCTPGFVMSLYGLWLT-KEKPGRREIEKALQGNLCRCTGYEPIVKAA--------------EQVSL---- 162
Cdd:PLN02906 82 LASMHGSQCGFCTPGFIMSMYALLRSsKTPPTEEQIEECLAGNLCRCTGYRPILDAFrvfaktddalytgvSSLSLqdge 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 163 ---------------------MRPSALFDPLE--------RTRSEII------ARLWAMQASGTiriaKGEDRLIVPASV 207
Cdd:PLN02906 162 picpstgkpcscgskttsaagTCKSDRFQPISyseidgswYTEKELIfppellLRKLTPLKLLG----NGGLTWYRPTSL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 208 QALAEVLSQEPDATVVAGSTDVGLwvtkQMR--RLSPVVFIN--HLSELQTVTESEDGVTIGAGVSYT---RAFEAI--- 277
Cdd:PLN02906 238 QHLLELKAEYPDAKLVVGNTEVGI----EMRfkNAQYPVLISptHVPELNAIKVKDDGLEIGAAVRLSelqNLFRKVvke 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 278 --ARKIPALGRLIDRI---GGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEG-QRKIPLEDFFIAYGKQDR 351
Cdd:PLN02906 314 rpAHETSACKAFIEQLkwfAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFVIISCDGdIRSVPASDFFLGYRKVDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 352 KPGEFVESVFVPYPANSRFAA-YKITKRRDEDITAVLGAFLLTLDDAE---IVTDIRIAYGGMAATPKRARTVETELIGK 427
Cdd:PLN02906 394 KPDEILLSVFLPWTRPFEYVKeFKQAHRRDDDIAIVNAGMRVKLEEKDgewIVSDASIAYGGVAPLSVSARKTEEFLIGK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2083981135 428 SWTEATIEAARPAFDVDFqPLTDWR--ATAEYRQLTAKNLLTRFYLETVG 475
Cdd:PLN02906 474 PWNKETLQDALKVLQKDI-LIKEDApgGMVEFRKSLALSFFFKFFLWVSH 522
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
200-365 |
1.31e-71 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 224.73 E-value: 1.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 200 RLIVPASVQALAEVLSQEPDATVVAGSTDVGLWVTKQMRRLSPVVFINHLSELQTVTESEDGVTIGAGVSYTRAFEA-IA 278
Cdd:pfam00941 4 GYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPlLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 279 RKIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVE 358
Cdd:pfam00941 84 EAYPALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPLEDFFLGYGKTALEPGELIT 163
|
....*..
gi 2083981135 359 SVFVPYP 365
Cdd:pfam00941 164 AVIIPLP 170
|
|
| glyceraldDH_beta |
NF041019 |
glyceraldehyde dehydrogenase subunit beta; |
202-468 |
9.74e-45 |
|
glyceraldehyde dehydrogenase subunit beta;
Pssm-ID: 468948 [Multi-domain] Cd Length: 280 Bit Score: 158.20 E-value: 9.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 202 IVPASVQALAEVLSQEPDATVVAGSTDvgLWVTKQMRRLSP--VVFINHLSELQTVTESEDGVTIGAgvsYTRAFEAIAR 279
Cdd:NF041019 9 VRPDSLDEALDFLEKHEDAKPLAGGQS--LIPMLKLRIIRPsyLVDINRLKELSYIKDEGNEVRIGA---LTTHYEISKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 280 -----KIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEGQRKIPLEDFFIAYGKQDRKPG 354
Cdd:NF041019 84 divksNLPLLSEAASKIGDPQVRNMGTIGGSLSNADPAADYPAVLLALDAKVVIRSKSGEREVKAKDFFKGPFTTDLNQG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 355 EFVESVFVPYPANSRFaAYKITKRRDEDITAVLGAFLLTLDDaEIVTDIRIAYGGMAATPKRARTVETELIGKSWTEATI 434
Cdd:NF041019 164 EIVTEIVVPALKGYKT-SYQKLVRRAGDFAIVGVAVLLKVSG-GVVEDVRIAYTGVNDKPYRAKEAEKALKGKKLSEELI 241
|
250 260 270
....*....|....*....|....*....|....
gi 2083981135 435 EAARPAFDVDFQPLTDWRATAEYRQLTAKNLLTR 468
Cdd:NF041019 242 EKAAEKASEGANPPSDIRGSSEYRKKVMKVLTKR 275
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
5-161 |
1.48e-40 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 143.01 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 5 IRFILNGEDIElTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVgrlvDGKlayeSVNACIRFTGSLHATHVVT 84
Cdd:NF041020 11 IRVKVNGVWYE-AEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIM----NGK----SVKSCTVLAVQADGAEITT 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2083981135 85 VEHLAgRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYglWLTKEK--PGRREIEKALQGNLCRCTGYEPIVKAAEQVS 161
Cdd:NF041020 82 IEGLS-KDGKLHPIQEAFWENHALQCGYCTPGMIMQAY--FLLKENpnPTEEEIRDGIHGNLCRCTGYQNIVKAVKEAS 157
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
372-473 |
1.45e-30 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 114.25 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 372 AYKITKRRDEDITAVLGAFLLTLDDaEIVTDIRIAYGGMAATPKRARTVETELIGKSWTEATI-EAARPAFDVDFQPLTD 450
Cdd:smart01092 1 AYKKSRRRDGDIALVSAAVALTLDG-GRVTEARIALGGVAPTPKRAAEAEAALVGKPLTDEALaRAAAAALAQDFTPLSD 79
|
90 100
....*....|....*....|...
gi 2083981135 451 WRATAEYRQLTAKNLLTRFYLET 473
Cdd:smart01092 80 MRASAEYRRQLAANLLRRALLEA 102
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
5-71 |
4.58e-05 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 42.00 E-value: 4.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2083981135 5 IRFILNGEDIELtDVGPTETLLDFLRlkRRLTGTKEGCAEGDCGACTVLV----------GRLVDGKLAYESVNACI 71
Cdd:cd00207 1 VTINVPGSGVEV-EVPEGETLLDAAR--EAGIDIPYSCRAGACGTCKVEVvegevdqsdpSLLDEEEAEGGYVLACQ 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
5-480 |
0e+00 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 834.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 5 IRFILNGEDIELTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVGRLVDGKLAYESVNACIRFTGSLHATHVVT 84
Cdd:COG4630 1 IRFLLNGELVELSDVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVGELDDGGLRYRAVNACILFLPQLDGKALVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 85 VEHLAGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAEQVSLMR 164
Cdd:COG4630 81 VEGLAGPDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARAMAEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 165 PSalfDPLERTRSEIIARLWAMQASGTIRIAKGEDRLIVPASVQALAEVLSQEPDATVVAGSTDVGLWVTKQMRRLSPVV 244
Cdd:COG4630 161 AP---DPFAADRAAVAAALRALADGETVELGAGGSRFLAPATLDELAALLAAHPDARLVAGATDVGLWVTKQLRDLPPVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 245 FINHLSELQTVTESEDGVTIGAGVSYTRAFEAIARKIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGA 324
Cdd:COG4630 238 FLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAHFPELAELLRRFASRQIRNAGTLGGNIANGSPIGDSPPALIALGA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 325 TLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVESVFVPYP-ANSRFAAYKITKRRDEDITAVLGAFLLTLDDaEIVTDI 403
Cdd:COG4630 318 ELVLRSGDGRRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPaAGQRLRAYKVSKRFDDDISAVCAAFALTLDD-GTVTEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2083981135 404 RIAYGGMAATPKRARTVETELIGKSWTEATIEAARPAFDVDFQPLTDWRATAEYRQLTAKNLLTRFYLETVGAPAEL 480
Cdd:COG4630 397 RIAFGGMAATPKRARAAEAALLGQPWTEATVAAAAAALAQDFTPLSDMRASAEYRLAVAANLLRRFFLETQGEAPAT 473
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
5-473 |
0e+00 |
|
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274365 [Multi-domain] Cd Length: 467 Bit Score: 807.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 5 IRFILNGEDIELTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVGRLVDG-KLAYESVNACIRFTGSLHATHVV 83
Cdd:TIGR02963 1 IRFFLNGETVTLSDVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVGELVDGgKLRYRSVNACIQFLPSLDGKAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 84 TVEHLAGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAEQVSLM 163
Cdd:TIGR02963 81 TVEDLRQPDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDAAEAAFDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 164 RPSalfDPLERTRSEIIARLWAMQASGTIRIAKGEDRLIVPASVQALAEVLSQEPDATVVAGSTDVGLWVTKQMRRLSPV 243
Cdd:TIGR02963 161 PCS---DPLDADRAPIIERLRALRAGETVELNFGGERFIAPTTLDDLAALKAAHPDARIVAGSTDVGLWVTKQMRDLPDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 244 VFINHLSELQTVTESEDGVTIGAGVSYTRAFEAIARKIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALG 323
Cdd:TIGR02963 238 IYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGELLRRFASLQIRNAGTLGGNIANGSPIGDSPPALIALG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 324 ATLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVESVFVPYPAN-SRFAAYKITKRRDEDITAVLGAFLLTLDDaEIVTD 402
Cdd:TIGR02963 318 ARLTLRKGEGRRTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPgERFRAYKISKRFDDDISAVCAAFNLELDG-GVVAE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2083981135 403 IRIAYGGMAATPKRARTVETELIGKSWTEATIEAARPAFDVDFQPLTDWRATAEYRQLTAKNLLTRFYLET 473
Cdd:TIGR02963 397 IRIAFGGMAATPKRAAATEAALLGKPWNEATVEAAMAALAGDFTPLSDMRASAEYRLLTAKNLLRRFFLET 467
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
24-475 |
5.41e-101 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 329.74 E-value: 5.41e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 24 TLLDFLRlKRRLTGTKEGCAEGDCGACTVLVGRL--VDGKLAYESVNACIRFTGSLHATHVVTVEHLAGRDGALHPVQQA 101
Cdd:PLN02906 3 TLLEYLR-DLGLTGTKLGCGEGGCGACTVMVSHYdrKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGNRRDGLHPVQEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 102 LVDCHGSQCGFCTPGFVMSLYGLWLT-KEKPGRREIEKALQGNLCRCTGYEPIVKAA--------------EQVSL---- 162
Cdd:PLN02906 82 LASMHGSQCGFCTPGFIMSMYALLRSsKTPPTEEQIEECLAGNLCRCTGYRPILDAFrvfaktddalytgvSSLSLqdge 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 163 ---------------------MRPSALFDPLE--------RTRSEII------ARLWAMQASGTiriaKGEDRLIVPASV 207
Cdd:PLN02906 162 picpstgkpcscgskttsaagTCKSDRFQPISyseidgswYTEKELIfppellLRKLTPLKLLG----NGGLTWYRPTSL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 208 QALAEVLSQEPDATVVAGSTDVGLwvtkQMR--RLSPVVFIN--HLSELQTVTESEDGVTIGAGVSYT---RAFEAI--- 277
Cdd:PLN02906 238 QHLLELKAEYPDAKLVVGNTEVGI----EMRfkNAQYPVLISptHVPELNAIKVKDDGLEIGAAVRLSelqNLFRKVvke 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 278 --ARKIPALGRLIDRI---GGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEG-QRKIPLEDFFIAYGKQDR 351
Cdd:PLN02906 314 rpAHETSACKAFIEQLkwfAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFVIISCDGdIRSVPASDFFLGYRKVDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 352 KPGEFVESVFVPYPANSRFAA-YKITKRRDEDITAVLGAFLLTLDDAE---IVTDIRIAYGGMAATPKRARTVETELIGK 427
Cdd:PLN02906 394 KPDEILLSVFLPWTRPFEYVKeFKQAHRRDDDIAIVNAGMRVKLEEKDgewIVSDASIAYGGVAPLSVSARKTEEFLIGK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2083981135 428 SWTEATIEAARPAFDVDFqPLTDWR--ATAEYRQLTAKNLLTRFYLETVG 475
Cdd:PLN02906 474 PWNKETLQDALKVLQKDI-LIKEDApgGMVEFRKSLALSFFFKFFLWVSH 522
|
|
| CutB |
COG1319 |
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion] ... |
204-468 |
3.01e-80 |
|
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440930 [Multi-domain] Cd Length: 285 Bit Score: 251.20 E-value: 3.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 204 PASVQALAEVLSQ-EPDATVVAGSTDVGLWVTKQMRRLSPVVFINHLSELQTVTESEDGVTIGAGVSYTR--AFEAIARK 280
Cdd:COG1319 9 PTSLEEALALLAEhGPDARVLAGGTDLLPLMKLRLARPEHLVDINRIPELRGIEEEGGGLRIGALVTHAElaASPLVRER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 281 IPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVESV 360
Cdd:COG1319 89 YPLLAEAARAIASPQIRNRGTIGGNLANADPAADLPPALLALDATVELAGPDGERTIPAADFFLGPGETALEPGELITAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 361 FVPYPANSRFAAY-KITKRRDEDITAVLGAFLLTLDDaEIVTDIRIAYGGMAATPKRARTVETELIGKSWTEATIEAARP 439
Cdd:COG1319 169 RLPAPPAGAGSAYlKVGRRASDAIALVSVAVALRLDG-GTIRDARIALGGVAPTPWRAREAEAALAGKPLSEEAIEAAAE 247
|
250 260
....*....|....*....|....*....
gi 2083981135 440 AFDVDFQPLTDWRATAEYRQLTAKNLLTR 468
Cdd:COG1319 248 AAAAAADPIDDVRASAEYRRHLARVLVRR 276
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
7-472 |
4.20e-78 |
|
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.
Pssm-ID: 132014 [Multi-domain] Cd Length: 1330 Bit Score: 265.72 E-value: 4.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 7 FILNGEDIELTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVGRL--VDGKLAYESVNACIRFTGSLHATHVVT 84
Cdd:TIGR02969 5 FYVNGRKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYnpSTKSIRHHPVNACLTPICSLYGAAVTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 85 VEHLAGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAA------- 157
Cdd:TIGR02969 85 VEGIGSTRTRLHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACktfckts 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 158 -----------------------EQVSLMRPSAL----FDPLERTRSEI----IARLWAMQASGTiRIAKGEDRL-IVPA 205
Cdd:TIGR02969 165 gccqskengvccldqginglpefEEGDETSPELFseeeFLPLDPTQELIfppeLMRMAEKQPQRT-RVFYSERMMwISPV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 206 SVQALAEVLSQEPDATVVAGSTDVGLWVtKQMRRLSPVVFI-NHLSELQTVTESEDGVTIGAGVSYTRAFEAIA---RKI 281
Cdd:TIGR02969 244 TLKELLEAKFKYPQAPVVMGNTSVGPEV-KFKGVFHPVIISpDRIEELSVVNHTGDGLTLGAGLSLAQVKDILAdvvQKL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 282 P--------ALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEGQRKIPL-EDFFIAYGKQDRK 352
Cdd:TIGR02969 323 PeettqtyrALLKHLGTLAGSQIRNMASLGGHIISRHLDSDLNPLLAVGNCTLNLLSKEGKRQIPLsEQFLSKCPDADLK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 353 PGEFVESVFVPYPANSRFAAYKITKRRDEDITAVL--GAFLLTLDDAEIVTDIRIAYGGMAATPKRARTVETELIGKSWT 430
Cdd:TIGR02969 403 PQEILVSVNIPYSRKWEFVSAFRQAQRQQNALAIVnsGMRVFFGEGDGIIRELSISYGGVGPTTICAKNSCQKLIGRPWN 482
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2083981135 431 EATIE-AARPAFDVDFQPLTDWRATAEYRQLTAKNLLTRFYLE 472
Cdd:TIGR02969 483 EEMLDtACRLILDEVSLAGSAPGGKVEFKRTLIISFLFKFYLE 525
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
200-365 |
1.31e-71 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 224.73 E-value: 1.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 200 RLIVPASVQALAEVLSQEPDATVVAGSTDVGLWVTKQMRRLSPVVFINHLSELQTVTESEDGVTIGAGVSYTRAFEA-IA 278
Cdd:pfam00941 4 GYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPlLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 279 RKIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVE 358
Cdd:pfam00941 84 EAYPALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPLEDFFLGYGKTALEPGELIT 163
|
....*..
gi 2083981135 359 SVFVPYP 365
Cdd:pfam00941 164 AVIIPLP 170
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
5-165 |
1.22e-62 |
|
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441683 [Multi-domain] Cd Length: 155 Bit Score: 200.70 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 5 IRFILNGEDIELtDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVgrlvDGKlayeSVNACIRFTGSLHATHVVT 84
Cdd:COG2080 4 ITLTVNGKPVEV-DVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLV----DGK----AVRSCLTLAVQADGKEITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 85 VEHLAgRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAEQVSLMR 164
Cdd:COG2080 75 IEGLA-EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRAAAAL 153
|
.
gi 2083981135 165 P 165
Cdd:COG2080 154 R 154
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
2-438 |
1.60e-59 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 211.88 E-value: 1.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 2 NDSIRFILNGEDIELTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVGRL--VDGKLAYESVNACIRFTGSLHA 79
Cdd:PLN00192 3 NMSLVFAVNGERFELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLSKYdpVLDQVEDFTVSSCLTLLCSVNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 80 THVVTVEHLAGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRR------------EIEKALQGNLCRC 147
Cdd:PLN00192 83 CSITTSEGLGNSKDGFHPIHKRFAGFHASQCGFCTPGMCISLFSALVNADKTDRPeppsgfskltvvEAEKAVSGNLCRC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 148 TGYEPIVKA----AEQVSLmrpSAL----FDPLERTRSEIIARLWAMQASGTI---------------RIAKGEDRLIVP 204
Cdd:PLN00192 163 TGYRPIVDAcksfAADVDI---EDLglnsFWKKGESEEAKLSKLPPYNHSDHIctfpeflkkeiksslLLDSSRYRWYTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 205 ASVQALAEVL-SQEPDAT---VVAGSTDVGlwVTKQMRRLSPVVFINHLSELQTVTESEDGVTIGAGVSYTRAFEA---- 276
Cdd:PLN00192 240 VSVEELQSLLeSNNFDGVsvkLVVGNTGTG--YYKDEELYDKYIDIRHIPELSMIRRDEKGIEIGAVVTISKAIEAlree 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 277 -----IARKIpalGRLIDRIGGEQVRNMGTIGGNI--ANGSPI-GDSPPPLIALGATLTLRSLEGQRKIPLEDFFiaygk 348
Cdd:PLN00192 318 skseyVFKKI---ADHMEKIASRFVRNTGSIGGNLvmAQRKQFpSDIATILLAAGSTVNIQNASKREKLTLEEFL----- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 349 qDRKPGE---FVESVFVPYPANSR-------FAAYKITKRRDEDITAVL-GAFL-----LTLDDAEIVTDIRIAYGGMAA 412
Cdd:PLN00192 390 -ERPPLDsksLLLSVEIPSWTSSSgsdtkllFETYRAAPRPLGNALPYLnAAFLaevsqDASSGGIVVNDCRLAFGAYGT 468
|
490 500
....*....|....*....|....*...
gi 2083981135 413 T-PKRARTVETELIGKSWTEATI-EAAR 438
Cdd:PLN00192 469 KhAIRARKVEEFLTGKVLSDSVLyEAVR 496
|
|
| PRK09971 |
PRK09971 |
xanthine dehydrogenase subunit XdhB; Provisional |
204-476 |
2.53e-52 |
|
xanthine dehydrogenase subunit XdhB; Provisional
Pssm-ID: 182175 [Multi-domain] Cd Length: 291 Bit Score: 178.69 E-value: 2.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 204 PASVQALAEVLSQEPDATVVAGSTDVGLWVTKQMRRLSPVVFINHLSELQTVTESEDG-VTIGAGVSYTRAFE--AIARK 280
Cdd:PRK09971 10 AATLEEAIELLADNPQAKLIAGGTDVLIQLHHHNDRYRHLVSIHNIAELRGITLAEDGsIRIGAATTFTQIIEdpIIQKH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 281 IPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEGQRKIPLEDFFIAYGKQDRKPGEFVESV 360
Cdd:PRK09971 90 LPALAEAAVSIGGPQIRNVATIGGNICNGATSADSAPPLFALDAKLEIHSPNGVRFVPINGFYTGPGKVSLEHDEILVAF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 361 -FVPYPANSRFAAY-KITKRRDEDITAVLGAFLLTLDDAEIvTDIRIAYGGMAATPKRARTVETELIGKSWTEATIEAAR 438
Cdd:PRK09971 170 iIPPEPYEHAGGAYiKYAMRDAMDIATIGCAVLCRLDNGNF-EDLRLAFGVAAPTPIRCQHAEQTAKGAPLNLETLEAIG 248
|
250 260 270
....*....|....*....|....*....|....*...
gi 2083981135 439 PAFDVDFQPLTDWRATAEYRQLTAKNLLTRFYLETVGA 476
Cdd:PRK09971 249 ELVLQDVAPRSSWRASKEFRLHLIQELTKRVIKEAVAA 286
|
|
| glyceraldDH_beta |
NF041019 |
glyceraldehyde dehydrogenase subunit beta; |
202-468 |
9.74e-45 |
|
glyceraldehyde dehydrogenase subunit beta;
Pssm-ID: 468948 [Multi-domain] Cd Length: 280 Bit Score: 158.20 E-value: 9.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 202 IVPASVQALAEVLSQEPDATVVAGSTDvgLWVTKQMRRLSP--VVFINHLSELQTVTESEDGVTIGAgvsYTRAFEAIAR 279
Cdd:NF041019 9 VRPDSLDEALDFLEKHEDAKPLAGGQS--LIPMLKLRIIRPsyLVDINRLKELSYIKDEGNEVRIGA---LTTHYEISKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 280 -----KIPALGRLIDRIGGEQVRNMGTIGGNIANGSPIGDSPPPLIALGATLTLRSLEGQRKIPLEDFFIAYGKQDRKPG 354
Cdd:NF041019 84 divksNLPLLSEAASKIGDPQVRNMGTIGGSLSNADPAADYPAVLLALDAKVVIRSKSGEREVKAKDFFKGPFTTDLNQG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 355 EFVESVFVPYPANSRFaAYKITKRRDEDITAVLGAFLLTLDDaEIVTDIRIAYGGMAATPKRARTVETELIGKSWTEATI 434
Cdd:NF041019 164 EIVTEIVVPALKGYKT-SYQKLVRRAGDFAIVGVAVLLKVSG-GVVEDVRIAYTGVNDKPYRAKEAEKALKGKKLSEELI 241
|
250 260 270
....*....|....*....|....*....|....
gi 2083981135 435 EAARPAFDVDFQPLTDWRATAEYRQLTAKNLLTR 468
Cdd:NF041019 242 EKAAEKASEGANPPSDIRGSSEYRKKVMKVLTKR 275
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
5-161 |
1.48e-40 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 143.01 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 5 IRFILNGEDIElTDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVgrlvDGKlayeSVNACIRFTGSLHATHVVT 84
Cdd:NF041020 11 IRVKVNGVWYE-AEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIM----NGK----SVKSCTVLAVQADGAEITT 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2083981135 85 VEHLAgRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYglWLTKEK--PGRREIEKALQGNLCRCTGYEPIVKAAEQVS 161
Cdd:NF041020 82 IEGLS-KDGKLHPIQEAFWENHALQCGYCTPGMIMQAY--FLLKENpnPTEEEIRDGIHGNLCRCTGYQNIVKAVKEAS 157
|
|
| CO_deh_flav_C |
pfam03450 |
CO dehydrogenase flavoprotein C-terminal domain; |
371-473 |
4.63e-37 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 460921 [Multi-domain] Cd Length: 102 Bit Score: 131.53 E-value: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 371 AAYKITKRRDEDITAVLGAFLLTLDDAeIVTDIRIAYGGMAATPKRARTVETELIGKSWTEATIEAARPAFDVDFQPLTD 450
Cdd:pfam03450 1 AAYKQAKRRDDDIAIVNAAFRVRLDGG-TVEDARIAFGGVAPTPIRATEAEAALIGKPWDEETLEAAAALLLEDLSPLSD 79
|
90 100
....*....|....*....|...
gi 2083981135 451 WRATAEYRQLTAKNLLTRFYLET 473
Cdd:pfam03450 80 PRGSAEYRRHLARSLLFRFLLEA 102
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
84-157 |
1.62e-34 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 123.69 E-value: 1.62e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2083981135 84 TVEHLAGRDGalHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKE-KPGRREIEKALQGNLCRCTGYEPIVKAA 157
Cdd:pfam01799 1 TIEGLAESGG--EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNPpPPTEAEIREALSGNLCRCTGYRRIVDAV 73
|
|
| pucE |
TIGR03198 |
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ... |
4-160 |
5.08e-34 |
|
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.
Pssm-ID: 132242 [Multi-domain] Cd Length: 151 Bit Score: 125.35 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 4 SIRFILNGEDIELTDVgPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVgrlvDGKLAyesvNACIRFTGSLHATHVV 83
Cdd:TIGR03198 3 QFRFTVNGQAWEVAAV-PTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLI----DGKLA----NACLTMAYQADGHEIT 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2083981135 84 TVEHLAgrDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAEQV 160
Cdd:TIGR03198 74 TIEGIA--ENELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSACRI 148
|
|
| 4hydroxCoAred |
TIGR03193 |
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ... |
25-158 |
2.08e-33 |
|
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts 4-hydroxybenzoyl-CoA to benzoyl-CoA, a common intermediate in the degradation of aromatic compounds. This protein family represents the gamma chain of this three-subunit enzyme.
Pssm-ID: 132237 [Multi-domain] Cd Length: 148 Bit Score: 123.45 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 25 LLDFLRLKRRLTGTKEGCAEGDCGACTVLVgrlvDGklayESVNACIRFTGSLHATHVVTVEHLAGrDGALHPVQQALVD 104
Cdd:TIGR03193 21 LVDYLRDTVGLTGTKQGCDGGECGACTVLV----DG----RPRLACSTLAHRVAGRKVETVEGLAT-NGRLSRLQQAFHE 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2083981135 105 CHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAE 158
Cdd:TIGR03193 92 RLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKIIESVE 145
|
|
| Se_dep_XDH |
TIGR03311 |
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ... |
7-158 |
1.02e-32 |
|
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional xanthine dehydrogenase enzymes, which depend on molybdenum cofactor - molybdopterin bound to molybdate with two sulfur atoms as ligands. But all members of this family occur in species that contain markers for the biosynthesis of enzymes with a selenium-containing form of molybdenum cofactor. The member of this family from Enterococcus faecalis has been shown to act as a xanthine dehydrogenenase, and its activity if dependent on SelD (selenophosphate synthase), selenium, and molybdenum. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132354 [Multi-domain] Cd Length: 848 Bit Score: 132.27 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 7 FILNGEDIeltDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVgrlvDGKlayeSVNACIRFTGSLHATHVVTVE 86
Cdd:TIGR03311 3 FIVNGREV---DVNEEKKLLEFLREDLRLTGVKNGCGEGACGACTVIV----NGK----AVRACRFTTAKLAGKEITTVE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2083981135 87 HLAGRDGALHpvQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAE 158
Cdd:TIGR03311 72 GLTEREKDVY--AWAFAKAGAVQCGFCIPGMVISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKAVR 141
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
4-156 |
8.02e-31 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 116.94 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 4 SIRFILNGEDIELTdVGPTETLLDFLRlKRRLTGTKEGCAEGDCGACTVLVgrlvDGKlayeSVNACIRFTGSLHATHVV 83
Cdd:PRK09908 8 TIECTINGMPFQLH-AAPGTPLSELLR-EQGLLSVKQGCCVGECGACTVLV----DGT----AIDSCLYLAAWAEGKEIR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2083981135 84 TVEHLaGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWltkEKPGRR-----EIEKALQGNLCRCTGYEPIVKA 156
Cdd:PRK09908 78 TLEGE-AKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAML---AKPREKpltitEIRRGLAGNLCRCTGYQMIVNT 151
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
372-473 |
1.45e-30 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 114.25 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 372 AYKITKRRDEDITAVLGAFLLTLDDaEIVTDIRIAYGGMAATPKRARTVETELIGKSWTEATI-EAARPAFDVDFQPLTD 450
Cdd:smart01092 1 AYKKSRRRDGDIALVSAAVALTLDG-GRVTEARIALGGVAPTPKRAAEAEAALVGKPLTDEALaRAAAAALAQDFTPLSD 79
|
90 100
....*....|....*....|...
gi 2083981135 451 WRATAEYRQLTAKNLLTRFYLET 473
Cdd:smart01092 80 MRASAEYRRQLAANLLRRALLEA 102
|
|
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
7-161 |
3.97e-26 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 105.62 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 7 FILNGEDIELtDVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVlvgrLVDGklayESVNACIrftgSLHATH----V 82
Cdd:PRK11433 54 LKVNGKTEQL-EVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTV----LVNG----RRLNACL----TLAVMHqgaeI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 83 VTVEHLaGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLwLTKEKPG----------------RREIEKALQGNLCR 146
Cdd:PRK11433 121 TTIEGL-GSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAV-LKEIKDGipshvtvdltaapeltADEIRERMSGNICR 198
|
170
....*....|....*
gi 2083981135 147 CTGYEPIVKAAEQVS 161
Cdd:PRK11433 199 CGAYSNILEAIEDVA 213
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
4-158 |
3.58e-08 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 55.99 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 4 SIRFILNGEDIELTdVGPTETLLDFLRLKRRLTGTKEGCAEGDCGACTVLVgrlvDGKLayesVNACIRFTGSLHATHVV 83
Cdd:PRK09800 2 IIHFTLNGAPQELT-VNPGENVQKLLFNMGMHSVRNSDDGFGFAGSDAIIF----NGNI----VNASLLIAAQLEKADIR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2083981135 84 TVEHLaGRDGALHPVQQALVDCHGSQCGFCTPGFVMSLYGLWLTKEKPGRREIEKALQGNLCRCTGYEPIVKAAE 158
Cdd:PRK09800 73 TAESL-GKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIE 146
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
5-71 |
4.58e-05 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 42.00 E-value: 4.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2083981135 5 IRFILNGEDIELtDVGPTETLLDFLRlkRRLTGTKEGCAEGDCGACTVLV----------GRLVDGKLAYESVNACI 71
Cdd:cd00207 1 VTINVPGSGVEV-EVPEGETLLDAAR--EAGIDIPYSCRAGACGTCKVEVvegevdqsdpSLLDEEEAEGGYVLACQ 74
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
7-54 |
2.54e-04 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 39.43 E-value: 2.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2083981135 7 FILNGEDIELTDVGPTETLLDFLRlkRRLTGTKEGCAEGDCGACTVLV 54
Cdd:pfam00111 1 VTINGKGVTIEVPDGETTLLDAAE--EAGIDIPYSCRGGGCGTCAVKV 46
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
18-103 |
2.06e-03 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.
Pssm-ID: 432963 [Multi-domain] Cd Length: 107 Bit Score: 37.60 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083981135 18 DVGPTETLLDFL-RLKRRLTGT---KEGCAEGDCGACTVlvgrLVDGKlayeSVNACIRFTGSLHATHvVTVEHLAGrdg 93
Cdd:pfam13085 24 PYEEGMTVLDALnKIKEEQDPTlafRRSCREGICGSCAM----NINGK----PRLACKTLIDDLLGQD-ITLEPLPG--- 91
|
90
....*....|
gi 2083981135 94 alHPVQQALV 103
Cdd:pfam13085 92 --FPVIRDLV 99
|
|
| |
