|
Name |
Accession |
Description |
Interval |
E-value |
| Se_dep_XDH |
TIGR03311 |
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ... |
2-851 |
0e+00 |
|
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: 1624.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEKVVAKEGKKLLDFLREDMNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSERERDV 81
Cdd:TIGR03311 1 YEFIVNGREVDVNEEKKLLEFLREDLRLTGVKNGCGEGACGACTVIVNGKAVRACRFTTAKLAGKEITTVEGLTEREKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 82 FAYSFASQGAVQCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKAVDLAAKIFRENIDVPKVNCKG 161
Cdd:TIGR03311 81 YAWAFAKAGAVQCGFCIPGMVISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKAVRLAAKAFREEIEPPRGEPKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 162 LVGENLPRVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGTIKVGHLKKD 241
Cdd:TIGR03311 161 KLGENFPRVDAVPKVLGEGVYVDDMQIEGMLYGSALRSKYPRALVKSIDITVALKHPGVVAVLTAKDIPGNRKIGHIFKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 242 WDTLIPEGEITRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALREDAPKIHETGNILVKEHLVRGNAKEK 321
Cdd:TIGR03311 241 WPALIAVGEITRYVGDAVALVAAKSKEALREALNLIKVDYEELPPLTSPEEALAEGAPAIHPKGNILSEEHVVRGDAEEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 322 IENSKYVVTKRYTTPATEHAFLEPECAVAGPyEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINKMVGGGFGGKED 401
Cdd:TIGR03311 321 LENSAYVVTNHYSTPFTEHAFLEPESALAVP-EGDGVIIYTSTQGVYDEQRELASLLGLPKEKIRVINKFVGGGFGGKED 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 402 MSVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASLGGPVLQRLCTHA 481
Cdd:TIGR03311 400 MSVQHHAALLAWATKRPVKVTLTRKESILVHPKRHAMEMTFTTGCDEAGNLTAMKADIIADTGAYASLGGPVLQRACTHA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 482 AGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVLPNGQFADEGTAM 561
Cdd:TIGR03311 480 AGPYKYPNVDIRGTAVYTNNPPAGAFRGFGVTQSNFAMECNLNLLAEKVGLSPWEIRFKNAVEPGDTLPNGQVVSEGTAI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 562 AETLEAVKEEYEKHPRAGIACAMKNSGVGVGIPDVGRCRLVIKDGKVHIRTSASCIGQGLGTVMTQVVCETANLLPENIV 641
Cdd:TIGR03311 560 KETLLAVKEVYEKSPCAGIACAFKNSGVGVGIPDTGRCNLAVEDGKVHIRTSAACIGQGLGTVLTQIVCETTGLPPEVIV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 642 HEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKEALdSGKTLLDLEGEEFYGEYESITDKMGCDKENPVSHVAYGYA 721
Cdd:TIGR03311 640 CELPDTALTPDSGTTTASRQSLFTGEATRRAAAKLKEAL-RGRTLAELEGEEFYGEYHSITDPLNSDKENPVSHVGYGYA 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 722 TQVVILDENGKLEKVVAAHDVGRAINPISLEGQIEGGVVMGLGYALTEDYPVVNSVPTAKFGTLGLFKSTDIPEIQALIV 801
Cdd:TIGR03311 719 TQVVILDDAGKVEKVVAAYDVGRAINPLNLEGQIEGGIVMGLGYALTEDFPLREGIPTAKFGTLGLFRSTQVPEIETHLI 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 544956309 802 EKNKDLLAYGAKGVGEICTVPTAPAVQNAYYVFDKEFRTELPLQNTPYSK 851
Cdd:TIGR03311 799 EKNGTPLAYGAKGVGELATIPTAPAVAGAYYRFDGKFRLSLPLENTPYTR 848
|
|
| CoxL |
COG1529 |
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ... |
160-848 |
0e+00 |
|
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 660.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 160 KGLVGENLPRVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGtIKVGHLK 239
Cdd:COG1529 7 FRIIGKPVPRVDGPAKVTGRARYTDDIRLPGMLYAAVVRSPHAHARIKSIDTSAALALPGVVAVLTGEDLPG-LKFGLPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 240 KDWDTLIPEGEITRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALREDAPKIHE--TGNILVKEHLVRGN 317
Cdd:COG1529 86 PDPDQPPLADDKVRYVGEPVAAVVAETREAARDAAELIKVEYEPLPAVVDPEAALAPGAPLVHEelPGNVAAEWRGERGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 318 AKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPYEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINKMVGGGFG 397
Cdd:COG1529 166 VDAAFAEADVVVEATYTTPRLAHAPMEPRAAVAEWDGDGRLTVWASTQGPHLVRRALARALGLPPEKVRVIAPDVGGGFG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 398 GKEDM-SVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASLGGPVLQR 476
Cdd:COG1529 246 GKLDVyPEEVLAALAARKLGRPVKLVLTREEDFLADTHRHATVQRVRLGADKDGKITALRHDVVADTGAYASFGEAVLPL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 477 LCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVLPNGQFAD 556
Cdd:COG1529 326 GATMATGPYAIPNVRVEARAVYTNTPPTGAYRGPGRPQAAFALESAMDELAEELGMDPVELRLRNLIRPGDFPPTGQPYD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 557 EGtAMAETLEAVKEEY---EKHPRA-----------GIACAMKNSGVGvgiPDVGRCRLVI-KDGKVHIRTSASCIGQGL 621
Cdd:COG1529 406 SG-RLAECLEKAAEAFgwgERRARPaearagklrgiGVAAYIEGSGGG---GDPESARVRLnPDGSVTVYTGATDIGQGH 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 622 GTVMTQVVCETANLLPENIVHEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKEA--------LDSGKTLLDLEGEE 693
Cdd:COG1529 482 ETVLAQIAAEELGVPPEDVRVVLGDTDLTPYGGGTGGSRSTAVGGSAVRKAAEKLREKllelaahlLGADPEDLEFEDGR 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 694 FYGEYESITDK-----------MGCDKENPVSHVAYGYATQVVILD---ENG--KLEKVVAAHDVGRAINPISLEGQIEG 757
Cdd:COG1529 562 VRVPGRSVSLAelaaaayygglEATGTYDPPTYPTYSFGAHVAEVEvdpETGevRVLRVVAVHDCGRVINPLLVEGQVEG 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 758 GVVMGLGYALTEDYPVVNS--VPTAKFGTLGLFKSTDIPEIQALIVEKNKDLLAYGAKGVGEICTVPTAPAVQNAyyVFD 835
Cdd:COG1529 642 GVVQGIGQALYEELVYDEDgqLLNANFADYLVPRAADVPEIEVIFVETPDPTNPLGAKGVGEPGTIGVAPAIANA--VYD 719
|
730
....*....|....*.
gi 544956309 836 ---KEFRtELPLqnTP 848
Cdd:COG1529 720 atgVRIR-DLPI--TP 732
|
|
| PRK09970 |
PRK09970 |
xanthine dehydrogenase subunit XdhA; Provisional |
162-830 |
6.36e-123 |
|
xanthine dehydrogenase subunit XdhA; Provisional
Pssm-ID: 236637 [Multi-domain] Cd Length: 759 Bit Score: 388.67 E-value: 6.36e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 162 LVGENLPRVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPgTIK---VGH- 237
Cdd:PRK09970 2 AIGKSIMRVDAIAKVTGRAKYTDDYVMAGMLYAKYVRSPIAHGKVKSIDTEEARSLPGVEAVFTWEDVP-DIPfptAGHp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 238 -----LKKD-WDTLIPEGEItRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALREDAPKIHET-GNILVK 310
Cdd:PRK09970 81 wsldpNHRDiADRALLTRHV-RHHGDAVAAVVARDELTAEKALKLIKVEYEELPVITDPEAALAEGAPPIHNGrGNLLKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 311 EHLVRGNAKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPYEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINK 390
Cdd:PRK09970 160 STMSTGNVQQTIKAADYQVQGHYETPIVQHCHMENVTSYAYMEDDGRITIVSSTQIPHIVRRVVGQALGIPWGKVRVIKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 391 MVGGGFGGKEDMSVQHHAALLAYHTK-RFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASL 469
Cdd:PRK09970 240 YVGGGFGNKQDVLEEPLAAFLTSKVGgRPVKVSLSREECFLATRTRHAFTIDIKMGVNRDGTLKGYSLDVLSNTGAYASH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 470 GGPVLQRLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVL 549
Cdd:PRK09970 320 GHSIASAGGNKVAYLYPRCAYKYSSKTVYTNLPSAGAMRGYGAPQVVFAVESMLDDAATALGIDPVEFRLRNAAREGDAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 550 PNGQFADEGTAMAETLE---------AVKEEYEKHP---RAGIACAM--KNSGV-GVGIpDVGRCRLVI-KDGKVHIRTS 613
Cdd:PRK09970 400 PLSGKRIYSAGLPECLEkgrkifewdKRRAECKNQQgnlRRGVGVACfsYTSGTwPVGL-EIAGARLLMnQDGTVQVQSG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 614 ASCIGQGLGTVMTQVVCETANLLPENI-VHEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKE-ALDSGKTLLDLEG 691
Cdd:PRK09970 479 ATEIGQGSDTVFSQMVAETVGIPVSDVrVISTQDTDVTPFDPGAYASRQSYVAGPAIRKAALELKEkILAHAAVMLHQSA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 692 EEFYGEYESITDK---------------------MGCDKENPVSH------VAYGYATQVVILD-ENGKLE--KVVAAHD 741
Cdd:PRK09970 559 MNLDIIDGHIVVKrpgeplmsleelamdayyhpeRGGQITAESSIktttnpPAFGCTFVDVEVDiALCKVTinRILNVHD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 742 VGRAINPISLEGQIEGGVVMGLGYALTEDY--------PVVNSVPTAKFGTlglfkSTDIPEIQALIVEKNKDLLAYGAK 813
Cdd:PRK09970 639 SGHILNPLLAEGQVHGGMGMGIGWALFEEMiidektgvVRNPNLLDYKLPT-----MMDLPQLESAFVEIYEPQSAYGHK 713
|
730
....*....|....*..
gi 544956309 814 GVGEICTVPTAPAVQNA 830
Cdd:PRK09970 714 SLGEPPIISPAPAIRNA 730
|
|
| MoCoBD_1 |
pfam02738 |
Molybdopterin cofactor-binding domain; |
301-542 |
2.58e-81 |
|
Molybdopterin cofactor-binding domain;
Pssm-ID: 460671 [Multi-domain] Cd Length: 244 Bit Score: 261.62 E-value: 2.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 301 IHETGNILVKEHLVRGNAKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPY-EDDGVIIYSTDQGVFATQHECADMLG 379
Cdd:pfam02738 1 LHEEPPNNVAFHREKGDVEAAFAEADHVVEGEYRTGRQEHFYMETRAALAVPDdEDGRLTVYSSTQGPHLVRRLVARVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 380 LPYEKVRVINKMVGGGFGGK-EDMSVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKAT 458
Cdd:pfam02738 81 IPENKVRVIVPRVGGGFGGKtQSYPEEALAALAARKTGRPVKWVLDREEDMLATGHRHPFLIKYKVGADKDGKILALDVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 459 IISDTGAYASLGGPVLQRLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIR 538
Cdd:pfam02738 161 LYADGGAYADLSPAVPERALSHLDGPYKIPNVRVDGRAVYTNTPPNGAFRGFGRPQGMFALERLMDELAEELGMDPLELR 240
|
....
gi 544956309 539 YKNA 542
Cdd:pfam02738 241 RRNL 244
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
15-150 |
5.56e-37 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 136.46 E-value: 5.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 15 EGKKLL-DFLREDMNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSERER-DVFAYSFASQGAV 92
Cdd:NF041020 25 EPRKLLvHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGKlHPIQEAFWENHAL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 544956309 93 QCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKAVDLAAKIFRE 150
Cdd:NF041020 105 QCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEASQKMKA 162
|
|
| Ald_Xan_dh_C |
smart01008 |
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses ... |
178-285 |
1.42e-33 |
|
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.
Pssm-ID: 214971 [Multi-domain] Cd Length: 107 Bit Score: 124.55 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 178 GYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGTIKVGHLKKDwDTLIPEGEItRYLGD 257
Cdd:smart01008 2 GEARYGDDIRLPGMLHAAVVRSPVAHARIKSIDTSAARAMPGVVAVLTAKDVPGLNDFGPLGPD-EPVLADDKV-RYVGQ 79
|
90 100
....*....|....*....|....*...
gi 544956309 258 GIVLVAAETREALEEAKKLVKIDYEELT 285
Cdd:smart01008 80 PVAAVVAETEEAARDAAEAVKVEYEELP 107
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
2-49 |
8.12e-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: 8.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEK--VVAKEGKKLLDFLREDmNITsVKNGCSEGACGTCMVIID 49
Cdd:cd00207 1 VTINVPGSGveVEVPEGETLLDAAREA-GID-IPYSCRAGACGTCKVEVV 48
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Se_dep_XDH |
TIGR03311 |
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ... |
2-851 |
0e+00 |
|
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: 1624.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEKVVAKEGKKLLDFLREDMNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSERERDV 81
Cdd:TIGR03311 1 YEFIVNGREVDVNEEKKLLEFLREDLRLTGVKNGCGEGACGACTVIVNGKAVRACRFTTAKLAGKEITTVEGLTEREKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 82 FAYSFASQGAVQCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKAVDLAAKIFRENIDVPKVNCKG 161
Cdd:TIGR03311 81 YAWAFAKAGAVQCGFCIPGMVISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKAVRLAAKAFREEIEPPRGEPKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 162 LVGENLPRVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGTIKVGHLKKD 241
Cdd:TIGR03311 161 KLGENFPRVDAVPKVLGEGVYVDDMQIEGMLYGSALRSKYPRALVKSIDITVALKHPGVVAVLTAKDIPGNRKIGHIFKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 242 WDTLIPEGEITRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALREDAPKIHETGNILVKEHLVRGNAKEK 321
Cdd:TIGR03311 241 WPALIAVGEITRYVGDAVALVAAKSKEALREALNLIKVDYEELPPLTSPEEALAEGAPAIHPKGNILSEEHVVRGDAEEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 322 IENSKYVVTKRYTTPATEHAFLEPECAVAGPyEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINKMVGGGFGGKED 401
Cdd:TIGR03311 321 LENSAYVVTNHYSTPFTEHAFLEPESALAVP-EGDGVIIYTSTQGVYDEQRELASLLGLPKEKIRVINKFVGGGFGGKED 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 402 MSVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASLGGPVLQRLCTHA 481
Cdd:TIGR03311 400 MSVQHHAALLAWATKRPVKVTLTRKESILVHPKRHAMEMTFTTGCDEAGNLTAMKADIIADTGAYASLGGPVLQRACTHA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 482 AGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVLPNGQFADEGTAM 561
Cdd:TIGR03311 480 AGPYKYPNVDIRGTAVYTNNPPAGAFRGFGVTQSNFAMECNLNLLAEKVGLSPWEIRFKNAVEPGDTLPNGQVVSEGTAI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 562 AETLEAVKEEYEKHPRAGIACAMKNSGVGVGIPDVGRCRLVIKDGKVHIRTSASCIGQGLGTVMTQVVCETANLLPENIV 641
Cdd:TIGR03311 560 KETLLAVKEVYEKSPCAGIACAFKNSGVGVGIPDTGRCNLAVEDGKVHIRTSAACIGQGLGTVLTQIVCETTGLPPEVIV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 642 HEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKEALdSGKTLLDLEGEEFYGEYESITDKMGCDKENPVSHVAYGYA 721
Cdd:TIGR03311 640 CELPDTALTPDSGTTTASRQSLFTGEATRRAAAKLKEAL-RGRTLAELEGEEFYGEYHSITDPLNSDKENPVSHVGYGYA 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 722 TQVVILDENGKLEKVVAAHDVGRAINPISLEGQIEGGVVMGLGYALTEDYPVVNSVPTAKFGTLGLFKSTDIPEIQALIV 801
Cdd:TIGR03311 719 TQVVILDDAGKVEKVVAAYDVGRAINPLNLEGQIEGGIVMGLGYALTEDFPLREGIPTAKFGTLGLFRSTQVPEIETHLI 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 544956309 802 EKNKDLLAYGAKGVGEICTVPTAPAVQNAYYVFDKEFRTELPLQNTPYSK 851
Cdd:TIGR03311 799 EKNGTPLAYGAKGVGELATIPTAPAVAGAYYRFDGKFRLSLPLENTPYTR 848
|
|
| CoxL |
COG1529 |
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ... |
160-848 |
0e+00 |
|
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 660.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 160 KGLVGENLPRVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGtIKVGHLK 239
Cdd:COG1529 7 FRIIGKPVPRVDGPAKVTGRARYTDDIRLPGMLYAAVVRSPHAHARIKSIDTSAALALPGVVAVLTGEDLPG-LKFGLPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 240 KDWDTLIPEGEITRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALREDAPKIHE--TGNILVKEHLVRGN 317
Cdd:COG1529 86 PDPDQPPLADDKVRYVGEPVAAVVAETREAARDAAELIKVEYEPLPAVVDPEAALAPGAPLVHEelPGNVAAEWRGERGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 318 AKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPYEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINKMVGGGFG 397
Cdd:COG1529 166 VDAAFAEADVVVEATYTTPRLAHAPMEPRAAVAEWDGDGRLTVWASTQGPHLVRRALARALGLPPEKVRVIAPDVGGGFG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 398 GKEDM-SVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASLGGPVLQR 476
Cdd:COG1529 246 GKLDVyPEEVLAALAARKLGRPVKLVLTREEDFLADTHRHATVQRVRLGADKDGKITALRHDVVADTGAYASFGEAVLPL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 477 LCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVLPNGQFAD 556
Cdd:COG1529 326 GATMATGPYAIPNVRVEARAVYTNTPPTGAYRGPGRPQAAFALESAMDELAEELGMDPVELRLRNLIRPGDFPPTGQPYD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 557 EGtAMAETLEAVKEEY---EKHPRA-----------GIACAMKNSGVGvgiPDVGRCRLVI-KDGKVHIRTSASCIGQGL 621
Cdd:COG1529 406 SG-RLAECLEKAAEAFgwgERRARPaearagklrgiGVAAYIEGSGGG---GDPESARVRLnPDGSVTVYTGATDIGQGH 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 622 GTVMTQVVCETANLLPENIVHEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKEA--------LDSGKTLLDLEGEE 693
Cdd:COG1529 482 ETVLAQIAAEELGVPPEDVRVVLGDTDLTPYGGGTGGSRSTAVGGSAVRKAAEKLREKllelaahlLGADPEDLEFEDGR 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 694 FYGEYESITDK-----------MGCDKENPVSHVAYGYATQVVILD---ENG--KLEKVVAAHDVGRAINPISLEGQIEG 757
Cdd:COG1529 562 VRVPGRSVSLAelaaaayygglEATGTYDPPTYPTYSFGAHVAEVEvdpETGevRVLRVVAVHDCGRVINPLLVEGQVEG 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 758 GVVMGLGYALTEDYPVVNS--VPTAKFGTLGLFKSTDIPEIQALIVEKNKDLLAYGAKGVGEICTVPTAPAVQNAyyVFD 835
Cdd:COG1529 642 GVVQGIGQALYEELVYDEDgqLLNANFADYLVPRAADVPEIEVIFVETPDPTNPLGAKGVGEPGTIGVAPAIANA--VYD 719
|
730
....*....|....*.
gi 544956309 836 ---KEFRtELPLqnTP 848
Cdd:COG1529 720 atgVRIR-DLPI--TP 732
|
|
| pucD |
TIGR03196 |
xanthine dehydrogenase D subunit; This gene has been characterized in B. subtilis as the ... |
169-833 |
2.27e-134 |
|
xanthine dehydrogenase D subunit; This gene has been characterized in B. subtilis as the molybdopterin binding-subunit of xanthine dehydrogenase (pucD), acting in conjunction with pucC, the FAD-binding subunit and pucE, the FeS-binding subunit. The more common XDH complex (GenProp0640) includes the xdhB gene which is related to pucD. It appears that most of the relatives of pucD outside of this narrow clade are involved in other processes as they are found in unrelated genomic contexts, contain the more common XDH complex and/or do not appear to process purines to allantoin.
Pssm-ID: 132240 [Multi-domain] Cd Length: 768 Bit Score: 419.06 E-value: 2.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 169 RVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGTIKVGHLKKDwDTLIPE 248
Cdd:TIGR03196 10 RPDGPDKVTGEFKYMGDLRFPGMLHAKTLRSAHAHAEIRRVCTDAAEKLEGVQAMVTAADVPGLARFGIIIAD-QPVFAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 249 GEItRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALREDAPKIHETGNILVKEHLVRGNAKEKIENSKYV 328
Cdd:TIGR03196 89 DEI-RYAGDAIAAVAAEDEEIAEAALAAIEVDYEELAPMDDPDKALQPDAEPLHEAGNILHEAEFRHGDPDEGFAAGDTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 329 VTKRYTTPATEHAFLEPECAVAGPYEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINKMVGGGFGGKEDMSVQHHA 408
Cdd:TIGR03196 168 FEDQYELGMQDHAFLAPEAALAMPAADGGFDLRAATQHGHKDREQIAACFDIPEEKIRITLAGMGGAFGGKDDLNIQIHA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 409 ALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASLGGPVLQRLCTHAAGPYNYQ 488
Cdd:TIGR03196 248 ALLALASGLPVKIAQDRKESFLGGIHRHPAKITFKHGADADGNLLAHDAKIVADGGAYASLGPAVLAFAVEHAAGPYRIP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 489 DIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVLPNGQFADEGTAMAETLEAV 568
Cdd:TIGR03196 328 NAHLEGISVFTNNGPAGAFRGFGGNQITFAHEAHLDRLADALGIDPLDLRRKNARKPGDLGPLEHRIAAPDGAAEVIEAI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 569 KEE-------YEKHPRA---------------------GIACAMKNSGVGVGIPD--VGRCRLVI-KDGKVHIRTSASC- 616
Cdd:TIGR03196 408 ASRplpkapiLKKANRAvtalpggrpaaaecgrlqrgtGAAIAMHGGGFGEGMDDaaVAGARLELaEDGTVKIRAHFACa 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 617 -IGQGLGTVMTQVVCETANLLPENIVHEVPDTHLTPDSGNTTASRQTVFTGEATK-----VASNKLKEALD-SGK----- 684
Cdd:TIGR03196 488 eCGQGFLAAAEQIAMEELGCAAEDISIAIADTAKGPKAGSSSASRGTSMSGGAIQgacaaFAAQLKARAAEtAGLpaevv 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 685 -------------------------TLLDLEGEEFYGEYESITDK----MGCDKENPVSHVAYGYATQVVILD---ENGK 732
Cdd:TIGR03196 568 eapaenlipgaaeivgdkneaalrvPLAEAAADGPIAAETAFHDFptsaLDADVGQGDGHFAFAAAAAAAEVDvdlDLGD 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 733 LEKVVAAH--DVGRAINPISLEGQIEGGVVMGLGYALTEDYPVVNSVPTAK-FGTLGLFKSTDIPEIQALIVEKNKDLLA 809
Cdd:TIGR03196 648 VKLIDCAHaiAAGPVLNPLALRGQIEGGAAMALGLALMEEAKMTDGRVAAEnFDDYLIPGIADVPDLDFIAIEDLMKDAP 727
|
730 740
....*....|....*....|....
gi 544956309 810 YGAKGVGEICTVPTAPAVQNAYYV 833
Cdd:TIGR03196 728 YGPKGVGEAGTCAATPAIIAAIHD 751
|
|
| PRK09970 |
PRK09970 |
xanthine dehydrogenase subunit XdhA; Provisional |
162-830 |
6.36e-123 |
|
xanthine dehydrogenase subunit XdhA; Provisional
Pssm-ID: 236637 [Multi-domain] Cd Length: 759 Bit Score: 388.67 E-value: 6.36e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 162 LVGENLPRVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPgTIK---VGH- 237
Cdd:PRK09970 2 AIGKSIMRVDAIAKVTGRAKYTDDYVMAGMLYAKYVRSPIAHGKVKSIDTEEARSLPGVEAVFTWEDVP-DIPfptAGHp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 238 -----LKKD-WDTLIPEGEItRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALREDAPKIHET-GNILVK 310
Cdd:PRK09970 81 wsldpNHRDiADRALLTRHV-RHHGDAVAAVVARDELTAEKALKLIKVEYEELPVITDPEAALAEGAPPIHNGrGNLLKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 311 EHLVRGNAKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPYEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINK 390
Cdd:PRK09970 160 STMSTGNVQQTIKAADYQVQGHYETPIVQHCHMENVTSYAYMEDDGRITIVSSTQIPHIVRRVVGQALGIPWGKVRVIKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 391 MVGGGFGGKEDMSVQHHAALLAYHTK-RFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASL 469
Cdd:PRK09970 240 YVGGGFGNKQDVLEEPLAAFLTSKVGgRPVKVSLSREECFLATRTRHAFTIDIKMGVNRDGTLKGYSLDVLSNTGAYASH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 470 GGPVLQRLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVL 549
Cdd:PRK09970 320 GHSIASAGGNKVAYLYPRCAYKYSSKTVYTNLPSAGAMRGYGAPQVVFAVESMLDDAATALGIDPVEFRLRNAAREGDAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 550 PNGQFADEGTAMAETLE---------AVKEEYEKHP---RAGIACAM--KNSGV-GVGIpDVGRCRLVI-KDGKVHIRTS 613
Cdd:PRK09970 400 PLSGKRIYSAGLPECLEkgrkifewdKRRAECKNQQgnlRRGVGVACfsYTSGTwPVGL-EIAGARLLMnQDGTVQVQSG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 614 ASCIGQGLGTVMTQVVCETANLLPENI-VHEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKE-ALDSGKTLLDLEG 691
Cdd:PRK09970 479 ATEIGQGSDTVFSQMVAETVGIPVSDVrVISTQDTDVTPFDPGAYASRQSYVAGPAIRKAALELKEkILAHAAVMLHQSA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 692 EEFYGEYESITDK---------------------MGCDKENPVSH------VAYGYATQVVILD-ENGKLE--KVVAAHD 741
Cdd:PRK09970 559 MNLDIIDGHIVVKrpgeplmsleelamdayyhpeRGGQITAESSIktttnpPAFGCTFVDVEVDiALCKVTinRILNVHD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 742 VGRAINPISLEGQIEGGVVMGLGYALTEDY--------PVVNSVPTAKFGTlglfkSTDIPEIQALIVEKNKDLLAYGAK 813
Cdd:PRK09970 639 SGHILNPLLAEGQVHGGMGMGIGWALFEEMiidektgvVRNPNLLDYKLPT-----MMDLPQLESAFVEIYEPQSAYGHK 713
|
730
....*....|....*..
gi 544956309 814 GVGEICTVPTAPAVQNA 830
Cdd:PRK09970 714 SLGEPPIISPAPAIRNA 730
|
|
| XdhB |
COG4631 |
Xanthine dehydrogenase, molybdopterin-binding subunit XdhB [Nucleotide transport and ... |
160-817 |
3.92e-90 |
|
Xanthine dehydrogenase, molybdopterin-binding subunit XdhB [Nucleotide transport and metabolism];
Pssm-ID: 443669 [Multi-domain] Cd Length: 769 Bit Score: 301.65 E-value: 3.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 160 KGLVGENLPRVDAVGKALGYSEYVDDMRI-EGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGTIKVGHL 238
Cdd:COG4631 11 AGAVGKSLPHESARLHVTGEARYIDDLPEpAGTLHAAPGLSPVAHARILSIDLSAVRAAPGVVAVLTAADIPGENDIGPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 239 KKDwDTLIPEGEItRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADAlredapkiHETGNILVKEH-LVRGN 317
Cdd:COG4631 91 IHD-EPLLADGEV-EYVGQPVFAVVAESREAARRAARLAKIEYEELPAILTIEEA--------LAAGSFVLPPHtLRRGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 318 AKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPYEDDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINKMVGGGFG 397
Cdd:COG4631 161 ADAALAAAPHRLEGEFEIGGQEHFYLEGQIALAIPGEDGGMLVHSSTQHPSEVQHLVAHVLGVPMHAVTVEVRRMGGGFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 398 GKEDMSVQH--HAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASLGGPVLQ 475
Cdd:COG4631 241 GKESQAALFaaLAALAARKTGRPVKLRLDRDDDMVMTGKRHPFRIDYEVGFDDDGRILGLDITLAARCGWSADLSGPVAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 476 RLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKN--AIRPGQVLPNGQ 553
Cdd:COG4631 321 RAMFHADNAYYLPAVRITGHRCKTNTQSNTAFRGFGGPQGMLAIERVIDDIARALGLDPLDVRRRNfyGPAERNTTPYGQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 554 FADEGTaMAETLEAVKE--EYEKHpRAGIACAMKNSGV---GVGIPDV--------------GRCRLVIKDGKVHIRTSA 614
Cdd:COG4631 401 PVEDNI-LHELVDELEEssDYAAR-RAAIAAFNAASPVlkrGLALTPVkfgisftathlnqaGALVHVYTDGSVQLNHGG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 615 SCIGQGLGTVMTQVVCETANLLPENIVHEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKEAL-------------- 680
Cdd:COG4631 479 TEMGQGLHTKVAQVVADELGVPLERVRITATDTDKVPNTSATAASSGSDLNGMAAQDACRQIRERLaafaaellgveped 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 681 --------DSGKTLLDLEGEEFYGEYESI---------TDKMGCDKE----NPVSHVAYGYA-TQVVIlD----ENgKLE 734
Cdd:COG4631 559 vrfadgrvRVGGQSLSFAELVKAAYLARVslsatgfykTPKIHWDRAtgqgRPFYYFAYGAAvSEVEI-DtltgEY-RVL 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 735 KVVAAHDVGRAINP-ISLeGQIEGGVVMGLGYALTED----------------YpvvnSVPTAKfgtlglfkstDIPEI- 796
Cdd:COG4631 637 RVDILHDVGRSLNPaIDI-GQIEGGFVQGMGWLTTEElvwddkgrllthapstY----KIPAAS----------DRPEDf 701
|
730 740
....*....|....*....|..
gi 544956309 797 -QALIVEKNKDLLAYGAKGVGE 817
Cdd:COG4631 702 nVALLERPNREDTIYRSKAVGE 723
|
|
| MoCoBD_1 |
pfam02738 |
Molybdopterin cofactor-binding domain; |
301-542 |
2.58e-81 |
|
Molybdopterin cofactor-binding domain;
Pssm-ID: 460671 [Multi-domain] Cd Length: 244 Bit Score: 261.62 E-value: 2.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 301 IHETGNILVKEHLVRGNAKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPY-EDDGVIIYSTDQGVFATQHECADMLG 379
Cdd:pfam02738 1 LHEEPPNNVAFHREKGDVEAAFAEADHVVEGEYRTGRQEHFYMETRAALAVPDdEDGRLTVYSSTQGPHLVRRLVARVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 380 LPYEKVRVINKMVGGGFGGK-EDMSVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKAT 458
Cdd:pfam02738 81 IPENKVRVIVPRVGGGFGGKtQSYPEEALAALAARKTGRPVKWVLDREEDMLATGHRHPFLIKYKVGADKDGKILALDVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 459 IISDTGAYASLGGPVLQRLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIR 538
Cdd:pfam02738 161 LYADGGAYADLSPAVPERALSHLDGPYKIPNVRVDGRAVYTNTPPNGAFRGFGRPQGMFALERLMDELAEELGMDPLELR 240
|
....
gi 544956309 539 YKNA 542
Cdd:pfam02738 241 RRNL 244
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
2-830 |
1.04e-72 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 257.45 E-value: 1.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEK--VVAKEGKKLLDFLReDMNITSVKNGCS-EGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSE-R 77
Cdd:PRK09800 3 IHFTLNGAPqeLTVNPGENVQKLLF-NMGMHSVRNSDDgFGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGKwN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 78 ERDVFAYSFASQGAVQCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKAVDLA------------- 144
Cdd:PRK09800 82 ELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIELAvarknnpqatidi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 145 AKIFRENIDVpkvnckglVGENLPRVDAVGKALGYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVL 224
Cdd:PRK09800 162 APTFRDDLEV--------IGKHYPKTDAAKMVQAKPCYVEDRVTADACVIKMLRSPHAHALITHLDVSKAEALPGVVHVI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 225 TAKDIPGTikvghlkkdWDTL----IPE---------GEITRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTA 291
Cdd:PRK09800 234 THLNCPDI---------YYTPggqsAPEpspldrrmfGKKMRHVGDRVAAVVAESEEIALEALKLIDVEYEVLKPVMSID 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 292 DALREDAPKIHET-------------------------------------GNILVKEHLVRGNAKEKIENSKYVVTKRYT 334
Cdd:PRK09800 305 EAMAEDAPVVHDEpvvyvagapdtleddnshaaqrgehmiinfpigsrprKNIAASIHGHIGDMDKGFADADVIIERTYN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 335 TPATEHAFLEPEcaVAGPYED-DGVIIYSTDQGVFATQHECADMLGLPYEKVRVINKMVGGGFGGKEDMSVQHHAALLAY 413
Cdd:PRK09800 385 STQAQQCPTETH--ICFTRMDgDRLVIHASTQVPWHLRRQVARLVGMKQHKVHVIKERVGGGFGSKQDILLEEVCAWATC 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 414 HTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYASLGGPVLQRLCTHAAGPYNYQDIDIT 493
Cdd:PRK09800 463 VTGRPVLFRYTREEEFIANTSRHVAKVTVKLGAKKDGRLTAVKMDFRANTGPYGNHSLTVPCNGPALSLPLYPCDNVDFQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 494 GTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQVLPNGQFADEG-------TAMAETLE 566
Cdd:PRK09800 543 VTTYYSNICPNGAYQGYGAPKGNFAITMALAELAEQLQIDQLEIIERNRVHEGQELKILGAIGEGkaptsvpSAASCALE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 567 AVKEEYEK--------------HPRAGIACAMKNSgvgvGIPDVGRCRLVIK---DGKVHIRTSASCIGQGLGTVMTQVV 629
Cdd:PRK09800 623 EILRQGREmiqwsspkpqngdwHIGRGVAIIMQKS----GIPDIDQANCMIKlesDGTFIVHSGGADIGTGLDTVVTKLA 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 630 CETANLLPENIVHEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKEA-LDSGKTLLDLEGEEFYGEYESIT-DKMGC 707
Cdd:PRK09800 699 AEVLHCPPQDVHVISGDTDHALFDKGAYASSGTCFSGNAARLAAENLREKiLFHGAQMLGEPVADVQLATPGVVrGKKGE 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 708 DKENPVSH-----------VAYG-YAT------------QVVILDENG--KLEKVVAAHDVGRAINPISLEGQIEGGVVM 761
Cdd:PRK09800 779 VSFGDIAHkgetgtgfgslVGTGsYITpdfafpyganfaEVAVNTRTGeiRLDKFYALLDCGTPVNPELALGQIYGATLR 858
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544956309 762 GLGYALTEDYPV-VNSVPTAK-FGTLGLFKSTDIP-EIQALIVEKNKDLLAYGAKGVGEICTVPTAPAVQNA 830
Cdd:PRK09800 859 AIGHSMSEEIIYdAEGHPLTRdLRSYGAPKIGDIPrDFRAVLVPSDDKVGPFGAKSISEIGVNGAAPAIATA 930
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
1-150 |
1.21e-63 |
|
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: 210.33 E-value: 1.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 1 MVEFILNGEK--VVAKEGKKLLDFLREDMNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSERE 78
Cdd:COG2080 3 MITLTVNGKPveVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544956309 79 R-DVFAYSFASQGAVQCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKAVDLAAKIFRE 150
Cdd:COG2080 83 ElHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRAAAALRG 155
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
165-770 |
2.03e-60 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 223.42 E-value: 2.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 165 ENLPRVDAVGKAL----------GYSEYVDDMRI-EGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGTI 233
Cdd:PLN02906 557 ETVKQGTAVGQPEvhlsaelqvtGEAEYADDIPMpPNTLHAALVLSTKPHARILSIDDSEAKSSPGFAGIFLAKDVPGDN 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 234 KVGHLKKDwDTLIPeGEITRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTADALreDAPKIHETgnilVKEHL 313
Cdd:PLN02906 637 MIGPVVHD-EELFA-TDVVTCVGQVIGVVVADTQENAKAAARKVKVEYEELPAILSIEEAI--EAGSFHPN----TERRL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 314 VRGNAKEKIENSK--YVVTKRYTTPATEHAFLEPECAVAGPYE-DDGVIIYSTDQGVFATQHECADMLGLPYEKVRVINK 390
Cdd:PLN02906 709 EKGDVELCFASGQcdRIIEGEVQMGGQEHFYLEPNSSLVWTSDsGNEVHMISSTQAPQKHQKYVAHVLGLPMSKVVCKTK 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 391 MVGGGFGGKEDMSVQHH--AALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGAYAS 468
Cdd:PLN02906 789 RIGGGFGGKETRSAFIAaaAAVPAYLLNRPVKLTLDRDVDMMITGQRHAFLGKYKVGFTNEGKILALDLEIYNNGGNSLD 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 469 LGGPVLQRLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKNAIRPGQV 548
Cdd:PLN02906 869 LSGAVLERAMFHSDNVYEIPNVRIVGNVCFTNFPSNTAFRGFGGPQGMLITENWIQRIAVELNKSPEEIREMNFQGEGSV 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 549 LPNGQFA---------DEGTAMAETLEAVKEEYE-----KHPRAGIacAMKNSGVGVG-----IPDVGRCRLVIKDGKVH 609
Cdd:PLN02906 949 THYGQVLqhctlpqlwDELKVSCDFLKRREEVDEfnaknRWKKRGV--AMVPTKFGISfttkfMNQAGALVHVYTDGTVL 1026
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 610 IRTSASCIGQGLGTVMTQvVCETANLLPENIVHeVPDTHL--TPDSGNTTASRQTVFTGEATKVASNKLKEAL------- 680
Cdd:PLN02906 1027 VTHGGVEMGQGLHTKVAQ-VAASAFNIPLSSVF-ISETSTdkVPNASPTAASASSDMYGAAVLDACEQIKARMepvaskl 1104
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 681 --DSGKTL--------LDLEGEEFYgeyesITDKMGCD----KENPVSHVAYGYATQVVILDE---NGKLEKVVAAHDVG 743
Cdd:PLN02906 1105 nfSSFAELvtacyfqrIDLSAHGFY-----ITPDIGFDwktgKGNPFNYFTYGAAFAEVEIDTltgDFHTRRVDIVMDLG 1179
|
650 660
....*....|....*....|....*..
gi 544956309 744 RAINPISLEGQIEGGVVMGLGYALTED 770
Cdd:PLN02906 1180 YSINPAIDIGQIEGAFVQGLGWVALEE 1206
|
|
| MoCoBD_2 |
pfam20256 |
Molybdopterin cofactor-binding domain; |
579-771 |
1.71e-37 |
|
Molybdopterin cofactor-binding domain;
Pssm-ID: 466407 [Multi-domain] Cd Length: 282 Bit Score: 141.91 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 579 GIACAMKNSGVGVGIPDVGRCRLVI-KDGKVHIRTSASCIGQGLGTVMTQVVCETANLLPENIVHEVPDTHLTPDSGNTT 657
Cdd:pfam20256 28 GIAPYVEGSGLGPGALNQAGALVRLnPDGSVTVYTGGTEMGQGLETKLAQIAAEALGIPPEDVRVVEGDTDTVPNGGGTG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 658 ASRQTVFTGEATKVASNKLKEAL---------------------------DSGKTLLDLEGEEFYGEY---ESITDKMGC 707
Cdd:pfam20256 108 ASRSTDVGGNAVLLAAEKLRERLlkiaahlleaspedlefedgkvyvkgdPRSVTFAELAAAAYGEGVglsATGFYTPPD 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 708 DKENPVS-HVAYGYATQVVILD---ENG--KLEKVVAAHDVGRAINPISLEGQIEGGVVMGLGYALTEDY 771
Cdd:pfam20256 188 DETGQGPpFAYYPYGAHAAEVEvdpETGevRVLRYVAVHDCGRVINPAIVEGQIEGGFVQGIGLALMEEL 257
|
|
| 4hydroxCoAred |
TIGR03193 |
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ... |
6-145 |
3.94e-37 |
|
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: 136.16 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 6 LNG---EKVVAkEGKKLLDFLREDMNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSERER-DV 81
Cdd:TIGR03193 6 VNGrwrEDAVA-DNMLLVDYLRDTVGLTGTKQGCDGGECGACTVLVDGRPRLACSTLAHRVAGRKVETVEGLATNGRlSR 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544956309 82 FAYSFASQGAVQCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKAVDLAA 145
Cdd:TIGR03193 85 LQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKIIESVEAAA 148
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
163-771 |
5.33e-37 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 150.64 E-value: 5.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 163 VGENLPRVDAVGKALGYSEYVDDM-RIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIP-GTIKVGHLKK 240
Cdd:PLN00192 579 VGEPIKKVGAALQASGEAVYVDDIpSPKNCLYGAFIYSTKPLARVKGIKFKSNLVPQGVLAVITFKDIPkGGQNIGSKTI 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 241 DWDTLIPEGEITRYLGDGIVLVAAETREALEEAKKLVKIDY--EEL-TPLSTTADALRED---------APKihETGNIL 308
Cdd:PLN00192 659 FGPEPLFADEVTRCAGQRIALVVADTQKHADMAANLAVVEYdtENLePPILTVEDAVKRSslfevppflYPK--PVGDIS 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 309 vkehlvRG--NAKEKIENSKYVVTKRYttpateHAFLEPECAVAGPYEDDGVIIYSTDQGVFATQHECADMLGLPYEKVR 386
Cdd:PLN00192 737 ------KGmaEADHKILSAEIKLGSQY------YFYMETQTALALPDEDNCIVVYSSTQCPEYVHSVIARCLGIPEHNVR 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 387 VINKMVGGGFGGK--EDMSVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTG 464
Cdd:PLN00192 805 VITRRVGGGFGGKavKSMPVATACALAAFKLQRPVRMYLNRKTDMIMAGGRHPMKITYSVGFKSDGKITALHLDILINAG 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 465 AYASLgGPVLQRLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIRYKN--- 541
Cdd:PLN00192 885 ISPDI-SPIMPRNIIGALKKYDWGALSFDIKVCKTNLSSRSAMRAPGEVQGSYIAEAIIEHVASTLSMDVDSVRKINlht 963
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 542 --AIRpgqvlpngQFADE--GTAMAETL-----------------EAVKE--EYEKHPRAGIACamknsgvgvgIPDVGR 598
Cdd:PLN00192 964 yeSLK--------LFYGDsaGEPSEYTLpsiwdklasssefkqrtEMVKEfnRSNKWKKRGISR----------VPIVHE 1025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 599 CRLVIKDGKVHIRTSASC--------IGQGLGTVMTQVV--------CETANLLPENIVHEVPDTHLTPDSGNTTASRQT 662
Cdd:PLN00192 1026 VMLRPTPGKVSILSDGSIavevggieIGQGLWTKVKQMAafglgmikCDGGEDLLDKIRVIQSDTLSMIQGGFTAGSTTS 1105
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 663 VFTGEATKVASNKLKEALDSGKTLLD-----------LEGEEFYGEYESITDKMGCDkENPVSHVAYGYATQVVILDE-N 730
Cdd:PLN00192 1106 ESSCEAVRLCCVILVERLKPIKERLQeqmgsvtwdmlISQAYMQSVNLSASSYYTPD-PSSMEYLNYGAAVSEVEVDLlT 1184
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 544956309 731 GKLEKVVA--AHDVGRAINPISLEGQIEGGVVMGLGYALTEDY 771
Cdd:PLN00192 1185 GETTILRSdiIYDCGQSLNPAVDLGQIEGAFVQGIGFFMLEEY 1227
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
15-150 |
5.56e-37 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 136.46 E-value: 5.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 15 EGKKLL-DFLREDMNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSERER-DVFAYSFASQGAV 92
Cdd:NF041020 25 EPRKLLvHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGKlHPIQEAFWENHAL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 544956309 93 QCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKAVDLAAKIFRE 150
Cdd:NF041020 105 QCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEASQKMKA 162
|
|
| Ald_Xan_dh_C |
smart01008 |
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses ... |
178-285 |
1.42e-33 |
|
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.
Pssm-ID: 214971 [Multi-domain] Cd Length: 107 Bit Score: 124.55 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 178 GYSEYVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGTIKVGHLKKDwDTLIPEGEItRYLGD 257
Cdd:smart01008 2 GEARYGDDIRLPGMLHAAVVRSPVAHARIKSIDTSAARAMPGVVAVLTAKDVPGLNDFGPLGPD-EPVLADDKV-RYVGQ 79
|
90 100
....*....|....*....|....*...
gi 544956309 258 GIVLVAAETREALEEAKKLVKIDYEELT 285
Cdd:smart01008 80 PVAAVVAETEEAARDAAEAVKVEYEELP 107
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
150-817 |
1.15e-32 |
|
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: 137.06 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 150 ENIDvPKVNCKGLVGENLPRVDAVGKALGYSEYVDDM-RIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKD 228
Cdd:TIGR02969 564 QNVD-SMQLPQDPIGHPIMHLSGVKHATGEAIYCDDMpAVDQELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITAEH 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 229 IPGTIKVGHlkkdwDTLIPEGEItRYLGDGIVLVAAETREALEEAKKLVKIDYEELTPLSTTAdalrEDApkIHETGNIL 308
Cdd:TIGR02969 643 LQDANTFGT-----EKLLATDKV-HCVGQLVCAVIADSEVQAKQAAKHVKIVYRDLEPLILTI----EEA--IQHKSFFE 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 309 VKEHLVRGNAKEKIENSKYVVTKRYTTPATEHAFLEPECAVAGPYEDDGVI-IYSTDQGVFATQHECADMLGLPYEKVRV 387
Cdd:TIGR02969 711 PERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMdVYVSTQFPKYIQDIVAATLKLPVNKVMC 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 388 INKMVGGGFGGK--EDMSVQHHAALLAYHTKRFVKVQLTRKESIIVHPKRHATEMEFTTACDENGYLTGMKATIISDTGA 465
Cdd:TIGR02969 791 HVRRVGGAFGGKvgKTSIMAAITAFAANKHGRAVRCTLERGEDMLITGGRHPYLGKYKAGFMNDGRIVALDVEHYSNGGS 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 466 YASLGGPVLQRLCTHAAGPYNYQDIDITGTAVYTNNPPGGAFRGFGVTQSCFATECNLNLLAEMVGISPWEIR------- 538
Cdd:TIGR02969 871 SLDESLWVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAGLITEACITEVAAKCGLSPEKVRtinmyke 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 539 -----YKNAIRPGQVLpngQFADEGTAMAETLE---AVK----EEYEKhpRAGIACAMKNSGVGVGIPDVGRCRLVIK-- 604
Cdd:TIGR02969 951 idqtpYKQEINAKNLF---QCWRECMAKSSYSErkvAVEkfnaENYWK--KRGLAVIPLKFPVGLGSVAMGQAAALVHiy 1025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 605 -DGKVHIRTSASCIGQGLGTVMTQVVCETANLLPENIVHEVPDTHLTPDSGNTTASRQTVFTGEATKVASNKLKEAL--- 680
Cdd:TIGR02969 1026 lDGSVLVTHGGIEMGQGVHTKMIQVVSRELKMPMSNVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLepi 1105
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 681 ----------DSGKTLLDLEGEEFYGEYESITDK-MGCDK--ENPVSHVAYGYATQVVILD------ENGKLEKVVaahD 741
Cdd:TIGR02969 1106 isknpqgtwkDWAQTAFDQSISLSAVGYFRGYESnINWEKgeGHPFEYFVYGAACSEVEIDcltgdhKNIRTDIVM---D 1182
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 742 VGRAINPISLEGQIEGGVVMGLGYALTEDypvVNSVPTAKFGTLGLfKSTDIPEIQALIVEKNKDLLA--------YGAK 813
Cdd:TIGR02969 1183 VGHSINPALDIGQVEGAFIQGMGLYTIEE---LSYSPQGILYSRGP-NQYKIPAICDIPTELHISFLPpsehsntlYSSK 1258
|
....
gi 544956309 814 GVGE 817
Cdd:TIGR02969 1259 GLGE 1262
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
16-146 |
8.77e-32 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 121.56 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 16 GKKLLDFLREDmNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSE-RERDVFAYSFASQGAVQC 94
Cdd:PRK09908 25 GTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKgGKLSHVQQAYAKSGAVQC 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 544956309 95 GFCIPGMVISSKALID-VNNNP-TEDDIKKALKGNICRCTGYVKIIKAVDLAAK 146
Cdd:PRK09908 104 GFCTPGLIMATTAMLAkPREKPlTITEIRRGLAGNLCRCTGYQMIVNTVLDCEK 157
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
70-141 |
2.32e-31 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 117.15 E-value: 2.32e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544956309 70 TIEGLSERERDVFAYSFASQGAVQCGFCIPGMVISSKALIDVN-NNPTEDDIKKALKGNICRCTGYVKIIKAV 141
Cdd:pfam01799 1 TIEGLAESGGEPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNpPPPTEAEIREALSGNLCRCTGYRRIVDAV 73
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
4-140 |
2.86e-28 |
|
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: 119.30 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 4 FILNGEKVVAKE---GKKLLDFLREDMNITSVKNGCSEGACGTCMVII----DG-----KATKACVFKTDKLAGKNITTI 71
Cdd:TIGR02963 3 FFLNGETVTLSDvdpTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVgelvDGgklryRSVNACIQFLPSLDGKAVVTV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544956309 72 EGLSERERDVFAysfASQGAV-----QCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKA 140
Cdd:TIGR02963 83 EDLRQPDGRLHP---VQQAMVechgsQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDA 153
|
|
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
2-140 |
1.86e-27 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 116.77 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEKVVAKE---GKKLLDFLREDMNITSVKNGCSEGACGTCMVII----DGK----ATKACVFKTDKLAGKNITT 70
Cdd:COG4630 1 IRFLLNGELVELSDvppTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVgeldDGGlryrAVNACILFLPQLDGKALVT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544956309 71 IEGLSERERD---VFAySFASQGAVQCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKA 140
Cdd:COG4630 81 VEGLAGPDGAlhpVQQ-AMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDA 152
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
4-140 |
5.41e-24 |
|
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: 108.94 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 4 FILNGEKVVAKE---GKKLLDFLREDMNITSVKNGCSEGACGTCMVIID--GKATK--------ACVFKTDKLAGKNITT 70
Cdd:TIGR02969 5 FYVNGRKVVEKNvdpETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISryNPSTKsirhhpvnACLTPICSLYGAAVTT 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544956309 71 IEGL-SERER-DVFAYSFASQGAVQCGFCIPGMVISSKALIDVNNNPTEDDIKKALKGNICRCTGYVKIIKA 140
Cdd:TIGR02969 85 VEGIgSTRTRlHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDA 156
|
|
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
2-145 |
8.12e-23 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 97.54 E-value: 8.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEKVVAKEGKK--LLDFLREDMNITSVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNITTIEGLSERER 79
Cdd:PRK11433 52 VTLKVNGKTEQLEVDTRttLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 80 -DVFAYSFASQGAVQCGFCIPGMVISSKALI-------------DVNNNP--TEDDIKKALKGNICRCTGYVKIIKAVDL 143
Cdd:PRK11433 132 lHPMQAAFVKHDGFQCGYCTPGQICSSVAVLkeikdgipshvtvDLTAAPelTADEIRERMSGNICRCGAYSNILEAIED 211
|
..
gi 544956309 144 AA 145
Cdd:PRK11433 212 VA 213
|
|
| Ald_Xan_dh_C |
pfam01315 |
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; |
182-284 |
3.40e-22 |
|
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain;
Pssm-ID: 426197 [Multi-domain] Cd Length: 107 Bit Score: 91.91 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 182 YVDDMRIEGMIYGSAVRAKYPRALVKKIDIEEAKAYPGVVAVLTAKDIPGtIKVGHLKKDWDTLIPEGEItRYLGDGIVL 261
Cdd:pfam01315 6 YVDDIPAPGNLYGAFVRSTIAHAKIVSIDTSAALALPGVVAVITAKDLPG-GNYNIGPIPLDPLFATDKV-RHVGQPIAA 83
|
90 100
....*....|....*....|...
gi 544956309 262 VAAETREALEEAKKLVKIDYEEL 284
Cdd:pfam01315 84 VVADDEETARRAAKLVKVEYEEL 106
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
19-146 |
4.62e-22 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 102.86 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 19 LLDFLReDMNITSVKNGCSEGACGTCMVIIDGK----------ATKACVFKTDKLAGKNITTIEGLSERERDV--FAYSF 86
Cdd:PLN02906 4 LLEYLR-DLGLTGTKLGCGEGGCGACTVMVSHYdrktgkcvhyAVNACLAPLYSVEGMHVITVEGIGNRRDGLhpVQEAL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544956309 87 ASQGAVQCGFCIPGMVISSKALIDVN-NNPTEDDIKKALKGNICRCTGYVKIIKAVDLAAK 146
Cdd:PLN02906 83 ASMHGSQCGFCTPGFIMSMYALLRSSkTPPTEEQIEECLAGNLCRCTGYRPILDAFRVFAK 143
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
2-154 |
1.53e-19 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 94.40 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEKVVAKE---GKKLLDFLREDMNITSVKNGCSEGACGTCMVII----------DGKATKACVFKTDKLAGKNI 68
Cdd:PLN00192 6 LVFAVNGERFELSSvdpSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLskydpvldqvEDFTVSSCLTLLCSVNGCSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 69 TTIEGLSErERDVF---AYSFASQGAVQCGFCIPGMVIS-SKALIDVNNNP-----------TEDDIKKALKGNICRCTG 133
Cdd:PLN00192 86 TTSEGLGN-SKDGFhpiHKRFAGFHASQCGFCTPGMCISlFSALVNADKTDrpeppsgfsklTVVEAEKAVSGNLCRCTG 164
|
170 180
....*....|....*....|.
gi 544956309 134 YVKIikaVDlAAKIFRENIDV 154
Cdd:PLN00192 165 YRPI---VD-ACKSFAADVDI 181
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
2-49 |
8.12e-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: 8.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 544956309 2 VEFILNGEK--VVAKEGKKLLDFLREDmNITsVKNGCSEGACGTCMVIID 49
Cdd:cd00207 1 VTINVPGSGveVEVPEGETLLDAAREA-GID-IPYSCRAGACGTCKVEVV 48
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
10-75 |
1.63e-04 |
|
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: 41.84 E-value: 1.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 10 KVVAKEGKKLLDFL---REDMNIT-SVKNGCSEGACGTCMVIIDGKATKACVFKTDKLAGKNItTIEGLS 75
Cdd:pfam13085 22 EVPYEEGMTVLDALnkiKEEQDPTlAFRRSCREGICGSCAMNINGKPRLACKTLIDDLLGQDI-TLEPLP 90
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
1-97 |
1.34e-03 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 42.38 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 1 MVEFILNGEKVVAKEGKKLLDFLR-EDMNITSV--KNGCSEG-ACGTCMVIIDGKATKACVFKTDKlaGKNITTIEGLSE 76
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARrNGIFIPAIcyLSGCSPTlACRLCMVEADGKRVYSCNTKAKE--GMNILTNTPNLM 78
|
90 100
....*....|....*....|.
gi 544956309 77 RERDVFAYSFASQGAVQCGFC 97
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVC 99
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
4-49 |
2.75e-03 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 37.50 E-value: 2.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 544956309 4 FILNGEKV---VAKEGKKLLDFLREdmNITSVKNGCSEGACGTCMVIID 49
Cdd:pfam00111 1 VTINGKGVtieVPDGETTLLDAAEE--AGIDIPYSCRGGGCGTCAVKVL 47
|
|
| LAL_C2 |
pfam18603 |
L-amino acid ligase C-terminal domain 2; l-amino-acid ligases (LALs; EC 6.3.2.28) were ... |
206-282 |
3.82e-03 |
|
L-amino acid ligase C-terminal domain 2; l-amino-acid ligases (LALs; EC 6.3.2.28) were discovered to be ATP-grasp superfamily enzymes that catalyze the formation of an alpha-peptide bond between two l-amino acids in an ATP-dependent manner. The members of this family share a common structural architecture that consists of three domains referred to as the A-domain, B-domain and C-domain. The C domain can be further divided into the C1-subdomain and the C2-subdomain. This entry represents the C2 subdomain.
Pssm-ID: 436613 Cd Length: 78 Bit Score: 36.77 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956309 206 VKKID-IEEAKAYPGVVAV-LTAKdiPGTiKVGHLKKDWDTLipegeitrylgdGIVLVAAETRE----ALEEAKKLVKI 279
Cdd:pfam18603 11 LRAVEgLEEARALPGVVEVeITVK--PGD-RVRPPRSSGDRL------------GYVIATGDTPEealaAAEAAAALIRI 75
|
...
gi 544956309 280 DYE 282
Cdd:pfam18603 76 EVE 78
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
2-49 |
3.93e-03 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 37.14 E-value: 3.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 544956309 2 VEFILNGEKVVAKEGKKLLD-FLREDMNITSvknGCSEGACGTCMVIID 49
Cdd:COG0633 4 VTFIPEGHTVEVPAGESLLEaALRAGIDLPY---SCRSGACGTCHVRVL 49
|
|
| |
