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Q8X6C7 (XDHA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthine dehydrogenase molybdenum-binding subunit

EC=1.17.1.4
Gene names
Name:xdhA
Ordered Locus Names:Z4205, ECs3739
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism) By similarity.

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH.

Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactor

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit By similarity.

Pathway

Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2.

Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 2/2.

Subunit structure

Heterotrimer of XdhA, XdhB and XdhC Probable.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Ontologies

Keywords
   Biological processPurine metabolism
Purine salvage
   LigandMetal-binding
Molybdenum
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhypoxanthine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

xanthine dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 752752Xanthine dehydrogenase molybdenum-binding subunit
PRO_0000166089

Sites

Metal binding2061Molybdenum By similarity
Metal binding2371Molybdenum; via carbonyl oxygen By similarity
Metal binding3501Molybdenum; via amide nitrogen By similarity
Metal binding5161Molybdenum; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X6C7 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C42D8B8B7B386BB4

FASTA75281,370
        10         20         30         40         50         60 
MRVDAIAKVT GRARYTDDYV MAGMCYAKYV RSPIAHGYAV SINDEQARSL PGVLAIFTWE 

        70         80         90        100        110        120 
DVPDIPFATA GHAWTLDENK RDTADRALLT RHVRHHGDAV AIVVARDELT AEKAAQLVSI 

       130        140        150        160        170        180 
EWEELPVITT PEAALAEDAA PIHNGGNLLK QSTMSTGNVQ QTIDAADYQV QGHYQTPVIQ 

       190        200        210        220        230        240 
HCHMESVTSL AWMEDDSRIT IVSSTQIPHI VRRVVGQALD IPWSCVRVIK TFVGGGFGNK 

       250        260        270        280        290        300 
QDVLEEPMAA FLTSKLGGIP VKVSLSREEC FLATRTRHAF TIDGQMGVNR DGTLKGYSLD 

       310        320        330        340        350        360 
VLSNTGAYVS HGHSIASAGG NKVAYLYPRC AYAYSSKTCY TNLPSAGAMR GYGAPQVVFA 

       370        380        390        400        410        420 
VESMLDDAAT ALGIDPVEIR LRNASREGDA NPLTGKRIYS AGLPECLEKG RKIFEWEKRR 

       430        440        450        460        470        480 
AECQNQQGNL RRGVGVACFS YTSNTWPVGV EIAGARLLMN QDGTINVQSG ATEIGQGADT 

       490        500        510        520        530        540 
VFSQMVAETV GVPVSDVRVI STQDTDVTPF DPGAFASRQS YVAAPALRSA ALLLKEKIIA 

       550        560        570        580        590        600 
HAAVMLHQSA MNLTLIKGHI VLVERPEEPL MSLKDLAMDA FYHPERGGQL SAESSIKTTT 

       610        620        630        640        650        660 
NPPAFGCTFV DLTVDIALCK VTINRILNVH DSGHILNPLL AEGQVHGGMG MGIGWALFEE 

       670        680        690        700        710        720 
MIIDAKSGVV RNPNLLDYKM PTMPDLPQLE SAFVEINEPQ SAYGHKSLGE PPIIPVAAAI 

       730        740        750 
RNAVKMATGV AINTLPLTPK RLYEEFHLAG LI 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG57995.1.
BA000007 Genomic DNA. Translation: BAB37162.1.
PIRC91096.
G85941.
RefSeqNP_289436.1. NC_002655.2.
NP_311766.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X6C7.
SMRQ8X6C7. Positions 1-750.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57995; AAG57995; Z4205.
BAB37162; BAB37162; BAB37162.
GeneID916443.
958353.
KEGGece:Z4205.
ecs:ECs3739.
PATRIC18356959. VBIEscCol44059_3658.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1529.
HOGENOMHOG000244715.
KOK00087.
OMASREGDAN.
OrthoDBEOG6ZSP3F.
ProtClustDBPRK09970.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3706-MONOMER.
ECOO157:Z4205-MONOMER.
UniPathwayUPA00604; UER00661.
UPA00604; UER00662.

Family and domain databases

Gene3D3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXDHA_ECO57
AccessionPrimary (citable) accession number: Q8X6C7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2002
Last modified: December 11, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways