Reviewed, UniProtKB/Swiss-Prot Q8X6C7 (XDHA_ECO57)

Names and origin

Protein names

Recommended name:
    Xanthine dehydrogenase molybdenum-binding subunit
    EC=1.17.1.4

Gene names

Name:	xdhA
Ordered Locus Names:	Z4205, ECs3739

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Protein existence	Inferred 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 ion (molybdopterin) 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 process	Purine metabolism Purine salvage
Ligand	Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW purine ribonucleoside salvage Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW xanthine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 752	752	Xanthine dehydrogenase molybdenum-binding subunit		PRO_0000166089
Sites
	Metal binding	206	1	Molybdenum By similarity
	Metal binding	237	1	Molybdenum; via carbonyl oxygen By similarity
	Metal binding	350	1	Molybdenum; via amide nitrogen By similarity
	Metal binding	516	1	Molybdenum; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X6C7-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: C42D8B8B7B386BB4	FASTA	752	81,370
	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

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. , 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: 11206551] [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. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [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.
PIR	C91096. G85941.
RefSeq	NP_289436.1. NP_311766.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	916443. 958353.
GenomeReviews	Gene locus Z4205 in contig AE005174_GR. Gene locus ECs3739 in contig BA000007_GR.
KEGG	ece:Z4205. ecs:ECs3739.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG705921.
OMA	YTNTVPA.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3739-MONOMER.
Family and domain databases
InterPro	IPR000674. Ald_Oxase/Xan_DH_a/b. IPR008274. AldOxase/xan_DH_Mopterin-bd. [Graphical view]
Gene3D	G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit.
Pfam	PF01315. Ald_Xan_dh_C. 1 hit. PF02738. Ald_Xan_dh_C2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XDHA_ECO57

Accession

Primary (citable) accession number: Q8X6C7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	March 1, 2002
Last modified:	January 19, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)