Q8X6C5 (XDHB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	xdhB
Ordered Locus Names:	Z4206, ECs3740

Organism

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

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	292 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	FAD 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	Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Biological process	Purine metabolism Purine salvage
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	hypoxanthine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway purine ribonucleoside salvage Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro 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 – 292	292	Xanthine dehydrogenase FAD-binding subunit		PRO_0000166093
Regions
	Domain	1 – 176	176	FAD-binding PCMH-type
	Nucleotide binding	27 – 34	8	FAD By similarity
	Nucleotide binding	109 – 113	5	FAD By similarity
Sites
	Binding site	165	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	184	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X6C5 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: FEC44F9990BF9BC1	FASTA	292	31,561
	10 20 30 40 50 60 MFDFASYHRA ATLADAINLL ADNPQAKLLA GGTDVLIQLH HHNDRYRHIV DIHNLAELRG 70 80 90 100 110 120 ITLAEDGSLR IGSATTFTQL IEDSITQRHL PALCAAASSI AGPQIRNVAT YGGNICNGAT 130 140 150 160 170 180 SADSATPTLI YDAKLEIHSP RGVRFVPING FHTGPGKVSL EHDEILVAFH FPPQPKEHVG 190 200 210 220 230 240 SAHFKYAMRD AMDISTIGCA AHCRLDNGNF SELRLAFGVA APTPIRCQHA EQTAQNAPLN 250 260 270 280 290 LQTLEAISES VLQDVAPRSS WRASKEFRLH LIQTMTKKVI SEAVAAAGGK LQ

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] [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. , 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: AAG57996.2. BA000007 Genomic DNA. Translation: BAB37163.1.
PIR	D91096. H85941.
RefSeq	NP_289437.2. NC_002655.2. NP_311767.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X6C5.
SMR	Q8X6C5. Positions 1-287.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z4206.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG57996; AAG57996; Z4206. BAB37163; BAB37163; BAB37163.
GeneID	916440. 958358.
KEGG	ece:Z4206. ecs:ECs3740.
PATRIC	18356961. VBIEscCol44059_3659.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1319.
HOGENOM	HOG000244729.
KO	K13479.
OMA	IEDPVTQ.
ProtClustDB	PRK09971.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-3707-MONOMER.
UniPathway	UPA00604; UER00661. UPA00604; UER00662.
Family and domain databases
Gene3D	3.30.43.10. 1 hit. 3.30.465.10. 1 hit.
InterPro	IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR002346. Mopterin_DH_FAD-bd. [Graphical view]
Pfam	PF03450. CO_deh_flav_C. 1 hit. PF00941. FAD_binding_5. 1 hit. [Graphical view]
SMART	SM01092. CO_deh_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF55447. CO_deh_flav_C. 1 hit. SSF56176. FAD-binding_2. 1 hit.
PROSITE	PS51387. FAD_PCMH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XDHB_ECO57

Accession

Primary (citable) accession number: Q8X6C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program