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UniProtKB/Swiss-Prot entry Q8X6C5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name XDHB_ECO57
Primary accession number Q8X6C5
Secondary accession numbers None
Integrated into Swiss-Prot on May 2, 2002
Sequence was last modified on March 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Xanthine dehydrogenase FAD-binding subunit
Synonym EC 1.17.1.4
Gene name
Name: xdhB
OrderedLocusNames: Z4206, ECs3740
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE005174; AAG57996.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB37163.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D91096; D91096.
H85941; H85941.
RefSeq NP_289437.2; -.
NP_311767.1; -.
3D structure databases
HSSP P19914; 1FFV. [HSSP ENTRY / PDB]
ModBase Q8X6C5.
Enzyme and pathway databases
BioCyc ECOL83334:ECS3740-MON; -.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004854; Molecular function: xanthine dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006144; Biological process: purine base metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006166; Biological process: purine ribonucleoside salvage (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR016167; FAD-bd_2_sub1.
IPR002346; Mopterin_DHase_FAD-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
Pfam PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
Pfam graphical view of domain structure.
PROSITE PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8X6C5.
Genome annotation databases
GeneID 916440; -.
958358; -.
GenomeReviews BA000007_GR; ECs3740.
AE005174_GR; Z4206.
KEGG ece:Z4206; -.
ecs:ECs3740; -.
Phylogenomic databases
HOGENOM Q8X6C5; -.
Genome annotation databases
CMR Q8X6C5; Z4206.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase; Purine metabolism; Purine salvage.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom To Length Description FTId
CHAIN   1   292  292     Xanthine dehydrogenase FAD-binding subunit. PRO_0000166093
DOMAIN   1   176  176     FAD-binding PCMH-type. 
Sequence information
Length: 292 AA [This is the length of the unprocessed precursor] Molecular weight: 31561 Da [This is the MW of the unprocessed precursor] CRC64: FEC44F9990BF9BC1 [This is a checksum on the sequence] 
        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
Q8X6C5 in FASTA format

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