Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q46800 (XDHB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 FAD-binding subunit

EC=1.17.1.4
Gene names
Name:xdhB
Synonyms:ygeT
Ordered Locus Names:b2867, JW2835
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length292 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). Ref.3

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292Xanthine dehydrogenase FAD-binding subunit
PRO_0000166092

Regions

Domain1 – 176176FAD-binding PCMH-type
Nucleotide binding27 – 348FAD By similarity
Nucleotide binding109 – 1135FAD By similarity

Sites

Binding site1651FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1841FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46800 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 74A07D137DA857E8

FASTA29231,557
        10         20         30         40         50         60 
MFDFASYHRA ATLADAINLL ADNPQAKLLA GGTDVLIQLH HHNDRYRHIV DIHNLAELRG 

        70         80         90        100        110        120 
ITLAEDGSLR IGSATTFTQL IEDPITQRHL PALCAAATSI AGPQIRNVAT YGGNICNGAT 

       130        140        150        160        170        180 
SADSATPTLI YDAKLEIHSP RGVRFVPING FHTGPGKVSL EHDEILVAFH FPPQPKEHAG 

       190        200        210        220        230        240 
SAHFKYAMRD AMDISTIGCA AHCRLDNGNF SELRLAFGVA APTPIRCQHA EQTAQNAPLN 

       250        260        270        280        290 
LQTLEAISES VLQDVAPRSS WRASKEFRLH LIQTMTKKVI SEAVAAAGGK LQ 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage."
Xi H., Schneider B.L., Reitzer L.
J. Bacteriol. 182:5332-5341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF FUNCTION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28375 Genomic DNA. Translation: AAA83048.1.
U00096 Genomic DNA. Translation: AAC75905.1.
AP009048 Genomic DNA. Translation: BAE76933.1.
PIRC65070.
RefSeqNP_417343.1. NC_000913.3.
YP_491069.1. NC_007779.1.

3D structure databases

ProteinModelPortalQ46800.
SMRQ46800. Positions 3-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ46800. 5 interactions.
STRING511145.b2867.

Proteomic databases

PaxDbQ46800.
PRIDEQ46800.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75905; AAC75905; b2867.
BAE76933; BAE76933; BAE76933.
GeneID12933326.
947205.
KEGGecj:Y75_p2800.
eco:b2867.
PATRIC32121144. VBIEscCol129921_2960.

Organism-specific databases

EchoBASEEB2862.
EcoGeneEG13050. xdhB.

Phylogenomic databases

eggNOGCOG1319.
HOGENOMHOG000244729.
KOK13479.
OMAHASPEYR.
OrthoDBEOG6ZSP3F.
PhylomeDBQ46800.
ProtClustDBPRK09971.

Enzyme and pathway databases

BioCycEcoCyc:G7486-MONOMER.
ECOL316407:JW2835-MONOMER.
MetaCyc:G7486-MONOMER.
UniPathwayUPA00604; UER00661.
UPA00604; UER00662.

Gene expression databases

GenevestigatorQ46800.

Family and domain databases

Gene3D3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProIPR005107. 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]
PfamPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]
SMARTSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ46800.

Entry information

Entry nameXDHB_ECOLI
AccessionPrimary (citable) accession number: Q46800
Secondary accession number(s): Q2M9X3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 102 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene