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Reviewed, UniProtKB/Swiss-Prot O32147 (XDHA_BACSU)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable xanthine dehydrogenase subunit A
      Short name=XDHase subunit A
    EC=1.17.1.4
Gene names
Name: pucA
Synonyms: yurF
Ordered Locus Names: BSU32510
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Oxidizes hypoxanthine and xanthine to uric acid. PucA subunit could exert a molybdenum cofactor recruiting function. Ref.2

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH.

Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Pathway

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

Purine metabolism; hypoxanthine degradation; uric acid from hypoxanthine: step 2/2.

Subunit structure

Could be composed of four subunits: pucA, pucC, pucD and pucE.

Induction

Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression decreases when allantoin is added during limiting-nitrogen conditions.

Ontologies

Keywords
   Biological processPurine metabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

purine base metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionxanthine dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Probable xanthine dehydrogenase subunit A
PRO_0000166100

Sequences

Sequence LengthMass (Da)Tools
O32147-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E4A70B2155BE1902

FASTA33036,746
        10         20         30         40         50         60 
MGNFHTMLDA LLEDQEEAVL ATIVQVEGSA YRKAGASMLF KKKGRRIGLL SGGCVEEDVF 

        70         80         90        100        110        120 
QRISALGDQL TSTLIPYDMR SEDDLSWGMG AGCNGIIHVH AERITQEKRR HYEKVRDCLH 

       130        140        150        160        170        180 
SGKAVTSVIK IESSHYLFLT ENGHFGNWPD APLQDIQRTV STLHLPHFDQ TTNMFIQRIE 

       190        200        210        220        230        240 
PKPRLILFGA GPDNVPLANL AADTGFSVIV TDWRPAYCTS SLFPKADQLI TAFPEQMLSE 

       250        260        270        280        290        300 
FQFFPHDAAV VATHHYQHDQ TIINFLFSQN LHYIGLLGSA NRTKRLLSGK HPPSHFYSPV 

       310        320        330 
GLKIGAEGPE EIAVSVVAEI IQTRKRVAVV 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
Schultz A.C., Nygaard P., Saxild H.H.
J. Bacteriol. 183:3293-3302(2001) [PubMed: 11344136] [Abstract]
Cited for: FUNCTION.
Strain: 168.

Cross-references

Sequence databases

AL009126 Genomic DNA. Translation: CAB15241.1.
PIRE70017.
RefSeqNP_391131.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID938865.
GenomeReviewsGene locus BSU32510 in contig AL009126_GR.
KEGGbsu:BSU32510.
NMPDRfig|224308.1.peg.3257.

Organism-specific databases

SubtiListBG13992. pucA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO32147.
OMAO32147. EDDLSWG.

Enzyme and pathway databases

BioCycBSUB224308:BSU3248-MON.
BRENDA1.17.1.4. 150.

Family and domain databases

InterProIPR003777. XdhC_CoxI.
[Graphical view]
PfamPF02625. XdhC_CoxI. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXDHA_BACSU
AccessionPrimary (citable) accession number: O32147
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents