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Reviewed, UniProtKB/Swiss-Prot O32145 (XDHC_BACSU)

Last modified February 9, 2010. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Probable xanthine dehydrogenase subunit C
      Short name=XDHase subunit C
    EC=1.17.1.4
Gene names
Name: pucC
Synonyms: yurD
Ordered Locus Names: BSU32490
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Oxidizes hypoxanthine and xanthine to uric acid. Ref.2

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

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.

Sequence similarities

Contains 1 FAD-binding PCMH-type domain.

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Ontologies

Keywords
   Biological processPurine metabolism
   LigandFAD
Flavoprotein
NAD
   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 functionFAD binding

Inferred from electronic annotation. Source: InterPro

xanthine dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Probable xanthine dehydrogenase subunit C
PRO_0000166099

Regions

Domain7 – 176170FAD-binding PCMH-type

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Sequences

Sequence LengthMass (Da)Tools
O32145-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 25D8C75D6D237961

FASTA27730,119
        10         20         30         40         50         60 
MNGQVTKARM NIQLWRPAAL DEAYSLLEKL APDVCAASGS TLLQLQWDKG TLPKQHLVSL 

        70         80         90        100        110        120 
EGIDEMRGIS TSDTHVSIGG LTSLNECRKN PLIKRALSCF SDAASAVAAP GIRSRATIGG 

       130        140        150        160        170        180 
NIASKIGDFI PLLLVLGAEL IVYQKELIRL PLGAWLSEED FRTAIVTRVI IPRAEGERVF 

       190        200        210        220        230        240 
YHKLGRRQAF TGAAAVAAGR FLKDGSIRLA AGHADITPRR LLDSEAKWMA PGWDPHELYK 

       250        260        270 
TLIHELPFSS DVFMSAAYRK KAAANVIMAE LMAEGGE

« Hide

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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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB15239.1.
PIRC70017.
RefSeqNP_391129.1.

3D structure databases

SMRO32145. Positions 12-271.
ModBaseSearch...

Genome annotation databases

GeneID936685.
GenomeReviewsGene locus BSU32490 in contig AL009126_GR.
KEGGbsu:BSU32490.
NMPDRfig|224308.1.peg.3255.

Organism-specific databases

SubtiListBG13990. pucC. [Micado]
CMRSearch...

Phylogenomic databases

OMAMITIKEY.

Enzyme and pathway databases

BRENDA1.17.1.4. 150.

Family and domain databases

InterProIPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR002346. Mopterin_DH_FAD-bd.
IPR017612. Xanthine_dehydrogenase_csu.
[Graphical view]
Gene3DG3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit.
PfamPF00941. FAD_binding_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR03199. pucC. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXDHC_BACSU
AccessionPrimary (citable) accession number: O32145
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 63 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)

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Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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