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O32144 (XDHD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 92. 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:
Probable xanthine dehydrogenase subunit D

Short name=XDHase subunit D
EC=1.17.1.4
Gene names
Name:pucD
Synonyms:yurC
Ordered Locus Names:BSU32480
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit 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

Belongs to the xanthine dehydrogenase family.

Ontologies

Keywords
   Biological processPurine metabolism
   LigandMetal-binding
Molybdenum
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhypoxanthine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

xanthine dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 745745Probable xanthine dehydrogenase subunit D
PRO_0000166098

Sites

Metal binding2041Molybdenum Potential
Metal binding2351Molybdenum; via carbonyl oxygen Potential
Metal binding5081Molybdenum; via amide nitrogen Potential

Sequences

Sequence LengthMass (Da)Tools
O32144 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C4A3EC5F0094EF8D

FASTA74580,434
        10         20         30         40         50         60 
MIINKPSRVR PDGRGKVTGE LKYMTDLSFP GMLYGKVLRS AYPHAEIVSV CTIKAEKMEG 

        70         80         90        100        110        120 
VQAVVTHKDV PGLNRFGIVI PDQPVLCEDR VRYVGDAIAA VAAETEEIAE AALELIQVEY 

       130        140        150        160        170        180 
KELEVMDSPE KALRPNAQRL HEDGNILHRA FFSNGDVEEG FQASDTVFEE TYELPRQMHT 

       190        200        210        220        230        240 
YMETEGGVAV PEDDGGFTMY AGTQHGYKDR FQLARIFDIP EEKIRIVSSP MGGSFGGKDE 

       250        260        270        280        290        300 
LNIQPYAALL ALKSGRPVKI HQTRKESVRS GIKRHPMKIT IKTGADHSGN LLAHDVKIVA 

       310        320        330        340        350        360 
DTGAYATLGP AVLDFSVEHA AGPYRIPNIR TEGISVFTNN GVAGEFRGFG GNQITFALET 

       370        380        390        400        410        420 
HLDRLSGMLG IDPLELRRKN IRKPHDLGPL EHRIAPTDGA AQVLNAISKS PILKKTSRNC 

       430        440        450        460        470        480 
GYLQRGTGAA ITMHGGGLGF GRMDAAGGRL SLSSEGKITA SFGFEECGQG ILAAIEQIVM 

       490        500        510        520        530        540 
EELGCAAEDI SIVIGDTAKV PKSGSSTASR GTSMVWHAIQ RLKKPFLAQL KKRAAEWSGC 

       550        560        570        580        590        600 
SAENLIPGAA GLRDKNTKAL VVTYKELAEK GPLAEETAFD FPTTPDPVVG GHFLYSFGAA 

       610        620        630        640        650        660 
AVEVEVDLLT GDVKLIDCEH AIAAGPVVSP QGYRGQIEGG AAMALGYTLM EEAKMTDGRY 

       670        680        690        700        710        720 
AAENLDHYLI PGIKDVPDMK LIAIEDLMKG DVYGPRGVGE IGTIAITPAI VKAVHDAVGC 

       730        740 
WINKLPISRE ELLEAIDRKG LKQWT 

« 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB15238.1.
PIRB70017.
RefSeqNP_391128.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32144.
SMRO32144. Positions 2-740.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU32480.

Proteomic databases

PaxDbO32144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15238; CAB15238; BSU32480.
GeneID936686.
KEGGbsu:BSU32480.
PATRIC18978470. VBIBacSub10457_3398.

Organism-specific databases

GenoListBSU32480. [Micado]

Phylogenomic databases

eggNOGCOG1529.
HOGENOMHOG000244715.
KOK00087.
OMAKVTGEFA.
OrthoDBEOG6ZSP3F.
ProtClustDBCLSK247866.

Enzyme and pathway databases

BioCycBSUB:BSU32480-MONOMER.
UniPathwayUPA00604; UER00661.
UPA00604; UER00662.

Family and domain databases

Gene3D3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR017609. Xanthine_dehydrogenase_dsu.
[Graphical view]
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
TIGRFAMsTIGR03196. pucD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXDHD_BACSU
AccessionPrimary (citable) accession number: O32144
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 92 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

Bacillus subtilis

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