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O32144

- XDHD_BACSU

UniProt

O32144 - XDHD_BACSU

Protein

Probable xanthine dehydrogenase subunit D

Gene

pucD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Oxidizes hypoxanthine and xanthine to uric acid.1 Publication

    Catalytic activityi

    Xanthine + NAD+ + H2O = urate + NADH.
    Hypoxanthine + NAD+ + H2O = xanthine + NADH.

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi204 – 2041MolybdenumSequence Analysis
    Metal bindingi235 – 2351Molybdenum; via carbonyl oxygenSequence Analysis
    Metal bindingi508 – 5081Molybdenum; via amide nitrogenSequence Analysis

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. xanthine dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. hypoxanthine catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Purine metabolism

    Keywords - Ligandi

    Metal-binding, Molybdenum, NAD

    Enzyme and pathway databases

    BioCyciBSUB:BSU32480-MONOMER.
    UniPathwayiUPA00604; UER00661.
    UPA00604; UER00662.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable xanthine dehydrogenase subunit D (EC:1.17.1.4)
    Short name:
    XDHase subunit D
    Gene namesi
    Name:pucD
    Synonyms:yurC
    Ordered Locus Names:BSU32480
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU32480. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745Probable xanthine dehydrogenase subunit DPRO_0000166098Add
    BLAST

    Proteomic databases

    PaxDbiO32144.

    Expressioni

    Inductioni

    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.

    Interactioni

    Subunit structurei

    Could be composed of four subunits: PucA, PucC, PucD and PucE.

    Protein-protein interaction databases

    STRINGi224308.BSU32480.

    Structurei

    3D structure databases

    ProteinModelPortaliO32144.
    SMRiO32144. Positions 2-740.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the xanthine dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1529.
    HOGENOMiHOG000244715.
    KOiK00087.
    OMAiDGNFRKK.
    OrthoDBiEOG6ZSP3F.
    PhylomeDBiO32144.

    Family and domain databases

    Gene3Di3.30.365.10. 6 hits.
    3.90.1170.50. 1 hit.
    InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR017609. Xanthine_dehydrogenase_dsu.
    [Graphical view]
    PfamiPF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    [Graphical view]
    SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54665. SSF54665. 1 hit.
    SSF56003. SSF56003. 1 hit.
    TIGRFAMsiTIGR03196. pucD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O32144-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIINKPSRVR PDGRGKVTGE LKYMTDLSFP GMLYGKVLRS AYPHAEIVSV    50
    CTIKAEKMEG VQAVVTHKDV PGLNRFGIVI PDQPVLCEDR VRYVGDAIAA 100
    VAAETEEIAE AALELIQVEY KELEVMDSPE KALRPNAQRL HEDGNILHRA 150
    FFSNGDVEEG FQASDTVFEE TYELPRQMHT YMETEGGVAV PEDDGGFTMY 200
    AGTQHGYKDR FQLARIFDIP EEKIRIVSSP MGGSFGGKDE LNIQPYAALL 250
    ALKSGRPVKI HQTRKESVRS GIKRHPMKIT IKTGADHSGN LLAHDVKIVA 300
    DTGAYATLGP AVLDFSVEHA AGPYRIPNIR TEGISVFTNN GVAGEFRGFG 350
    GNQITFALET HLDRLSGMLG IDPLELRRKN IRKPHDLGPL EHRIAPTDGA 400
    AQVLNAISKS PILKKTSRNC GYLQRGTGAA ITMHGGGLGF GRMDAAGGRL 450
    SLSSEGKITA SFGFEECGQG ILAAIEQIVM EELGCAAEDI SIVIGDTAKV 500
    PKSGSSTASR GTSMVWHAIQ RLKKPFLAQL KKRAAEWSGC SAENLIPGAA 550
    GLRDKNTKAL VVTYKELAEK GPLAEETAFD FPTTPDPVVG GHFLYSFGAA 600
    AVEVEVDLLT GDVKLIDCEH AIAAGPVVSP QGYRGQIEGG AAMALGYTLM 650
    EEAKMTDGRY AAENLDHYLI PGIKDVPDMK LIAIEDLMKG DVYGPRGVGE 700
    IGTIAITPAI VKAVHDAVGC WINKLPISRE ELLEAIDRKG LKQWT 745
    Length:745
    Mass (Da):80,434
    Last modified:January 1, 1998 - v1
    Checksum:iC4A3EC5F0094EF8D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15238.1.
    PIRiB70017.
    RefSeqiNP_391128.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15238; CAB15238; BSU32480.
    GeneIDi936686.
    KEGGibsu:BSU32480.
    PATRICi18978470. VBIBacSub10457_3398.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15238.1 .
    PIRi B70017.
    RefSeqi NP_391128.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O32144.
    SMRi O32144. Positions 2-740.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU32480.

    Proteomic databases

    PaxDbi O32144.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15238 ; CAB15238 ; BSU32480 .
    GeneIDi 936686.
    KEGGi bsu:BSU32480.
    PATRICi 18978470. VBIBacSub10457_3398.

    Organism-specific databases

    GenoListi BSU32480. [Micado ]

    Phylogenomic databases

    eggNOGi COG1529.
    HOGENOMi HOG000244715.
    KOi K00087.
    OMAi DGNFRKK.
    OrthoDBi EOG6ZSP3F.
    PhylomeDBi O32144.

    Enzyme and pathway databases

    UniPathwayi UPA00604 ; UER00661 .
    UPA00604 ; UER00662 .
    BioCyci BSUB:BSU32480-MONOMER.

    Family and domain databases

    Gene3Di 3.30.365.10. 6 hits.
    3.90.1170.50. 1 hit.
    InterProi IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR017609. Xanthine_dehydrogenase_dsu.
    [Graphical view ]
    Pfami PF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    [Graphical view ]
    SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54665. SSF54665. 1 hit.
    SSF56003. SSF56003. 1 hit.
    TIGRFAMsi TIGR03196. pucD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiXDHD_BACSU
    AccessioniPrimary (citable) accession number: O32144
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3