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O32145

- XDHC_BACSU

UniProt

O32145 - XDHC_BACSU

Protein

Probable xanthine dehydrogenase subunit C

Gene

pucC

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

    FAD.By similarity

    Pathwayi

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
    3. 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

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciBSUB:BSU32490-MONOMER.
    UniPathwayiUPA00604; UER00661.
    UPA00604; UER00662.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable xanthine dehydrogenase subunit C (EC:1.17.1.4)
    Short name:
    XDHase subunit C
    Gene namesi
    Name:pucC
    Synonyms:yurD
    Ordered Locus Names:BSU32490
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU32490. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 277277Probable xanthine dehydrogenase subunit CPRO_0000166099Add
    BLAST

    Proteomic databases

    PaxDbiO32145.

    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.BSU32490.

    Structurei

    3D structure databases

    ProteinModelPortaliO32145.
    SMRiO32145. Positions 11-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 176170FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1319.
    HOGENOMiHOG000154870.
    KOiK00087.
    OMAiKARMNIQ.
    OrthoDBiEOG686NMM.
    PhylomeDBiO32145.

    Family and domain databases

    Gene3Di3.30.465.10. 1 hit.
    InterProiIPR005107. 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]
    PfamiPF00941. FAD_binding_5. 1 hit.
    [Graphical view]
    SUPFAMiSSF55447. SSF55447. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsiTIGR03199. pucC. 1 hit.
    PROSITEiPS51387. FAD_PCMH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O32145-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGQVTKARM NIQLWRPAAL DEAYSLLEKL APDVCAASGS TLLQLQWDKG    50
    TLPKQHLVSL EGIDEMRGIS TSDTHVSIGG LTSLNECRKN PLIKRALSCF 100
    SDAASAVAAP GIRSRATIGG NIASKIGDFI PLLLVLGAEL IVYQKELIRL 150
    PLGAWLSEED FRTAIVTRVI IPRAEGERVF YHKLGRRQAF TGAAAVAAGR 200
    FLKDGSIRLA AGHADITPRR LLDSEAKWMA PGWDPHELYK TLIHELPFSS 250
    DVFMSAAYRK KAAANVIMAE LMAEGGE 277
    Length:277
    Mass (Da):30,119
    Last modified:January 1, 1998 - v1
    Checksum:i25D8C75D6D237961
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15239.1.
    PIRiC70017.
    RefSeqiNP_391129.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15239; CAB15239; BSU32490.
    GeneIDi936685.
    KEGGibsu:BSU32490.
    PATRICi18978472. VBIBacSub10457_3399.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15239.1 .
    PIRi C70017.
    RefSeqi NP_391129.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O32145.
    SMRi O32145. Positions 11-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU32490.

    Proteomic databases

    PaxDbi O32145.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15239 ; CAB15239 ; BSU32490 .
    GeneIDi 936685.
    KEGGi bsu:BSU32490.
    PATRICi 18978472. VBIBacSub10457_3399.

    Organism-specific databases

    GenoListi BSU32490. [Micado ]

    Phylogenomic databases

    eggNOGi COG1319.
    HOGENOMi HOG000154870.
    KOi K00087.
    OMAi KARMNIQ.
    OrthoDBi EOG686NMM.
    PhylomeDBi O32145.

    Enzyme and pathway databases

    UniPathwayi UPA00604 ; UER00661 .
    UPA00604 ; UER00662 .
    BioCyci BSUB:BSU32490-MONOMER.

    Family and domain databases

    Gene3Di 3.30.465.10. 1 hit.
    InterProi IPR005107. 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 ]
    Pfami PF00941. FAD_binding_5. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55447. SSF55447. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsi TIGR03199. pucC. 1 hit.
    PROSITEi PS51387. FAD_PCMH. 1 hit.
    [Graphical view ]
    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 nameiXDHC_BACSU
    AccessioniPrimary (citable) accession number: O32145
    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