Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25971

- PYRF_BACSU

UniProt

P25971 - PYRF_BACSU

Protein

Orotidine 5'-phosphate decarboxylase

Gene

pyrF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).

    Catalytic activityi

    Orotidine 5'-phosphate = UMP + CO2.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111Substrate
    Binding sitei33 – 331Substrate
    Active sitei62 – 621Proton donor
    Binding sitei123 – 1231Substrate
    Binding sitei185 – 1851Substrate
    Binding sitei194 – 1941Substrate
    Binding sitei214 – 2141Substrate; via amide nitrogen
    Binding sitei215 – 2151Substrate

    GO - Molecular functioni

    1. orotidine-5'-phosphate decarboxylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
    2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Enzyme and pathway databases

    BioCyciBSUB:BSU15550-MONOMER.
    UniPathwayiUPA00070; UER00120.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Orotidine 5'-phosphate decarboxylase (EC:4.1.1.23)
    Alternative name(s):
    OMP decarboxylase
    Short name:
    OMPDCase
    Short name:
    OMPdecase
    Gene namesi
    Name:pyrF
    Ordered Locus Names:BSU15550
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU15550. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 239239Orotidine 5'-phosphate decarboxylasePRO_0000134527Add
    BLAST

    Proteomic databases

    PaxDbiP25971.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP25971. 1 interaction.
    MINTiMINT-8366633.
    STRINGi224308.BSU15550.

    Structurei

    Secondary structure

    1
    239
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93
    Helixi15 – 217
    Helixi23 – 253
    Beta strandi31 – 344
    Helixi36 – 427
    Helixi44 – 529
    Beta strandi56 – 638
    Helixi67 – 7812
    Turni79 – 813
    Beta strandi83 – 886
    Helixi89 – 913
    Helixi93 – 10614
    Beta strandi115 – 1195
    Helixi127 – 1326
    Helixi140 – 15314
    Beta strandi157 – 1604
    Helixi163 – 1653
    Helixi166 – 1694
    Turni170 – 1723
    Beta strandi178 – 1814
    Helixi200 – 2056
    Beta strandi209 – 2135
    Helixi215 – 2184
    Helixi223 – 23513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DBTX-ray2.40A/B/C1-239[»]
    ProteinModelPortaliP25971.
    SMRiP25971. Positions 1-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25971.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni60 – 6910Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0284.
    HOGENOMiHOG000226071.
    KOiK01591.
    OMAiRPITQSA.
    OrthoDBiEOG6N6815.
    PhylomeDBiP25971.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01200_B. OMPdecase_type1_B.
    InterProiIPR013785. Aldolase_TIM.
    IPR014732. OMPdecase.
    IPR018089. OMPdecase_AS.
    IPR001754. OMPdeCOase_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00215. OMPdecase. 1 hit.
    [Graphical view]
    SMARTiSM00934. OMPdecase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    TIGRFAMsiTIGR01740. pyrF. 1 hit.
    PROSITEiPS00156. OMPDECASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25971-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNNLPIIAL DFASAEETLA FLAPFQQEPL FVKVGMELFY QEGPSIVKQL    50
    KERNCELFLD LKLHDIPTTV NKAMKRLASL GVDLVNVHAA GGKKMMQAAL 100
    EGLEEGTPAG KKRPSLIAVT QLTSTSEQIM KDELLIEKSL IDTVVHYSKQ 150
    AEESGLDGVV CSVHEAKAIY QAVSPSFLTV TPGIRMSEDA ANDQVRVATP 200
    AIAREKGSSA IVVGRSITKA EDPVKAYKAV RLEWEGIKS 239
    Length:239
    Mass (Da):25,992
    Last modified:May 1, 1992 - v1
    Checksum:iDB1743714ED052E7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59757 Genomic DNA. Translation: AAA21273.1.
    AL009126 Genomic DNA. Translation: CAB13429.1.
    PIRiI39845.
    RefSeqiNP_389438.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13429; CAB13429; BSU15550.
    GeneIDi935960.
    KEGGibsu:BSU15550.
    PATRICi18974917. VBIBacSub10457_1650.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59757 Genomic DNA. Translation: AAA21273.1 .
    AL009126 Genomic DNA. Translation: CAB13429.1 .
    PIRi I39845.
    RefSeqi NP_389438.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DBT X-ray 2.40 A/B/C 1-239 [» ]
    ProteinModelPortali P25971.
    SMRi P25971. Positions 1-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P25971. 1 interaction.
    MINTi MINT-8366633.
    STRINGi 224308.BSU15550.

    Proteomic databases

    PaxDbi P25971.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13429 ; CAB13429 ; BSU15550 .
    GeneIDi 935960.
    KEGGi bsu:BSU15550.
    PATRICi 18974917. VBIBacSub10457_1650.

    Organism-specific databases

    GenoListi BSU15550. [Micado ]

    Phylogenomic databases

    eggNOGi COG0284.
    HOGENOMi HOG000226071.
    KOi K01591.
    OMAi RPITQSA.
    OrthoDBi EOG6N6815.
    PhylomeDBi P25971.

    Enzyme and pathway databases

    UniPathwayi UPA00070 ; UER00120 .
    BioCyci BSUB:BSU15550-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P25971.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01200_B. OMPdecase_type1_B.
    InterProi IPR013785. Aldolase_TIM.
    IPR014732. OMPdecase.
    IPR018089. OMPdecase_AS.
    IPR001754. OMPdeCOase_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00215. OMPdecase. 1 hit.
    [Graphical view ]
    SMARTi SM00934. OMPdecase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    TIGRFAMsi TIGR01740. pyrF. 1 hit.
    PROSITEi PS00156. OMPDECASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon."
      Quinn C.L., Stephenson B.T., Switzer R.L.
      J. Biol. Chem. 266:9113-9127(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. "The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase."
      Appleby T.C., Kinsland C., Begley T.P., Ealick S.E.
      Proc. Natl. Acad. Sci. U.S.A. 97:2005-2010(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH UMP, SUBUNIT.

    Entry informationi

    Entry nameiPYRF_BACSU
    AccessioniPrimary (citable) accession number: P25971
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 110 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3