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)

Q3AYG9

- PYRC_SYNS9

UniProt

Q3AYG9 - PYRC_SYNS9

Protein

Dihydroorotase

Gene

pyrC

Organism
Synechococcus sp. (strain CC9902)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.UniRule annotation

    Cofactori

    Binds 2 zinc ions per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi14 – 141Zinc 1; via tele nitrogenUniRule annotation
    Metal bindingi16 – 161Zinc 1; via tele nitrogenUniRule annotation
    Metal bindingi100 – 1001Zinc 1; via carbamate groupUniRule annotation
    Metal bindingi100 – 1001Zinc 2; via carbamate groupUniRule annotation
    Metal bindingi137 – 1371Zinc 2; via pros nitrogenUniRule annotation
    Metal bindingi175 – 1751Zinc 2; via tele nitrogenUniRule annotation
    Metal bindingi248 – 2481Zinc 1UniRule annotation

    GO - Molecular functioni

    1. dihydroorotase activity Source: UniProtKB-HAMAP
    2. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciSSP316279:GJCI-903-MONOMER.
    UniPathwayiUPA00070; UER00117.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DihydroorotaseUniRule annotation (EC:3.5.2.3UniRule annotation)
    Short name:
    DHOaseUniRule annotation
    Gene namesi
    Name:pyrCUniRule annotation
    Ordered Locus Names:Syncc9902_0892
    OrganismiSynechococcus sp. (strain CC9902)
    Taxonomic identifieri316279 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000002712: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 343343DihydroorotasePRO_1000024069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi316279.Syncc9902_0892.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3AYG9.
    SMRiQ3AYG9. Positions 2-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DHOase family. Type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0418.
    HOGENOMiHOG000256259.
    KOiK01465.
    OMAiLKRNVHQ.
    OrthoDBiEOG6TFCMH.

    Family and domain databases

    HAMAPiMF_00219. PyrC_type1.
    InterProiIPR006680. Amidohydro_1.
    IPR004721. DHOdimr.
    IPR002195. Dihydroorotase_CS.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001237. DHOdimr. 1 hit.
    TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
    PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
    PS00483. DIHYDROOROTASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q3AYG9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDQIQLIAP DDWHVHLRDG EMLKQVVPYT AQMFRRAIVM PNLRPPVVTV    50
    EAAKAYRDQI VAACHPNWGF TPLMTAYLTD DIAPEEIERG FHEGVFTAAK 100
    LYPANATTNS AAGVTELRHI HGVLLVMERI GMPLLIHGEV TDVDVDVFDR 150
    EAVFIERSLK PIRDRYPGLK VVLEHITTEQ AVDFVGSADQ NLAATITPHH 200
    LHINRNAMFA GGLRSDFYCL PVAKRERHRL ALRRAAMSGD RRFFLGTDSA 250
    PHARPGKESS CGCAGIFNAP HALESYAMAF AQDDKLDKLE AFASLHGPAF 300
    YGLPVNEGIV TLQRDDKLVP NVVNGLVPFH AGETLPWRLQ PCT 343
    Length:343
    Mass (Da):38,057
    Last modified:November 22, 2005 - v1
    Checksum:i8479D756696FD2CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000097 Genomic DNA. Translation: ABB25858.1.
    RefSeqiWP_011359695.1. NC_007513.1.
    YP_376902.1. NC_007513.1.

    Genome annotation databases

    EnsemblBacteriaiABB25858; ABB25858; Syncc9902_0892.
    GeneIDi3743497.
    KEGGisye:Syncc9902_0892.
    PATRICi23799033. VBISynSp76179_0979.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000097 Genomic DNA. Translation: ABB25858.1 .
    RefSeqi WP_011359695.1. NC_007513.1.
    YP_376902.1. NC_007513.1.

    3D structure databases

    ProteinModelPortali Q3AYG9.
    SMRi Q3AYG9. Positions 2-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 316279.Syncc9902_0892.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB25858 ; ABB25858 ; Syncc9902_0892 .
    GeneIDi 3743497.
    KEGGi sye:Syncc9902_0892.
    PATRICi 23799033. VBISynSp76179_0979.

    Phylogenomic databases

    eggNOGi COG0418.
    HOGENOMi HOG000256259.
    KOi K01465.
    OMAi LKRNVHQ.
    OrthoDBi EOG6TFCMH.

    Enzyme and pathway databases

    UniPathwayi UPA00070 ; UER00117 .
    BioCyci SSP316279:GJCI-903-MONOMER.

    Family and domain databases

    HAMAPi MF_00219. PyrC_type1.
    InterProi IPR006680. Amidohydro_1.
    IPR004721. DHOdimr.
    IPR002195. Dihydroorotase_CS.
    [Graphical view ]
    Pfami PF01979. Amidohydro_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001237. DHOdimr. 1 hit.
    TIGRFAMsi TIGR00856. pyrC_dimer. 1 hit.
    PROSITEi PS00482. DIHYDROOROTASE_1. 1 hit.
    PS00483. DIHYDROOROTASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Synechococcus sp. CC9902."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CC9902.

    Entry informationi

    Entry nameiPYRC_SYNS9
    AccessioniPrimary (citable) accession number: Q3AYG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 57 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3