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P22098

- TRPC_VIBPA

UniProt

P22098 - TRPC_VIBPA

Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (04 Apr 2003)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain By similarity.By similarity

    Catalytic activityi

    N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
    1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.

    Pathwayi

    GO - Molecular functioni

    1. indole-3-glycerol-phosphate synthase activity Source: UniProtKB-EC
    2. phosphoribosylanthranilate isomerase activity Source: UniProtKB-EC

    GO - Biological processi

    1. tryptophan biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Decarboxylase, Isomerase, Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

    Enzyme and pathway databases

    BioCyciVPAR223926:GHK4-2014-MONOMER.
    UniPathwayiUPA00035; UER00042.
    UPA00035; UER00043.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptophan biosynthesis protein TrpCF
    Including the following 2 domains:
    Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
    Short name:
    IGPS
    N-(5'-phospho-ribosyl)anthranilate isomerase (EC:5.3.1.24)
    Short name:
    PRAI
    Gene namesi
    Name:trpC
    Synonyms:trpC-TRPF
    Ordered Locus Names:VP1959
    OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
    Taxonomic identifieri223926 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000002493: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481Tryptophan biosynthesis protein TrpCFPRO_0000154286Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi223926.VP1959.

    Structurei

    3D structure databases

    ProteinModelPortaliP22098.
    SMRiP22098. Positions 25-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 283283Indole-3-glycerol phosphate synthaseAdd
    BLAST
    Regioni284 – 481198N-(5'-phosphoribosyl)anthranilate isomeraseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the TrpC family.Curated
    In the C-terminal section; belongs to the TrpF family.Curated

    Phylogenomic databases

    eggNOGiCOG0134.
    HOGENOMiHOG000280458.
    KOiK13498.
    OMAiEKYFQGD.
    OrthoDBiEOG6WT8JX.

    Family and domain databases

    Gene3Di3.20.20.70. 2 hits.
    HAMAPiMF_00134_B. IGPS_B.
    MF_00135. PRAI.
    InterProiIPR013785. Aldolase_TIM.
    IPR013798. Indole-3-glycerol_P_synth.
    IPR001468. Indole-3-GlycerolPSynthase_CS.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00218. IGPS. 1 hit.
    PF00697. PRAI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 2 hits.
    PROSITEiPS00614. IGPS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22098-1 [UniParc]FASTAAdd to Basket

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    MKMTDFNTQQ ANNLSEHVSK KEAEMAEVLA KIVRDKYQWV AERKASQHLS    50
    TFQSDLLPSD RSFYDALSGD KTVFITECKK ASPSKGLIRN DFDLDYIASV 100
    YNNYADAISV LTDEKYFQGS FDFLPQVRRQ VKQPVLCKDF MVDTYQVYLA 150
    RHYGADAVLL MLSVLNDEEY KALEEAAHSL NMGILTEVSN EEELHRAVQL 200
    GARVIGINNR NLRDLTTDLN RTKALAPTIR KLAPNATVIS ESGIYTHQQV 250
    RDLAEYADGF LIGSSLMAED NLELAVRKVT LGENKVCGLT HPDDAAKAYQ 300
    AGAVFGGLIF VEKSKRAVDF ESARLTMSGA PLNYVGVFQN HDVDYVASIV 350
    TSLGLKAVQL HGLEDQEYVN QLKTELPVGV EIWKAYGVAD TKPSLLADNI 400
    DRHLLDAQVG TQTGGTGHVF DWSLIGDPSQ IMLAGGLSPE NAQQAAKLGC 450
    LGLDLNSGVE SAPGKKDSQK LQAAFHAIRN Y 481
    Length:481
    Mass (Da):52,974
    Last modified:April 4, 2003 - v2
    Checksum:iBC575AD8FB57FC00
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti203 – 2031R → K in CAA35034. (PubMed:1773058)Curated
    Sequence conflicti449 – 4491G → A in CAA35034. (PubMed:1773058)Curated
    Sequence conflicti476 – 4761H → R in CAA35034. (PubMed:1773058)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17149 Genomic DNA. Translation: CAA35034.1.
    BA000031 Genomic DNA. Translation: BAC60222.1.
    RefSeqiNP_798338.1. NC_004603.1.
    WP_011105994.1. NC_004603.1.

    Genome annotation databases

    EnsemblBacteriaiBAC60222; BAC60222; BAC60222.
    GeneIDi1189470.
    KEGGivpa:VP1959.
    PATRICi20142086. VBIVibPar50997_1874.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17149 Genomic DNA. Translation: CAA35034.1 .
    BA000031 Genomic DNA. Translation: BAC60222.1 .
    RefSeqi NP_798338.1. NC_004603.1.
    WP_011105994.1. NC_004603.1.

    3D structure databases

    ProteinModelPortali P22098.
    SMRi P22098. Positions 25-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 223926.VP1959.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC60222 ; BAC60222 ; BAC60222 .
    GeneIDi 1189470.
    KEGGi vpa:VP1959.
    PATRICi 20142086. VBIVibPar50997_1874.

    Phylogenomic databases

    eggNOGi COG0134.
    HOGENOMi HOG000280458.
    KOi K13498.
    OMAi EKYFQGD.
    OrthoDBi EOG6WT8JX.

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00042 .
    UPA00035 ; UER00043 .
    BioCyci VPAR223926:GHK4-2014-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 2 hits.
    HAMAPi MF_00134_B. IGPS_B.
    MF_00135. PRAI.
    InterProi IPR013785. Aldolase_TIM.
    IPR013798. Indole-3-glycerol_P_synth.
    IPR001468. Indole-3-GlycerolPSynthase_CS.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00218. IGPS. 1 hit.
    PF00697. PRAI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 2 hits.
    PROSITEi PS00614. IGPS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and features of the tryptophan operon of Vibrio parahemolyticus."
      Crawford I.P., Han C.Y., Silverman M.
      DNA Seq. 1:189-196(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BB22.
    2. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
      Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
      Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RIMD 2210633.

    Entry informationi

    Entry nameiTRPC_VIBPA
    AccessioniPrimary (citable) accession number: P22098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: April 4, 2003
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3