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)

P57855

- TRPC_PASMU

UniProt

P57855 - TRPC_PASMU

Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (27 Apr 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    BioCyciPMUL272843:GC8W-601-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
    Ordered Locus Names:PM0580
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469Tryptophan biosynthesis protein TrpCFPRO_0000154282Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi272843.PM0580.

    Structurei

    3D structure databases

    ProteinModelPortaliP57855.
    SMRiP57855. Positions 5-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 267267Indole-3-glycerol phosphate synthaseAdd
    BLAST
    Regioni268 – 469202N-(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.

    P57855-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQAFPSILQ KIIQDKTTWI AEKQAQLPLA SFQDQLERSD RDFYQAMQQG    50
    SKQRPSYILE CKKASPSKGL IRAAFDLTEI AEVYQHYATV ISVLTDEKYF 100
    QGHFADIAQV RQRVTQPILC KDFILSEYQV YLARYAQADA ILLMLSVLND 150
    ERYTQLATLA HQLGMGVLTE TSNEAEFARA LALKAKVIGV NNRNLHDLSV 200
    DIQRVAQITQ HYADQIPPET KIISESGIYQ HQQIRDLRHV ADGFLIGSSL 250
    MQHTDLNHAV RSLLFGEHKV CGLTRPQDVR AVYQQGALYG GLIFVTHSKR 300
    CISLRQAQEL VTQAPLRFVG VFQDQSIAFI CHLATQLRLH AVQLHGNESH 350
    EFIRQLRDEL PVNCEIWRAI CIESSGTSPC QIVENKNIDR YIFDSKTHQQ 400
    RGGTGKTFDW QLIPHHLKPK SMLAGGITPE NIPLALAQGC LGLDLNSGLE 450
    TYPGVKSHQK VVAAFAQLR 469
    Length:469
    Mass (Da):52,851
    Last modified:April 27, 2001 - v1
    Checksum:iCD1FD2866ADF10C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK02664.1.
    RefSeqiNP_245517.1. NC_002663.1.
    WP_010906737.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK02664; AAK02664; PM0580.
    GeneIDi1243927.
    KEGGipmu:PM0580.
    PATRICi22870342. VBIPasMul88067_0587.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK02664.1 .
    RefSeqi NP_245517.1. NC_002663.1.
    WP_010906737.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali P57855.
    SMRi P57855. Positions 5-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM0580.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK02664 ; AAK02664 ; PM0580 .
    GeneIDi 1243927.
    KEGGi pmu:PM0580.
    PATRICi 22870342. VBIPasMul88067_0587.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00042 .
    UPA00035 ; UER00043 .
    BioCyci PMUL272843:GC8W-601-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pm70.

    Entry informationi

    Entry nameiTRPC_PASMU
    AccessioniPrimary (citable) accession number: P57855
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 85 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, 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