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P00906

- TRPG_SHIDY

UniProt

P00906 - TRPG_SHIDY

Protein

Anthranilate synthase component II

Gene

trpG-TRPD

Organism
Shigella dysenteriae
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    • Comment

    Functioni

    Catalytic activityi

    Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
    N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei84 – 841For GATase activityPROSITE-ProRule annotation
    Active sitei170 – 1701For GATase activityPROSITE-ProRule annotation
    Active sitei172 – 1721For GATase activityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. anthranilate phosphoribosyltransferase activity Source: UniProtKB-EC
    2. anthranilate synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB-KW
    2. tryptophan biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase, Transferase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    UniPathwayiUPA00035; UER00040.
    UPA00035; UER00041.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anthranilate synthase component II (EC:4.1.3.27)
    Including the following 2 domains:
    Glutamine amidotransferase
    Anthranilate phosphoribosyltransferase (EC:2.4.2.18)
    Gene namesi
    Name:trpG-TRPD
    OrganismiShigella dysenteriae
    Taxonomic identifieri622 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – ›201›200Anthranilate synthase component IIPRO_0000056899Add
    BLAST

    Interactioni

    Subunit structurei

    Tetramer of two components I and two components II.

    Structurei

    3D structure databases

    ProteinModelPortaliP00906.
    SMRiP00906. Positions 2-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 196194Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR006221. TrpG/PapA_dom.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00906-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP    50
    VLMLSPGPGV PSEAGCMPEL LTRLSGKLPI IGICLGHQAI VEAYGGYVGQ 100
    AGEILHGKAS SIEHDGQAMF AGLTNPLPVA RYHSLVGSNI PAGLTINAHF 150
    NGMVMAVRHD ADRICGFQFH PESILTTQGA RLLEQTLAWA QRKLEPTNTL 200
    Q 201
    Length:201
    Mass (Da):21,700
    Last modified:January 23, 2007 - v2
    Checksum:i943E3DBE4F0E59AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei201 – 2011

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01787 Genomic DNA. Translation: AAA57307.1.
    PIRiB92860. NNEB2D.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01787 Genomic DNA. Translation: AAA57307.1 .
    PIRi B92860. NNEB2D.

    3D structure databases

    ProteinModelPortali P00906.
    SMRi P00906. Positions 2-193.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00040 .
    UPA00035 ; UER00041 .

    Family and domain databases

    Gene3Di 3.40.50.880. 1 hit.
    InterProi IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR006221. TrpG/PapA_dom.
    [Graphical view ]
    Pfami PF00117. GATase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52317. SSF52317. 1 hit.
    TIGRFAMsi TIGR00566. trpG_papA. 1 hit.
    PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens."
      Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.
      J. Mol. Biol. 142:503-517(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiTRPG_SHIDY
    AccessioniPrimary (citable) accession number: P00906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
    In E.coli and certain other bacteria, component II is larger and its C-terminal two thirds has anthranilate phosphoribosyltransferase activity.

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

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

    External Data

    Dasty 3