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P00900

- TRPG_SERMA

UniProt

P00900 - TRPG_SERMA

Protein

Anthranilate synthase component 2

Gene

trpG

Organism
Serratia marcescens
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia Probable.1 Publication

    Catalytic activityi

    Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei84 – 841For GATase activity1 Publication
    Binding sitei84 – 841Glutamine
    Binding sitei88 – 881Glutamine
    Active sitei170 – 1701For GATase activityPROSITE-ProRule annotation
    Active sitei172 – 1721For GATase activityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. anthranilate synthase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    UniPathwayiUPA00035; UER00040.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anthranilate synthase component 2 (EC:4.1.3.27)
    Short name:
    AS
    Short name:
    ASII
    Alternative name(s):
    Anthranilate synthase, GATase component
    Anthranilate synthase, glutamine amidotransferase component
    Gene namesi
    Name:trpG
    OrganismiSerratia marcescens
    Taxonomic identifieri615 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 193192Anthranilate synthase component 2PRO_0000056898Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    trpEP008972EBI-1031352,EBI-1031345

    Protein-protein interaction databases

    IntActiP00900. 1 interaction.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi14 – 2310
    Beta strandi27 – 326
    Helixi37 – 4610
    Beta strandi48 – 547
    Helixi61 – 633
    Helixi67 – 748
    Turni75 – 773
    Beta strandi80 – 834
    Helixi85 – 939
    Beta strandi97 – 11418
    Helixi118 – 1203
    Beta strandi125 – 13915
    Beta strandi144 – 1507
    Beta strandi153 – 1597
    Turni160 – 1634
    Beta strandi164 – 1696
    Helixi179 – 19113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I7QX-ray1.95B/D1-193[»]
    1I7SX-ray2.40B/D1-193[»]
    ProteinModelPortaliP00900.
    SMRiP00900. Positions 2-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00900.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 193191Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni57 – 593Glutamine binding
    Regioni134 – 1352Glutamine binding

    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: Complete.

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

    P00900-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADILLLDNV DSFTYNLVDQ LRASGHQVVI YRNQIGAEVI IERLQHMEQP    50
    VLMLSPGPGT PSEAGCMPEL LQRLRGQLPI IGICLGHQAI VEAYGGQVGQ 100
    AGEILHGKAS AIAHDGEGMF AGMANPLPVA RYHSLVGSNI PADLTVNARS 150
    GEMVMAVRDD RRRVCGFQFH PESILTTHGA RLLEQTLAWA LAK 193
    Length:193
    Mass (Da):20,868
    Last modified:January 23, 2007 - v2
    Checksum:i8F53EBFEC7F4524A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361G → A AA sequence (PubMed:6986371)Curated
    Sequence conflicti38 – 381E → Q AA sequence (PubMed:6986371)Curated
    Sequence conflicti38 – 381E → Q AA sequence (PubMed:4598537)Curated
    Sequence conflicti45 – 451Q → E AA sequence (PubMed:6986371)Curated
    Sequence conflicti46 – 461H → Q AA sequence (PubMed:4598537)Curated
    Sequence conflicti48 – 481E → T AA sequence (PubMed:6986371)Curated
    Sequence conflicti60 – 623TPS → ASV AA sequence (PubMed:4598537)Curated
    Sequence conflicti77 – 771Q → R AA sequence (PubMed:6986371)Curated
    Sequence conflicti150 – 1501S → F AA sequence (PubMed:6986371)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY027546 Genomic DNA. Translation: AAK37409.1.
    PIRiD92860. NNSE2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY027546 Genomic DNA. Translation: AAK37409.1 .
    PIRi D92860. NNSE2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I7Q X-ray 1.95 B/D 1-193 [» ]
    1I7S X-ray 2.40 B/D 1-193 [» ]
    ProteinModelPortali P00900.
    SMRi P00900. Positions 2-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00900. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00040 .

    Miscellaneous databases

    EvolutionaryTracei P00900.

    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].
    2. "Primary structure of Serratia marcescens anthranilate synthase component II."
      Tso J.Y., Hermodson M.A., Zalkin H.
      J. Biol. Chem. 255:1451-1457(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-193.
    3. "Separation of anthranilate synthetase components I and II of Escherichia coli, Salmonella typhimurium, and Serratia marcescens and determination of their amino-terminal sequences by automatic Edman degradation."
      Li S.-L., Hanlon J., Yanofsky C.
      Biochemistry 13:1736-1744(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-62.
    4. "The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan."
      Spraggon G., Kim C., Nguyen-Huu X., Yee M.-C., Yanofsky C., Mills S.E.
      Proc. Natl. Acad. Sci. U.S.A. 98:6021-6026(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, ACTIVE SITE, SUBUNIT.

    Entry informationi

    Entry nameiTRPG_SERMA
    AccessioniPrimary (citable) accession number: P00900
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 95 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

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3