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P00929

- TRPA_SALTY

UniProt

P00929 - TRPA_SALTY

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Protein
Tryptophan synthase alpha chain
Gene
trpA, STM1727
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.UniRule annotation

Catalytic activityi

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491Proton acceptor
Active sitei60 – 601Proton acceptor

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. tryptophan synthase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-1736-MONOMER.
    UniPathwayiUPA00035; UER00044.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptophan synthase alpha chain (EC:4.2.1.20)
    Gene namesi
    Name:trpA
    Ordered Locus Names:STM1727
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 268268Tryptophan synthase alpha chainUniRule annotation
    PRO_0000098839Add
    BLAST

    Proteomic databases

    PRIDEiP00929.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta chains.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    trpBP0A2K122EBI-1028423,EBI-1028431

    Protein-protein interaction databases

    DIPiDIP-1033N.
    IntActiP00929. 1 interaction.
    MINTiMINT-112862.
    STRINGi99287.STM1727.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Beta strandi18 – 247
    Turni25 – 284
    Helixi30 – 4213
    Beta strandi46 – 516
    Beta strandi58 – 603
    Helixi62 – 7312
    Helixi78 – 9114
    Beta strandi93 – 953
    Beta strandi97 – 1015
    Helixi103 – 1075
    Helixi111 – 12111
    Beta strandi125 – 1284
    Helixi133 – 1353
    Helixi137 – 1459
    Beta strandi149 – 1513
    Helixi160 – 16910
    Beta strandi174 – 1818
    Beta strandi185 – 1873
    Helixi194 – 2029
    Beta strandi208 – 2136
    Helixi217 – 2259
    Beta strandi229 – 2335
    Helixi235 – 2439
    Turni244 – 2463
    Helixi248 – 26417
    Turni265 – 2673

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A50X-ray2.30A1-268[»]
    1A5AX-ray1.90A1-268[»]
    1A5BX-ray2.00A1-268[»]
    1A5SX-ray2.30A1-268[»]
    1BEUX-ray1.90A1-268[»]
    1BKSX-ray2.20A1-268[»]
    1C29X-ray2.30A1-268[»]
    1C8VX-ray2.20A1-268[»]
    1C9DX-ray2.30A1-268[»]
    1CW2X-ray2.00A1-268[»]
    1CX9X-ray2.30A1-268[»]
    1FUYX-ray2.25A1-268[»]
    1K3UX-ray1.70A1-268[»]
    1K7EX-ray2.30A1-268[»]
    1K7FX-ray1.90A1-268[»]
    1K7XX-ray1.70A1-268[»]
    1K8XX-ray1.90A1-268[»]
    1K8YX-ray1.50A1-268[»]
    1K8ZX-ray1.70A1-268[»]
    1KFBX-ray1.90A1-268[»]
    1KFCX-ray1.50A1-268[»]
    1KFEX-ray1.75A1-268[»]
    1KFJX-ray1.80A1-268[»]
    1KFKX-ray2.40A1-268[»]
    1QOPX-ray1.40A1-268[»]
    1QOQX-ray1.80A1-268[»]
    1TJPX-ray1.50A1-268[»]
    1TTPX-ray2.30A1-268[»]
    1TTQX-ray2.00A1-268[»]
    1UBSX-ray1.90A1-268[»]
    1WBJX-ray1.50A1-268[»]
    2CLEX-ray1.50A1-268[»]
    2CLFX-ray1.70A1-268[»]
    2CLHX-ray1.70A1-268[»]
    2CLIX-ray1.70A1-268[»]
    2CLKX-ray1.50A1-268[»]
    2CLLX-ray1.60A1-268[»]
    2CLMX-ray1.51A1-268[»]
    2CLOX-ray1.50A1-268[»]
    2J9XX-ray1.90A1-268[»]
    2J9YX-ray1.80A1-268[»]
    2J9ZX-ray1.80A1-268[»]
    2RH9X-ray1.70A1-268[»]
    2RHGX-ray2.00A1-268[»]
    2TRSX-ray2.04A1-268[»]
    2TSYX-ray2.50A1-268[»]
    2TYSX-ray1.90A1-268[»]
    2WSYX-ray3.05A1-268[»]
    3CEPX-ray2.10A1-268[»]
    3PR2X-ray1.85A2-267[»]
    4HN4X-ray1.64A1-268[»]
    4HPJX-ray1.45A1-268[»]
    4HPXX-ray1.65A1-268[»]
    4HT3X-ray1.30A1-268[»]
    4KKXX-ray1.77A1-268[»]
    ProteinModelPortaliP00929.
    SMRiP00929. Positions 1-268.

    Miscellaneous databases

    EvolutionaryTraceiP00929.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TrpA family.

    Phylogenomic databases

    HOGENOMiHOG000223814.
    KOiK01695.
    OMAiNSEGYTY.
    OrthoDBiEOG6RVG0K.
    PhylomeDBiP00929.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00131. Trp_synth_alpha.
    InterProiIPR013785. Aldolase_TIM.
    IPR011060. RibuloseP-bd_barrel.
    IPR018204. Trp_synthase_alpha_AS.
    IPR002028. Trp_synthase_suA.
    [Graphical view]
    PfamiPF00290. Trp_syntA. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    TIGRFAMsiTIGR00262. trpA. 1 hit.
    PROSITEiPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00929-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERYENLFAQ LNDRREGAFV PFVTLGDPGI EQSLKIIDTL IDAGADALEL    50
    GVPFSDPLAD GPTIQNANLR AFAAGVTPAQ CFEMLALIRE KHPTIPIGLL 100
    MYANLVFNNG IDAFYARCEQ VGVDSVLVAD VPVEESAPFR QAALRHNIAP 150
    IFICPPNADD DLLRQVASYG RGYTYLLSRS GVTGAENRGA LPLHHLIEKL 200
    KEYHAAPALQ GFGISSPEQV SAAVRAGAAG AISGSAIVKI IEKNLASPKQ 250
    MLAELRSFVS AMKAASRA 268
    Length:268
    Mass (Da):28,671
    Last modified:July 21, 1986 - v1
    Checksum:iF409BF1A931581B5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01376 Genomic DNA. Translation: CAA24666.1.
    J01810 Genomic DNA. Translation: AAA27235.1.
    AE006468 Genomic DNA. Translation: AAL20645.1.
    PIRiA93837. TSEBAT.
    RefSeqiNP_460686.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL20645; AAL20645; STM1727.
    GeneIDi1253246.
    KEGGistm:STM1727.
    PATRICi32381967. VBISalEnt20916_1823.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01376 Genomic DNA. Translation: CAA24666.1 .
    J01810 Genomic DNA. Translation: AAA27235.1 .
    AE006468 Genomic DNA. Translation: AAL20645.1 .
    PIRi A93837. TSEBAT.
    RefSeqi NP_460686.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A50 X-ray 2.30 A 1-268 [» ]
    1A5A X-ray 1.90 A 1-268 [» ]
    1A5B X-ray 2.00 A 1-268 [» ]
    1A5S X-ray 2.30 A 1-268 [» ]
    1BEU X-ray 1.90 A 1-268 [» ]
    1BKS X-ray 2.20 A 1-268 [» ]
    1C29 X-ray 2.30 A 1-268 [» ]
    1C8V X-ray 2.20 A 1-268 [» ]
    1C9D X-ray 2.30 A 1-268 [» ]
    1CW2 X-ray 2.00 A 1-268 [» ]
    1CX9 X-ray 2.30 A 1-268 [» ]
    1FUY X-ray 2.25 A 1-268 [» ]
    1K3U X-ray 1.70 A 1-268 [» ]
    1K7E X-ray 2.30 A 1-268 [» ]
    1K7F X-ray 1.90 A 1-268 [» ]
    1K7X X-ray 1.70 A 1-268 [» ]
    1K8X X-ray 1.90 A 1-268 [» ]
    1K8Y X-ray 1.50 A 1-268 [» ]
    1K8Z X-ray 1.70 A 1-268 [» ]
    1KFB X-ray 1.90 A 1-268 [» ]
    1KFC X-ray 1.50 A 1-268 [» ]
    1KFE X-ray 1.75 A 1-268 [» ]
    1KFJ X-ray 1.80 A 1-268 [» ]
    1KFK X-ray 2.40 A 1-268 [» ]
    1QOP X-ray 1.40 A 1-268 [» ]
    1QOQ X-ray 1.80 A 1-268 [» ]
    1TJP X-ray 1.50 A 1-268 [» ]
    1TTP X-ray 2.30 A 1-268 [» ]
    1TTQ X-ray 2.00 A 1-268 [» ]
    1UBS X-ray 1.90 A 1-268 [» ]
    1WBJ X-ray 1.50 A 1-268 [» ]
    2CLE X-ray 1.50 A 1-268 [» ]
    2CLF X-ray 1.70 A 1-268 [» ]
    2CLH X-ray 1.70 A 1-268 [» ]
    2CLI X-ray 1.70 A 1-268 [» ]
    2CLK X-ray 1.50 A 1-268 [» ]
    2CLL X-ray 1.60 A 1-268 [» ]
    2CLM X-ray 1.51 A 1-268 [» ]
    2CLO X-ray 1.50 A 1-268 [» ]
    2J9X X-ray 1.90 A 1-268 [» ]
    2J9Y X-ray 1.80 A 1-268 [» ]
    2J9Z X-ray 1.80 A 1-268 [» ]
    2RH9 X-ray 1.70 A 1-268 [» ]
    2RHG X-ray 2.00 A 1-268 [» ]
    2TRS X-ray 2.04 A 1-268 [» ]
    2TSY X-ray 2.50 A 1-268 [» ]
    2TYS X-ray 1.90 A 1-268 [» ]
    2WSY X-ray 3.05 A 1-268 [» ]
    3CEP X-ray 2.10 A 1-268 [» ]
    3PR2 X-ray 1.85 A 2-267 [» ]
    4HN4 X-ray 1.64 A 1-268 [» ]
    4HPJ X-ray 1.45 A 1-268 [» ]
    4HPX X-ray 1.65 A 1-268 [» ]
    4HT3 X-ray 1.30 A 1-268 [» ]
    4KKX X-ray 1.77 A 1-268 [» ]
    ProteinModelPortali P00929.
    SMRi P00929. Positions 1-268.
    ModBasei Search...

    Protein-protein interaction databases

    DIPi DIP-1033N.
    IntActi P00929. 1 interaction.
    MINTi MINT-112862.
    STRINGi 99287.STM1727.

    Proteomic databases

    PRIDEi P00929.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL20645 ; AAL20645 ; STM1727 .
    GeneIDi 1253246.
    KEGGi stm:STM1727.
    PATRICi 32381967. VBISalEnt20916_1823.

    Phylogenomic databases

    HOGENOMi HOG000223814.
    KOi K01695.
    OMAi NSEGYTY.
    OrthoDBi EOG6RVG0K.
    PhylomeDBi P00929.

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00044 .
    BioCyci SENT99287:GCTI-1736-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00929.
    PROi P00929.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00131. Trp_synth_alpha.
    InterProi IPR013785. Aldolase_TIM.
    IPR011060. RibuloseP-bd_barrel.
    IPR018204. Trp_synthase_alpha_AS.
    IPR002028. Trp_synthase_suA.
    [Graphical view ]
    Pfami PF00290. Trp_syntA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    TIGRFAMsi TIGR00262. trpA. 1 hit.
    PROSITEi PS00167. TRP_SYNTHASE_ALPHA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia coli: an evolutionary comparison."
      Nichols B.P., Yanofsky C.
      Proc. Natl. Acad. Sci. U.S.A. 76:5244-5248(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides."
      Schneider W.P., Nichols B.P., Yanofsky C.
      Proc. Natl. Acad. Sci. U.S.A. 78:2169-2173(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    4. "Amino acid sequence studies with the tryptophan synthetase alpha chain of Salmonella typhimurium."
      Li S.-L., Yanofsky C.
      J. Biol. Chem. 248:1830-1836(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    5. "Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium."
      Hyde C.C., Ahmed S.A., Padlan E.A., Miles E.W., Davies D.R.
      J. Biol. Chem. 263:17857-17871(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    6. "Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes."
      Rhee S., Parris K.D., Hyde C.C., Ahmed S.A., Miles E.W., Davies D.R.
      Biochemistry 36:7664-7680(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    7. "Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49."
      Rhee S., Miles E.W., Davies D.R.
      J. Biol. Chem. 273:8553-8555(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    8. "Refined structure of the native form of the tryptophan synthase multienzyme complex from Salmonella typhimurium."
      Hyde C.C., Parris K.D., Bhat T.N., Brown C., Ahmed S.A., Miles E.W., Davies D.R.
      Submitted (JUL-1998) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    9. "Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase."
      Sachpatzidis A., Dealwis C., Lubetsky J.B., Liang P.-H., Anderson K.S., Lolis E.
      Biochemistry 38:12665-12674(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    10. "Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase."
      Weyand M., Schlichting I.
      J. Biol. Chem. 275:41058-41063(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    11. "On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase."
      Kulik V., Weyand M., Seidel R., Niks D., Arac D., Dunn M.F., Schlichting I.
      J. Mol. Biol. 324:677-690(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 17-268.

    Entry informationi

    Entry nameiTRPA_SALTY
    AccessioniPrimary (citable) accession number: P00929
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: July 9, 2014
    This is version 142 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

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    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

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