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P00934

- THRC_ECOLI

UniProt

P00934 - THRC_ECOLI

Protein

Threonine synthase

Gene

thrC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction.1 Publication

    Catalytic activityi

    O-phospho-L-homoserine + H2O = L-threonine + phosphate.1 Publication

    Cofactori

    Pyridoxal phosphate.1 Publication

    Enzyme regulationi

    Is competitively inhibited by L-threo-3-hydroxyhomoserine phosphate.1 Publication

    Kineticsi

    1. KM=0.5 mM for O-phospho-L-homoserine1 Publication

    Vmax=9.3 µmol/min/mg enzyme1 Publication

    Pathwayi

    GO - Molecular functioni

    1. pyridoxal phosphate binding Source: InterPro
    2. threonine synthase activity Source: EcoCyc

    GO - Biological processi

    1. threonine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:THRESYN-MONOMER.
    ECOL316407:JW0003-MONOMER.
    MetaCyc:THRESYN-MONOMER.
    UniPathwayiUPA00050; UER00065.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Threonine synthase (EC:4.2.3.1)
    Short name:
    TS
    Gene namesi
    Name:thrC
    Ordered Locus Names:b0004, JW0003
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11000. thrC.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Threonine synthasePRO_0000185631Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei107 – 1071N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP00934.
    PRIDEiP00934.

    2D gel databases

    SWISS-2DPAGEP00934.

    Expressioni

    Gene expression databases

    GenevestigatoriP00934.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    fusAP0A6M81EBI-1112675,EBI-370503

    Protein-protein interaction databases

    DIPiDIP-10993N.
    IntActiP00934. 2 interactions.
    STRINGi511145.b0004.

    Structurei

    Secondary structure

    1
    428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi8 – 136
    Helixi15 – 217
    Helixi25 – 273
    Beta strandi30 – 345
    Helixi40 – 467
    Helixi51 – 6313
    Helixi64 – 663
    Helixi69 – 7911
    Beta strandi86 – 905
    Beta strandi93 – 975
    Helixi107 – 12115
    Turni122 – 1243
    Beta strandi127 – 1326
    Beta strandi134 – 1363
    Helixi137 – 1448
    Turni145 – 1473
    Beta strandi151 – 1588
    Helixi164 – 1718
    Beta strandi177 – 1848
    Helixi186 – 19510
    Helixi196 – 1983
    Helixi200 – 2067
    Helixi216 – 2216
    Helixi224 – 2307
    Turni235 – 2395
    Beta strandi240 – 2467
    Helixi251 – 26111
    Beta strandi267 – 2737
    Helixi278 – 2858
    Helixi299 – 3013
    Helixi309 – 31810
    Helixi323 – 3253
    Beta strandi326 – 3305
    Helixi333 – 34513
    Helixi352 – 36211
    Beta strandi370 – 3756
    Helixi379 – 3824
    Helixi383 – 3908
    Helixi398 – 4047
    Beta strandi411 – 4155
    Helixi417 – 4248

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VB3X-ray2.20A1-428[»]
    ProteinModelPortaliP00934.
    SMRiP00934. Positions 1-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00934.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0498.
    HOGENOMiHOG000230743.
    KOiK01733.
    OMAiHGAIAYQ.
    OrthoDBiEOG65BDJX.
    PhylomeDBiP00934.

    Family and domain databases

    Gene3Di3.90.1380.10. 1 hit.
    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR029144. Thr_synth_N.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    PF14821. Thr_synth_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR00260. thrC. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00934-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLYNLKDHN EQVSFAQAVT QGLGKNQGLF FPHDLPEFSL TEIDEMLKLD    50
    FVTRSAKILS AFIGDEIPQE ILEERVRAAF AFPAPVANVE SDVGCLELFH 100
    GPTLAFKDFG GRFMAQMLTH IAGDKPVTIL TATSGDTGAA VAHAFYGLPN 150
    VKVVILYPRG KISPLQEKLF CTLGGNIETV AIDGDFDACQ ALVKQAFDDE 200
    ELKVALGLNS ANSINISRLL AQICYYFEAV AQLPQETRNQ LVVSVPSGNF 250
    GDLTAGLLAK SLGLPVKRFI AATNVNDTVP RFLHDGQWSP KATQATLSNA 300
    MDVSQPNNWP RVEELFRRKI WQLKELGYAA VDDETTQQTM RELKELGYTS 350
    EPHAAVAYRA LRDQLNPGEY GLFLGTAHPA KFKESVEAIL GETLDLPKEL 400
    AERADLPLLS HNLPADFAAL RKLMMNHQ 428
    Length:428
    Mass (Da):47,114
    Last modified:July 21, 1986 - v1
    Checksum:i5F7C20BE00B437E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14003 Genomic DNA. Translation: AAA97303.1.
    J01706 Genomic DNA. Translation: AAA83916.1.
    U00096 Genomic DNA. Translation: AAC73115.1.
    AP009048 Genomic DNA. Translation: BAB96581.1.
    PIRiA01157. SYECR.
    RefSeqiNP_414545.1. NC_000913.3.
    YP_488310.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73115; AAC73115; b0004.
    BAB96581; BAB96581; BAB96581.
    GeneIDi12932941.
    945198.
    KEGGiecj:Y75_p0004.
    eco:b0004.
    PATRICi32115103. VBIEscCol129921_0003.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14003 Genomic DNA. Translation: AAA97303.1 .
    J01706 Genomic DNA. Translation: AAA83916.1 .
    U00096 Genomic DNA. Translation: AAC73115.1 .
    AP009048 Genomic DNA. Translation: BAB96581.1 .
    PIRi A01157. SYECR.
    RefSeqi NP_414545.1. NC_000913.3.
    YP_488310.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VB3 X-ray 2.20 A 1-428 [» ]
    ProteinModelPortali P00934.
    SMRi P00934. Positions 1-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10993N.
    IntActi P00934. 2 interactions.
    STRINGi 511145.b0004.

    2D gel databases

    SWISS-2DPAGE P00934.

    Proteomic databases

    PaxDbi P00934.
    PRIDEi P00934.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73115 ; AAC73115 ; b0004 .
    BAB96581 ; BAB96581 ; BAB96581 .
    GeneIDi 12932941.
    945198.
    KEGGi ecj:Y75_p0004.
    eco:b0004.
    PATRICi 32115103. VBIEscCol129921_0003.

    Organism-specific databases

    EchoBASEi EB0993.
    EcoGenei EG11000. thrC.

    Phylogenomic databases

    eggNOGi COG0498.
    HOGENOMi HOG000230743.
    KOi K01733.
    OMAi HGAIAYQ.
    OrthoDBi EOG65BDJX.
    PhylomeDBi P00934.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .
    BioCyci EcoCyc:THRESYN-MONOMER.
    ECOL316407:JW0003-MONOMER.
    MetaCyc:THRESYN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00934.
    PROi P00934.

    Gene expression databases

    Genevestigatori P00934.

    Family and domain databases

    Gene3Di 3.90.1380.10. 1 hit.
    InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR029144. Thr_synth_N.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    PF14821. Thr_synth_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR00260. thrC. 1 hit.
    PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of thrC and of the transcription termination region of the threonine operon in Escherichia coli K12."
      Parsot C., Cossart P., Saint-Girons I., Cohen G.N.
      Nucleic Acids Res. 11:7331-7345(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    7. Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors."
      Laber B., Gerbling K.P., Harde C., Neff K.H., Nordhoff E., Pohlenz H.D.
      Biochemistry 33:3413-3423(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, KINETIC PARAMETERS.
    9. "Crystal structure of threonine synthase from Escherichia coli."
      Omi R., Goto M., Miyahara I., Mizuguchi H., Hayashi H., Kagamiyama H., Hirotsu K.
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiTHRC_ECOLI
    AccessioniPrimary (citable) accession number: P00934
    Secondary accession number(s): Q6LEK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 135 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3