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P29363

- THRC_PSEAE

UniProt

P29363 - THRC_PSEAE

Protein

Threonine synthase

Gene

thrC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 3 (11 Jan 2001)
      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.By similarity

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.By similarity

    Pathwayi

    GO - Molecular functioni

    1. pyridoxal phosphate binding Source: InterPro
    2. threonine synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. threonine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-999-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:PA3735
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA3735.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469Threonine synthasePRO_0000185639Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei112 – 1121N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Protein-protein interaction databases

    STRINGi208964.PA3735.

    Structurei

    3D structure databases

    ProteinModelPortaliP29363.
    SMRiP29363. Positions 1-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0498.
    HOGENOMiHOG000230745.
    KOiK01733.
    OMAiVFILFPH.
    OrthoDBiEOG65BDJX.
    PhylomeDBiP29363.

    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.

    P29363-1 [UniParc]FASTAAdd to Basket

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    MRYISTRGQA PALNFEDVLL AGLASDGGLY VPENLPRFTL EEIASWVGLP    50
    YHELAFRVMR PFVAGSIADA DFKKILEETY GVFAHDAVAP LRQLNGNEWV 100
    LELFHGPTLA FKDFALQLLG RLLDHVLAKR GERVVIMGAT SGDTGSAAIE 150
    GCRRCDNVDI FIMHPHNRVS EVQRRQMTTI LGDNIHNIAI EGNFDDCQEM 200
    VKASFADQGF LKGTRLVAVN SINWARIMAQ IVYYFHAALQ LGAPHRSVAF 250
    SVPTGNFGDI FAGYLARNMG LPVSQLIVAT NRNDILHRFM SGNRYDKDTL 300
    HPSLSPSMDI MVSSNFERLL FDLHGRNGKA VAELLDAFKA SGKLSVEDQR 350
    WTEARKLFDS LAVSDEQTCE TIAEVYRSSG ELLDPHTAIG VRAARECRRS 400
    LSVPMVTLGT AHPVKFPEAV EKAGIGQAPA LPAHLADLFE REERCTVLPN 450
    ELAKVQAFVS QHGNRGKPL 469
    Length:469
    Mass (Da):51,795
    Last modified:January 11, 2001 - v3
    Checksum:i224032B86272C79C
    GO

    Sequence cautioni

    The sequence CAA46168.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 10114VAPLR…NEWVL → SGAAAPVERRTNGCV(PubMed:1333566)CuratedAdd
    BLAST
    Sequence conflicti151 – 1555GCRRC → AAAVA in CAA46168. (PubMed:1333566)Curated
    Sequence conflicti163 – 1642MH → ID in CAA46168. (PubMed:1333566)Curated
    Sequence conflicti173 – 1731Q → E in CAA46168. (PubMed:1333566)Curated
    Sequence conflicti181 – 1811L → H in CAA46168. (PubMed:1333566)Curated
    Sequence conflicti280 – 2801T → R in CAA46168. (PubMed:1333566)Curated
    Sequence conflicti294 – 30411RYDKDTLHPSL → ASTRHTLTPSV in CAA46168. (PubMed:1333566)CuratedAdd
    BLAST
    Sequence conflicti465 – 4651R → P in CAA46168. (PubMed:1333566)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65033 Genomic DNA. Translation: CAA46168.1. Different initiation.
    AE004091 Genomic DNA. Translation: AAG07122.1.
    PIRiG83179.
    S27980. SYPSRA.
    RefSeqiNP_252424.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG07122; AAG07122; PA3735.
    GeneIDi880336.
    KEGGipae:PA3735.
    PATRICi19842099. VBIPseAer58763_3907.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65033 Genomic DNA. Translation: CAA46168.1 . Different initiation.
    AE004091 Genomic DNA. Translation: AAG07122.1 .
    PIRi G83179.
    S27980. SYPSRA.
    RefSeqi NP_252424.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali P29363.
    SMRi P29363. Positions 1-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA3735.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG07122 ; AAG07122 ; PA3735 .
    GeneIDi 880336.
    KEGGi pae:PA3735.
    PATRICi 19842099. VBIPseAer58763_3907.

    Organism-specific databases

    PseudoCAPi PA3735.

    Phylogenomic databases

    eggNOGi COG0498.
    HOGENOMi HOG000230745.
    KOi K01733.
    OMAi VFILFPH.
    OrthoDBi EOG65BDJX.
    PhylomeDBi P29363.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .
    BioCyci RETL1328306-WGS:GSTH-999-MONOMER.

    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. "Isolation, organization and expression of the Pseudomonas aeruginosa threonine genes."
      Clepet C., Borne F., Krishnapillai V., Baird C., Patte J.-C., Cami B.
      Mol. Microbiol. 6:3109-3119(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiTHRC_PSEAE
    AccessioniPrimary (citable) accession number: P29363
    Secondary accession number(s): Q9HXQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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