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P45837

- THRC_MYCLE

UniProt

P45837 - THRC_MYCLE

Protein

Threonine synthase

Gene

thrC

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951Pyridoxal phosphateBy similarity
    Binding sitei326 – 3261Pyridoxal phosphateBy similarity

    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

    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:ML1130
    OrganismiMycobacterium leprae (strain TN)
    Taxonomic identifieri272631 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000806: Chromosome

    Organism-specific databases

    LepromaiML1130.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 360360Threonine synthasePRO_0000185636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi272631.ML1130.

    Structurei

    3D structure databases

    ProteinModelPortaliP45837.
    SMRiP45837. Positions 10-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni196 – 2005Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0498.
    HOGENOMiHOG000076503.
    KOiK01733.
    OMAiDPDWAVA.
    OrthoDBiEOG6HMX9M.

    Family and domain databases

    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR026260. Thr_Synthase_bac/arc.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038945. Thr_synthase. 1 hit.
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR00260. thrC. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P45837-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGQQTTTHQ PWPGVIAAYR DRLPVGDDWT PVTLLEGGTP LIAAPRLSEQ    50
    TGCTIHLKVE GLNPTGSFKD RGMTMAVTDA LARGQRAVLC ASTGNTSASA 100
    AAYAARAGIT CAVLIPQGKI AMGKLAQAVM HGAKIIQIDG NFDDCLELAR 150
    KMAADFPMIS LVNSVNPVRI EGQKTAVFEI VDALGTAPHV HALPVGNAGN 200
    ITAYWKGYTE YHADGLIDRL PRMLGTQAAG AAPLVLGEPV SHPETIATAI 250
    RIGSPASWTS AVEAQQQSKG RFLAATDEEI LAAYHLVARA EGVFVEPASA 300
    ASIAGLLKAI DGGWVARGST VVCTITGNGL KDPDTALKDM PSVSPVPVDA 350
    VAVVEQLGLV 360
    Length:360
    Mass (Da):37,385
    Last modified:November 1, 1995 - v1
    Checksum:i96A06F7B17B2688B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15186 Genomic DNA. Translation: AAA63090.1.
    AL583920 Genomic DNA. Translation: CAC31511.1.
    PIRiT09991.
    RefSeqiNP_301824.1. NC_002677.1.
    WP_010908148.1. NC_002677.1.

    Genome annotation databases

    EnsemblBacteriaiCAC31511; CAC31511; CAC31511.
    GeneIDi910224.
    KEGGimle:ML1130.
    PATRICi18054215. VBIMycLep78757_2052.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15186 Genomic DNA. Translation: AAA63090.1 .
    AL583920 Genomic DNA. Translation: CAC31511.1 .
    PIRi T09991.
    RefSeqi NP_301824.1. NC_002677.1.
    WP_010908148.1. NC_002677.1.

    3D structure databases

    ProteinModelPortali P45837.
    SMRi P45837. Positions 10-358.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272631.ML1130.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC31511 ; CAC31511 ; CAC31511 .
    GeneIDi 910224.
    KEGGi mle:ML1130.
    PATRICi 18054215. VBIMycLep78757_2052.

    Organism-specific databases

    Lepromai ML1130.

    Phylogenomic databases

    eggNOGi COG0498.
    HOGENOMi HOG000076503.
    KOi K01733.
    OMAi DPDWAVA.
    OrthoDBi EOG6HMX9M.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .

    Family and domain databases

    InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR026260. Thr_Synthase_bac/arc.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038945. Thr_synthase. 1 hit.
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR00260. thrC. 1 hit.
    PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Smith D.R., Robison K.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TN.

    Entry informationi

    Entry nameiTHRC_MYCLE
    AccessioniPrimary (citable) accession number: P45837
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 93 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

    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