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Q9MT28

- THRC_SOLTU

UniProt

Q9MT28 - THRC_SOLTU

Protein

Threonine synthase, chloroplastic

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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

    Enzyme regulationi

    Allosterically activated by S-adenosyl-methionine (SAM).By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei465 – 4651Pyridoxal 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, S-adenosyl-L-methionine

    Enzyme and pathway databases

    UniPathwayiUPA00050; UER00065.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Threonine synthase, chloroplastic (EC:4.2.3.1)
    Short name:
    TS
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: Unplaced

    Subcellular locationi

    Plastidchloroplast By similarity

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4040ChloroplastBy similarityAdd
    BLAST
    Chaini41 – 519479Threonine synthase, chloroplasticPRO_0000033618Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei196 – 1961N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9MT28.
    SMRiQ9MT28. Positions 48-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni328 – 3325Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK01733.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    Q9MT28-1 [UniParc]FASTAAdd to Basket

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    MAASCMLRSS FISPGLPQLH HQSTSKPNNG IHFFTPIKAT ATNDAISQQK    50
    HRRPADENIR EEARRHCSSH NFSARYVPFN AGPNSDEWYS LDEIVYRSRS 100
    GGLLDVQHDM DALKKFDGQY WRSLFDSRVG KTTWPYGSGV WSKKEWVLPE 150
    IDSDDIVSAF EGNSNLFWAE RFGKQFLGMT DLWVKHCGIS HTGSFKDLGM 200
    TVLVSQVNRL RKMHKPVVGV GCASTGDTSA ALSAYCASAG IPSIVFLPAN 250
    KISMAQLVQP IANGAFVLSI DTDFDGCMQL IREVTAELPI YLANSLNSLR 300
    LEGQKTAAIE ILQQFDWEVP EWVIVPGGNL GNIYAFYKGF QMCKELGLVD 350
    RIPRLVCAQA ANANPLYLHY KSGWKDFKPV KANTTFASAI QIGDPVSIDR 400
    AVFALQQCNG IVEEATEEEL MDAMAQADST GMFICPHTGV ALTALFKLRN 450
    SGVIAPTDRT VVVSTAHGLK FTQSKIDYHS KEIKDMECRF ANPPVEVKAD 500
    FGSVMDVLKS YLLSQNSKL 519
    Length:519
    Mass (Da):57,412
    Last modified:October 1, 2000 - v1
    Checksum:i114C0979CD231464
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082894 mRNA. Translation: AAF74984.1.
    RefSeqiNP_001274994.1. NM_001288065.1.
    UniGeneiStu.478.

    Genome annotation databases

    GeneIDi102577745.
    KEGGisot:102577745.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082894 mRNA. Translation: AAF74984.1 .
    RefSeqi NP_001274994.1. NM_001288065.1.
    UniGenei Stu.478.

    3D structure databases

    ProteinModelPortali Q9MT28.
    SMRi Q9MT28. Positions 48-517.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 102577745.
    KEGGi sot:102577745.

    Phylogenomic databases

    KOi K01733.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .

    Family and domain databases

    InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 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. "Expression of threonine synthase from Solanum tuberosum L. is not metabolically regulated by photosynthesis-related signals or by nitrogenous compounds."
      Casazza A.P., Basner A., Hoefgen R., Hesse H.
      Plant Sci. 157:43-50(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.

    Entry informationi

    Entry nameiTHRC_SOLTU
    AccessioniPrimary (citable) accession number: Q9MT28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, 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