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Q8TQD4

- THRC_METAC

UniProt

Q8TQD4 - THRC_METAC

Protein

Threonine synthase

Gene

thrC

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      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. Does not catalyze the conversion of O-acetyl-L-homoserine into threonine.1 Publication

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei130 – 1301Pyridoxal phosphateBy similarity
    Binding sitei369 – 3691Pyridoxal 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

    BioCyciMACE188937:GI2O-1626-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:MA_1610
    OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
    Taxonomic identifieri188937 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000002487: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405Threonine synthasePRO_0000392651Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PRIDEiQ8TQD4.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    STRINGi188937.MA1610.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TQD4.
    SMRiQ8TQD4. Positions 51-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni231 – 2355Pyridoxal phosphate bindingBy similarity

    Domaini

    The N-terminal 41 amino acids are required for activity.1 Publication

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0498.
    KOiK01733.
    OMAiLAQAMFH.
    PhylomeDBiQ8TQD4.

    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.

    Q8TQD4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYHLKCIECG AEYSRDEVIY TCSKCDGLLD VIYDYSSIKI DMEKLKTECP    50
    SVWKYAKLLP VEREPVTIQE GGTPLYKCDR LAEKIGIKKL YVKHEGMNPT 100
    GSFKDRGMTV GVTKALELGM NTVACASTGN TSAALAIYGA KAGIPVVVLL 150
    PAGKVALGKV AQALMHGAKV LSIRGNFDDA LALVRTLCSQ EKIYLLNSIN 200
    PYRLEGQKTI GFEIADQLDF KVPDRIVLPV GNAGNITAIY KGFREFKILG 250
    ITDSLPKMTG IQAEGSCPIV KAIKSGAPAI TPEENPETVA TAIRIGNPVN 300
    ATKALSAIRE SGGTAESVTD EEILAAQKDL ARLEGIGVEP ASAASVAGLR 350
    KLVDMGVIGR DETVVCITTG HLLKDPQTVI DVCEEPTVVD ANIDAIREAI 400
    FGKAK 405
    Length:405
    Mass (Da):43,285
    Last modified:June 1, 2002 - v1
    Checksum:i3D2A303B42A4D942
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010299 Genomic DNA. Translation: AAM05023.1.
    RefSeqiNP_616543.1. NC_003552.1.

    Genome annotation databases

    EnsemblBacteriaiAAM05023; AAM05023; MA_1610.
    GeneIDi1473498.
    KEGGimac:MA1610.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010299 Genomic DNA. Translation: AAM05023.1 .
    RefSeqi NP_616543.1. NC_003552.1.

    3D structure databases

    ProteinModelPortali Q8TQD4.
    SMRi Q8TQD4. Positions 51-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 188937.MA1610.

    Proteomic databases

    PRIDEi Q8TQD4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM05023 ; AAM05023 ; MA_1610 .
    GeneIDi 1473498.
    KEGGi mac:MA1610.

    Phylogenomic databases

    eggNOGi COG0498.
    KOi K01733.
    OMAi LAQAMFH.
    PhylomeDBi Q8TQD4.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .
    BioCyci MACE188937:GI2O-1626-MONOMER.

    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. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
      Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
      , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
      Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
    2. "Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase."
      Graham D.E., Taylor S.M., Wolf R.Z., Namboori S.C.
      Biochem. J. 424:467-478(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, SUBUNIT.

    Entry informationi

    Entry nameiTHRC_METAC
    AccessioniPrimary (citable) accession number: Q8TQD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 69 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