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P04990

- THRC_BACSU

UniProt

P04990 - THRC_BACSU

Protein

Threonine synthase

Gene

thrC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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 sitei85 – 851Pyridoxal phosphateBy similarity
    Binding sitei314 – 3141Pyridoxal 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

    BioCyciBSUB:BSU32250-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:BSU32250
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU32250. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Threonine synthasePRO_0000185626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP04990.

    Interactioni

    Protein-protein interaction databases

    IntActiP04990. 1 interaction.
    MINTiMINT-8366482.
    STRINGi224308.BSU32250.

    Structurei

    3D structure databases

    ProteinModelPortaliP04990.
    SMRiP04990. Positions 2-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni185 – 1895Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0498.
    HOGENOMiHOG000076503.
    KOiK01733.
    OMAiGITHMAM.
    OrthoDBiEOG6HMX9M.
    PhylomeDBiP04990.

    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.

    P04990-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWKGLIHQYK EFLPVTDQTP ALTLHEGNTP LIHLPKLSEQ LGIELHVKTE    50
    GVNPTGSFKD RGMVMAVAKA KEEGNDTIMC ASTGNTSAAA AAYAARANMK 100
    CIVIIPNGKI AFGKLAQAVM YGAEIIAIDG NFDDALKIVR SICEKSPIAL 150
    VNSVNPYRIE GQKTAAFEVC EQLGEAPDVL AIPVGNAGNI TAYWKGFKEY 200
    HEKNGTGLPK MRGFEAEGAA AIVRNEVIEN PETIATAIRI GNPASWDKAV 250
    KAAEESNGKI DEVTDDEILH AYQLIARVEG VFAEPGSCAS IAGVLKQVKS 300
    GEIPKGSKVV AVLTGNGLKD PNTAVDISEI KPVTLPTDED SILEYVKGAA 350
    RV 352
    Length:352
    Mass (Da):37,464
    Last modified:August 13, 1987 - v1
    Checksum:iF478003AA330C6A0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04603 Genomic DNA. Translation: CAA28270.1.
    AL009126 Genomic DNA. Translation: CAB15215.1.
    M23217 Genomic DNA. Translation: AAA50610.1.
    PIRiA25364.
    RefSeqiNP_391105.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15215; CAB15215; BSU32250.
    GeneIDi936660.
    KEGGibsu:BSU32250.
    PATRICi18978422. VBIBacSub10457_3374.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04603 Genomic DNA. Translation: CAA28270.1 .
    AL009126 Genomic DNA. Translation: CAB15215.1 .
    M23217 Genomic DNA. Translation: AAA50610.1 .
    PIRi A25364.
    RefSeqi NP_391105.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P04990.
    SMRi P04990. Positions 2-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P04990. 1 interaction.
    MINTi MINT-8366482.
    STRINGi 224308.BSU32250.

    Proteomic databases

    PaxDbi P04990.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15215 ; CAB15215 ; BSU32250 .
    GeneIDi 936660.
    KEGGi bsu:BSU32250.
    PATRICi 18978422. VBIBacSub10457_3374.

    Organism-specific databases

    GenoListi BSU32250. [Micado ]

    Phylogenomic databases

    eggNOGi COG0498.
    HOGENOMi HOG000076503.
    KOi K01733.
    OMAi GITHMAM.
    OrthoDBi EOG6HMX9M.
    PhylomeDBi P04990.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .
    BioCyci BSUB:BSU32250-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. "Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase."
      Parsot C.
      EMBO J. 5:3013-3019(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II."
      Parsot C., Cohen G.N.
      J. Biol. Chem. 263:14654-14660(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
      Strain: 168.

    Entry informationi

    Entry nameiTHRC_BACSU
    AccessioniPrimary (citable) accession number: P04990
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 108 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. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3