ID   THRC_HELPY              Reviewed;         486 AA.
AC   O24924;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=HP_0098;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC       phosphohomoserine and the beta-addition of water to produce L-
CC       threonine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC         Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD07166.1; -; Genomic_DNA.
DR   PIR; B64532; B64532.
DR   RefSeq; NP_206898.1; NC_000915.1.
DR   RefSeq; WP_001117321.1; NC_018939.1.
DR   AlphaFoldDB; O24924; -.
DR   SMR; O24924; -.
DR   STRING; 85962.HP_0098; -.
DR   PaxDb; 85962-C694_00480; -.
DR   EnsemblBacteria; AAD07166; AAD07166; HP_0098.
DR   KEGG; hpy:HP_0098; -.
DR   PATRIC; fig|85962.47.peg.104; -.
DR   eggNOG; COG0498; Bacteria.
DR   InParanoid; O24924; -.
DR   OrthoDB; 9763107at2; -.
DR   PhylomeDB; O24924; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01560; Thr-synth_2; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR   PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Threonine biosynthesis.
FT   CHAIN           1..486
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185633"
FT   MOD_RES         109
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   486 AA;  54707 MW;  CD9637799B508988 CRC64;
     MPFVPTRSLK EKKIDFIEAI LNPNAPKGGL YTLERFETLQ WQDCLNLSYN DLVECVFERL
     GLEIPKNLLA SALKRYENFD NPKNPAPIFA LNERLFVQEL YHGPSLAFKD MALQPLASLF
     SNLAVGKNEK YLMLVSTSGD TGPATLESLA GMPNVFVVCL YPKDGTSLVQ KLQMVTQSAS
     NLKVFGISGD FDDAQNALKN LLKDDDFNEA LKACQLKLSV ANSVNFGRIA FQIVYHIWGF
     LELYKKGAIN SKEKITLAIP SGNFGNALGA FYAKKMGLNI DKIKVVTNSN DVLREFIETG
     RYDLTHRSLK QTYSPAMDIL KSSNVERALF SLFGFERTLE LMQALEEEKF YALKPKELAL
     LQEHFSCASC SDEACLKTIQ EVYAEHQYLI DPHTATALNA SLKTHEKTLV SATASYEKFP
     RITLLALNEQ KKNDNDKAAL ETLKNSYNTP DSQRLDDLFE RGIKHQEVLK LNEIKSSILL
     WLESLH
//