THRC_HELPY
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 03-AUG-2022, entry version 116.
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; Proteobacteria; 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.C694_00480; -.
DR PaxDb; O24924; -.
DR PRIDE; O24924; -.
DR EnsemblBacteria; AAD07166; AAD07166; HP_0098.
DR KEGG; hpy:HP_0098; -.
DR PATRIC; fig|85962.47.peg.104; -.
DR eggNOG; COG0498; Bacteria.
DR OMA; FGRIAFQ; -.
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 Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; -; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00260; thrC; 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