THRC_HELPJ
ID THRC_HELPJ Reviewed; 486 AA.
AC Q9ZMX5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC; OrderedLocusNames=jhp_0090;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD05671.1; -; Genomic_DNA.
DR PIR; A71975; A71975.
DR RefSeq; WP_001117379.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZMX5; -.
DR SMR; Q9ZMX5; -.
DR STRING; 85963.jhp_0090; -.
DR EnsemblBacteria; AAD05671; AAD05671; jhp_0090.
DR KEGG; hpj:jhp_0090; -.
DR PATRIC; fig|85963.30.peg.940; -.
DR eggNOG; COG0498; Bacteria.
DR OMA; FGRIAFQ; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000000804; Chromosome.
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;
KW Threonine biosynthesis.
FT CHAIN 1..486
FT /note="Threonine synthase"
FT /id="PRO_0000185634"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 486 AA; 54654 MW; 3A3C66613ADB4920 CRC64;
MPFVPTRSLK ERKIDFIEAV LNPNAPKGGL YTLEHFETLE WQDCLGMSYS ELVEHVFELL
NLEIPKNLLA SALKRYENFD NPKNPAPIFA LNERLFVQEL YHGPSLAFKD MALQPLASLF
SNLAVGKNEK YLVLVSTSGD TGPATLEGLA GMPNVFVVCL YPKDGTSLVQ KLQMVTQNAS
NLKVFGVSGD FDDAQNALKN LLKDDDFNEA LKARQLKLSV ANSVNFGRIA FQIVYHIWGF
LELYKKGAIN SKEKITLAIP SGNFGNALGA FYAKKMGLNI AKIKVVTNSN DVLREFIETG
RYDLTKRSLK QTFSPAMDIL KSSNVERALF SLFGFERTLE LMQALEEEKF YALKPKELAL
LQEHFSCASC SDEDCLKTIQ EVYAEHQYLI DPHTATALNA SLKTHEKTLV SATASYEKFP
KTTLLALNEQ KKNDDDKAAL ETLKNSYNTP DSQRLDDLFE RGIKHQEVLK LNEIKSSILL
WLENTH
