ID   V5NLV2_HELPX            Unreviewed;       486 AA.
AC   V5NLV2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=U064_0442 {ECO:0000313|EMBL:AHA89374.1};
OS   Helicobacter pylori BM012S.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1407463 {ECO:0000313|EMBL:AHA89374.1, ECO:0000313|Proteomes:UP000018543};
RN   [1] {ECO:0000313|EMBL:AHA89374.1, ECO:0000313|Proteomes:UP000018543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM012S {ECO:0000313|EMBL:AHA89374.1,
RC   ECO:0000313|Proteomes:UP000018543};
RX   DOI=10.1371/journal.pone.0082187;
RA   Linz B., Windsor H.M., Gajewski J.P., Hake C.M., Drautz D.I.,
RA   Schuster S.C., Marshall B.J.;
RT   "Helicobacter pylori genomic microevolution during naturally occurring
RT   transmission between adults.";
RL   PLoS ONE 8:E82187-E82187(2013).
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         Evidence={ECO:0000256|ARBA:ARBA00000051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR604450-51};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family.
CC       {ECO:0000256|ARBA:ARBA00005517}.
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DR   EMBL; CP006889; AHA89374.1; -; Genomic_DNA.
DR   RefSeq; WP_023591781.1; NC_022911.1.
DR   AlphaFoldDB; V5NLV2; -.
DR   KEGG; hez:U064_0442; -.
DR   PATRIC; fig|1407463.3.peg.450; -.
DR   HOGENOM; CLU_015170_3_1_7; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000018543; 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   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 {ECO:0000256|ARBA:ARBA00022605};
KW   Lyase {ECO:0000313|EMBL:AHA89374.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          87..407
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         109
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   486 AA;  54876 MW;  756F05E2B373D8DD CRC64;
     MPFVPTRSLK EKKIDFIEAV LNPNAPKGGL YTLERFETLE WQDCLNLSYN ELVECVFERL
     GLEIPKGLLT SALKRYENFD NPKNPAPIFA LNERLFVQEL YHGPSLAFKD MALQPLASLF
     SNLAVGKNEK YLMLVSTSGD TGPATLESLA GMPNVFVVCL YPKDGTSLVQ KLQMVTQSAS
     NLKVFGVSGD FDDAQNALKN LLKDDDFNEA LKMHQLKLSV ANSVNFGRIA FQIVYHIWGF
     LELYKKGAIN SKEKITLAIP SGNFGNALGA FYAKKMGLNI AKIKVVTNSN DVLREFIETG
     RYDLTHRSLK QTFSPAMDIL KSSNVERVLF SLFGFERTLE LMQALEEERF YALKPKELAL
     LQEHFSCASC SDEDCLKTIQ EVYAEHQYLI DPHTATALNA SLKTHEKTLV SATASYEKFP
     RTTLLALNEP KKNDNDKIAL ETLKNSYNTP DSKRLDDLFE RGIKHQEVLK LNEIKYSILL
     WLESLH
//