ID   Q9CPD2_PASMU            Unreviewed;       424 AA.
AC   Q9CPD2;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   10-JUN-2026, entry version 124.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|NCBIfam:TIGR00260};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028, ECO:0000256|NCBIfam:TIGR00260};
GN   Name=thrC {ECO:0000313|EMBL:AAK02199.1};
GN   OrderedLocusNames=PM0115 {ECO:0000313|EMBL:AAK02199.1};
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK02199.1, ECO:0000313|Proteomes:UP000000809};
RN   [1] {ECO:0000313|EMBL:AAK02199.1, ECO:0000313|Proteomes:UP000000809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70 {ECO:0000313|EMBL:AAK02199.1,
RC   ECO:0000313|Proteomes:UP000000809};
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-homoserine + H2O = 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:ARBA00049144};
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; AE004439; AAK02199.1; -; Genomic_DNA.
DR   RefSeq; WP_010906492.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPD2; -.
DR   STRING; 272843.PM0115; -.
DR   EnsemblBacteria; AAK02199; AAK02199; PM0115.
DR   KEGG; pmu:PM0115; -.
DR   PATRIC; fig|272843.6.peg.119; -.
DR   HOGENOM; CLU_015170_0_0_6; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.40.50.1100:FF:000026; Threonine synthase; 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; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR051166; Threonine_Synthase.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 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:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000809};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          10..78
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          87..371
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         105
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   424 AA;  46410 MW;  E2917665BC015CF5 CRC64;
     MNLYNIKHPE EQVNFAQAVR QGLGKNQGLF FPETLPHFED MDALLALPLV ERSQKILSAL
     IGEEISPTQL AKMVENAFTF PAPVAKVEEG VYALELFHGP TLAFKDFGGR FMAQALATVR
     GEGKITILTA TSGDTGAAVA HAFYGLENID VVILYPQGKI SPLQEKLFCT LGGNIRTIAI
     NGDFDDCQAL VKQAFDDAEL RQAIGLNSAN SINISRLLAQ VCYYFEAVAQ LPKAARDNLV
     VSVPSGNFGN LTAGLIAKSL GLPIKRFVAS TNVNDTVPRY LRSGNWQPHD TVATLSNAMD
     VSRPNNWPRV EELFKRNGWA LSDLHSDAVN DNETEQTLKD MYAKGYLCEP HGAVAYRVLK
     QDLQPGETGL FLCTAHPAKF KESVERILAL ELPLPDALAK HAALPLLSDI MENDFAKLRA
     YLLA
//