ID   THRC_PSEAE              Reviewed;         469 AA.
AC   P29363; Q9HXQ7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 3.
DT   10-JUN-2026, entry version 148.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=PA3735;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=1333566; DOI=10.1111/j.1365-2958.1992.tb01768.x;
RA   Clepet C., Borne F., Krishnapillai V., Baird C., Patte J.-C., Cami B.;
RT   "Isolation, organization and expression of the Pseudomonas aeruginosa
RT   threonine genes.";
RL   Mol. Microbiol. 6:3109-3119(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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=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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA46168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X65033; CAA46168.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE004091; AAG07122.1; -; Genomic_DNA.
DR   PIR; G83179; G83179.
DR   PIR; S27980; SYPSRA.
DR   RefSeq; NP_252424.1; NC_002516.2.
DR   RefSeq; WP_003113831.1; NC_002516.2.
DR   AlphaFoldDB; P29363; -.
DR   SMR; P29363; -.
DR   FunCoup; P29363; 498.
DR   STRING; 208964.PA3735; -.
DR   PaxDb; 208964-PA3735; -.
DR   GeneID; 880336; -.
DR   KEGG; pae:PA3735; -.
DR   PATRIC; fig|208964.12.peg.3907; -.
DR   PseudoCAP; PA3735; -.
DR   HOGENOM; CLU_015170_1_0_6; -.
DR   InParanoid; P29363; -.
DR   OrthoDB; 9763107at2; -.
DR   PhylomeDB; P29363; -.
DR   BioCyc; PAER208964:G1FZ6-3806-MONOMER; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000002438; 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:L-threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01560; Thr-synth_2; 1.
DR   FunFam; 3.40.50.1100:FF:000052; Threonine synthase; 1.
DR   FunFam; 3.90.1380.10:FF:000002; 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; PF24857; THR4_C; 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; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Threonine biosynthesis.
FT   CHAIN           1..469
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185639"
FT   MOD_RES         112
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        88..101
FT                   /note="VAPLRQLNGNEWVL -> SGAAAPVERRTNGCV (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151..155
FT                   /note="GCRRC -> AAAVA (in Ref. 1; CAA46168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163..164
FT                   /note="MH -> ID (in Ref. 1; CAA46168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="Q -> E (in Ref. 1; CAA46168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="L -> H (in Ref. 1; CAA46168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="T -> R (in Ref. 1; CAA46168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294..304
FT                   /note="RYDKDTLHPSL -> ASTRHTLTPSV (in Ref. 1; CAA46168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465
FT                   /note="R -> P (in Ref. 1; CAA46168)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  51795 MW;  224032B86272C79C CRC64;
     MRYISTRGQA PALNFEDVLL AGLASDGGLY VPENLPRFTL EEIASWVGLP YHELAFRVMR
     PFVAGSIADA DFKKILEETY GVFAHDAVAP LRQLNGNEWV LELFHGPTLA FKDFALQLLG
     RLLDHVLAKR GERVVIMGAT SGDTGSAAIE GCRRCDNVDI FIMHPHNRVS EVQRRQMTTI
     LGDNIHNIAI EGNFDDCQEM VKASFADQGF LKGTRLVAVN SINWARIMAQ IVYYFHAALQ
     LGAPHRSVAF SVPTGNFGDI FAGYLARNMG LPVSQLIVAT NRNDILHRFM SGNRYDKDTL
     HPSLSPSMDI MVSSNFERLL FDLHGRNGKA VAELLDAFKA SGKLSVEDQR WTEARKLFDS
     LAVSDEQTCE TIAEVYRSSG ELLDPHTAIG VRAARECRRS LSVPMVTLGT AHPVKFPEAV
     EKAGIGQAPA LPAHLADLFE REERCTVLPN ELAKVQAFVS QHGNRGKPL
//