ID   A0A1H2GJ31_9PSED        Unreviewed;       469 AA.
AC   A0A1H2GJ31;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=SAMN05216296_2335 {ECO:0000313|EMBL:SDU19595.1};
OS   Pseudomonas pohangensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=364197 {ECO:0000313|EMBL:SDU19595.1, ECO:0000313|Proteomes:UP000243232};
RN   [1] {ECO:0000313|Proteomes:UP000243232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17875 {ECO:0000313|Proteomes:UP000243232};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; LT629785; SDU19595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2GJ31; -.
DR   STRING; 364197.SAMN05216296_2335; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000243232; Chromosome i.
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; IPR029144; Thr_synth_N.
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; 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:UP000243232};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          2..80
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          93..399
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         112
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   469 AA;  51896 MW;  224A433220BC30D8 CRC64;
     MRYISTRGQA PALNFEDVLL AGLASDGGLY VPENLPRFTQ EEIASWAGLP YHELAFRVMR
     PFVAGSIADA DFKQILEETY AVFEHSAVAP LRQLHGNEWV LELFHGPTLA FKDFALQLLG
     RLLDHILARR NERVVIMGAT SGDTGSAAIE GCKACDNVDI FIMHPHNRVS EVQRRQMTTI
     FGDNIHNIAI EGNFDDCQEM VKASFADQSF LKGTRLVAVN SINWARIMAQ IVYYFYAALQ
     LGGPARSIAF SVPTGNFGDI FAGYLARNMG LPISQLIVAT NRNDILHRFM SGNRYDKDTL
     HPSLSPSMDI MVSSNFERLL FDLHGRNGLA LSGLMDNFKA SGKLSVSEER WTEARKLFDS
     LAVDDAQTCA TIAEVYQECG ELLDPHTAIG VRAARECRRS LATPMVILGT AHPVKFPEAV
     EKAGISRALA LPAHLADLFQ RDERCTVLAN DLQTVQQFVS QHGNRGKPL
//