ID   A0A2Z2KUT8_9BACL        Unreviewed;       462 AA.
AC   A0A2Z2KUT8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=B9T62_37485 {ECO:0000313|EMBL:ASA25912.1};
OS   Paenibacillus donghaensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=414771 {ECO:0000313|EMBL:ASA25912.1, ECO:0000313|Proteomes:UP000249890};
RN   [1] {ECO:0000313|EMBL:ASA25912.1, ECO:0000313|Proteomes:UP000249890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13049 {ECO:0000313|EMBL:ASA25912.1,
RC   ECO:0000313|Proteomes:UP000249890};
RA   Jung B.K., Hong S.-J., Shin J.-H.;
RT   "Complete genome sequence of Paenibacillus donghaensis KCTC 13049T isolated
RT   from East Sea sediment, South Korea.";
RL   Submitted (JUN-2017) 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; CP021780; ASA25912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2KUT8; -.
DR   KEGG; pdh:B9T62_37485; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000249890; 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; 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:UP000249890};
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          98..395
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   462 AA;  51107 MW;  877AAF4FBA3C38B7 CRC64;
     MKFISTRGNV EPKGFIDTVL MGLADDGGLM VPSEIPQVSA ATLAEWRTLS YQELFLKIVT
     LYTNDEIPYE DLKQMAYTSY GNFRAPEVTP LHKVSDSLHV LELFHGPTFA FKDVALQFMG
     ELYSYISKKR GEIIHILGAT SGDTGAAAIQ GVRGKEGIKI CILHPHGKVS KVQELQMTTV
     DDSNVLNLSV EGNFDDCQQV IKELFGDLDF KSRYHLRAIN SINFVRILAQ TVYYFYAYLQ
     IDGSADKQIN FSVPSGNFGN IFSGYLAKRM GLPIRKLMIA TNENNILERF VNTGEYKPGG
     FTSTYSPSMD IQVASNFERY LYYLVGEDSA KLSAYMSGLQ REGSITVSGA DLQRVQADFS
     ALGVKNAQCL ETITKYSGES GYLLDPHTAC GVAAYEALGG PDETTITFAT AHPAKFNEAI
     QLTGIGQEFP APIQALFEMP QHQTLVDYDK AEIVRQLQAF YG
//