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Database: UniProt
Entry: A0A089LQI2_9BACL
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ID   A0A089LQI2_9BACL        Unreviewed;       463 AA.
AC   A0A089LQI2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=PSTEL_03795 {ECO:0000313|EMBL:AIQ62355.1};
OS   Paenibacillus stellifer.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ62355.1, ECO:0000313|Proteomes:UP000029507};
RN   [1] {ECO:0000313|EMBL:AIQ62355.1, ECO:0000313|Proteomes:UP000029507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ62355.1,
RC   ECO:0000313|Proteomes:UP000029507};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009286; AIQ62355.1; -; Genomic_DNA.
DR   RefSeq; WP_038693537.1; NZ_CP009286.1.
DR   AlphaFoldDB; A0A089LQI2; -.
DR   STRING; 169760.PSTEL_03795; -.
DR   KEGG; pste:PSTEL_03795; -.
DR   HOGENOM; CLU_015170_1_0_9; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000029507; 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, ECO:0000313|EMBL:AIQ62355.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029507};
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          89..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   463 AA;  51154 MW;  BC0862557CD1AA89 CRC64;
     MQYISTRGKV EPRGFIDTVL MGLADDGGLM VPDVIPSVSS ATLEEWRNLS FQELFLKIFS
     YYTNGEIPDG DLKEMVERSY GTFRHPEVTP LKEINDSLYI LELFHGPTFA FKDVALQFMG
     ELYSYISRVR GEIIHILGAT SGDTGAAAIA GVRGKEGIKI CILHPHNKVS KVQELQMTTV
     DDANVLNLSV QGNFDDCQKV IKELFADLEF KSKYHLRAIN SINFVRILAQ TVYYFYAVLK
     LPQAAQGKTV NISVPSGNFG NIFSGYLAKK MGLPIGKLII ATNENNILER FVKTGEYKPG
     DFKSTHSPSM DIQVASNFER YLYYLTGEDS AAVNGYMSKL AGEGAIKVDG QLLEQVQTDF
     AALGVKNDEC LNIIGKYKSE AGYLLDPHTA CGVAAYEAHN GPGEVCITFA TAHPAKFDEA
     ISLLKIAQEF PPQIAGLAAL PQHMTVVEHD KAEITRQLEE FYI
//
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