THRC_BACSL
ID THRC_BACSL Reviewed; 352 AA.
AC P09123;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC;
OS Bacillus sp. (strain ULM1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=231717;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3186450; DOI=10.1093/nar/16.20.9859;
RA Malumbres M., Mateos L.M., Guerrero C., Martin J.F.;
RT "Nucleotide sequence of the threonine synthase (thrC) gene of
RT Brevibacterium lactofermentum.";
RL Nucleic Acids Res. 16:9859-9859(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8768250; DOI=10.1007/bf02818515;
RA Malumbres M., Mateos L.M., Guerrero C., Martin J.F.;
RT "Molecular cloning of the hom-thrC-thrB cluster from Bacillus sp. ULM1:
RT expression of the thrC gene in Escherichia coli and corynebacteria, and
RT evolutionary relationships of the threonine genes.";
RL Folia Microbiol. (Praha) 40:595-606(1995).
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=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 -!- 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 -!- CAUTION: Was originally thought to originate from
CC B.lactofermentum=C.glutamicum. {ECO:0000305|PubMed:3186450}.
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DR EMBL; Z29562; CAA82669.1; -; Genomic_DNA.
DR AlphaFoldDB; P09123; -.
DR SMR; P09123; -.
DR UniPathway; UPA00050; UER00065.
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 Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR026260; Thr_Synthase_bac/arc.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF038945; Thr_synthase; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00260; thrC; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Lyase; Pyridoxal phosphate;
KW Threonine biosynthesis.
FT CHAIN 1..352
FT /note="Threonine synthase"
FT /id="PRO_0000185625"
FT BINDING 85
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 185..189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 352 AA; 37458 MW; 192550176FAD7930 CRC64;
MYKGLLKQYA SYLPVNEKTP DVSLMEGNTP LIPLLNISKQ LGVQLYGKYE GANPTGSFKD
RGMVMAVAKA KEEGSEAIIC ASTGNTSASA AAYAARLGMK CIIVIPEGKI AHGKLAQAVA
YGAEIISIEG NFDDALKAVR NIAAEEPITL VNSVNPYRIE GQKTAAFEIC DQLQNAPDVL
AIPVGNAGNI TAYWKGFCEY EKEKGYKKPR IHGFEAEGAA AIVKGHVIEE PETIATAIRI
GNPASWSYAV EAAEQSHGEI DMVSDEEILH AYRLLAKTEG VFAEPGSNAS LAGVIKHVES
GKIKKGETVV AVLTGNGLKD PDIAISSNQL DIASVSNDIE QIKDHIKGVI MS
