THRC_BACSU
ID THRC_BACSU Reviewed; 352 AA.
AC P04990;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC; OrderedLocusNames=BSU32250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=3098560; DOI=10.1002/j.1460-2075.1986.tb04600.x;
RA Parsot C.;
RT "Evolution of biosynthetic pathways: a common ancestor for threonine
RT synthase, threonine dehydratase and D-serine dehydratase.";
RL EMBO J. 5:3013-3019(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RC STRAIN=168;
RX PubMed=3139660; DOI=10.1016/s0021-9258(18)68087-1;
RA Parsot C., Cohen G.N.;
RT "Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding
RT for homoserine dehydrogenase. Structural and evolutionary relationships
RT with Escherichia coli aspartokinases-homoserine dehydrogenases I and II.";
RL J. Biol. Chem. 263:14654-14660(1988).
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}.
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DR EMBL; X04603; CAA28270.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15215.1; -; Genomic_DNA.
DR EMBL; M23217; AAA50610.1; -; Genomic_DNA.
DR PIR; A25364; A25364.
DR RefSeq; NP_391105.1; NC_000964.3.
DR RefSeq; WP_003228697.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P04990; -.
DR SMR; P04990; -.
DR IntAct; P04990; 1.
DR MINT; P04990; -.
DR STRING; 224308.BSU32250; -.
DR PaxDb; P04990; -.
DR PRIDE; P04990; -.
DR EnsemblBacteria; CAB15215; CAB15215; BSU_32250.
DR GeneID; 936660; -.
DR KEGG; bsu:BSU32250; -.
DR PATRIC; fig|224308.179.peg.3491; -.
DR eggNOG; COG0498; Bacteria.
DR InParanoid; P04990; -.
DR OMA; MWGFQAS; -.
DR PhylomeDB; P04990; -.
DR BioCyc; BSUB:BSU32250-MON; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
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; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..352
FT /note="Threonine synthase"
FT /id="PRO_0000185626"
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; 37464 MW; F478003AA330C6A0 CRC64;
MWKGLIHQYK EFLPVTDQTP ALTLHEGNTP LIHLPKLSEQ LGIELHVKTE GVNPTGSFKD
RGMVMAVAKA KEEGNDTIMC ASTGNTSAAA AAYAARANMK CIVIIPNGKI AFGKLAQAVM
YGAEIIAIDG NFDDALKIVR SICEKSPIAL VNSVNPYRIE GQKTAAFEVC EQLGEAPDVL
AIPVGNAGNI TAYWKGFKEY HEKNGTGLPK MRGFEAEGAA AIVRNEVIEN PETIATAIRI
GNPASWDKAV KAAEESNGKI DEVTDDEILH AYQLIARVEG VFAEPGSCAS IAGVLKQVKS
GEIPKGSKVV AVLTGNGLKD PNTAVDISEI KPVTLPTDED SILEYVKGAA RV
