THRC_CORGL
ID THRC_CORGL Reviewed; 481 AA.
AC P23669; Q59211;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC; OrderedLocusNames=Cgl2220, cg2437;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2127631; DOI=10.1111/j.1365-2958.1990.tb00546.x;
RA Han K.S., Archer J.A.C., Sinskey A.J.;
RT "The molecular structure of the Corynebacterium glutamicum threonine
RT synthase gene.";
RL Mol. Microbiol. 4:1693-1702(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=8074505; DOI=10.1128/aem.60.7.2209-2219.1994;
RA Malumbres M., Mateos L.M., Lumbreras M.A., Guerrero C., Martin J.F.;
RT "Analysis and expression of the thrC gene of Brevibacterium lactofermentum
RT and characterization of the encoded threonine synthase.";
RL Appl. Environ. Microbiol. 60:2209-2219(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. {ECO:0000269|PubMed:8074505}.
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:0000269|PubMed:8074505};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:8074505};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8074505}.
CC -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR EMBL; X56037; CAA39510.1; -; Genomic_DNA.
DR EMBL; Z29563; CAA82670.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99613.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20560.1; -; Genomic_DNA.
DR PIR; S11979; S11979.
DR RefSeq; NP_601423.1; NC_003450.3.
DR RefSeq; WP_011014964.1; NC_006958.1.
DR AlphaFoldDB; P23669; -.
DR SMR; P23669; -.
DR STRING; 196627.cg2437; -.
DR KEGG; cgb:cg2437; -.
DR KEGG; cgl:Cgl2220; -.
DR PATRIC; fig|196627.13.peg.2157; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_1_0_11; -.
DR OMA; FGRIAFQ; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000000582; 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 Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; -; 1.
DR InterPro; IPR001926; PLP-dep.
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; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00260; thrC; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..481
FT /note="Threonine synthase"
FT /id="PRO_0000185630"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="A -> R (in Ref. 1; CAA39510)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="R -> A (in Ref. 2; CAA82670)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="V -> S (in Ref. 2; CAA82670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52931 MW; BB9155C3317EE220 CRC64;
MDYISTRDAS RTPARFSDIL LGGLAPDGGL YLPATYPQLD DAQLSKWREV LANEGYAALA
AEVISLFVDD IPVEDIKAIT ARAYTYPKFN SEDIVPVTEL EDNIYLGHLS EGPTAAFKDM
AMQLLGELFE YELRRRNETI NILGATSGDT GSSAEYAMRG REGIRVFMLT PAGRMTPFQQ
AQMFGLDDPN IFNIALDGVF DDCQDVVKAV SADAEFKKDN RIGAVNSINW ARLMAQVVYY
VSSWIRTTTS NDQKVSFSVP TGNFGDICAG HIARQMGLPI DRLIVATNEN DVLDEFFRTG
DYRVRSSADT HETSSPSMDI SRASNFERFI FDLLGRDATR VNDLFGTQVR QGGFSLADDA
NFEKAAAEYG FASGRSTHAD RVATIADVHS RLDVLIDPHT ADGVHVARQW RDEVNTPIIV
LETALPVKFA DTIVEAIGEA PQTPERFAAI MDAPFKVSDL PNDTDAVKQY IVDAIANTSV
K
