THRC_BUCBP
ID THRC_BUCBP Reviewed; 430 AA.
AC Q89AR5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC; OrderedLocusNames=bbp_181;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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: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; AE016826; AAO26913.1; -; Genomic_DNA.
DR RefSeq; WP_011091314.1; NC_004545.1.
DR AlphaFoldDB; Q89AR5; -.
DR SMR; Q89AR5; -.
DR STRING; 224915.bbp_181; -.
DR EnsemblBacteria; AAO26913; AAO26913; bbp_181.
DR GeneID; 56470723; -.
DR KEGG; bab:bbp_181; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_0_0_6; -.
DR OMA; KGYLCEP; -.
DR OrthoDB; 428821at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000000601; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..430
FT /note="Threonine synthase"
FT /id="PRO_0000185629"
FT MOD_RES 108
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 430 AA; 48632 MW; 27FEEAFCFC7FB260 CRC64;
MKLYNLKKKQ DQVNFSKAVK LGLGKNQGLF FPKELPILTK EQLYKLLKMD FLTRSSKILS
MFIGDEIHYS ELTKRIKNAF SFTTPKIVSI SKNIACFELF HGPTLAFKDF GARFMAQILS
FLNHDKNDTI TILTATSGDT GAAVAHAFFK MKNVRVIILY PKGKISELQE KLFCTLGENI
ITIAVNGSFD ECQKLVKQAF NDDQLRIETG LNSANSINIS RLLAQICYYF EAFALLTKKQ
QKNLVISVPC GNFGNLTAGL LAKALGLPIK SFIASTNSND TVPRFLKTGF WKPNNTVSTI
SNAMDISQPN NWPRVEELFK RKFWSLKTLK YGSVSDILTK KSLKKLAFLG YVSEPHAAVA
YYTLKNKLKQ NEFGLFLGTA HPAKFKKTIE KILQITLFLP SKLRNQIKLP LLSHNIRPDF
SKLKKFLLEK
