THRC_BUCAI
ID THRC_BUCAI Reviewed; 429 AA.
AC P57289;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC; OrderedLocusNames=BU192;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12909.1; -; Genomic_DNA.
DR RefSeq; NP_240023.1; NC_002528.1.
DR RefSeq; WP_009874149.1; NC_002528.1.
DR AlphaFoldDB; P57289; -.
DR SMR; P57289; -.
DR STRING; 107806.10038874; -.
DR EnsemblBacteria; BAB12909; BAB12909; BAB12909.
DR KEGG; buc:BU192; -.
DR PATRIC; fig|107806.10.peg.203; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_0_0_6; -.
DR OMA; KGYLCEP; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000001806; 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..429
FT /note="Threonine synthase"
FT /id="PRO_0000185627"
FT MOD_RES 108
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 48660 MW; F66C73E6F5FAFFC6 CRC64;
MKLYNLKNHN EQVNFEAAVK LGLGQQQGLF FPVELPTITP IELSKILKMD FITRSTEILS
KFICHEISKE ELYKHVKQAF SFKHPLKIKI TKDIHCFELF HGPTLAFKDF GARFMAQMIL
LLNKKNESVT ILTATSGDTG AAVANAFYGM KNVRVIILYP KGKISELQEK LFCTLGRNIK
TISINGSFDD CQKLVKEAFN DKKLKESIGL NSANSINISR LLAQICYYFE AFSLISEEQR
KNLVIAVPCG NFGNLTAGLL SKSLGLPIKS FIACTNANDT VPRFLNNGTW NPKKTVSTIS
NAMDISQPNN WTRIEELFYR KKWDLKKLRF GSVSDHTTEE TLKELFKLGY VSEPHAAIAY
RLLRDQLKEN EFGLFLGTAH PAKFKNTVEK ILKNKISLPS ELQNRIDLPL LSHNINPVFS
KLKTFLLEK
