THRC_ECOLI
ID THRC_ECOLI Reviewed; 428 AA.
AC P00934; Q6LEK8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=thrC; OrderedLocusNames=b0004, JW0003;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6316258; DOI=10.1093/nar/11.21.7331;
RA Parsot C., Cossart P., Saint-Girons I., Cohen G.N.;
RT "Nucleotide sequence of thrC and of the transcription termination region of
RT the threonine operon in Escherichia coli K12.";
RL Nucleic Acids Res. 11:7331-7345(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, AND KINETIC PARAMETERS.
RX PubMed=7907888; DOI=10.1021/bi00177a035;
RA Laber B., Gerbling K.P., Harde C., Neff K.H., Nordhoff E., Pohlenz H.D.;
RT "Mechanisms of interaction of Escherichia coli threonine synthase with
RT substrates and inhibitors.";
RL Biochemistry 33:3413-3423(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RA Omi R., Goto M., Miyahara I., Mizuguchi H., Hayashi H., Kagamiyama H.,
RA Hirotsu K.;
RT "Crystal structure of threonine synthase from Escherichia coli.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. To a lesser extent, is able to slowly catalyze the
CC deamination of L-threonine into alpha-ketobutyrate and that of L-serine
CC and 3-chloroalanine into pyruvate. Is also able to rapidly convert
CC vinylglycine to threonine, which proves that the pyridoxal p-quinonoid
CC of vinylglycine is an intermediate in the TS reaction.
CC {ECO:0000269|PubMed:7907888}.
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:7907888};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:7907888};
CC -!- ACTIVITY REGULATION: Is competitively inhibited by L-threo-3-
CC hydroxyhomoserine phosphate. {ECO:0000269|PubMed:7907888}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for O-phospho-L-homoserine {ECO:0000269|PubMed:7907888};
CC Vmax=9.3 umol/min/mg enzyme {ECO:0000269|PubMed:7907888};
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; U14003; AAA97303.1; -; Genomic_DNA.
DR EMBL; J01706; AAA83916.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73115.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96581.1; -; Genomic_DNA.
DR PIR; A01157; SYECR.
DR RefSeq; NP_414545.1; NC_000913.3.
DR RefSeq; WP_000781074.1; NZ_LN832404.1.
DR PDB; 1VB3; X-ray; 2.20 A; A=1-428.
DR PDBsum; 1VB3; -.
DR AlphaFoldDB; P00934; -.
DR SMR; P00934; -.
DR BioGRID; 4261935; 247.
DR BioGRID; 849584; 1.
DR DIP; DIP-10993N; -.
DR IntAct; P00934; 4.
DR STRING; 511145.b0004; -.
DR SWISS-2DPAGE; P00934; -.
DR jPOST; P00934; -.
DR PaxDb; P00934; -.
DR PRIDE; P00934; -.
DR EnsemblBacteria; AAC73115; AAC73115; b0004.
DR EnsemblBacteria; BAB96581; BAB96581; BAB96581.
DR GeneID; 945198; -.
DR KEGG; ecj:JW0003; -.
DR KEGG; eco:b0004; -.
DR PATRIC; fig|1411691.4.peg.2279; -.
DR EchoBASE; EB0993; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_0_0_6; -.
DR InParanoid; P00934; -.
DR OMA; KGYLCEP; -.
DR PhylomeDB; P00934; -.
DR BioCyc; EcoCyc:THRESYN-MON; -.
DR BioCyc; MetaCyc:THRESYN-MON; -.
DR BRENDA; 4.2.3.1; 2026.
DR SABIO-RK; P00934; -.
DR UniPathway; UPA00050; UER00065.
DR EvolutionaryTrace; P00934; -.
DR PRO; PR:P00934; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IDA:EcoCyc.
DR GO; GO:0009088; P:threonine biosynthetic process; IMP:EcoCyc.
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 3D-structure; Amino-acid biosynthesis; Direct protein sequencing; Lyase;
KW Pyridoxal phosphate; Reference proteome; Threonine biosynthesis.
FT CHAIN 1..428
FT /note="Threonine synthase"
FT /id="PRO_0000185631"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:1VB3"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:1VB3"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:1VB3"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:1VB3"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:1VB3"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:1VB3"
SQ SEQUENCE 428 AA; 47114 MW; 5F7C20BE00B437E2 CRC64;
MKLYNLKDHN EQVSFAQAVT QGLGKNQGLF FPHDLPEFSL TEIDEMLKLD FVTRSAKILS
AFIGDEIPQE ILEERVRAAF AFPAPVANVE SDVGCLELFH GPTLAFKDFG GRFMAQMLTH
IAGDKPVTIL TATSGDTGAA VAHAFYGLPN VKVVILYPRG KISPLQEKLF CTLGGNIETV
AIDGDFDACQ ALVKQAFDDE ELKVALGLNS ANSINISRLL AQICYYFEAV AQLPQETRNQ
LVVSVPSGNF GDLTAGLLAK SLGLPVKRFI AATNVNDTVP RFLHDGQWSP KATQATLSNA
MDVSQPNNWP RVEELFRRKI WQLKELGYAA VDDETTQQTM RELKELGYTS EPHAAVAYRA
LRDQLNPGEY GLFLGTAHPA KFKESVEAIL GETLDLPKEL AERADLPLLS HNLPADFAAL
RKLMMNHQ
