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P00934 (THRC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine synthase

Short name=TS
EC=4.2.3.1
Gene names
Name:thrC
Ordered Locus Names:b0004, JW0003
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction. Ref.8

Catalytic activity

O-phospho-L-homoserine + H2O = L-threonine + phosphate. Ref.8

Cofactor

Pyridoxal phosphate. Ref.8

Enzyme regulation

Is competitively inhibited by L-threo-3-hydroxyhomoserine phosphate. Ref.8

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.

Sequence similarities

Belongs to the threonine synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.5 mM for O-phospho-L-homoserine Ref.8

Vmax=9.3 µmol/min/mg enzyme

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fusAP0A6M81EBI-1112675,EBI-370503

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Threonine synthase
PRO_0000185631

Amino acid modifications

Modified residue1071N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

............................................................................. 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00934 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5F7C20BE00B437E2

FASTA42847,114
        10         20         30         40         50         60 
MKLYNLKDHN EQVSFAQAVT QGLGKNQGLF FPHDLPEFSL TEIDEMLKLD FVTRSAKILS 

        70         80         90        100        110        120 
AFIGDEIPQE ILEERVRAAF AFPAPVANVE SDVGCLELFH GPTLAFKDFG GRFMAQMLTH 

       130        140        150        160        170        180 
IAGDKPVTIL TATSGDTGAA VAHAFYGLPN VKVVILYPRG KISPLQEKLF CTLGGNIETV 

       190        200        210        220        230        240 
AIDGDFDACQ ALVKQAFDDE ELKVALGLNS ANSINISRLL AQICYYFEAV AQLPQETRNQ 

       250        260        270        280        290        300 
LVVSVPSGNF GDLTAGLLAK SLGLPVKRFI AATNVNDTVP RFLHDGQWSP KATQATLSNA 

       310        320        330        340        350        360 
MDVSQPNNWP RVEELFRRKI WQLKELGYAA VDDETTQQTM RELKELGYTS EPHAAVAYRA 

       370        380        390        400        410        420 
LRDQLNPGEY GLFLGTAHPA KFKESVEAIL GETLDLPKEL AERADLPLLS HNLPADFAAL 


RKLMMNHQ 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of thrC and of the transcription termination region of the threonine operon in Escherichia coli K12."
Parsot C., Cossart P., Saint-Girons I., Cohen G.N.
Nucleic Acids Res. 11:7331-7345(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[3]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[7]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-4.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors."
Laber B., Gerbling K.P., Harde C., Neff K.H., Nordhoff E., Pohlenz H.D.
Biochemistry 33:3413-3423(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, KINETIC PARAMETERS.
[9]"Crystal structure of threonine synthase from Escherichia coli."
Omi R., Goto M., Miyahara I., Mizuguchi H., Hayashi H., Kagamiyama H., Hirotsu K.
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14003 Genomic DNA. Translation: AAA97303.1.
J01706 Genomic DNA. Translation: AAA83916.1.
U00096 Genomic DNA. Translation: AAC73115.1.
AP009048 Genomic DNA. Translation: BAB96581.1.
PIRSYECR. A01157.
RefSeqNP_414545.1. NC_000913.3.
YP_488310.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VB3X-ray2.20A1-428[»]
ProteinModelPortalP00934.
SMRP00934. Positions 1-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10993N.
IntActP00934. 2 interactions.
STRING511145.b0004.

2D gel databases

SWISS-2DPAGEP00934.

Proteomic databases

PaxDbP00934.
PRIDEP00934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73115; AAC73115; b0004.
BAB96581; BAB96581; BAB96581.
GeneID12932941.
945198.
KEGGecj:Y75_p0004.
eco:b0004.
PATRIC32115103. VBIEscCol129921_0003.

Organism-specific databases

EchoBASEEB0993.
EcoGeneEG11000. thrC.

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000230743.
KOK01733.
OMALAFKDYG.
OrthoDBEOG65BDJX.
PhylomeDBP00934.
ProtClustDBPRK09225.

Enzyme and pathway databases

BioCycEcoCyc:THRESYN-MONOMER.
ECOL316407:JW0003-MONOMER.
MetaCyc:THRESYN-MONOMER.
UniPathwayUPA00050; UER00065.

Gene expression databases

GenevestigatorP00934.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00934.
PROP00934.

Entry information

Entry nameTHRC_ECOLI
AccessionPrimary (citable) accession number: P00934
Secondary accession number(s): Q6LEK8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene