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Protein

Threonine synthase

Gene

thrC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

O-phospho-L-homoserine + H2O = L-threonine + phosphate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Is competitively inhibited by L-threo-3-hydroxyhomoserine phosphate.1 Publication

Kineticsi

  1. KM=0.5 mM for O-phospho-L-homoserine1 Publication
  1. Vmax=9.3 µmol/min/mg enzyme1 Publication

Pathwayi: L-threonine biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-threonine from L-aspartate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  4. Homoserine kinase (thrB)
  5. Threonine synthase (thrC)
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • pyridoxal phosphate binding Source: GO_Central
  • threonine synthase activity Source: EcoCyc

GO - Biological processi

  • threonine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:THRESYN-MONOMER.
ECOL316407:JW0003-MONOMER.
MetaCyc:THRESYN-MONOMER.
UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase (EC:4.2.3.1)
Short name:
TS
Gene namesi
Name:thrC
Ordered Locus Names:b0004, JW0003
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11000. thrC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001856311 – 428Threonine synthaseAdd BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei107N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

EPDiP00934.
PaxDbiP00934.
PRIDEiP00934.

2D gel databases

SWISS-2DPAGEP00934.

Interactioni

Protein-protein interaction databases

BioGridi4261935. 235 interactors.
DIPiDIP-10993N.
IntActiP00934. 2 interactors.
STRINGi511145.b0004.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi8 – 13Combined sources6
Helixi15 – 21Combined sources7
Helixi25 – 27Combined sources3
Beta strandi30 – 34Combined sources5
Helixi40 – 46Combined sources7
Helixi51 – 63Combined sources13
Helixi64 – 66Combined sources3
Helixi69 – 79Combined sources11
Beta strandi86 – 90Combined sources5
Beta strandi93 – 97Combined sources5
Helixi107 – 121Combined sources15
Turni122 – 124Combined sources3
Beta strandi127 – 132Combined sources6
Beta strandi134 – 136Combined sources3
Helixi137 – 144Combined sources8
Turni145 – 147Combined sources3
Beta strandi151 – 158Combined sources8
Helixi164 – 171Combined sources8
Beta strandi177 – 184Combined sources8
Helixi186 – 195Combined sources10
Helixi196 – 198Combined sources3
Helixi200 – 206Combined sources7
Helixi216 – 221Combined sources6
Helixi224 – 230Combined sources7
Turni235 – 239Combined sources5
Beta strandi240 – 246Combined sources7
Helixi251 – 261Combined sources11
Beta strandi267 – 273Combined sources7
Helixi278 – 285Combined sources8
Helixi299 – 301Combined sources3
Helixi309 – 318Combined sources10
Helixi323 – 325Combined sources3
Beta strandi326 – 330Combined sources5
Helixi333 – 345Combined sources13
Helixi352 – 362Combined sources11
Beta strandi370 – 375Combined sources6
Helixi379 – 382Combined sources4
Helixi383 – 390Combined sources8
Helixi398 – 404Combined sources7
Beta strandi411 – 415Combined sources5
Helixi417 – 424Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VB3X-ray2.20A1-428[»]
ProteinModelPortaliP00934.
SMRiP00934.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00934.

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105D98. Bacteria.
COG0498. LUCA.
HOGENOMiHOG000230743.
InParanoidiP00934.
KOiK01733.
OMAiLAFKDYG.
PhylomeDBiP00934.

Family and domain databases

Gene3Di3.90.1380.10. 1 hit.
InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00934-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLYNLKDHN EQVSFAQAVT QGLGKNQGLF FPHDLPEFSL TEIDEMLKLD
60 70 80 90 100
FVTRSAKILS AFIGDEIPQE ILEERVRAAF AFPAPVANVE SDVGCLELFH
110 120 130 140 150
GPTLAFKDFG GRFMAQMLTH IAGDKPVTIL TATSGDTGAA VAHAFYGLPN
160 170 180 190 200
VKVVILYPRG KISPLQEKLF CTLGGNIETV AIDGDFDACQ ALVKQAFDDE
210 220 230 240 250
ELKVALGLNS ANSINISRLL AQICYYFEAV AQLPQETRNQ LVVSVPSGNF
260 270 280 290 300
GDLTAGLLAK SLGLPVKRFI AATNVNDTVP RFLHDGQWSP KATQATLSNA
310 320 330 340 350
MDVSQPNNWP RVEELFRRKI WQLKELGYAA VDDETTQQTM RELKELGYTS
360 370 380 390 400
EPHAAVAYRA LRDQLNPGEY GLFLGTAHPA KFKESVEAIL GETLDLPKEL
410 420
AERADLPLLS HNLPADFAAL RKLMMNHQ
Length:428
Mass (Da):47,114
Last modified:July 21, 1986 - v1
Checksum:i5F7C20BE00B437E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97303.1.
J01706 Genomic DNA. Translation: AAA83916.1.
U00096 Genomic DNA. Translation: AAC73115.1.
AP009048 Genomic DNA. Translation: BAB96581.1.
PIRiA01157. SYECR.
RefSeqiNP_414545.1. NC_000913.3.
WP_000781074.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73115; AAC73115; b0004.
BAB96581; BAB96581; BAB96581.
GeneIDi945198.
KEGGiecj:JW0003.
eco:b0004.
PATRICi32115103. VBIEscCol129921_0003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97303.1.
J01706 Genomic DNA. Translation: AAA83916.1.
U00096 Genomic DNA. Translation: AAC73115.1.
AP009048 Genomic DNA. Translation: BAB96581.1.
PIRiA01157. SYECR.
RefSeqiNP_414545.1. NC_000913.3.
WP_000781074.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VB3X-ray2.20A1-428[»]
ProteinModelPortaliP00934.
SMRiP00934.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261935. 235 interactors.
DIPiDIP-10993N.
IntActiP00934. 2 interactors.
STRINGi511145.b0004.

2D gel databases

SWISS-2DPAGEP00934.

Proteomic databases

EPDiP00934.
PaxDbiP00934.
PRIDEiP00934.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73115; AAC73115; b0004.
BAB96581; BAB96581; BAB96581.
GeneIDi945198.
KEGGiecj:JW0003.
eco:b0004.
PATRICi32115103. VBIEscCol129921_0003.

Organism-specific databases

EchoBASEiEB0993.
EcoGeneiEG11000. thrC.

Phylogenomic databases

eggNOGiENOG4105D98. Bacteria.
COG0498. LUCA.
HOGENOMiHOG000230743.
InParanoidiP00934.
KOiK01733.
OMAiLAFKDYG.
PhylomeDBiP00934.

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.
BioCyciEcoCyc:THRESYN-MONOMER.
ECOL316407:JW0003-MONOMER.
MetaCyc:THRESYN-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00934.
PROiP00934.

Family and domain databases

Gene3Di3.90.1380.10. 1 hit.
InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHRC_ECOLI
AccessioniPrimary (citable) accession number: P00934
Secondary accession number(s): Q6LEK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.