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P00934

- THRC_ECOLI

UniProt

P00934 - THRC_ECOLI

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Protein

Threonine synthase

Gene
thrC, b0004, JW0003
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 phosphate.1 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

Vmax=9.3 µmol/min/mg enzyme

Pathwayi

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. threonine synthase activity Source: EcoCyc

GO - Biological processi

  1. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11000. thrC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Threonine synthasePRO_0000185631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

PaxDbiP00934.
PRIDEiP00934.

2D gel databases

SWISS-2DPAGEP00934.

Expressioni

Gene expression databases

GenevestigatoriP00934.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
fusAP0A6M81EBI-1112675,EBI-370503

Protein-protein interaction databases

DIPiDIP-10993N.
IntActiP00934. 2 interactions.
STRINGi511145.b0004.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi8 – 136
Helixi15 – 217
Helixi25 – 273
Beta strandi30 – 345
Helixi40 – 467
Helixi51 – 6313
Helixi64 – 663
Helixi69 – 7911
Beta strandi86 – 905
Beta strandi93 – 975
Helixi107 – 12115
Turni122 – 1243
Beta strandi127 – 1326
Beta strandi134 – 1363
Helixi137 – 1448
Turni145 – 1473
Beta strandi151 – 1588
Helixi164 – 1718
Beta strandi177 – 1848
Helixi186 – 19510
Helixi196 – 1983
Helixi200 – 2067
Helixi216 – 2216
Helixi224 – 2307
Turni235 – 2395
Beta strandi240 – 2467
Helixi251 – 26111
Beta strandi267 – 2737
Helixi278 – 2858
Helixi299 – 3013
Helixi309 – 31810
Helixi323 – 3253
Beta strandi326 – 3305
Helixi333 – 34513
Helixi352 – 36211
Beta strandi370 – 3756
Helixi379 – 3824
Helixi383 – 3908
Helixi398 – 4047
Beta strandi411 – 4155
Helixi417 – 4248

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VB3X-ray2.20A1-428[»]
ProteinModelPortaliP00934.
SMRiP00934. Positions 1-428.

Miscellaneous databases

EvolutionaryTraceiP00934.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0498.
HOGENOMiHOG000230743.
KOiK01733.
OMAiHGAIAYQ.
OrthoDBiEOG65BDJX.
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. Trp_syn_b_sub_like_PLP_eny_SF.
[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

MKLYNLKDHN EQVSFAQAVT QGLGKNQGLF FPHDLPEFSL TEIDEMLKLD    50
FVTRSAKILS AFIGDEIPQE ILEERVRAAF AFPAPVANVE SDVGCLELFH 100
GPTLAFKDFG GRFMAQMLTH IAGDKPVTIL TATSGDTGAA VAHAFYGLPN 150
VKVVILYPRG KISPLQEKLF CTLGGNIETV AIDGDFDACQ ALVKQAFDDE 200
ELKVALGLNS ANSINISRLL AQICYYFEAV AQLPQETRNQ LVVSVPSGNF 250
GDLTAGLLAK SLGLPVKRFI AATNVNDTVP RFLHDGQWSP KATQATLSNA 300
MDVSQPNNWP RVEELFRRKI WQLKELGYAA VDDETTQQTM RELKELGYTS 350
EPHAAVAYRA LRDQLNPGEY GLFLGTAHPA KFKESVEAIL GETLDLPKEL 400
AERADLPLLS HNLPADFAAL RKLMMNHQ 428
Length:428
Mass (Da):47,114
Last modified:July 21, 1986 - v1
Checksum:i5F7C20BE00B437E2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_488310.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73115; AAC73115; b0004.
BAB96581; BAB96581; BAB96581.
GeneIDi12932941.
945198.
KEGGiecj:Y75_p0004.
eco:b0004.
PATRICi32115103. VBIEscCol129921_0003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A01157. SYECR.
RefSeqi NP_414545.1. NC_000913.3.
YP_488310.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VB3 X-ray 2.20 A 1-428 [» ]
ProteinModelPortali P00934.
SMRi P00934. Positions 1-428.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10993N.
IntActi P00934. 2 interactions.
STRINGi 511145.b0004.

2D gel databases

SWISS-2DPAGE P00934.

Proteomic databases

PaxDbi P00934.
PRIDEi P00934.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73115 ; AAC73115 ; b0004 .
BAB96581 ; BAB96581 ; BAB96581 .
GeneIDi 12932941.
945198.
KEGGi ecj:Y75_p0004.
eco:b0004.
PATRICi 32115103. VBIEscCol129921_0003.

Organism-specific databases

EchoBASEi EB0993.
EcoGenei EG11000. thrC.

Phylogenomic databases

eggNOGi COG0498.
HOGENOMi HOG000230743.
KOi K01733.
OMAi HGAIAYQ.
OrthoDBi EOG65BDJX.
PhylomeDBi P00934.

Enzyme and pathway databases

UniPathwayi UPA00050 ; UER00065 .
BioCyci EcoCyc:THRESYN-MONOMER.
ECOL316407:JW0003-MONOMER.
MetaCyc:THRESYN-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00934.
PROi P00934.

Gene expression databases

Genevestigatori P00934.

Family and domain databases

Gene3Di 3.90.1380.10. 1 hit.
InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR00260. thrC. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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).

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: June 11, 2014
This is version 134 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

External Data

Dasty 3

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