Threonine synthase - Escherichia coli (strain K12)

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P00934 (THRC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Threonine synthase
Short name=TS
EC=4.2.3.1

Gene names

Name:	thrC
Ordered Locus Names:	b0004, JW0003

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=0.5 mM for O-phospho-L-homoserine Ref.8 V_max=9.3 µmol/min/mg enzyme

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	threonine biosynthetic process Inferred from mutant phenotype PubMed 4148765 PubMed 4364333. Source: EcoCyc
Molecular_function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threonine synthase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fusA	P0A6M8	1	EBI-1112675,EBI-370503

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 428

428

Threonine synthase

PRO_0000185631

Amino acid modifications

Modified residue

107

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

428

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00934 [UniParc].

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

428

47,114

        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' referencesShow '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 277:1453-1474(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.

PIR

SYECR. A01157.

RefSeq

NP_414545.1. NC_000913.2.
YP_488310.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VB3	X-ray	2.20	A	1-428	[»]

ProteinModelPortal

P00934.

SMR

P00934. Positions 1-428.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10993N.

IntAct

P00934. 1 interaction.

STRING

511145.b0004.

2D gel databases

SWISS-2DPAGE

P00934.

Proteomic databases

PaxDb

P00934.

PRIDE

P00934.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73115; AAC73115; b0004.
BAB96581; BAB96581; BAB96581.

GeneID

12932941.
945198.

KEGG

ecj:Y75_p0004.
eco:b0004.

PATRIC

32115103. VBIEscCol129921_0003.

Organism-specific databases

EchoBASE

EB0993.

EcoGene

EG11000. thrC.

Phylogenomic databases

eggNOG

COG0498.

HOGENOM

HOG000230743.

K01733.

OMA

MNLYNIK.

ProtClustDB

PRK09225.

Enzyme and pathway databases

BioCyc

EcoCyc:THRESYN-MONOMER.
ECOL316407:JW0003-MONOMER.
MetaCyc:THRESYN-MONOMER.

UniPathway

UPA00050; UER00065.

Gene expression databases

Genevestigator

P00934.

Family and domain databases

InterPro

IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

SUPFAM

SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.

TIGRFAMs

TIGR00260. thrC. 1 hit.

PROSITE

PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00934.

Entry information

Entry name

THRC_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents