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P09123 (THRC_BACSL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismBacillus sp. (strain ULM1)
Taxonomic identifier231717 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

Sequence similarities

Belongs to the threonine synthase family.

Caution

Was originally (Ref.1) thought to originate from B.lactofermentum=C.glutamicum.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionLyase
Gene Ontology (GO)
   Biological_processthreonine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

threonine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Threonine synthase
PRO_0000185625

Regions

Region185 – 1895Pyridoxal phosphate binding By similarity

Sites

Binding site851Pyridoxal phosphate By similarity
Binding site3141Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue591N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P09123 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 192550176FAD7930

FASTA35237,458
        10         20         30         40         50         60 
MYKGLLKQYA SYLPVNEKTP DVSLMEGNTP LIPLLNISKQ LGVQLYGKYE GANPTGSFKD 

        70         80         90        100        110        120 
RGMVMAVAKA KEEGSEAIIC ASTGNTSASA AAYAARLGMK CIIVIPEGKI AHGKLAQAVA 

       130        140        150        160        170        180 
YGAEIISIEG NFDDALKAVR NIAAEEPITL VNSVNPYRIE GQKTAAFEIC DQLQNAPDVL 

       190        200        210        220        230        240 
AIPVGNAGNI TAYWKGFCEY EKEKGYKKPR IHGFEAEGAA AIVKGHVIEE PETIATAIRI 

       250        260        270        280        290        300 
GNPASWSYAV EAAEQSHGEI DMVSDEEILH AYRLLAKTEG VFAEPGSNAS LAGVIKHVES 

       310        320        330        340        350 
GKIKKGETVV AVLTGNGLKD PDIAISSNQL DIASVSNDIE QIKDHIKGVI MS 

« Hide

References

[1]"Nucleotide sequence of the threonine synthase (thrC) gene of Brevibacterium lactofermentum."
Malumbres M., Mateos L.M., Guerrero C., Martin J.F.
Nucleic Acids Res. 16:9859-9859(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular cloning of the hom-thrC-thrB cluster from Bacillus sp. ULM1: expression of the thrC gene in Escherichia coli and corynebacteria, and evolutionary relationships of the threonine genes."
Malumbres M., Mateos L.M., Guerrero C., Martin J.F.
Folia Microbiol. (Praha) 40:595-606(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29562 Genomic DNA. Translation: CAA82669.1.

3D structure databases

ProteinModelPortalP09123.
SMRP09123. Positions 2-325.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00050; UER00065.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_Gram_pos_bac.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
PIRSFPIRSF038945. Thr_synthase. 1 hit.
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHRC_BACSL
AccessionPrimary (citable) accession number: P09123
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 16, 2013
This is version 73 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

PATHWAY comments

Index of metabolic and biosynthesis pathways