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Q8K9V1 (THRC_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:BUsg_186
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length429 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.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
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 – 429429Threonine synthase
PRO_0000185628

Amino acid modifications

Modified residue1081N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9V1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 36AAB233D3C47BE6

FASTA42948,585
        10         20         30         40         50         60 
MKLYNLKNHN EQVNFETAVK LGLGQKQGLF FPVKLPIMTP VELSKILKMD FITRSTEILS 

        70         80         90        100        110        120 
KFISSEISKE VLHEHVKKAF SFSKPLKICI NKNISCFELF HGPTLAFKDF GARFMAQMIL 

       130        140        150        160        170        180 
CLNKKNESFT ILTATSGDTG AAVAHAFYGM KNIRVIILYP KGKITLLQEQ LFCTLGKNIK 

       190        200        210        220        230        240 
TISINGSFDD CQKLVKKAFD DKKLKESIGL NSANSINISR LLAQICYYFE AFSLISEEKR 

       250        260        270        280        290        300 
KNLVIAVPCG NFGNLTAGLL AKSLGLPIQS FIACTNSNDT VPRFLNSGKW NPKKTVSTIS 

       310        320        330        340        350        360 
NAMDISCPNN WPRIEELFRR KKWDLKELRF GSVSDNVTKE TLKELFRMGY VSEPHAAIAY 

       370        380        390        400        410        420 
RLLHDQLKKE EFGLFLGTAH PSKFKDTVEK ILENSISLPK ELKNRNNLPL LSHNINPDFN 


KLKEFLLEK 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67751.1.
RefSeqNP_660540.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9V1.
SMRQ8K9V1. Positions 1-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg186.

Proteomic databases

PRIDEQ8K9V1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67751; AAM67751; BUsg_186.
GeneID1005383.
KEGGbas:BUsg186.
PATRIC21247155. VBIBucAph100086_0191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0498.
KOK01733.
OMACAINAVE.
OrthoDBEOG65BDJX.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-196-MONOMER.
UniPathwayUPA00050; UER00065.

Family and domain databases

Gene3D3.90.1380.10. 1 hit.
InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHRC_BUCAP
AccessionPrimary (citable) accession number: Q8K9V1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 71 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names