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Q89AR5 (THRC_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. 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
Ordered Locus Names:bbp_181
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length430 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 – 430430Threonine synthase
PRO_0000185629

Amino acid modifications

Modified residue1081N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89AR5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 27FEEAFCFC7FB260

FASTA43048,632
        10         20         30         40         50         60 
MKLYNLKKKQ DQVNFSKAVK LGLGKNQGLF FPKELPILTK EQLYKLLKMD FLTRSSKILS 

        70         80         90        100        110        120 
MFIGDEIHYS ELTKRIKNAF SFTTPKIVSI SKNIACFELF HGPTLAFKDF GARFMAQILS 

       130        140        150        160        170        180 
FLNHDKNDTI TILTATSGDT GAAVAHAFFK MKNVRVIILY PKGKISELQE KLFCTLGENI 

       190        200        210        220        230        240 
ITIAVNGSFD ECQKLVKQAF NDDQLRIETG LNSANSINIS RLLAQICYYF EAFALLTKKQ 

       250        260        270        280        290        300 
QKNLVISVPC GNFGNLTAGL LAKALGLPIK SFIASTNSND TVPRFLKTGF WKPNNTVSTI 

       310        320        330        340        350        360 
SNAMDISQPN NWPRVEELFK RKFWSLKTLK YGSVSDILTK KSLKKLAFLG YVSEPHAAVA 

       370        380        390        400        410        420 
YYTLKNKLKQ NEFGLFLGTA HPAKFKKTIE KILQITLFLP SKLRNQIKLP LLSHNIRPDF 

       430 
SKLKKFLLEK 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26913.1.
RefSeqNP_777808.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AR5.
SMRQ89AR5. Positions 1-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp181.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26913; AAO26913; bbp_181.
GeneID1058160.
KEGGbab:bbp181.
PATRIC21245137. VBIBucAph80364_0175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0498.
KOK01733.
OMASDTANFA.
OrthoDBEOG65BDJX.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-181-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_BUCBP
AccessionPrimary (citable) accession number: Q89AR5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2003
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