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Q9K7E3 (THRC_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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:BH3421
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length354 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 – 354354Threonine synthase
PRO_0000185624

Regions

Region187 – 1915Pyridoxal phosphate binding By similarity

Sites

Binding site871Pyridoxal phosphate By similarity
Binding site3161Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue611N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K7E3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D25EABAB4952C691

FASTA35437,665
        10         20         30         40         50         60 
MSQWRGLLQE YKEFLPVTEE TPLLTLGEGN TPLIPLENLS KEWGVKAYVK YEGANPTGSF 

        70         80         90        100        110        120 
KDRGMVMAVA KAKEEGSRTI ICASTGNTSA AAAAYGARAG LRCIVVIPEG KIALGKLAQA 

       130        140        150        160        170        180 
VMYGAEVLEI KGNFDHALDI VRSISEKEPI TLVNSVNPYR IEGQKTSAFE ICDALGQAPD 

       190        200        210        220        230        240 
VLAIPVGNAG NITAYWKGFK EYHEKKGTGL PQMRGFEAEG AAAIVRNQVI EEPETIATAI 

       250        260        270        280        290        300 
RIGNPASWTY AVEAAAESNG KIDEVTDEEI LAAYQLLAQK EGVFAEPASC ASIAGLRKQI 

       310        320        330        340        350 
ASGEIKKGST VVCVLTGNGL KDPNTAMSTI DVNPAVLPND EQAFLDHIKG GVPK 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB07140.1.
PIRE84077.
RefSeqNP_244288.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K7E3.
SMRQ9K7E3. Positions 4-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH3421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB07140; BAB07140; BAB07140.
GeneID894384.
KEGGbha:BH3421.
PATRIC18944114. VBIBacHal18977_3555.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000076503.
KOK01733.
OMALAQAMFH.
OrthoDBEOG6HMX9M.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-3522-MONOMER.
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_BACHD
AccessionPrimary (citable) accession number: Q9K7E3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 81 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