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Reviewed, UniProtKB/Swiss-Prot Q5HS07 (THLA_STAEQ)

Last modified February 9, 2010. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable acetyl-CoA acyltransferase
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase
Gene names
Ordered Locus Names: SERP0032
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Probable acetyl-CoA acyltransferase
PRO_0000270509

Sites

Active site881Acyl-thioester intermediate By similarity
Active site3491Proton acceptor By similarity
Active site3781Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HS07-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: C95DCBE16F213195

FASTA39441,595
        10         20         30         40         50         60 
MSRIVLAEAY RTPIGVFGGV FKDIPAYELG ATVIRQILEH SQIDPNEINE VILGNVLQAG 

        70         80         90        100        110        120 
QGQNPARIAA IHGGVPEAVP SFTVNKVCGS GLKAIQLAYQ SIVAGDNEIV IAGGMESMSQ 

       130        140        150        160        170        180 
SPMLLKNSRF GFKMGNQTLE DSMIADGLTD KFNDYHMGIT AENLVEQYQI SRKEQDQFAF 

       190        200        210        220        230        240 
DSQQKASRAQ QAGVFDAEIV PVEVPQRKGD PLIISQDEGI RPQTTIDKLA QLRPAFKKDG 

       250        260        270        280        290        300 
SVTAGNASGI NDGAAAMLVM TEDKAKALGL QPIAVLDSFG ASGVAPSIMG IGPVEAIHKA 

       310        320        330        340        350        360 
LKRSNKVIND VDIFELNEAF AAQSIAVNRE LQLPQDKVNV NGGAIALGHP IGASGARTLV 

       370        380        390 
SLLHQLSDAK PTGVASLCIG GGQGIATVVS KYEV 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW53454.1.
RefSeqYP_187632.1.

3D structure databases

HSSPHSSP built from PDB template 1M3K based on UniProtKB P07097.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HS07.

Genome annotation databases

GeneID3242978.
GenomeReviewsGene locus SERP0032 in contig CP000029_GR.
KEGGser:SERP0032.
TIGRSERP0032.

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHBG370930.
OMADPATMGM.

Enzyme and pathway databases

BioCycSEPI176279:SERP0032-MONOMER.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHLA_STAEQ
AccessionPrimary (citable) accession number: Q5HS07
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: February 15, 2005
Last modified: February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents