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P10551 (THIL_SACBA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 76. 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:
Acetyl-CoA acetyltransferase

EC=2.3.1.9
Alternative name(s):
Acetoacetyl-CoA thiolase
Ergosterol biosynthesis protein 10
Gene names
Name:ERG10
OrganismSaccharomyces bayanus (Yeast) (Saccharomyces uvarum)
Taxonomic identifier4931 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids By similarity.

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.

Subunit structure

Multimeric.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Potassium
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 398397Acetyl-CoA acetyltransferase
PRO_0000206417

Sites

Active site911Acyl-thioester intermediate By similarity
Active site3541Proton acceptor By similarity
Active site3841Proton acceptor By similarity
Metal binding1861Potassium By similarity
Metal binding2481Potassium; via carbonyl oxygen By similarity
Metal binding2491Potassium; via carbonyl oxygen By similarity
Metal binding2511Potassium; via carbonyl oxygen By similarity
Metal binding3501Potassium; via carbonyl oxygen By similarity
Binding site1861Coenzyme A By similarity
Binding site2311Coenzyme A By similarity
Binding site2521Coenzyme A By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P10551 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: C0AC394C17A925AB

FASTA39841,659
        10         20         30         40         50         60 
MSQNVYIVST ARTPIGSFQG SLSSKTAVEL GAAALKGALA KVPELDASKD FDEIIFGNVL 

        70         80         90        100        110        120 
SANLGQAPAR QVALTAGLGN HIVATTVNKV CASAMKAIIL GAQSIKCGNA DVVVAGGCES 

       130        140        150        160        170        180 
MTNAPYYMPA ARGGAKFGQT VLIDGVERDG LNDAYDGLAM GVHAEKCARD WDITRDQQDS 

       190        200        210        220        230        240 
FAIESYQKSQ QSQKEGKFDN EIVPVTIKGF RGKPDTQVTN DEEPARLHVE KLKSARTVFQ 

       250        260        270        280        290        300 
RENGTVTAAN ASPINDGAAA IILVSERVLK EKNLKPLAIV KGWGEAAHLP ADFTWAPSLA 

       310        320        330        340        350        360 
VPKALKHAGI EDINSVDYFE FNEAFSVVGL VNTKILKLDP SKVNVYGGAV ALGHPLGCSG 

       370        380        390 
ARVVVTLLSI LQQEGGKIGV AAICNGGGGA SSVVIEKL 

« Hide

References

[1]"Cloning, sequencing and analysis of the yeast S. uvarum ERG10 gene encoding acetoacetyl CoA thiolase."
Dequin S., Gloeckler R., Herbert C.J., Boutelet B.
Curr. Genet. 13:471-478(1988) [PubMed: 2900076] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07976 Genomic DNA. Translation: CAA30788.1.

3D structure databases

ProteinModelPortalP10551.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 4 hits.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
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 nameTHIL_SACBA
AccessionPrimary (citable) accession number: P10551
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 21, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families