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P54810 (THIL_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 57. 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
Gene names
Name:phaA
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processPHB biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processpoly-hydroxybutyrate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 391391Acetyl-CoA acetyltransferase
PRO_0000206460

Sites

Active site881Acyl-thioester intermediate By similarity
Active site3471Proton acceptor By similarity
Active site3771Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
P54810 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A6278FD632EC697B

FASTA39140,745
        10         20         30         40         50         60 
MTKAVIVSAA RTPVGSFLGS FANLPAHELG AIVLKAVVER AGIDPSEVSE TILGQVLTAA 

        70         80         90        100        110        120 
QGQNPARQAH IKVGLPRESA AWVINQVCGS GLRTVALAAQ QVLLGDARIV VAGGQESMSL 

       130        140        150        160        170        180 
APHAAYIAPG QKMGDMKMLD TMIKDGLWDA FNDYHMGTTA ENVAGKWEIS RAEQDQFAVA 

       190        200        210        220        230        240 
SQNKAEAAQK AGKFADEIVP VTIKSRKGET VVDADEYIRH GATLEAMENV RPAFSKEGTV 

       250        260        270        280        290        300 
TAGNASGLND GAAAVLVMTE DEAARRGLTP LARIASYATA GVDPQIMGTG PIPASRKALE 

       310        320        330        340        350        360 
KAGWSVGDLD LVEANEAFAA QAIAVNRDMG WDPSIVNVNG GAIAIGHPIG ASGCRILNTL 

       370        380        390 
LFEMQRRDAK KGLATLCIGG GMGVALCLER P 

« Hide

References

[1]"Analysis of beta-ketothiolase and acetoacetyl-CoA reductase genes of a methylotrophic bacterium, Paracoccus denitrificans, and their expression in Escherichia coli."
Yabutani T., Maehara A., Ueda S., Yamane T.
FEMS Microbiol. Lett. 133:85-90(1995) [PubMed: 8566717] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49362 Genomic DNA. Translation: BAA08357.1.

3D structure databases

ProteinModelPortalP54810.
SMRP54810. Positions 5-389.
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_PARDE
AccessionPrimary (citable) accession number: P54810
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 31, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families