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Reviewed, UniProtKB/Swiss-Prot Q9ZHI1 (THIL_CHRVO)

Last modified February 9, 2010. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Acetyl-CoA acetyltransferase
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase
Gene names
Name: phaA
Ordered Locus Names: CV_2790
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in the production of polyhydroxyalkonic acids (PHAs), composed primarily of 3-hydroxybutyric acid (3HB) and 3-hydroxyvaleric acid (3HV).

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Pathway

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

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processPHA biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpoly(3-hydroxyalkanoate) 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 – 392392Acetyl-CoA acetyltransferase
PRO_0000206420

Sites

Active site871Acyl-thioester intermediate By similarity
Active site3481Proton acceptor By similarity
Active site3781Proton acceptor By similarity

Experimental info

Sequence conflict9 – 113QRT → HAP in AAC69616. Ref.2
Sequence conflict1221H → Y in AAC69616. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9ZHI1-1 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: CCE21993747EF8DB

FASTA39240,119
        10         20         30         40         50         60 
MEVAIVAAQR TAIGSFGGGL AKIPAPELGA TVIKALLEKT GVKPEDVSEV ILGQVLTAGS 

        70         80         90        100        110        120 
GQNPARQALI KAGLPVTTPA TTLNVVCGSG LRAVHLAAQA ILAGDADIVI AGGQESMSLS 

       130        140        150        160        170        180 
PHILPGSRDG FRMGNAQLVD TMVNDGLTDA YNAYHMGITA ENVAAKYGIG REEQDAFSLQ 

       190        200        210        220        230        240 
SQQRAAAAQK AGKFRDEIVP VLVPQRKGDP LAFDADEFIK HDASADGLAK LRPAFKKDGT 

       250        260        270        280        290        300 
VTAGNASGIN DGAAAVLLMS TQKADQLGLK PLAIIKGYAL TGCEPEIMGI GPVSATRKAL 

       310        320        330        340        350        360 
SKAGWTVEDL DLVEANEAFA AQALGVAKEL GWGSDKVNVN GGAIALGHPI GASGCRVLVT 

       370        380        390 
LLHEMQRRGA KKGLATLCIG GGMGVALAVE RP 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.
[2]"Cloning, molecular analysis, and expression of the polyhydroxyalkanoic acid synthase (phaC) gene from Chromobacterium violaceum."
Kolibachuk D., Miller A., Dennis D.
Appl. Environ. Microbiol. 65:3561-3565(1999) [PubMed: 10427049] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ60458.1.
AF061446 Genomic DNA. Translation: AAC69616.1.
RefSeqNP_902460.1.

3D structure databases

SMRQ9ZHI1. Positions 3-390.
ModBaseSearch...

Genome annotation databases

GeneID2547100.
GenomeReviewsGene locus CV_2790 in contig AE016825_GR.
KEGGcvi:CV_2790.
NMPDRfig|243365.1.peg.2790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG370930.
OMADPATMGM.
PhylomeDBQ9ZHI1.

Enzyme and pathway databases

BioCycCVIO243365:CV_2790-MONOMER.
BRENDA2.3.1.9. 415.

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 nameTHIL_CHRVO
AccessionPrimary (citable) accession number: Q9ZHI1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 24, 2003
Last modified: February 9, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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