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P45369 (THIL_ALLVD) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 83. 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:phbA
Ordered Locus Names:Alvin_0063
OrganismAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum) [Complete proteome] [HAMAP]
Taxonomic identifier572477 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium

Protein attributes

Sequence length394 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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processPHB biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Acetyl-CoA acetyltransferase
PRO_0000206419

Sites

Active site891Acyl-thioester intermediate By similarity
Active site3501Proton acceptor By similarity
Active site3801Proton acceptor By similarity

Experimental info

Sequence conflict21N → S in AAA23322. Ref.1
Sequence conflict191S → G in AAA23322. Ref.1
Sequence conflict731K → H in AAA23322. Ref.1
Sequence conflict2391R → K in AAA23322. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P45369 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 8AECC7EB26B29344

FASTA39441,129
        10         20         30         40         50         60 
MNENIVIVDA GRSAIGTFSG SLSSLSATEI GTAVLKGLLA RTGLAPEQID EVILGQVLTA 

        70         80         90        100        110        120 
GVGQNPARQT TLKAGLPHSV PAMTINKVCG SGLKAVHLAM QAIACGDADI VIAGGQESMS 

       130        140        150        160        170        180 
QSSHVLPRSR DGQRMGDWSM KDTMIVDGLW DAFNNYHMGT TAENIAQKYG FTREQQDAFA 

       190        200        210        220        230        240 
AASQQKTEAA QKAGRFQDEI IPIEIPQRKG DPKVFDADEF PRHGTTAESL GKLRPAFSRD 

       250        260        270        280        290        300 
GSVTAGNASG INDGAAMVVV MKESKAKELG LKPMARLVAF ASAGVDPAIM GTGPIPASTK 

       310        320        330        340        350        360 
CLEKAGWTPA DLDLIEANEA FAAQAMSVNQ DMGWDLSKVN VNGGAIAIGH PIGASGARVL 

       370        380        390 
VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERM 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequences of genes relevant for biosynthesis of poly(3-hydroxybutyric acid) in Chromatium vinosum strain D."
Liebergesell M., Steinbuechel A.
Eur. J. Biochem. 209:135-150(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome of Allochromatium vinosum DSM 180."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01112 Genomic DNA. Translation: AAA23322.1.
CP001896 Genomic DNA. Translation: ADC61035.1.
PIRS29276.
RefSeqYP_003442067.1. NC_013851.1.

3D structure databases

ProteinModelPortalP45369.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADC61035; ADC61035; Alvin_0063.
GeneID8785390.
KEGGalv:Alvin_0063.
PATRIC31919867. VBIAllVin64954_0065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000012238.
KOK00626.
ProtClustDBCLSK2782295.

Enzyme and pathway databases

BioCycAVIN572477:GCJK-63-MONOMER.
UniPathwayUPA00058; UER00101.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
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]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 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_ALLVD
AccessionPrimary (citable) accession number: P45369
Secondary accession number(s): D3RUY6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 15, 2010
Last modified: October 16, 2013
This is version 83 of the entry and version 2 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