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Protein

Acetyl-CoA acetyltransferase

Gene

phbA

Organism
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891Acyl-thioester intermediateBy similarity
Active sitei350 – 3501Proton acceptorPROSITE-ProRule annotation
Active sitei380 – 3801Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. acetyl-CoA C-acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. poly-hydroxybutyrate biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

PHB biosynthesis

Enzyme and pathway databases

BioCyciAVIN572477:GCJK-63-MONOMER.
UniPathwayiUPA00058; UER00101.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase (EC:2.3.1.9)
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene namesi
Name:phbA
Ordered Locus Names:Alvin_0063
OrganismiAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Taxonomic identifieri572477 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium
ProteomesiUP000001441 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Acetyl-CoA acetyltransferasePRO_0000206419Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP45369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

HOGENOMiHOG000012238.
KOiK00626.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. 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]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNENIVIVDA GRSAIGTFSG SLSSLSATEI GTAVLKGLLA RTGLAPEQID
60 70 80 90 100
EVILGQVLTA GVGQNPARQT TLKAGLPHSV PAMTINKVCG SGLKAVHLAM
110 120 130 140 150
QAIACGDADI VIAGGQESMS QSSHVLPRSR DGQRMGDWSM KDTMIVDGLW
160 170 180 190 200
DAFNNYHMGT TAENIAQKYG FTREQQDAFA AASQQKTEAA QKAGRFQDEI
210 220 230 240 250
IPIEIPQRKG DPKVFDADEF PRHGTTAESL GKLRPAFSRD GSVTAGNASG
260 270 280 290 300
INDGAAMVVV MKESKAKELG LKPMARLVAF ASAGVDPAIM GTGPIPASTK
310 320 330 340 350
CLEKAGWTPA DLDLIEANEA FAAQAMSVNQ DMGWDLSKVN VNGGAIAIGH
360 370 380 390
PIGASGARVL VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERM
Length:394
Mass (Da):41,129
Last modified:June 15, 2010 - v2
Checksum:i8AECC7EB26B29344
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21N → S in AAA23322 (PubMed:1396692).Curated
Sequence conflicti19 – 191S → G in AAA23322 (PubMed:1396692).Curated
Sequence conflicti73 – 731K → H in AAA23322 (PubMed:1396692).Curated
Sequence conflicti239 – 2391R → K in AAA23322 (PubMed:1396692).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01112 Genomic DNA. Translation: AAA23322.1.
CP001896 Genomic DNA. Translation: ADC61035.1.
PIRiS29276.
RefSeqiWP_012969311.1. NC_013851.1.
YP_003442067.1. NC_013851.1.

Genome annotation databases

EnsemblBacteriaiADC61035; ADC61035; Alvin_0063.
KEGGialv:Alvin_0063.
PATRICi31919867. VBIAllVin64954_0065.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01112 Genomic DNA. Translation: AAA23322.1.
CP001896 Genomic DNA. Translation: ADC61035.1.
PIRiS29276.
RefSeqiWP_012969311.1. NC_013851.1.
YP_003442067.1. NC_013851.1.

3D structure databases

ProteinModelPortaliP45369.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADC61035; ADC61035; Alvin_0063.
KEGGialv:Alvin_0063.
PATRICi31919867. VBIAllVin64954_0065.

Phylogenomic databases

HOGENOMiHOG000012238.
KOiK00626.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
BioCyciAVIN572477:GCJK-63-MONOMER.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. 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]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 / NCIMB 10441 / D.

Entry informationi

Entry nameiTHIL_ALLVD
AccessioniPrimary (citable) accession number: P45369
Secondary accession number(s): D3RUY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 15, 2010
Last modified: April 29, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.