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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: (R)-mevalonate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Acetyl-CoA acetyltransferase (phbA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei89Acyl-thioester intermediateBy similarity1
Active sitei350Proton acceptorPROSITE-ProRule annotation1
Active sitei380Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

PHB biosynthesis

Enzyme and pathway databases

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
Proteomesi
  • UP000001441 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002064191 – 394Acetyl-CoA acetyltransferaseAdd BLAST394

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi572477.Alvin_0063.

Structurei

3D structure databases

ProteinModelPortaliP45369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012238.
KOiK00626.
OMAiESTEKHN.
OrthoDBiPOG091H023S.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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)DescriptionActionsGraphical viewLength
Sequence conflicti2N → S in AAA23322 (PubMed:1396692).Curated1
Sequence conflicti19S → G in AAA23322 (PubMed:1396692).Curated1
Sequence conflicti73K → H in AAA23322 (PubMed:1396692).Curated1
Sequence conflicti239R → K in AAA23322 (PubMed:1396692).Curated1

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.

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.

3D structure databases

ProteinModelPortaliP45369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi572477.Alvin_0063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012238.
KOiK00626.
OMAiESTEKHN.
OrthoDBiPOG091H023S.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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...

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: November 2, 2016
This is version 97 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

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 one 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.