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Protein

Acetyl-CoA acetyltransferase

Gene

atoB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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 (atoB)
  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 sitei88Acyl-thioester intermediateBy similarity1
Active sitei349Proton acceptorPROSITE-ProRule annotation1
Active sitei379Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:ACETYL-COA-ACETYLTRANSFER-MONOMER.
ECOL316407:JW2218-MONOMER.
MetaCyc:ACETYL-COA-ACETYLTRANSFER-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:atoB
Ordered Locus Names:b2224, JW2218
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11672. atoB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002064061 – 394Acetyl-CoA acetyltransferaseAdd BLAST394

Proteomic databases

PaxDbiP76461.
PRIDEiP76461.

Interactioni

Protein-protein interaction databases

BioGridi4263266. 7 interactors.
IntActiP76461. 3 interactors.
STRINGi511145.b2224.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Turni20 – 23Combined sources4
Helixi26 – 41Combined sources16
Helixi45 – 47Combined sources3
Beta strandi50 – 54Combined sources5
Helixi65 – 72Combined sources8
Beta strandi80 – 85Combined sources6
Helixi87 – 89Combined sources3
Helixi90 – 103Combined sources14
Beta strandi108 – 118Combined sources11
Beta strandi123 – 125Combined sources3
Helixi127 – 129Combined sources3
Beta strandi138 – 142Combined sources5
Helixi143 – 147Combined sources5
Turni152 – 154Combined sources3
Beta strandi155 – 157Combined sources3
Helixi158 – 169Combined sources12
Helixi173 – 193Combined sources21
Turni194 – 199Combined sources6
Beta strandi203 – 206Combined sources4
Beta strandi211 – 214Combined sources4
Helixi226 – 231Combined sources6
Helixi244 – 246Combined sources3
Beta strandi251 – 261Combined sources11
Helixi262 – 267Combined sources6
Beta strandi274 – 283Combined sources10
Helixi286 – 291Combined sources6
Helixi293 – 303Combined sources11
Helixi308 – 310Combined sources3
Beta strandi312 – 316Combined sources5
Helixi321 – 331Combined sources11
Helixi335 – 337Combined sources3
Helixi344 – 347Combined sources4
Helixi351 – 368Combined sources18
Beta strandi372 – 380Combined sources9
Turni381 – 383Combined sources3
Beta strandi384 – 391Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WYSX-ray2.10A/B/C/D1-393[»]
5F0VX-ray1.80A/B/C/D1-393[»]
5F38X-ray1.90A1-394[»]
B/C1-393[»]
D1-392[»]
ProteinModelPortaliP76461.
SMRiP76461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012240.
InParanoidiP76461.
KOiK00626.
OMAiCLSRAGW.
PhylomeDBiP76461.

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.

P76461-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNCVIVSAV RTAIGSFNGS LASTSAIDLG ATVIKAAIER AKIDSQHVDE
60 70 80 90 100
VIMGNVLQAG LGQNPARQAL LKSGLAETVC GFTVNKVCGS GLKSVALAAQ
110 120 130 140 150
AIQAGQAQSI VAGGMENMSL APYLLDAKAR SGYRLGDGQV YDVILRDGLM
160 170 180 190 200
CATHGYHMGI TAENVAKEYG ITREMQDELA LHSQRKAAAA IESGAFTAEI
210 220 230 240 250
VPVNVVTRKK TFVFSQDEFP KANSTAEALG ALRPAFDKAG TVTAGNASGI
260 270 280 290 300
NDGAAALVIM EESAALAAGL TPLARIKSYA SGGVPPALMG MGPVPATQKA
310 320 330 340 350
LQLAGLQLAD IDLIEANEAF AAQFLAVGKN LGFDSEKVNV NGGAIALGHP
360 370 380 390
IGASGARILV TLLHAMQARD KTLGLATLCI GGGQGIAMVI ERLN
Length:394
Mass (Da):40,352
Last modified:February 1, 1997 - v1
Checksum:iDE27C394C3E6BDFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75284.1.
AP009048 Genomic DNA. Translation: BAA16020.1.
PIRiF64992.
RefSeqiNP_416728.1. NC_000913.3.
WP_000786547.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75284; AAC75284; b2224.
BAA16020; BAA16020; BAA16020.
GeneIDi946727.
KEGGiecj:JW2218.
eco:b2224.
PATRICi32119807. VBIEscCol129921_2313.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75284.1.
AP009048 Genomic DNA. Translation: BAA16020.1.
PIRiF64992.
RefSeqiNP_416728.1. NC_000913.3.
WP_000786547.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WYSX-ray2.10A/B/C/D1-393[»]
5F0VX-ray1.80A/B/C/D1-393[»]
5F38X-ray1.90A1-394[»]
B/C1-393[»]
D1-392[»]
ProteinModelPortaliP76461.
SMRiP76461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263266. 7 interactors.
IntActiP76461. 3 interactors.
STRINGi511145.b2224.

Proteomic databases

PaxDbiP76461.
PRIDEiP76461.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75284; AAC75284; b2224.
BAA16020; BAA16020; BAA16020.
GeneIDi946727.
KEGGiecj:JW2218.
eco:b2224.
PATRICi32119807. VBIEscCol129921_2313.

Organism-specific databases

EchoBASEiEB1623.
EcoGeneiEG11672. atoB.

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012240.
InParanoidiP76461.
KOiK00626.
OMAiCLSRAGW.
PhylomeDBiP76461.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
BioCyciEcoCyc:ACETYL-COA-ACETYLTRANSFER-MONOMER.
ECOL316407:JW2218-MONOMER.
MetaCyc:ACETYL-COA-ACETYLTRANSFER-MONOMER.

Miscellaneous databases

PROiP76461.

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 nameiATOB_ECOLI
AccessioniPrimary (citable) accession number: P76461
Secondary accession number(s): P78176
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.