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Protein

Acetyl-CoA acetyltransferase

Gene

erg10

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids.By similarity

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 (erg10)
  2. Hydroxymethylglutaryl-CoA synthase (hcs1)
  3. 3-hydroxy-3-methylglutaryl-coenzyme A reductase (hmg1)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Acyl-thioester intermediateBy similarity
Metal bindingi185 – 1851PotassiumBy similarity
Binding sitei185 – 1851Coenzyme ABy similarity
Binding sitei230 – 2301Coenzyme ABy similarity
Metal bindingi246 – 2461Potassium; via carbonyl oxygenBy similarity
Metal bindingi247 – 2471Potassium; via carbonyl oxygenBy similarity
Metal bindingi249 – 2491Potassium; via carbonyl oxygenBy similarity
Binding sitei250 – 2501Coenzyme ABy similarity
Metal bindingi347 – 3471Potassium; via carbonyl oxygenBy similarity
Active sitei351 – 3511Proton acceptorPROSITE-ProRule annotation
Active sitei381 – 3811Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Potassium

Enzyme and pathway databases

ReactomeiR-SPO-70895. Branched-chain amino acid catabolism.
R-SPO-77108. Utilization of Ketone Bodies.
R-SPO-77111. Synthesis of Ketone Bodies.
UniPathwayiUPA00058; UER00101.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase (EC:2.3.1.9)
Alternative name(s):
Acetoacetyl-CoA thiolase
Ergosterol biosynthesis protein 10
Gene namesi
Name:erg10
ORF Names:SPBC215.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC215.09c.
PomBaseiSPBC215.09c. erg10.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Acetyl-CoA acetyltransferasePRO_0000310395Add
BLAST

Proteomic databases

MaxQBiQ9UQW6.

Interactioni

Protein-protein interaction databases

BioGridi277142. 3 interactions.
MINTiMINT-4706810.

Structurei

3D structure databases

ProteinModelPortaliQ9UQW6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

HOGENOMiHOG000012238.
InParanoidiQ9UQW6.
KOiK00626.
OMAiHENKHIG.
OrthoDBiEOG092C2K2G.
PhylomeDBiQ9UQW6.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UQW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNTEVYIVS AVRTPMGSFG GSFASLPATK LGSIAIKGAL ERVNIKPSDV
60 70 80 90 100
DEVFMGNVVS ANLGQNPARQ CALGAGLPRS IVCTTVNKVC ASGMKATILG
110 120 130 140 150
AQTIMTGNAE IVVAGGTESM SNAPYYAPKN RFGAKYGNVE LVDGLLRDGL
160 170 180 190 200
SDAYDGLPMG NAAELCAEEH SIDRASQDAF AISSYKRAQN AQATKAFEQE
210 220 230 240 250
IVPVEVPVGR GKPNKLVTED EEPKNLNEDK LKSVRAVFKS NGTVTAANAS
260 270 280 290 300
TLNDGASALV LMSAAKVKEL GLKPLAKIIG WGEAAQDPER FTTSPSLAIP
310 320 330 340 350
KALKHAGIEA SQVDYYEINE AFSVVAVANT KILGLDPERV NINGGGVAMG
360 370 380 390
HPLGSSGSRI ICTLAYILAQ KDAKIGVAAV CNGGGGASSI VIERV
Length:395
Mass (Da):40,998
Last modified:May 1, 2000 - v1
Checksum:i382822A9EF686544
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti387 – 3871A → P in BAA13846 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89184 mRNA. Translation: BAA13846.1.
CU329671 Genomic DNA. Translation: CAA22123.1.
PIRiT39899.
T42741.
RefSeqiNP_596686.1. NM_001022609.2.

Genome annotation databases

EnsemblFungiiSPBC215.09c.1; SPBC215.09c.1:pep; SPBC215.09c.
GeneIDi2540616.
KEGGispo:SPBC215.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89184 mRNA. Translation: BAA13846.1.
CU329671 Genomic DNA. Translation: CAA22123.1.
PIRiT39899.
T42741.
RefSeqiNP_596686.1. NM_001022609.2.

3D structure databases

ProteinModelPortaliQ9UQW6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277142. 3 interactions.
MINTiMINT-4706810.

Proteomic databases

MaxQBiQ9UQW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC215.09c.1; SPBC215.09c.1:pep; SPBC215.09c.
GeneIDi2540616.
KEGGispo:SPBC215.09c.

Organism-specific databases

EuPathDBiFungiDB:SPBC215.09c.
PomBaseiSPBC215.09c. erg10.

Phylogenomic databases

HOGENOMiHOG000012238.
InParanoidiQ9UQW6.
KOiK00626.
OMAiHENKHIG.
OrthoDBiEOG092C2K2G.
PhylomeDBiQ9UQW6.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
ReactomeiR-SPO-70895. Branched-chain amino acid catabolism.
R-SPO-77108. Utilization of Ketone Bodies.
R-SPO-77111. Synthesis of Ketone Bodies.

Miscellaneous databases

PROiQ9UQW6.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIL_SCHPO
AccessioniPrimary (citable) accession number: Q9UQW6
Secondary accession number(s): P78835, Q1L848
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.