Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q29RZ0 (THIL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
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, mitochondrial
EC=2.3.1.9
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene names
Name:ACAT1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a major role in ketone body metabolism By similarity.

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Enzyme regulation

Activated by potassium ions, but not sodium ions By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Potassium
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion By similarity
Chain29 – 422394Acetyl-CoA acetyltransferase, mitochondrial
PRO_0000356274

Regions

Region253 – 2553Coenzyme A binding By similarity

Sites

Active site1211Acyl-thioester intermediate By similarity
Active site3801Proton acceptor By similarity
Active site4081Proton acceptor By similarity
Metal binding2141Potassium By similarity
Metal binding2751Potassium; via carbonyl oxygen By similarity
Metal binding2761Potassium; via carbonyl oxygen By similarity
Metal binding2781Potassium; via carbonyl oxygen By similarity
Metal binding3761Potassium; via carbonyl oxygen By similarity
Binding site2141Coenzyme A By similarity
Binding site2581Coenzyme A By similarity
Binding site2791Coenzyme A By similarity

Amino acid modifications

Modified residue781N6-acetyllysine By similarity
Modified residue1691N6-acetyllysine By similarity
Modified residue1761N6-acetyllysine By similarity
Modified residue1851N6-acetyllysine By similarity
Modified residue2461N6-acetyllysine By similarity
Modified residue2581N6-acetyllysine By similarity
Modified residue3331N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29RZ0 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 17B8975F0DB3FE9D

FASTA42244,889
        10         20         30         40         50         60 
MPVLAALLRR GPLLQRRVQE IRYAERSYVS KPTLNEVVIV SAIRTPIGSF LGSLSSLPAT 

        70         80         90        100        110        120 
KLGSIAIQGA IEKAGIPKEE VKEAYMGNVL QGGEGQAPTR QAVLGAGLPI STPCTTINKV 

       130        140        150        160        170        180 
CASGMKAIMM ASQNLMCGHQ DVMVAGGMES MSNVPYVMNR GATPYGGVKL EDLIVKDGLT 

       190        200        210        220        230        240 
DVYNKIHMGN CAENTAKKLN ITREEQDTYA LNSYTRSKAA WEAGRFGNEV VPVTITVKGK 

       250        260        270        280        290        300 
PDVVVKEDEE YKRVDFSKIP KLKTVFQREN GTVTAANAST LNDGAAAVVL MTADAAKRLN 

       310        320        330        340        350        360 
VKPLARIAAF ADAAVEPIDF PLAPAYAVPK VLKDAGLKKE DITMWEVNEA FSVVVLANIK 

       370        380        390        400        410        420 
MLEMDPQKVN INGGAVSLGH PIGMSGARIV VHLAHALKQG EYGLASICNG GGGASAMLIQ 


KL

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC113328 mRNA. Translation: AAI13329.1.
IPIIPI00711918.
RefSeqNP_001039540.1. NM_001046075.1.
UniGeneBt.57598.

3D structure databases

ProteinModelPortalQ29RZ0.
SMRQ29RZ0. Positions 30-422.
ModBaseSearch...

Protein-protein interaction databases

IntActQ29RZ0. 1 interaction.
STRINGQ29RZ0.

Proteomic databases

PRIDEQ29RZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017122; ENSBTAP00000017122; ENSBTAG00000012885.
GeneID511082.
KEGGbta:511082.

Organism-specific databases

CTD38.

Phylogenomic databases

eggNOGmaNOG09562.
GeneTreeENSGT00390000009412.
HOVERGENHBG003112.
InParanoidQ29RZ0.
OMAAYAVPKV.
OrthoDBEOG4ZW5B8.
PhylomeDBQ29RZ0.

Family and domain databases

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]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KOK00626.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 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_BOVIN
AccessionPrimary (citable) accession number: Q29RZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 4, 2006
Last modified: November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents