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Reviewed, UniProtKB/Swiss-Prot Q6NU46 (THILA_XENLA)

Last modified September 1, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetyl-CoA acetyltransferase A, mitochondrial
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase A
Gene names
Name: acat1-A
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length420 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.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Potassium
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: EC

potassium 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 – 3333Mitochondrion By similarity
Chain34 – 420387Acetyl-CoA acetyltransferase A, mitochondrial
PRO_0000356276

Regions

Region251 – 2533Coenzyme A binding By similarity

Sites

Active site1191Acyl-thioester intermediate By similarity
Active site3781Proton acceptor By similarity
Active site4061Proton acceptor By similarity
Metal binding2121Potassium By similarity
Metal binding2731Potassium; via carbonyl oxygen By similarity
Metal binding2741Potassium; via carbonyl oxygen By similarity
Metal binding3741Potassium; via carbonyl oxygen By similarity
Binding site2121Coenzyme A By similarity
Binding site2561Coenzyme A By similarity
Binding site2771Coenzyme A By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NU46-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 19527789ABD7FFF5

FASTA42044,128
        10         20         30         40         50         60 
MAFCGTRTAA RLSHSTRALH NTHRNFASQR TLNEVVIASA ARTPIGSFQG TLSSLPATKL 

        70         80         90        100        110        120 
GSIAIKAAVE RAGIPADEVK EVYMGNVLQA GQGQAPSRQA TLGAGLAIST PTTTINKVCA 

       130        140        150        160        170        180 
SGMKSVMLAA QSLMCGHQQV MVAGGMESMS NVPYCMSRGA TPYGGVKLED LIVKDGLTDV 

       190        200        210        220        230        240 
YNKIHMGNCA ENTAKKFSIS REEQDSFAIH SYTRSKAAWD SGLIANEIAP VTIAQKGKPD 

       250        260        270        280        290        300 
IIVQEDEEYK RVDFSKFPKL KTVFQKDNGT VTAANSSTLN DGAAALLLMT TEAANRLNVT 

       310        320        330        340        350        360 
PLARIVAFAD AAVDPIDFPI APAYAVPKLL SEAGLKKEDI AMWEINEAFS VVVLANIKML 

       370        380        390        400        410        420 
GIDPARVNMN GGAVSLGHPI GMSGARIVGH MAHALKKGQF GIAGICNGGG GASAVLIEKL 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

BC068755 mRNA. Translation: AAH68755.1.
RefSeqNP_001084679.1.
UniGeneXl.25595

3D structure databases

HSSPHSSP built from PDB template 1AFW based on UniProtKB P27796.
SMRQ6NU46. Positions 28-420.
ModBaseSearch...

Proteomic databases

PRIDEQ6NU46.

Genome annotation databases

GeneID414639.
KEGGxla:414639.

Organism-specific databases

CTD414639.
XenbaseXB-FEAT-977281. acat1.

Phylogenomic databases

HOVERGENQ6NU46.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
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 nameTHILA_XENLA
AccessionPrimary (citable) accession number: Q6NU46
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 5, 2004
Last modified: September 1, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents