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Reviewed, UniProtKB/Swiss-Prot Q6GN02 (THILB_XENLA)

Last modified November 24, 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 B, mitochondrial
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase B
Gene names
Name: acat1-B
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 B, mitochondrial
PRO_0000356277

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
Q6GN02-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: ECECDAC11AB7836B

FASTA42044,073
        10         20         30         40         50         60 
MAFCGPRTAA RLSHSTRALH YTHRSFASPR 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 IIVKDGLTDV 

       190        200        210        220        230        240 
YNKFHMGNCA ENTAKKLSIS REEQDGFAIT SYTRSKAAWD SGLIANEIAP VTIAQKGKPD 

       250        260        270        280        290        300 
IIVQEDEEYK RVDFSKFPKL KTVFQKDNGT VTAANSSTLN DGAAALVLMT AEAANRLNVT 

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

       370        380        390        400        410        420 
DIDPARVNVN GGAVSLGHPI GMSGARIVGH MAHALRKGQF GIAGICNGGG GASAVLIEKL 

« Hide

References

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

Cross-references

Sequence databases

BC073720 mRNA. Translation: AAH73720.1.
RefSeqNP_001086028.1.
UniGeneXl.25209

3D structure databases

HSSPHSSP built from PDB template 2F2S based on UniProtKB P24752.
SMRQ6GN02. Positions 31-420.
ModBaseSearch...

Genome annotation databases

GeneID444457.
KEGGxla:444457.

Phylogenomic databases

HOVERGENQ6GN02.

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. 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 nameTHILB_XENLA
AccessionPrimary (citable) accession number: Q6GN02
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 19, 2004
Last modified: November 24, 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