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Reviewed, UniProtKB/Swiss-Prot P81347 (THL_CLOPA)

Last modified September 22, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase
    CP 13
Gene names
Name: thl
OrganismClostridium pasteurianum
Taxonomic identifier1501 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›15›15Acetyl-CoA acetyltransferase
PRO_0000206405

Experimental info

Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P81347-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 9735820D61BB35FC

FASTA151,498
        10 
MKEVVIASAV XTAXG 

« Hide

References

[1]"Two-dimensional gel electrophoresis separation and N-terminal sequence analysis of proteins from Clostridium pasteurianum W5."
Flengsrud R., Skjeldal L.
Electrophoresis 19:802-806(1998) [PubMed: 9629918] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.9. 871.

Family and domain databases

InterProIPR002155. Thiolase.
[Graphical view]
PROSITEPS00098. THIOLASE_1. Partial match.
PS00737. THIOLASE_2. Partial match.
PS00099. THIOLASE_3. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHL_CLOPA
AccessionPrimary (citable) accession number: P81347
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: September 22, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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