Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07097 (THIL_ZOORA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Acetyl-CoA acetyltransferase

EC=2.3.1.9
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene names
Name:phbA
OrganismZoogloea ramigera
Taxonomic identifier350 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeZoogloea

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processPHB biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processpoly-hydroxybutyrate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 392391Acetyl-CoA acetyltransferase
PRO_0000206463

Sites

Active site891Acyl-thioester intermediate
Active site3481Proton acceptor
Active site3781Proton acceptor

Experimental info

Mutagenesis641Q → A: Slightly lower activity. Ref.6
Mutagenesis891C → A: Loss of activity. Ref.6
Mutagenesis3781C → G: Loss of activity. Ref.3

Secondary structure

...................................................................... 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07097 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 88A6298751A42B7E

FASTA39240,473
        10         20         30         40         50         60 
MSTPSIVIAS ARTAVGSFNG AFANTPAHEL GATVISAVLE RAGVAAGEVN EVILGQVLPA 

        70         80         90        100        110        120 
GEGQNPARQA AMKAGVPQEA TAWGMNQLCG SGLRAVALGM QQIATGDASI IVAGGMESMS 

       130        140        150        160        170        180 
MAPHCAHLAG GVKMGDFKMI DTMIKDGLTD AFYGYHMGTT AENVAKQWQL SRDEQDAFAV 

       190        200        210        220        230        240 
ASQNKAEAAQ KDGRFKDEIV PFIVKGRKGD ITVDADEYIR HGATLDSMAK LRPAFDKEGT 

       250        260        270        280        290        300 
VTAGNASGLN DGAAAALLMS EAEASRRGIQ PLGRIVSWAT VGVDPKVMGT GPIPASRKAL 

       310        320        330        340        350        360 
ERAGWKIGDL DLVEANEAFA AQACAVNKDL GWDPSIVNVN GGAIAIGHPI GASGARILNT 

       370        380        390 
LLFEMKRRGA RKGLATLCIG GGMGVAMCIE SL 

« Hide

References

[1]"Biosynthetic thiolase from Zoogloea ramigera. III. Isolation and characterization of the structural gene."
Peoples O.P., Masamune S., Walsh C.T., Sinskey A.J.
J. Biol. Chem. 262:97-102(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482.
[2]"Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase."
Peoples O.P., Sinskey A.J.
J. Biol. Chem. 264:15293-15297(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 131.
[3]"Biosynthetic thiolase from Zoogloea ramigera. Evidence for a mechanism involving Cys-378 as the active site base."
Palmer M.A.J., Differding E., Gamboni R., Williams S.F., Peoples O.P., Walsh C.T., Sinskey S.J., Masamune S.
J. Biol. Chem. 266:8369-8375(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-378.
[4]"Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase."
Modis Y., Wierenga R.K.
J. Mol. Biol. 297:1171-1182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[5]"A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism."
Modis Y., Wierenga R.K.
Structure 7:1279-1290(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF THE THIOESTER INTERMEDIATE AND OF COMPLEX WITH SUBSTRATE.
[6]"The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes."
Kursula P., Ojala J., Lambeir A.-M., Wierenga R.K.
Biochemistry 41:15543-15556(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF THE THIOESTER INTERMEDIATE; OF COMPLEX WITH SUBSTRATE AND OF MUTANTS ALA-64 AND ALA-89, MUTAGENESIS OF GLN-64 AND CYS-89.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02631 Genomic DNA. Translation: AAA27706.1. Sequence problems.
PIRXXGZAC. A26121.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DLUX-ray2.25A/B/C/D11-392[»]
1DLVX-ray2.29A/B/C/D11-392[»]
1DM3X-ray2.00A/B/C/D11-392[»]
1M1OX-ray1.95A/B/C/D11-392[»]
1M1TX-ray1.94A/B/C/D11-392[»]
1M3KX-ray1.70A/B/C/D11-392[»]
1M3ZX-ray1.87A/B/C/D11-392[»]
1M4SX-ray1.87A/B/C/D11-392[»]
1M4TX-ray1.77A/B/C/D11-392[»]
1NL7X-ray1.90A/B/C/D11-391[»]
1OU6X-ray2.07A/B/C/D11-391[»]
1QFLX-ray1.92A/B/C/D11-392[»]
2VTZX-ray2.30A/B/C/D2-392[»]
2VU0X-ray1.87A/B/C/D11-392[»]
2VU1X-ray1.51A/B/C/D2-392[»]
2VU2X-ray2.65A/B/C/D2-392[»]
2WKTX-ray2.00A/B/C/D11-392[»]
2WKUX-ray2.30A/B/C/D11-392[»]
2WKVX-ray2.50A/B/C/D11-392[»]
2WL4X-ray1.80A/B/C/D11-392[»]
2WL5X-ray1.80A/B/C/D11-392[»]
2WL6X-ray2.98A/B/C/D11-392[»]
ProteinModelPortalP07097.
SMRP07097. Positions 5-392.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP07097.
UniPathwayUPA00058; UER00101.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
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]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 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...

Other

EvolutionaryTraceP07097.

Entry information

Entry nameTHIL_ZOORA
AccessionPrimary (citable) accession number: P07097
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 102 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways