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5XZ5

Purification,crystallization and structural analysis of cytoplastic acetoacetyl-CoA thiolase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005773cellular_componentvacuole
A0005829cellular_componentcytosol
A0006696biological_processergosterol biosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0046872molecular_functionmetal ion binding
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005773cellular_componentvacuole
B0005829cellular_componentcytosol
B0006696biological_processergosterol biosynthetic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNKvCASAMkAIilgaqsI
ChainResidueDetails
AVAL87-ILE105

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GVAAICNGgGgAsS
ChainResidueDetails
AGLY379-SER392

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvyGGaVAlGHPlGcSG
ChainResidueDetails
AASN344-GLY360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"UniProtKB","id":"P24752","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10020","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P24752","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Peters C."]}},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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