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4O9A

Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0005737cellular_componentcytoplasm
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0042619biological_processpoly-hydroxybutyrate biosynthetic process
A0044281biological_processsmall molecule metabolic process
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0005737cellular_componentcytoplasm
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0042619biological_processpoly-hydroxybutyrate biosynthetic process
B0044281biological_processsmall molecule metabolic process
C0003985molecular_functionacetyl-CoA C-acetyltransferase activity
C0003988molecular_functionacetyl-CoA C-acyltransferase activity
C0005737cellular_componentcytoplasm
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0042619biological_processpoly-hydroxybutyrate biosynthetic process
C0044281biological_processsmall molecule metabolic process
D0003985molecular_functionacetyl-CoA C-acetyltransferase activity
D0003988molecular_functionacetyl-CoA C-acyltransferase activity
D0005737cellular_componentcytoplasm
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0042619biological_processpoly-hydroxybutyrate biosynthetic process
D0044281biological_processsmall molecule metabolic process
Functional Information from PROSITE/UniProt
site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GLASLCIGgGmGvA
ChainResidueDetails
AGLY374-ALA387

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvnGGaIAiGHPiGaSG
ChainResidueDetails
AASN339-GLY355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"25152395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25152395","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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