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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
A0005737cellular_componentcytoplasm
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0042619biological_processpoly-hydroxybutyrate biosynthetic process
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0005737cellular_componentcytoplasm
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0042619biological_processpoly-hydroxybutyrate biosynthetic process
C0003985molecular_functionacetyl-CoA C-acetyltransferase activity
C0005737cellular_componentcytoplasm
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0042619biological_processpoly-hydroxybutyrate biosynthetic process
D0003985molecular_functionacetyl-CoA C-acetyltransferase activity
D0005737cellular_componentcytoplasm
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0042619biological_processpoly-hydroxybutyrate biosynthetic 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
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000269|PubMed:25152395
ChainResidueDetails
ASER88
BSER88
CSER88
DSER88

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395
ChainResidueDetails
AHIS349
ACYS379
BHIS349
BCYS379
CHIS349
CCYS379
DHIS349
DCYS379

224931

PDB entries from 2024-09-11

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