4O99
Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| A | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| B | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| C | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| D | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 401 |
| Chain | Residue |
| A | MET103 |
| A | SER278 |
| A | TYR279 |
| A | ARG303 |
| A | HOH611 |
| A | HOH668 |
| B | ALA104 |
| B | ASP106 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 401 |
| Chain | Residue |
| C | HOH536 |
| D | SER20 |
| D | ALA213 |
| D | PHE214 |
| D | HOH478 |
| C | ARG368 |
Functional Information from PROSITE/UniProt
| site_id | PS00098 |
| Number of Residues | 19 |
| Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. INKvCGSGLkAVmlaanaI |
| Chain | Residue | Details |
| A | ILE84-ILE102 |
| site_id | PS00099 |
| Number of Residues | 14 |
| Details | THIOLASE_3 Thiolases active site. GLASLCIGgGmGvA |
| Chain | Residue | Details |
| A | GLY374-ALA387 |
| site_id | PS00737 |
| Number of Residues | 17 |
| Details | THIOLASE_2 Thiolases signature 2. NvnGGaIAiGHPiGaSG |
| Chain | Residue | Details |
| A | ASN339-GLY355 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"25152395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25152395","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
