2WU9
Crystal structure of peroxisomal KAT2 from Arabidopsis thaliana
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000325 | cellular_component | plant-type vacuole |
| A | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009514 | cellular_component | glyoxysome |
| A | 0009611 | biological_process | response to wounding |
| A | 0009695 | biological_process | jasmonic acid biosynthetic process |
| A | 0009789 | biological_process | positive regulation of abscisic acid-activated signaling pathway |
| A | 0010111 | biological_process | glyoxysome organization |
| A | 0010124 | biological_process | phenylacetate catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0031408 | biological_process | oxylipin biosynthetic process |
| B | 0000325 | cellular_component | plant-type vacuole |
| B | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009514 | cellular_component | glyoxysome |
| B | 0009611 | biological_process | response to wounding |
| B | 0009695 | biological_process | jasmonic acid biosynthetic process |
| B | 0009789 | biological_process | positive regulation of abscisic acid-activated signaling pathway |
| B | 0010111 | biological_process | glyoxysome organization |
| B | 0010124 | biological_process | phenylacetate catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0031408 | biological_process | oxylipin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1449 |
| Chain | Residue |
| A | ASP50 |
| A | HOH2595 |
| A | HOH2596 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 1450 |
| Chain | Residue |
| A | THR170 |
| A | ASN171 |
| A | HOH2597 |
| A | PRO75 |
| A | ALA107 |
| A | PRO108 |
| A | GLN111 |
| A | ARG112 |
| A | GLU115 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1451 |
| Chain | Residue |
| A | GLY155 |
| A | ASP158 |
| A | HOH2255 |
| A | HOH2454 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1452 |
| Chain | Residue |
| A | ALA217 |
| A | SER221 |
| A | LYS224 |
| A | GLU362 |
| A | PHE368 |
| A | HOH2527 |
| A | HOH2599 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1453 |
| Chain | Residue |
| A | CYS192 |
| A | LEU194 |
| A | MET196 |
| A | THR199 |
| A | PRO330 |
| A | MET333 |
| A | THR428 |
| A | HOH2600 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1454 |
| Chain | Residue |
| A | GLN216 |
| A | VAL219 |
| A | LEU270 |
| A | HOH2358 |
| A | HOH2601 |
| B | HOH2531 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 1449 |
| Chain | Residue |
| B | ALA217 |
| B | ASP220 |
| B | SER221 |
| B | LYS224 |
| B | GLU362 |
| B | PHE368 |
| B | HOH2297 |
| B | HOH2532 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 1450 |
| Chain | Residue |
| B | LEU47 |
| B | ARG306 |
| B | VAL316 |
| B | VAL319 |
| B | ARG321 |
| B | GLY439 |
| B | ASP440 |
| B | GLU444 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1451 |
| Chain | Residue |
| A | PHE156 |
| B | THR322 |
| B | PHE323 |
| B | ALA347 |
| B | HOH2424 |
| B | HOH2533 |
Functional Information from PROSITE/UniProt
| site_id | PS00098 |
| Number of Residues | 19 |
| Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNRqCSSGLqAVadvaaaI |
| Chain | Residue | Details |
| A | VAL134-ILE152 |
| site_id | PS00099 |
| Number of Residues | 14 |
| Details | THIOLASE_3 Thiolases active site. GVVSMCIGtGmGaA |
| Chain | Residue | Details |
| A | GLY420-ALA433 |
| site_id | PS00737 |
| Number of Residues | 17 |
| Details | THIOLASE_2 Thiolases signature 2. NvnGGaMAiGHPlGaTG |
| Chain | Residue | Details |
| A | ASN383-GLY399 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10020","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
