5XZ5
Purification,crystallization and structural analysis of cytoplastic acetoacetyl-CoA thiolase from Saccharomyces cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005773 | cellular_component | vacuole |
A | 0005829 | cellular_component | cytosol |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0006696 | biological_process | ergosterol biosynthetic process |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0046872 | molecular_function | metal ion binding |
B | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005773 | cellular_component | vacuole |
B | 0005829 | cellular_component | cytosol |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0006696 | biological_process | ergosterol biosynthetic process |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00098 |
Number of Residues | 19 |
Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNKvCASAMkAIilgaqsI |
Chain | Residue | Details |
A | VAL87-ILE105 |
site_id | PS00099 |
Number of Residues | 14 |
Details | THIOLASE_3 Thiolases active site. GVAAICNGgGgAsS |
Chain | Residue | Details |
A | GLY379-SER392 |
site_id | PS00737 |
Number of Residues | 17 |
Details | THIOLASE_2 Thiolases signature 2. NvyGGaVAlGHPlGcSG |
Chain | Residue | Details |
A | ASN344-GLY360 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000250|UniProtKB:P24752 |
Chain | Residue | Details |
A | CYS91 | |
B | CYS91 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020 |
Chain | Residue | Details |
A | HIS354 | |
A | CYS384 | |
B | HIS354 | |
B | CYS384 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P24752 |
Chain | Residue | Details |
A | TYR186 | |
B | ALA248 | |
B | ALA249 | |
B | ALA251 | |
B | SER252 | |
B | VAL350 | |
A | LYS231 | |
A | ALA248 | |
A | ALA249 | |
A | ALA251 | |
A | SER252 | |
A | VAL350 | |
B | TYR186 | |
B | LYS231 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | SER2 | |
B | SER2 |