1NM8
Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003997 | molecular_function | acyl-CoA oxidase activity |
A | 0004092 | molecular_function | carnitine O-acetyltransferase activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005777 | cellular_component | peroxisome |
A | 0005782 | cellular_component | peroxisomal matrix |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005829 | cellular_component | cytosol |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0008458 | molecular_function | carnitine O-octanoyltransferase activity |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0019254 | biological_process | carnitine metabolic process, CoA-linked |
A | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
A | 0046459 | biological_process | short-chain fatty acid metabolic process |
A | 0051791 | biological_process | medium-chain fatty acid metabolic process |
Functional Information from PROSITE/UniProt
site_id | PS00439 |
Number of Residues | 16 |
Details | ACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPVPpLqQSLdhY |
Chain | Residue | Details |
A | LEU14-TYR29 |
site_id | PS00440 |
Number of Residues | 28 |
Details | ACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKtLqFIvaeDGscglvyEHaaaEG |
Chain | Residue | Details |
A | ARG300-GLY327 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305 |
Chain | Residue | Details |
A | HIS322 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P47934 |
Chain | Residue | Details |
A | LYS398 | |
A | LYS402 | |
A | SER435 | |
A | ARG483 | |
A | GLN534 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15099582 |
Chain | Residue | Details |
A | TYR431 | |
A | SER433 | |
A | THR444 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P47934 |
Chain | Residue | Details |
A | LYS72 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P47934 |
Chain | Residue | Details |
A | LYS240 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS247 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1q6x |
Chain | Residue | Details |
A | HIS322 | |
A | TYR86 | |
A | SER533 | |
A | PRO99 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1q6x |
Chain | Residue | Details |
A | HIS322 | |
A | SER533 |