5CSK
Crystal structure of yeast acetyl-CoA carboxylase, unbiotinylated
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
A | 0004075 | molecular_function | biotin carboxylase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005829 | cellular_component | cytosol |
A | 0006085 | biological_process | acetyl-CoA biosynthetic process |
A | 0006606 | biological_process | protein import into nucleus |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
A | 0016020 | cellular_component | membrane |
A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
A | 0016874 | molecular_function | ligase activity |
A | 0042759 | biological_process | long-chain fatty acid biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 1905502 | molecular_function | acetyl-CoA binding |
A | 2001295 | biological_process | malonyl-CoA biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
B | 0004075 | molecular_function | biotin carboxylase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0005829 | cellular_component | cytosol |
B | 0006085 | biological_process | acetyl-CoA biosynthetic process |
B | 0006606 | biological_process | protein import into nucleus |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
B | 0016020 | cellular_component | membrane |
B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
B | 0016874 | molecular_function | ligase activity |
B | 0042759 | biological_process | long-chain fatty acid biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 1905502 | molecular_function | acetyl-CoA binding |
B | 2001295 | biological_process | malonyl-CoA biosynthetic process |
Functional Information from PROSITE/UniProt
site_id | PS00188 |
Number of Residues | 18 |
Details | BIOTIN Biotin-requiring enzymes attachment site. GQpYaeIeVMKMqmpLvS |
Chain | Residue | Details |
A | GLY725-SER742 |
site_id | PS00866 |
Number of Residues | 15 |
Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPVMIKASeggGGkG |
Chain | Residue | Details |
A | PHE247-GLY261 |
site_id | PS00867 |
Number of Residues | 8 |
Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL |
Chain | Residue | Details |
A | PHE377-LEU384 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1018 |
Details | Domain: {"description":"Biotin carboxylation"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 384 |
Details | Domain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 672 |
Details | Domain: {"description":"CoA carboxyltransferase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01136","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 12 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15665377","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |