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5CSK

Crystal structure of yeast acetyl-CoA carboxylase, unbiotinylated

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003989molecular_functionacetyl-CoA carboxylase activity
A0004075molecular_functionbiotin carboxylase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0006085biological_processacetyl-CoA biosynthetic process
A0006606biological_processprotein import into nucleus
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0009317cellular_componentacetyl-CoA carboxylase complex
A0016020cellular_componentmembrane
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0016874molecular_functionligase activity
A0042759biological_processlong-chain fatty acid biosynthetic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A1905502molecular_functionacetyl-CoA binding
A2001295biological_processmalonyl-CoA biosynthetic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003989molecular_functionacetyl-CoA carboxylase activity
B0004075molecular_functionbiotin carboxylase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006085biological_processacetyl-CoA biosynthetic process
B0006606biological_processprotein import into nucleus
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0009317cellular_componentacetyl-CoA carboxylase complex
B0016020cellular_componentmembrane
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0016874molecular_functionligase activity
B0042759biological_processlong-chain fatty acid biosynthetic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B1905502molecular_functionacetyl-CoA binding
B2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GQpYaeIeVMKMqmpLvS
ChainResidueDetails
AGLY725-SER742

site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPVMIKASeggGGkG
ChainResidueDetails
APHE247-GLY261

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL
ChainResidueDetails
APHE377-LEU384

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1018
DetailsDomain: {"description":"Biotin carboxylation"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues384
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues672
DetailsDomain: {"description":"CoA carboxyltransferase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01136","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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