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9E4O

E. coli acetyl-CoA carboxylase, wide stacked tube, 3.98 Angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0009317cellular_componentacetyl-CoA carboxylase complex
A0009329cellular_componentacetate CoA-transferase complex
A0016740molecular_functiontransferase activity
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0042759biological_processlong-chain fatty acid biosynthetic process
A0042802molecular_functionidentical protein binding
A2001295biological_processmalonyl-CoA biosynthetic process
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003989molecular_functionacetyl-CoA carboxylase activity
C0004075molecular_functionbiotin carboxylase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0016874molecular_functionligase activity
C0042803molecular_functionprotein homodimerization activity
C0045717biological_processnegative regulation of fatty acid biosynthetic process
C0046872molecular_functionmetal ion binding
C2001295biological_processmalonyl-CoA biosynthetic process
D0000166molecular_functionnucleotide binding
D0003677molecular_functionDNA binding
D0003723molecular_functionRNA binding
D0003729molecular_functionmRNA binding
D0003989molecular_functionacetyl-CoA carboxylase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006417biological_processregulation of translation
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0008270molecular_functionzinc ion binding
D0009329cellular_componentacetate CoA-transferase complex
D0016740molecular_functiontransferase activity
D0016743molecular_functioncarboxyl- or carbamoyltransferase activity
D0017148biological_processnegative regulation of translation
D0042759biological_processlong-chain fatty acid biosynthetic process
D0046872molecular_functionmetal ion binding
D2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GDtLciVeAMKMmnqIeA
ChainResidueDetails
BGLY112-ALA129

site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKASgggGGrG
ChainResidueDetails
CTYR154-GLY168

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRI
ChainResidueDetails
CPHE286-ILE293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues261
DetailsDomain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"324999","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues444
DetailsDomain: {"description":"Biotin carboxylation"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues197
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues22
DetailsZinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

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PDB entries from 2026-01-28

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