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4RCN

Structure and function of a single-chain, multi-domain long-chain acyl-coa carboxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003989molecular_functionacetyl-CoA carboxylase activity
A0004075molecular_functionbiotin carboxylase activity
A0005524molecular_functionATP binding
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A2001295biological_processmalonyl-CoA biosynthetic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003989molecular_functionacetyl-CoA carboxylase activity
B0004075molecular_functionbiotin carboxylase activity
B0005524molecular_functionATP binding
B0016874molecular_functionligase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLEVNPRI
ChainResidueDetails
APHE286-ILE293

238895

PDB entries from 2025-07-16

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