8XKZ

Core region of the citrate-induced human acetyl-CoA carboxylase 1 filament (ACC1-citrate)

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0003989	molecular_function	acetyl-CoA carboxylase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006084	biological_process	acetyl-CoA metabolic process
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0006637	biological_process	acyl-CoA metabolic process
C	0008610	biological_process	lipid biosynthetic process
C	0016874	molecular_function	ligase activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0046949	biological_process	fatty-acyl-CoA biosynthetic process
C	0051289	biological_process	protein homotetramerization
C	2001295	biological_process	malonyl-CoA biosynthetic process
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0003989	molecular_function	acetyl-CoA carboxylase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006084	biological_process	acetyl-CoA metabolic process
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0006637	biological_process	acyl-CoA metabolic process
D	0008610	biological_process	lipid biosynthetic process
D	0016874	molecular_function	ligase activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0046949	biological_process	fatty-acyl-CoA biosynthetic process
D	0051289	biological_process	protein homotetramerization
D	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. GQcYaeIeVMKMvmtLtA

Chain	Residue	Details
C	GLY776-ALA793

---

site_id	PS00866
Number of Residues	15
Details	CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASeggGGkG

Chain	Residue	Details
C	TYR306-GLY320

---

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL

Chain	Residue	Details
C	PHE435-LEU442

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1002
Details	Domain: {"description":"Biotin carboxylation","evidences":[{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	382
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	148
Details	Domain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	676
Details	Domain: {"description":"CoA carboxyltransferase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01136","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	632
Details	Domain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1316
Details	Region: {"description":"Carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01138","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"UniProtKB","id":"P11497","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---