5CSL

Crystal structure of the 500 kD yeast acetyl-CoA carboxylase holoenzyme dimer

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	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
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	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	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
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	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 PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue BTI A 2301

Chain	Residue
A	LYS735
A	LEU1756
A	THR1757
A	MET1765
B	PHE1956
B	GLY1998
B	VAL2024

---

site_id	AC2
Number of Residues	4
Details	binding site for residue BTI A 2302

Chain	Residue
A	GLY1958
B	ILE1762
A	PHE1956
A	SER1957

---

site_id	AC3
Number of Residues	11
Details	binding site for residue COA A 2303

Chain	Residue
A	ILE1593
A	SER1625
A	ALA1627
A	ARG1628
A	ILE1629
A	GLY1734
A	ILE1735
A	LEU1756
B	ILE2033
B	LYS2034
B	ARG2036

---

site_id	AC4
Number of Residues	10
Details	binding site for residue COA B 2301

Chain	Residue
A	LYS2034
B	ILE1593
B	SER1625
B	ALA1627
B	ARG1628
B	ILE1629
B	ARG1731
B	GLY1734
B	LEU1756
B	ASN1774

---

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	74
Details	Domain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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_FI3
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-biotinyllysine","evidences":[{"evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

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

---