4HQ6

BC domain in the presence of citrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003989	molecular_function	acetyl-CoA carboxylase activity
A	0005524	molecular_function	ATP binding
A	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE449-GLY463

---

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

Chain	Residue	Details
A	PHE578-LEU585

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	195
Details	Domain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
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_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q13085","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---