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

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

Chain	Residue	Details
A	PHE578-LEU585

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	ARG584

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409

Chain	Residue	Details
A	GLY458

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969

Chain	Residue	Details
A	GLU567
A	GLU580
A	ASN582

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11497

Chain	Residue	Details
A	SER220

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by AMPK => ECO:0000269|PubMed:12488245, ECO:0000269|PubMed:19900410

Chain	Residue	Details
A	SEP222

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER469

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q13085

Chain	Residue	Details
A	THR753

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