7PT4

Actinobacterial 2-hydroxyacyl-CoA lyase (AcHACL) structure in complex with a covalently bound reaction intermediate as well as products formyl-CoA and acetone

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0003984	molecular_function	acetolactate synthase activity
A	0005948	cellular_component	acetolactate synthase complex
A	0009097	biological_process	isoleucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016829	molecular_function	lyase activity
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003984	molecular_function	acetolactate synthase activity
B	0005948	cellular_component	acetolactate synthase complex
B	0009097	biological_process	isoleucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016829	molecular_function	lyase activity
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PROSITE/UniProt

site_id	PS00187
Number of Residues	20
Details	TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaalayPdrpvVaVtGDGA

Chain	Residue	Details
A	ILE443-ALA462

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:34952003