1DQU

CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004451	molecular_function	isocitrate lyase activity
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0009062	biological_process	fatty acid catabolic process
A	0009514	cellular_component	glyoxysome
A	0015976	biological_process	carbon utilization
A	0016829	molecular_function	lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0045733	biological_process	acetate catabolic process
A	0046421	molecular_function	methylisocitrate lyase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00161
Number of Residues	6
Details	ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHM

Chain	Residue	Details
A	LYS204-MET209

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:10801489

Chain	Residue	Details
A	CYS206

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P9WKK7

Chain	Residue	Details
A	SER97
A	ASP168
A	GLY207
A	ARG243
A	ASN423
A	THR457

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1f8m

Chain	Residue	Details
A	HIS195
A	ARG243

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