Annotations: 1F61

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1f61b_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Phosphoenolpyruvate/pyruvate domain	Phosphoenolpyruvate mutase/Isocitrate lyase-like	Isocitrate lyase	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
A	d1f61a_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Phosphoenolpyruvate/pyruvate domain	Phosphoenolpyruvate mutase/Isocitrate lyase-like	Isocitrate lyase	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8043663	3000510	SCOP2B (2022-06-29)
A	SCOP2 Family	Phosphoenolpyruvate mutase/Isocitrate lyase-like	8031285	4003532	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphoenolpyruvate/pyruvate domain	8043663	3000510	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PEP_mutase	e1f61B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PEP_mutase	ECOD (1.6)
A	PEP_mutase	e1f61A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PEP_mutase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.20.20.60	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Phosphoenolpyruvate-binding domains	CATH (4.3.0)
A	3.20.20.60	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Phosphoenolpyruvate-binding domains	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00463	Isocitrate lyase family (ICL)	Isocitrate lyase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	ISOCITRATE LYASE	oxo-acid-lyase activity methylisocitrate lyase activity lyase activity catalytic activity carbon-carbon lyase activity isocitrate lyase activity protein binding binding enzyme binding zymogen binding cation binding ion binding metal ion binding small molecule binding	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy carbohydrate metabolic process glyoxylate metabolic process glyoxylate cycle oxoacid metabolic process carboxylic acid metabolic process organic acid metabolic process aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy carbohydrate metabolic process glyoxylate metabolic process glyoxylate cycle oxoacid metabolic process carboxylic acid metabolic process organic acid metabolic process aldehyde metabolic process small molecule metabolic process monocarboxylic acid metabolic process isocitrate metabolic process tricarboxylic acid metabolic process organic hydroxy compound metabolic process alcohol metabolic process secondary alcohol metabolic process response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to defenses of other organism response to external stimulus response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction response to host immune response response to host response to external biotic stimulus response to decreased oxygen levels cellular response to stimulus cellular response to oxygen levels cellular response to hypoxia cellular response to decreased oxygen levels cellular response to chemical stimulus cellular response to stress response to hypoxia response to stress response to chemical response to oxygen levels response to abiotic stimulus	cellular anatomical structure extracellular region intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily	Homologous Superfamily
A, B	IPR018523	Isocitrate lyase/phosphorylmutase, conserved site	Conserved Site
A, B	IPR040442	Pyruvate kinase-like domain superfamily	Homologous Superfamily
A, B	IPR006254	Isocitrate lyase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	isocitrate lyase M-CSA #272	Isocitrate lyase catalyses the reversible lysis of a C-C bond of isocitrate to form glycoxylate and succinate. The enzyme directs acetyl-CoA away from beta-oxidation of fatty acids into the glyoxylate shunt pathway, giving a net carbon gain. It plays a key role in the persistence of Mycobacterium tuberculosis within humans.	Defined by 7 residues: ASP:A-154 [auth A-153]HIS:A-181 [auth A-180]CYS:A-192 [auth A-191]HIS:A-194 [auth A-193]ARG:A-229 [auth A-228]SER:A-316 [auth A-315]SER:A-318 [auth A-317] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.1.3.1 (PDB Primary Data) Search M-CSA Motif + EC 4.1.3.1

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.