Annotations: 1FGH

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1fgha1	Alpha and beta proteins (a/b)	The 'swivelling' beta/beta/alpha domain	LeuD/IlvD-like	LeuD-like	Aconitase A, C-terminal domain	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
A	d1fgha2	Alpha and beta proteins (a/b)	Aconitase iron-sulfur domain	Aconitase iron-sulfur domain	Aconitase iron-sulfur domain	Aconitase A, N-terminal domain	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Aconitase iron-sulfur domain	8033064	3001516	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	LeuD/IlvD-like	8043900	3000947	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00694	e1fghA2	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: PF00694	ECOD (1.6)
A	PF00330	e1fghA4	A: a/b three-layered sandwiches	X: Aconitase iron-sulfur domain (From Homology)	H: Aconitase iron-sulfur domain	T: Aconitase iron-sulfur domain	F: PF00330	ECOD (1.6)
A	PF00330	e1fghA3	A: a/b three-layered sandwiches	X: Aconitase iron-sulfur domain (From Homology)	H: Aconitase iron-sulfur domain	T: Aconitase iron-sulfur domain II	F: PF00330	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.499.10	Alpha Beta	2-Layer Sandwich	Aconitase	domain 3	CATH (4.3.0)
A	3.40.1060.10	Alpha Beta	3-Layer(aba) Sandwich	Aconitase	Domain 2	CATH (4.3.0)
A	3.20.19.10	Alpha Beta	Alpha-Beta Barrel	Aconitase	domain 4	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00330	Aconitase family (aconitate hydratase) (Aconitase)	Aconitase family (aconitate hydratase)	-	Family
A	PF00694	Aconitase C-terminal domain (Aconitase_C)	Aconitase C-terminal domain	Members of this family usually also match to Pfam:PF00330. This domain undergoes conformational change in the enzyme mechanism [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ACONITASE	cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding aconitate hydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity iron-sulfur cluster binding cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding aconitate hydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity iron-sulfur cluster binding 3 iron, 4 sulfur cluster binding metal cluster binding 4 iron, 4 sulfur cluster binding	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds cellular metabolic process metabolic process cellular process primary metabolic process generation of precursor metabolites and energy organic substance metabolic process tricarboxylic acid metabolic process oxoacid metabolic process carboxylic acid metabolic process small molecule metabolic process aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds cellular metabolic process metabolic process cellular process primary metabolic process generation of precursor metabolites and energy organic substance metabolic process tricarboxylic acid metabolic process oxoacid metabolic process carboxylic acid metabolic process small molecule metabolic process organic acid metabolic process citrate metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000573	Aconitase A/isopropylmalate dehydratase small subunit, swivel domain	Domain
A	IPR015932	Aconitase, domain 2	Homologous Superfamily
A	IPR006248	Aconitase, mitochondrial-like	Family
A	IPR036008	Aconitase, iron-sulfur domain	Homologous Superfamily
A	IPR001030	Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain	Domain
A	IPR015928	Aconitase/3-isopropylmalate dehydratase, swivel	Homologous Superfamily
A	IPR015931	Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomain 1/3	Homologous Superfamily
A	IPR018136	Aconitase family, 4Fe-4S cluster binding site	Binding Site

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	PCA	Parent Component: GLN RESID: AA0031 PSI-MOD : 2-pyrrolidone-5-carboxylic acid (Gln) MOD:00040 , 2-pyrrolidone-5-carboxylic acid (Glu) MOD:00420

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

Chains	Enzyme Name	Description	Catalytic Residues
A	aconitate hydratase M-CSA #552	Aconitase (aconitate hydratase) contains an Fe-S cluster within the active site. This can be in the form 4Fe-4S in which case the enzyme functions as an aconitate hydratase, performing the dehydration-rehydration of citrate to isocitrate via cis-aconitate in the second and third steps of the Krebs cycle. When the Fe-S cluster is in the form 3Fe-4S (cytosolic aconitase) the enzyme functions as an Iron Regulatory Protein (IRP) which binds to a conserved sequence (Iron Responsive Element; IRE) in mRNAs encoding proteins that function in the maintenance of iron homeostasis thus regulating the translation of that mRNA. Aconitase occurs in bacteria, plants, animals and fungi in mitochondrial and cytosolic forms.	Defined by 6 residues: ASP:A-100HIS:A-101ASP:A-165ARG:A-447SER:A-642ARG:A-644 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.2.1.3 (PDB Primary Data) Search M-CSA Motif + EC 4.2.1.3

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.