Annotations: 1FUQ

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1fuqa_	All alpha proteins	L-aspartase-like	L-aspartase-like	L-aspartase/fumarase	Fumarase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1fuqb_	All alpha proteins	L-aspartase-like	L-aspartase-like	L-aspartase/fumarase	Fumarase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	L-aspartase-like	8038814	3001572	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	L-aspartase-like	8038814	3001572	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	Lyase_1_N	e1fuqA3	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
A	FumaraseC_C	e1fuqA2	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: FumaraseC_C	ECOD (1.6)
A	Lyase_1_C	e1fuqA1	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)
B	Lyase_1_N	e1fuqB3	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
B	FumaraseC_C	e1fuqB2	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: FumaraseC_C	ECOD (1.6)
B	Lyase_1_C	e1fuqB1	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
A	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
A	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)
B	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
B	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
B	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00206	Lyase (Lyase_1)	Lyase	-	Domain
A, B	PF10415	Fumarase C C-terminus (FumaraseC_C)	Fumarase C C-terminus	Fumarase C catalyses the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The ...	Fumarase C catalyses the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit [1]. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	FUMARASE C	hydro-lyase activity lyase activity catalytic activity fumarate hydratase activity carbon-oxygen lyase activity identical protein binding protein binding 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 oxoacid metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process small molecule metabolic process fumarate 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 oxoacid metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process small molecule metabolic process fumarate metabolic process organic acid metabolic process malate metabolic process response to oxidative stress response to stimulus response to stress	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000362	Fumarate lyase family	Family
A, B	IPR022761	Fumarate lyase, N-terminal	Domain
A, B	IPR024083	Fumarase/histidase, N-terminal	Homologous Superfamily
A, B	IPR005677	Fumarate hydratase, class II	Family
A, B	IPR008948	L-Aspartase-like	Homologous Superfamily
A, B	IPR018951	Fumarase C, C-terminal	Domain
A, B	IPR020557	Fumarate lyase, conserved site	Conserved Site

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

Chains	Enzyme Name	Description	Catalytic Residues
A, B	fumarate hydratase (class II) M-CSA #569	Fumarase catalyses the reversible stereospecific hydration/dehydration of fumarate to L-malate during Kreb's cycle. Fumarase C is a member of the class II enzymes, a family which also includes aspartase, adenylosuccinate lyase and arginosuccinate, with high sequence similarity among its members. Fumarse C differs from the class I fumarase A and B enzymes in its lack of an apparent iron sulphur cluster.	Defined by 4 residues: HIS:A-188SER:B-318LYS:B-324GLU:B-331 Some residues are not modelled and lack atomic coordinates. Visualization is not available. Some residues are not modelled and lack atomic coordinates. Structure Motif searching is not available. EC: 4.2.1.2 (PDB Primary Data)

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.