Annotations: 1QJD

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1qjda1	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Flavocytochrome c3 (respiratory fumarate reductase), N-terminal domain	(Shewanella frigidimarina ) [TaxId: 56812 ],	SCOPe (2.08)
A	d1qjda2	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	Succinate dehydrogenase/fumarate reductase flavoprotein N-terminal domain	Flavocytochrome c3 (respiratory fumarate reductase)	(Shewanella frigidimarina ) [TaxId: 56812 ],	SCOPe (2.08)
A	d1qjda3	Alpha and beta proteins (a+b)	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain	Flavocytochrome c3 (respiratory fumarate reductase)	(Shewanella frigidimarina ) [TaxId: 56812 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	flavo_cyto_c_like	e1qjdA2	A: alpha arrays	X: HTH	H: HTH	T: HTH motif inserted in other structures	F: flavo_cyto_c_like	ECOD (1.6)
A	FAD_binding_2_1	e1qjdA3	A: a+b complex topology	X: Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain (From Topology)	H: Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain (From Topology)	T: Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain	F: FAD_binding_2_1	ECOD (1.6)
A	FAD_binding_3_1st	e1qjdA4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
A	Cytochrom_c3_2	e1qjdA1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: Cytochrom_c3_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.700.10	Alpha Beta	Alpha-Beta Complex	Flavocytochrome C3	Chain A, domain 1	CATH (4.3.0)
A	1.10.1130.10	Mainly Alpha	Orthogonal Bundle	Flavocytochrome C3	Chain A, domain 2	CATH (4.3.0)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF14537	Cytochrome c3 (Cytochrom_c3_2)	Cytochrome c3	-	Family
A	PF00890	FAD binding domain (FAD_binding_2)	FAD binding domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	FLAVOCYTOCHROME C3	oxidoreductase activity catalytic activity FMN binding binding nucleoside phosphate binding ion binding anion binding nucleotide binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding metal ion binding	-	cellular anatomical structure periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036280	Multiheme cytochrome superfamily	Homologous Superfamily
A	IPR003953	FAD-dependent oxidoreductase 2, FAD-binding domain	Domain
A	IPR012286	Tetrahaem cytochrome domain	Domain
A	IPR013087	Zinc finger C2H2-type	Domain
A	IPR050315	FAD-dependent oxidoreductase 2	Family
A	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR010960	Flavocytochrome c	Family
A	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	fumarate reductase (quinol) M-CSA #20	Fumarate respiration is the most commonly occurring type of anaerobic respiration with fumarate acting as a terminal electron acceptor. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). In Shewanella species, fumarate reductase is a soluble periplasmic, tetaheme, FAD-containing enzyme called flavocytochrome c3 (Fcc3). Fumarate reductases, which catalyse the interconversion of fumarate and succinate are known to be membrane bound in bacteria although soluble versions also exist in yeast, procyclic Trypanosoma brucei and several Shewanella species. The active site is located in the centre of the protein, at the interface between the three catalytic domains. Catalysis in the soluble fumarate reductase is essentially unidirectional (from fumarte to succinate).	Defined by 7 residues: HIS:A-365GLU:A-378ARG:A-381ARG:A-402HIS:A-504HIS:A-505ARG:A-544 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.3.2.4 (UniProt) Search M-CSA Motif + EC 1.3.2.4

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.