HAMAP rule MF_00709
General rule information
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Accession | MF_00709 |
Dates | 9-SEP-2003 (Created) 15-MAY-2020 (Last updated, Version 27) |
Name | Fumarate_red_D |
Scope | Bacteria; Gammaproteobacteria
Bacteria; Mycobacterium |
Template | P0A8Q3 (FRDD_ECOLI) |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
case <OC:Enterobacterales>
Protein name |
|
else
Protein name |
|
end case
Gene name |
|
Comments
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case <OC:Enterobacterales>
Function | Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones. |
else
Function | Anchors the catalytic components of the fumarate reductase complex to the cell membrane, binds quinones. |
end case
Subunit | Part of an enzyme complex containing four subunits: a flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic anchor proteins (FrdC and FrdD). |
case not defined <Property:Membrane> or <Property:Membrane=1>
Subcellular location | Cell membrane; Multi-pass membrane protein. |
else case <Property:Membrane=2>
Subcellular location | Cell inner membrane; Multi-pass membrane protein. |
end case
Similarity | Belongs to the FrdD family. |
Keywords
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case defined <Property:Membrane> and <Property:Membrane=2>
end case
Gene Ontology
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GO:0005886; Cellular component: plasma membrane.
GO:0045284; Cellular component: plasma membrane fumarate reductase complex.
GO:0000104; Molecular function: succinate dehydrogenase activity.
GO:0045284; Cellular component: plasma membrane fumarate reductase complex.
GO:0000104; Molecular function: succinate dehydrogenase activity.
Cross-references
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Pfam | PF02313; Fumarate_red_D; 1; |
Computed features
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General | Transmembrane; -; 3; trigger=yes; |
Additional information
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Size range | 114-130 amino acids |
Related rules | None |
Fusion | None |