Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BFer4_8e1yq4B1 A: alpha arraysX: alpha-helical ferredoxin-likeH: alpha-helical ferredoxin (From Topology)T: alpha-helical ferredoxinF: Fer4_8ECOD (1.6)
BFer2_3e1yq4B2 A: a+b two layersX: beta-GraspH: Ubiquitin-relatedT: Ubiquitin-likeF: Fer2_3ECOD (1.6)
CSdh_cyte1yq4C1 A: alpha bundlesX: Transmembrane heme-binding four-helical bundle (From Homology)H: Transmembrane heme-binding four-helical bundleT: Fumarate reductase respiratory complex transmembrane subunitsF: Sdh_cytECOD (1.6)
DCybSe1yq4D1 A: alpha bundlesX: Transmembrane heme-binding four-helical bundle (From Homology)H: Transmembrane heme-binding four-helical bundleT: Fumarate reductase respiratory complex transmembrane subunitsF: CybSECOD (1.6)
ASucc_DH_flav_Ce1yq4A5 A: alpha bundlesX: Spectrin repeat-likeH: Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain (From Topology)T: Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domainF: Succ_DH_flav_CECOD (1.6)
AFAD_binding_2e1yq4A1 A: a+b complex topologyX: 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 domainF: FAD_binding_2ECOD (1.6)
AFAD_binding_3_1ste1yq4A4 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: FAD_binding_3_1stECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF130852Fe-2S iron-sulfur cluster binding domain (Fer2_3)2Fe-2S iron-sulfur cluster binding domainThe 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.Domain
PF135344Fe-4S dicluster domain (Fer4_17)4Fe-4S dicluster domainThis family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.Domain
PF01127Succinate dehydrogenase/Fumarate reductase transmembrane subunit (Sdh_cyt)Succinate dehydrogenase/Fumarate reductase transmembrane subunit- Family
PF02910Fumarate reductase flavoprotein C-term (Succ_DH_flav_C)Fumarate reductase flavoprotein C-termThis family contains fumarate reductases, succinate dehydrogenases and L-aspartate oxidases.Domain
PF00890FAD binding domain (FAD_binding_2)FAD binding domain- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
succinate dehydrogenase Ip subunit
SUCCINATE DEHYDROGENASE CYTOCHROME B, LARGE SUBUNIT
SUCCINATE DEHYDROGENASE CYTOCHROME B, SMALL SUBUNIT
Succinate dehydrogenase flavoprotein subunit

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR025192Succinate dehydogenase/fumarate reductase N-terminalDomain
IPR0360102Fe-2S ferredoxin-like superfamilyHomologous Superfamily
IPR0010412Fe-2S ferredoxin-type iron-sulfur binding domainDomain
IPR0060582Fe-2S ferredoxin, iron-sulphur binding siteBinding Site
IPR004489Succinate dehydrogenase/fumarate reductase iron-sulphur proteinFamily
IPR009051Alpha-helical ferredoxinHomologous Superfamily
IPR050573Succinate Dehydrogenase/Fumarate Reductase Iron-SulfurFamily
IPR0179004Fe-4S ferredoxin, iron-sulphur binding, conserved siteConserved Site
IPR0178964Fe-4S ferredoxin-type, iron-sulphur binding domainDomain
IPR012675Beta-grasp domain superfamilyHomologous Superfamily
IPR018495Succinate dehydrogenase, cytochrome b subunit, conserved siteConserved Site
IPR034804Fumarate reductase/succinate dehydrogenase, transmembrane subunitHomologous Superfamily
IPR000701Succinate dehydrogenase/fumarate reductase type B, transmembrane subunitFamily
IPR014314Succinate dehydrogenase, cytochrome b556 subunitFamily
IPR034804Fumarate reductase/succinate dehydrogenase, transmembrane subunitHomologous Superfamily
IPR007992Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, CybSFamily
IPR015939Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminalDomain
IPR003952Fumarate reductase/succinate dehydrogenase, FAD-binding siteBinding Site
IPR037099Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamilyHomologous Superfamily
IPR036188FAD/NAD(P)-binding domain superfamilyHomologous Superfamily
IPR003953FAD-dependent oxidoreductase 2, FAD binding domainDomain
IPR030664FAD-dependent oxidoreductase SdhA/FrdA/AprAFamily
IPR027477Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamilyHomologous Superfamily
IPR014006Succinate dehydrogenase/fumarate reductase, flavoprotein subunitFamily
IPR011281Succinate dehydrogenase, flavoprotein subunitFamily

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

ChainsEnzyme NameDescriptionCatalytic Residues
succinate dehydrogenase (ubiquinone)  M-CSA #294

succinate dehydrogenase is a flavoprotein complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilise ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone.

Defined by 8 residues: PHE:A-130GLN:A-251HIS:A-253LEU:A-263GLU:A-266ARG:A-297HIS:A-364ARG:A-408
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