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0DHSB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSDHB
DescriptionSuccinate dehydrogenase iron-sulfur protein, mitochondrial precursor (ec 1.3.5.1) (ip) (iron-sulfur subunit of complex ii).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (TAS)
0006099 tricarboxylic acid cycle (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The ferredoxin protein family are electron carrier proteins with an iron-sulphur cofactor that act in a wide variety of metabolic reactions. Ferredoxins can be divided into several subgroups depending upon the physiological nature of the iron-sulphur cluster(s) and according to sequence similarities. This entry represents members of the 2Fe-2S ferredoxin family that have a general core structure consisting of beta(2)-alpha-beta(2).hich includes putidaredoxin and terpredoxin.nd adrenodoxin . This entry also represents 2Fe-2S ferredoxin domains from multidomain proteins.uch as aldehyde oxidoreductase (N-terminal).anthine oxidase (N-terminal).hthalate dioxygenase reductase (C-terminal).uccinate dehydrogenase iron-sulphur protein (N-terminal).nd methane monooxygenase reductase (N-terminal). In addition.his entry includes the N-terminal additional domain of threonyl-tRNA synthetase (ThrRS). class II multi-domain enzyme that represses its own translation; the N-terminal additional domain has a beta(2)-alpha-beta(2) core structure .
  IPR012675:2Fe-2S Ferredoxin-like fold
The ferredoxin protein family are electron carrier proteins with an iron-sulphur cofactor that act in a wide variety of metabolic reactions. Ferredoxins can be divided into several subgroups depending upon the physiological nature of the iron-sulphur cluster(s) and according to sequence similarities. This entry represents members of the 2Fe-2S ferredoxin family that have a general core structure consisting of beta(2)-alpha-beta(2).hich includes putidaredoxin and terpredoxin.nd adrenodoxin . They are proteins of around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This conserved region is also found as a domain in various metabolic enzymes and in multidomain proteins.uch as aldehyde oxidoreductase (N-terminal).anthine oxidase (N-terminal).hthalate dioxygenase reductase (C-terminal).uccinate dehydrogenase iron-sulphur protein (N-terminal).nd methane monooxygenase reductase (N-terminal).
  IPR001041:Ferredoxin
Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion.uccinate + FAD+ = fumarate + FADH2 (). In Escherichia coli.he forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This group also includes a region of the B subunit of a cytosolic archaeal fumarate reductase.
  IPR004489:Succinate dehydrogenase/fumarate reductase iron-sulfur protein
The alpha-helical ferredoxin domain contains two Fe4-S4 clusters.ypical of bacterial ferredoxin. Iron-sulphur proteins play an important role in electron transfer processes and in various enzymatic reactions. In eukaryotes.he mitochondria are the major site of Fe-S cluster biosynthesis in the cell.sed for the assembly of mitochondrial and non-mitochondrial Fe-S proteins. The alpha-helical ferredoxin domain is present in several proteins involved in redox reactions.ncluding the C-terminal of the respiratory proteins succinate dehydrogenase (SQR) in bacteria/mitochondria.nd fumarate reductase (QFR) in bacteria. SQR is analogous to the mitochondrial respiratory complex II.nd is involved in the electron transport pathway from succinate as a donor to the acceptor ubiquinone . SQR helps prevent the formation of reactive oxygen species and is used during aerobic respiration.hereas QFR does not and.onsequently.s used to catalyse the final step of anaerobic respiration using the acceptor fumarate .The alpha-helical ferredoxin domain is also present in the N-terminal of the cytosolic protein dihydropyrimidine dehydrogenase.DPD) which catalyses the NADPH-dependent.ate-limiting step in pyrimidine degradation.onverting pyrimidines to 5.-dihydro compounds . DPD catalysis involves electron transfer from NADPH to the substrate via the Fe4-S4 centre and FAD. In mammals.his pathway produces the neurotransmitter beta-alanine.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009051:Alpha-helical ferredoxin
Fumarate reductase catalyses the reduction of fumarate to succinate.oupling the reaction to the oxidation of quinol to quinine . This reaction is opposite to that catalysed by succinate dehydrogenase. This entry represents the C-terminal domain of fumarate reductase.hich is structurally related to the N-terminal domain of dihydropyrimidine dehydrogenase.n enzyme that catalyses the NADPH-dependent conversion of pyrimidines to 5.-dihydro compounds .
  IPR012285:Fumarate reductase, C-terminal
IPR012675:Ferredoxin_fold 
Evalue:-37.1191864013672 
Location:36-142IPR009051:Helical_ferredxn 
Evalue:0 
Location:143-270
SequencesProtein: DHSB_HUMAN (280 aa)
mRNA: NM_003000
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK00235
  Level 3 annotation:
    succinate dehydrogenase (ubiquinone) iron-sulfur protein precursor
  Level 2 annotation:
    Citrate cycle (TCA cycle)
    Oxidative phosphorylation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 67 residues, 17217840-17218040Exon2: 43 residues, 17221689-17221812Exon3: 36 residues, 17223054-17223156Exon4: 41 residues, 17226830-17226947Exon5: 47 residues, 17227681-17227818Exon6: 30 residues, 17232141-17232227Exon7: 44 residues, 17243842-17243970Exon8: 70 residues, 17253029-17253233Exon9: 2 residues, -Jump to DHSB_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3774 17605865-17638807 ~-33K 519(RCC2)(-)Loci: 3773 17217840-17253233 ~-35K 510(SDHB)(-)Link out to UCSC