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0DHSA_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSDHA
DescriptionSuccinate dehydrogenase flavoprotein subunit, mitochondrial precursor (ec 1.3.5.1) (fp) (flavoprotein subunit of complex ii).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (TAS)
0005489 electron transporter activity (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:
In bacteria two distinct.embrane-bound.nzyme complexes are responsible forthe interconversion of fumarate and succinate (): fumaratereductase (Frd) is used in anaerobic growth.nd succinate dehydrogenase (Sdh)is used in aerobic growth. Both complexes consist of two main components: amembrane-extrinsic component composed of a FAD-binding flavoprotein and aniron-sulphur protein; and an hydrophobic component composed of a membraneanchor protein and/or a cytochrome B.In eukaryotes mitochondrial succinate dehydrogenase (ubiquinone) ()is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulphurprotein.The flavoprotein subunit is a protein of about 60 to 70 Kd to which FAD iscovalently bound to a histidine residue which is located in the N-terminalsection of the protein . The sequence around that histidine is wellconserved in Frd and Sdh from various bacterial and eukaryotic species .This family includes members that bind FAD such as the flavoprotein subunits fromsuccinate and fumarate dehydrogenase.spartate oxidase and the alpha subunit of adenylylsulphatereductase.
  IPR003953:Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
In bacteria two distinct.embrane-bound.nzyme complexes are responsible forthe interconversion of fumarate and succinate (): fumaratereductase (Frd) is used in anaerobic growth.nd succinate dehydrogenase (Sdh)is used in aerobic growth. Both complexes consist of two main components: amembrane-extrinsic component composed of a FAD-binding flavoprotein and aniron-sulphur protein; and an hydrophobic component composed of a membraneanchor protein and/or a cytochrome B.In eukaryotes mitochondrial succinate dehydrogenase (ubiquinone) ()is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulphurprotein.The flavoprotein subunit is a protein of about 60 to 70 Kd to which FAD iscovalently bound to a histidine residue which is located in the N-terminalsection of the protein . The sequence around that histidine is wellconserved in Frd and Sdh from various bacterial and eukaryotic species .This family includes members that bind FAD such as the flavoprotein subunits fromsuccinate and fumarate dehydrogenase.spartate oxidase and the alpha subunit of adenylylsulphatereductase.
  IPR004112:Fumarate reductase/succinate dehydrogenase flavoprotein, C-terminal
The pyridine nucleotide-disulphide reductases (PNDR) use the isoalloxazine ring of FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step.he reduced disulphide reduces the substrate. On the basis of sequence and structural similarities .NDR can be categorised into 2 groups. Class I includes glutathione reductase.rypanothione reductase.ipoamide dehydrogenase and mercuric reductase. They cover a wide range of catalytic functions: glutathione reductase ensures that the cell has enough reduced glutathione to maintain protein thiol groups in the reduced state ; trypanothione reductase carries out the analogous reaction in trypanosomal cells (trypanothione is an analogue of glutathione) ; lipoamide dehydrogenase.he E3 component of alpha-ketoacid dehydrogenase multienzyme complex.xidises the dihydrolypoyl groups of lipoate acyltransferase.nd so couples glycolysis to the tricarboxylic acid cycle ; and mercuric reductase enables bacteria to detoxify the mercuric ion by reducing it to elemental mercury.hich evaporates from the cell .
  IPR001100:Pyridine nucleotide-disulphide oxidoreductase, class I
This entry represents the succinate dehydrogenase flavoprotein subunit as found in the low-GC Gram-positive bacteria and a few other lineages. This enzyme may act in a complete or partial TCA cycle.r act in the opposite direction as fumarate reductase. In some but not all species.uccinate dehydrogenase and fumarate reductase may be encoded as separate isozymes.
  IPR011280:Succinate dehydrogenase or fumarate reductase, flavoprotein subunit, low-GC Gram-positive bacteria
Succinate dehydrogenase and fumarate reductase are homologous enzymes reversible in principle but favoured under different circumstances. This entry represents a narrowly defined clade of the succinate dehydrogenase flavoprotein subunit as found in mitochondria.n Rickettsia.n Escherichia coli and other proteobacteria.nd in a few other lineages. However.xcluded are all known fumarate reductases. It also excludes putative succinate dehydrogenases that appear to diverged before the split between E. coli succinate dehydrogenase and fumarate reductase.
  IPR011281:Succinate dehydrogenase, flavoprotein subunit
This entry describes both class I and class II oxidoreductases. FAD flavoproteins belonging to the family of pyridine nucleotide-disulphide oxidoreductases (glutathione reductase.rypanothione reductase.ipoamide dehydrogenase.ercuric reductase.hioredoxin reductase.lkyl hydroperoxide reductase) share sequence similarity with a number of other flavoprotein oxidoreductases.n particular with ferredoxin-NAD+ reductases involved in oxidative metabolism of a variety of hydrocarbons (rubredoxin reductase.utidaredoxin reductase.erpredoxin reductase.erredoxin-NAD+ reductase components of benzene 1.-dioxygenase.oluene 1.-dioxygenase.hlorobenzene dioxygenase.iphenyl dioxygenase).ADH oxidase and NADH peroxidase . Comparison of the crystal structures of human glutathione reductase and Escherichia coli thioredoxin reductase reveals different locations of their active sites.uggesting that the enzymes diverged from an ancestral FAD/NAD(P)H reductase and acquired their disulphide reductase activities independently . Despite functional similarities.xidoreductases of this family show no sequence similarity with adrenodoxin reductases and flavoprotein pyridine nucleotidecytochrome reductases (FPNCR) . Assuming that disulphide reductase activity emerged later.uring divergent evolution.he family can be referred to as FAD-dependent pyridine nucleotide reductases.ADPNR.To date.D structures of glutathione reductase .hioredoxin reductase .ercuric reductase .ipoamide dehydrogenase .rypanothione reductase and NADH peroxidase have been solved. The enzymes share similar tertiary structures based on a doubly-wound alpha/beta fold.ut the relative orientations of their FAD- and NAD(P)H-binding domains may vary significantly. By contrast with the FPNCR family.he folds of the FAD- and NAD(P)H-binding domains are similar.uggesting that the domains evolved by gene duplication .
  IPR013027:FAD-dependent pyridine nucleotide-disulphide oxidoreductase
This entry represents the succinate dehydrogenase flavoproteinsubunit as found in Gram-negative bacteria.itochondria.nd someArchaea. Mitochondrial forms interact with ubiquinone and are designated.ut can be degraded to . Some isozymes in Escherichiacoli and other species run primarily in the opposite direction andare designated fumarate reductase.
  IPR014006:Succinate dehydrogenase or fumarate reductase, flavoprotein subunit
IPR003953:FAD_binding_2 
Evalue:-181.721252441406 
Location:63-457IPR004112:Succ_DH_flav_C 
Evalue:-99.3665313720703 
Location:512-664
SequencesProtein: DHSA_HUMAN (664 aa)
mRNA: NM_004168
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 assignmentK00234
  Level 3 annotation:
    succinate dehydrogenase (ubiquinone) flavoprotein subunit precursor
  Level 2 annotation:
    Citrate cycle (TCA cycle)
    Oxidative phosphorylation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 30 residues, 271446-271533Exon2: 31 residues, 276596-276683Exon3: 56 residues, 277474-277636Exon4: 50 residues, 278533-278677Exon5: 57 residues, 278997-279162Exon6: 51 residues, 281299-281448Exon7: 43 residues, 283990-284115Exon8: 58 residues, 286591-286760Exon9: 67 residues, 288258-288454Exon10: 59 residues, 289542-289714Exon11: 41 residues, 293472-293591Exon12: 39 residues, 304106-304218Exon13: 45 residues, 304452-304583Exon14: 40 residues, 307507-307621Exon15: 116 residues, 309448-309792Exon16: 2 residues, -Jump to DHSA_HUMAN  
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Loci Cluster (Details)Loci: 4703 713890-746421 ~-33K 28538(-)Loci: 4704 1103499-1165150 ~-62K 28551(SLC12A7)(-)Loci: 3442 1278469-1299303 ~-21K 28553(SLC6A18)(+)Loci: 4705 1445908-1498543 ~-53K 28561(SLC6A3)(-)Loci: 3441 271446-309792 ~-38K 28525(SDHA)(+)Link out to UCSC